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Conserved domains on  [gi|568979055|ref|XP_006515653|]
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serine/threonine-protein kinase D1 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
422-681 0e+00

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 588.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 422 TVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14082    1 QLYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKS 581
Cdd:cd14082   81 MEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINN 661
Cdd:cd14082  161 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPNPWKEISPDAIDLINN 240
                        250       260
                 ....*....|....*....|
gi 568979055 662 LLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14082  241 LLQVKMRKRYSVDKSLSHPW 260
PH_PKD cd01239
Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain; Protein Kinase C family is ...
259-386 1.23e-71

Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain; Protein Kinase C family is composed of three members, PKD1 (PKCmu), PKD2 and PKD3 (PKCnu). Like the C-type protein kinases (PKCs), PKDs are activated by diacylglycerol (DAG). They are involved in vesicular transport, cell proliferation, survival, migration and immune responses. PKD consists of tandem C1 domains, followed by a PH domain and a kinase domain. While the PKD PH domain has not been shown to bind phosphorylated inositol lipids and is not required for membrane translocation, it is required for nuclear export. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269945  Cd Length: 127  Bit Score: 229.58  E-value: 1.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 259 TKRRSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILCLEPAKPSALTPvGATPHCFEIT 338
Cdd:cd01239    1 TKRRSSKVLKEGWMVHYTNKDPLRKRHYWRLDTKCITLFQNETTSRYYKEIPLSEILSVEPADNPSLPP-GTPPHCFEIR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 339 TANVVYYVGENVVNPSSSPPNNSVLPSGIGPDVARMWEVAIQHALMPV 386
Cdd:cd01239   80 TANLVYYVGEDPDGESGPPKLIPPPESGSGTESARMWETAIRQALMPV 127
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
80-173 1.74e-65

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20842:

Pssm-ID: 412127  Cd Length: 94  Bit Score: 211.80  E-value: 1.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  80 SESFIGREKRSNSQSYIGRPIQLDKLLMSKVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKV 159
Cdd:cd20842    1 SESFIGREKRSNSQSYIGRPIQLDKILLSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCKFNCHKRCAPKV 80
                         90
                 ....*....|....
gi 568979055 160 PNNCLGEVTINGEL 173
Cdd:cd20842   81 PNNCLGEVAINGDL 94
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1-46 8.45e-27

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20839:

Pssm-ID: 412127  Cd Length: 72  Bit Score: 103.95  E-value: 8.45e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTG 46
Cdd:cd20839   27 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLTG 72
 
Name Accession Description Interval E-value
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
422-681 0e+00

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 588.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 422 TVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14082    1 QLYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKS 581
Cdd:cd14082   81 MEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINN 661
Cdd:cd14082  161 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPNPWKEISPDAIDLINN 240
                        250       260
                 ....*....|....*....|
gi 568979055 662 LLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14082  241 LLQVKMRKRYSVDKSLSHPW 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
430-682 1.47e-94

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 294.44  E-value: 1.47e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGD 508
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKK-KKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCeGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   509 MLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:smart00220  84 LFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYP--PNPWKEISHEAIDLINNLLQVK 666
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPpfPPPEWDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 568979055   667 MRKRYSVDKTLSHPWL 682
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
PH_PKD cd01239
Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain; Protein Kinase C family is ...
259-386 1.23e-71

Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain; Protein Kinase C family is composed of three members, PKD1 (PKCmu), PKD2 and PKD3 (PKCnu). Like the C-type protein kinases (PKCs), PKDs are activated by diacylglycerol (DAG). They are involved in vesicular transport, cell proliferation, survival, migration and immune responses. PKD consists of tandem C1 domains, followed by a PH domain and a kinase domain. While the PKD PH domain has not been shown to bind phosphorylated inositol lipids and is not required for membrane translocation, it is required for nuclear export. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269945  Cd Length: 127  Bit Score: 229.58  E-value: 1.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 259 TKRRSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILCLEPAKPSALTPvGATPHCFEIT 338
Cdd:cd01239    1 TKRRSSKVLKEGWMVHYTNKDPLRKRHYWRLDTKCITLFQNETTSRYYKEIPLSEILSVEPADNPSLPP-GTPPHCFEIR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 339 TANVVYYVGENVVNPSSSPPNNSVLPSGIGPDVARMWEVAIQHALMPV 386
Cdd:cd01239   80 TANLVYYVGEDPDGESGPPKLIPPPESGSGTESARMWETAIRQALMPV 127
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
80-173 1.74e-65

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 211.80  E-value: 1.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  80 SESFIGREKRSNSQSYIGRPIQLDKLLMSKVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKV 159
Cdd:cd20842    1 SESFIGREKRSNSQSYIGRPIQLDKILLSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCKFNCHKRCAPKV 80
                         90
                 ....*....|....
gi 568979055 160 PNNCLGEVTINGEL 173
Cdd:cd20842   81 PNNCLGEVAINGDL 94
Pkinase pfam00069
Protein kinase domain;
430-682 1.94e-59

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 200.16  E-value: 1.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:pfam00069   5 RKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  510 LEMILsSEKGRLPEHITKFLITQILVALRHlhfknivhcdlkpenvllasadpfpqvklcdfgfariigeKSFRRSVVGT 589
Cdd:pfam00069  85 LFDLL-SEKGAFSEREAKFIMKQILEGLES----------------------------------------GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMY-PPNPWKEISHEAIDLINNLLQVKMR 668
Cdd:pfam00069 124 PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYaFPELPSNLSEEAKDLLKKLLKKDPS 203
                         250
                  ....*....|....
gi 568979055  669 KRYSVDKTLSHPWL 682
Cdd:pfam00069 204 KRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
424-672 1.78e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 189.45  E-value: 1.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:COG0515    9 YRI--LRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSF 582
Cdd:COG0515   87 EYVEGESLADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL---TPDGRVKLIDFGIARALGGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRS--VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPPNPWKEISHEAIDL 658
Cdd:COG0515  163 TQTgtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSpaELLRAHLREPPPPPSELRPDLPPALDAI 242
                        250
                 ....*....|....
gi 568979055 659 INNLLQVKMRKRYS 672
Cdd:COG0515  243 VLRALAKDPEERYQ 256
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
430-670 2.13e-47

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 171.15  E-value: 2.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:PTZ00263  24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKreiLKM--KQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFrrSV 586
Cdd:PTZ00263 102 GGELFTHLRK-AGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL---DNKGHVKVTDFGFAKKVPDRTF--TL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnPWKEisHEAIDLINNLLQ 664
Cdd:PTZ00263 176 CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTpfRIYEKILAGRLKFP--NWFD--GRARDLVKGLLQ 251

                 ....*.
gi 568979055 665 VKMRKR 670
Cdd:PTZ00263 252 TDHTKR 257
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1-46 8.45e-27

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 103.95  E-value: 8.45e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTG 46
Cdd:cd20839   27 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLTG 72
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
424-629 1.78e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 108.34  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIidkLR--FPTKQESQLR--NEVailQN---LHHPGVVNlecMFETPE 496
Cdd:NF033483   9 YEI--GERIGRGGMAEVYLAKDTRLDRDVAVKV---LRpdLARDPEFVARfrREA---QSaasLSHPNIVS---VYDVGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 ---RVFVVMEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGF 573
Cdd:NF033483  78 dggIPYIVMEYVDGRTLKDYIR-EHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI---TKDGRVKVTDFGI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 ARIIGEKSFRR--SVVGTPAYLAPEVLRNkGY--NRSlDMWSVGVIIYVSLSGTFPFNED 629
Cdd:NF033483 154 ARALSSTTMTQtnSVLGTVHYLSPEQARG-GTvdARS-DIYSLGIVLYEMLTGRPPFDGD 211
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
448-622 5.86e-24

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 108.39  E-value: 5.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   448 TGRDVAIKIIDKLRfPT--KQESQLRNEVAILQNLHHPGVVNLECMFET-PERVFVVMEKLHGDMLEMILSSEkGRLPEH 524
Cdd:TIGR03903    2 TGHEVAIKLLRTDA-PEeeHQRARFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAAD-GALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   525 ITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGF------ARIIGEKSFRRS--VVGTPAYLAPE 596
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIgtllpgVRDADVATLTRTteVLGTPTYCAPE 159
                          170       180
                   ....*....|....*....|....*.
gi 568979055   597 VLRNKGYNRSLDMWSVGVIIYVSLSG 622
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTG 185
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
114-163 1.68e-18

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 79.43  E-value: 1.68e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568979055   114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
114-163 4.14e-18

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 78.64  E-value: 4.14e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568979055  114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPEC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1-31 2.55e-08

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 50.52  E-value: 2.55e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568979055    1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:pfam00130  20 FLWGLGKQGLKCSWCKLNVHKRCHEKVPPEC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1-31 4.98e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 44.00  E-value: 4.98e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568979055     1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:smart00109  20 SIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
 
Name Accession Description Interval E-value
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
422-681 0e+00

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 588.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 422 TVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14082    1 QLYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKS 581
Cdd:cd14082   81 MEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINN 661
Cdd:cd14082  161 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPNPWKEISPDAIDLINN 240
                        250       260
                 ....*....|....*....|
gi 568979055 662 LLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14082  241 LLQVKMRKRYSVDKSLSHPW 260
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
423-681 3.54e-116

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 350.62  E-value: 3.54e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 423 VYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd05117    1 KYEL--GKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLH-GDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKS 581
Cdd:cd05117   79 ELCTgGELFDRIV--KKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEISHEAIDLI 659
Cdd:cd05117  157 KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGEteQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd05117  237 KRLLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
430-682 1.47e-94

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 294.44  E-value: 1.47e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGD 508
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKK-KKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCeGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   509 MLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:smart00220  84 LFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYP--PNPWKEISHEAIDLINNLLQVK 666
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPpfPPPEWDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 568979055   667 MRKRYSVDKTLSHPWL 682
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
430-681 2.02e-79

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 254.75  E-value: 2.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGD 508
Cdd:cd14003    6 KTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYAsGGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd14003   86 LFDYI--VNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL---DKNGNLKIIDFGLSNEFRGGSLLKTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQV 665
Cdd:cd14003  161 TPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDNDskLFRKILKGKYPIPSH----LSPDARDLIRRMLVV 236
                        250
                 ....*....|....*.
gi 568979055 666 KMRKRYSVDKTLSHPW 681
Cdd:cd14003  237 DPSKRITIEEILNHPW 252
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
431-682 4.19e-73

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 238.83  E-value: 4.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ------LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd14084   13 TLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREinkprnIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLEL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHG-DMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFR 583
Cdd:cd14084   93 MEGgELFDRVVSNK--RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLSKILGETSLM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVGTPAYLAPEVLRNKG---YNRSLDMWSVGVIIYVSLSGTFPFNE---DEDIHDQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd14084  171 KTLCGTPTYLAPEVLRSFGtegYTRAVDCWSLGVILFICLSGYPPFSEeytQMSLKEQILSGKYTFIPKAWKNVSEEAKD 250
                        250       260
                 ....*....|....*....|....*
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14084  251 LVKKMLVVDPSRRPSIEEALEHPWL 275
PH_PKD cd01239
Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain; Protein Kinase C family is ...
259-386 1.23e-71

Protein kinase D (PKD/PKCmu) pleckstrin homology (PH) domain; Protein Kinase C family is composed of three members, PKD1 (PKCmu), PKD2 and PKD3 (PKCnu). Like the C-type protein kinases (PKCs), PKDs are activated by diacylglycerol (DAG). They are involved in vesicular transport, cell proliferation, survival, migration and immune responses. PKD consists of tandem C1 domains, followed by a PH domain and a kinase domain. While the PKD PH domain has not been shown to bind phosphorylated inositol lipids and is not required for membrane translocation, it is required for nuclear export. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269945  Cd Length: 127  Bit Score: 229.58  E-value: 1.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 259 TKRRSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILCLEPAKPSALTPvGATPHCFEIT 338
Cdd:cd01239    1 TKRRSSKVLKEGWMVHYTNKDPLRKRHYWRLDTKCITLFQNETTSRYYKEIPLSEILSVEPADNPSLPP-GTPPHCFEIR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 339 TANVVYYVGENVVNPSSSPPNNSVLPSGIGPDVARMWEVAIQHALMPV 386
Cdd:cd01239   80 TANLVYYVGEDPDGESGPPKLIPPPESGSGTESARMWETAIRQALMPV 127
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
431-681 6.18e-69

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 227.21  E-value: 6.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-GDM 509
Cdd:cd14095    7 VIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGK-EHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKgGDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENvLLASADPFPQ--VKLCDFGFARIIGEKSFrrSVV 587
Cdd:cd14095   86 FDAITSS--TKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPEN-LLVVEHEDGSksLKLADFGLATEVKEPLF--TVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF----NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLL 663
Cdd:cd14095  161 GTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrspdRDQEELFDLILAGEFEFLSPYWDNISDSAKDLISRML 240
                        250
                 ....*....|....*...
gi 568979055 664 QVKMRKRYSVDKTLSHPW 681
Cdd:cd14095  241 VVDPEKRYSAGQVLDHPW 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
424-681 6.21e-68

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 224.66  E-value: 6.21e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF-PTKQESQL-RNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14098    2 YQII--DRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVaGNDKNLQLfQREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLH-GDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARIIGEK 580
Cdd:cd14098   80 MEYVEgGDLMDFI--MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPV-IVKISDFGLAKVIHTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNK------GYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEIS 652
Cdd:cd14098  157 TFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSsqLPVEKRIRKGRYTQPPLVDFNIS 236
                        250       260
                 ....*....|....*....|....*....
gi 568979055 653 HEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14098  237 EEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
432-683 3.17e-67

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 222.35  E-value: 3.17e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDK--LRFpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14007    8 LGKGKFGNVYLAREKKSGFIVALKVISKsqLQK-SGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSfRRSVVGT 589
Cdd:cd14007   87 LYKELKK-QKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNG---ELKLADFGWSVHAPSNR-RKTFCGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQVKM 667
Cdd:cd14007  162 LDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFesKSHQETYKRIQNVDIKFPSS----VSPEAKDLISKLLQKDP 237
                        250
                 ....*....|....*.
gi 568979055 668 RKRYSVDKTLSHPWLQ 683
Cdd:cd14007  238 SKRLSLEQVLNHPWIK 253
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
80-173 1.74e-65

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 211.80  E-value: 1.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  80 SESFIGREKRSNSQSYIGRPIQLDKLLMSKVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKV 159
Cdd:cd20842    1 SESFIGREKRSNSQSYIGRPIQLDKILLSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCKFNCHKRCAPKV 80
                         90
                 ....*....|....
gi 568979055 160 PNNCLGEVTINGEL 173
Cdd:cd20842   81 PNNCLGEVAINGDL 94
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
419-682 1.03e-64

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 216.45  E-value: 1.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQIFPdEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAIL-QNLHHPGVVNLECMFETPER 497
Cdd:cd14106    4 NINEVYTVES-TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLeLCKDCPRVVNLHEVYETRSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 VFVVMEKLHGDMLEMILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARII 577
Cdd:cd14106   83 LILILELAAGGELQTLLDEE-ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEISHEA 655
Cdd:cd14106  162 GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDdkQETFLNISQCNLDFPEELFKDVSPLA 241
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14106  242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
432-681 1.39e-63

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 212.51  E-value: 1.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPK---RDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdPFPQVKLCDFGFARIIGEKSFRRSVVGTPA 591
Cdd:cd14006   78 DRLA-ERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR-PSPQIKIIDFGLARKLNPGEELKEIFGTPE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 592 YLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRK 669
Cdd:cd14006  156 FVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFlgEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPRK 235
                        250
                 ....*....|..
gi 568979055 670 RYSVDKTLSHPW 681
Cdd:cd14006  236 RPTAQEALQHPW 247
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
424-682 1.50e-63

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 212.81  E-value: 1.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPdeVLGSGQFGIVYGGKHRKTG--RDVAIKIIDKLRFPTK-QESQLRNEVAILQNLHHPGVVNLECMFETPERVFV 500
Cdd:cd14080    2 YRLGK--TIGEGSYSKVKLAEYTKSGlkEKVACKIIDKKKAPKDfLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKL-HGDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE 579
Cdd:cd14080   80 FMEYAeHGDLLEYIQ--KRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNN---NVKLSDFGFARLCPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFR---RSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNED---EDIHDQiQNAAFMYPPNPWKeIS 652
Cdd:cd14080  155 DDGDvlsKTFCGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDDSnikKMLKDQ-QNRKVRFPSSVKK-LS 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 653 HEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14080  233 PECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
420-681 5.50e-63

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 211.46  E-value: 5.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESqLRNEVAILQNLHHPGVVNLECMFETPERVF 499
Cdd:cd14083    1 IRDKYEF--KEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDS-LENEIAVLRKIKHPNIVQLLDIYESKSHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG-DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIg 578
Cdd:cd14083   78 LVMELVTGgELFDRIV--EKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSKME- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKEISHEAI 656
Cdd:cd14083  155 DSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDskLFAQILKAEYEFDSPYWDDISDSAK 234
                        250       260
                 ....*....|....*....|....*
gi 568979055 657 DLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14083  235 DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
432-681 3.77e-62

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 208.91  E-value: 3.77e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRfpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKkeiIK--RKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFR-RSVV 587
Cdd:cd05123   79 ELFSHLSKE-GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL---DSDGHIKLTDFGLAKELSSDGDRtYTFC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQV 665
Cdd:cd05123  155 GTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFyaENRKEIYEKILKSPLKFPEY----VSPEAKSLISGLLQK 230
                        250
                 ....*....|....*....
gi 568979055 666 KMRKR---YSVDKTLSHPW 681
Cdd:cd05123  231 DPTKRlgsGGAEEIKAHPF 249
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
432-681 4.54e-62

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 208.62  E-value: 4.54e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPA 591
Cdd:cd14009   81 QYIR-KRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAETLCGSPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 592 YLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRK 669
Cdd:cd14009  160 YMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNhvQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                        250
                 ....*....|..
gi 568979055 670 RYSVDKTLSHPW 681
Cdd:cd14009  240 RISFEEFFAHPF 251
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
434-684 5.30e-61

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 206.30  E-value: 5.30e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 434 SGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-QESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEM 512
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKnQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 513 ILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--------IGEKSFR- 583
Cdd:cd05579   83 LLENV-GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANG---HLKLTDFGLSKVglvrrqikLSIQKKSn 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 -------RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPwkEISHE 654
Cdd:cd05579  159 gapekedRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAEtpEEIFQNILNGKIEWPEDP--EVSDE 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568979055 655 AIDLINNLLQVKMRKR---YSVDKTLSHPWLQD 684
Cdd:cd05579  237 AKDLISKLLTPDPEKRlgaKGIEEIKNHPFFKG 269
Pkinase pfam00069
Protein kinase domain;
430-682 1.94e-59

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 200.16  E-value: 1.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:pfam00069   5 RKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  510 LEMILsSEKGRLPEHITKFLITQILVALRHlhfknivhcdlkpenvllasadpfpqvklcdfgfariigeKSFRRSVVGT 589
Cdd:pfam00069  85 LFDLL-SEKGAFSEREAKFIMKQILEGLES----------------------------------------GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMY-PPNPWKEISHEAIDLINNLLQVKMR 668
Cdd:pfam00069 124 PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYaFPELPSNLSEEAKDLLKKLLKKDPS 203
                         250
                  ....*....|....
gi 568979055  669 KRYSVDKTLSHPWL 682
Cdd:pfam00069 204 KRLTATQALQHPWF 217
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
431-681 2.60e-59

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 201.33  E-value: 2.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-DM 509
Cdd:cd14185    7 TIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGK-EDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGgDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLA-SADPFPQVKLCDFGFARIIGEKSFrrSVVG 588
Cdd:cd14185   86 FDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhNPDKSTTLKLADFGLAKYVTGPIF--TVCG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQ----IQNAAFMYPPNPWKEISHEAIDLINNLLQ 664
Cdd:cd14185  162 TPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQEElfqiIQLGHYEFLPPYWDNISEAAKDLISRLLV 241
                        250
                 ....*....|....*..
gi 568979055 665 VKMRKRYSVDKTLSHPW 681
Cdd:cd14185  242 VDPEKRYTAKQVLQHPW 258
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
430-682 1.48e-58

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 200.22  E-value: 1.48e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLrfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14166    9 EVLGSGAFSEVYLVKQRSTGKLYALKCIKKS--PLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGgE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIiGEKSFRRSVVG 588
Cdd:cd14166   87 LFDRIL--ERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLSKM-EQNGIMSTACG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVK 666
Cdd:cd14166  164 TPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETEsrLFEKIKEGYYEFESPFWDDISESAKDFIRHLLEKN 243
                        250
                 ....*....|....*.
gi 568979055 667 MRKRYSVDKTLSHPWL 682
Cdd:cd14166  244 PSKRYTCEKALSHPWI 259
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
424-672 4.27e-58

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 198.19  E-value: 4.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQ--LRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14014    2 YRL--VRLLGRGGMGEVYRARDTLLGRPVAIKVL-RPELAEDEEFRerFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKS 581
Cdd:cd14014   79 MEYVEGGSLADLLR-ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL---TEDGRVKLTDFGIARALGDSG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRS--VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd14014  155 LTQTgsVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDspAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                        250
                 ....*....|....*
gi 568979055 658 LINNLLQVKMRKRYS 672
Cdd:cd14014  235 IILRALAKDPEERPQ 249
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
430-693 4.89e-58

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 198.96  E-value: 4.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd05580    7 KTLGTGSFGRVRLVKHKDSGKYYALKILKKakiIKL--KQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 -GDMLEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFrrS 585
Cdd:cd05580   85 gGELFSLLRRS--GRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL---DSDGHIKITDFGFAKRVKDRTY--T 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnpwKEISHEAIDLINNLL 663
Cdd:cd05580  158 LCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENpmKIYEKILEGKIRFP----SFFDPDAKDLIKRLL 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 664 QVKMRKRYSVDK-----TLSHPWLQDYQtWLDLRE 693
Cdd:cd05580  234 VVDLTKRLGNLKngvedIKNHPWFAGID-WDALLQ 267
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
430-682 7.54e-58

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 197.56  E-value: 7.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14167    9 EVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGK-ETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGgE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd14167   88 LFDRIV--EKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSGSVMSTACG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVK 666
Cdd:cd14167  166 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDakLFEQILKAEYEFDSPYWDDISDSAKDFIQHLMEKD 245
                        250
                 ....*....|....*.
gi 568979055 667 MRKRYSVDKTLSHPWL 682
Cdd:cd14167  246 PEKRFTCEQALQHPWI 261
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
432-682 6.30e-57

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 194.78  E-value: 6.30e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTkqESQLRN---EVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSK--ESVLMKverEIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd14081   87 ELFDYLV-KKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL---DEKNNIKIADFGMASLQPEGSLLETSCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQV 665
Cdd:cd14081  163 SPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDnlRQLLEKVKRGVFHIPHF----ISPDAQDLLRRMLEV 238
                        250
                 ....*....|....*..
gi 568979055 666 KMRKRYSVDKTLSHPWL 682
Cdd:cd14081  239 NPEKRITIEEIKKHPWF 255
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-682 6.65e-57

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 196.10  E-value: 6.65e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd14086    3 YDL--KEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHG-DMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARII-GEKS 581
Cdd:cd14086   81 LVTGgELFEDIVARE--FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVqGDQQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIH---DQIQNAAFMYPPNPWKEISHEAIDL 658
Cdd:cd14086  159 AWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPF-WDEDQHrlyAQIKAGAYDYPSPEWDTVTPEAKDL 237
                        250       260
                 ....*....|....*....|....
gi 568979055 659 INNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14086  238 INQMLTVNPAKRITAAEALKHPWI 261
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
430-682 1.49e-56

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 193.62  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14002    7 ELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS-FRRSVVG 588
Cdd:cd14002   87 FQIL--EDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGG---VVKLCDFGFARAMSCNTlVLTSIKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQVK 666
Cdd:cd14002  162 TPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFytNSIYQLVQMIVKDPVKWPSN----MSPEFKSFLQGLLNKD 237
                        250
                 ....*....|....*.
gi 568979055 667 MRKRYSVDKTLSHPWL 682
Cdd:cd14002  238 PSKRLSWPDLLEHPFV 253
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
432-680 3.43e-56

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 191.33  E-value: 3.43e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPK-EKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVGT-- 589
Cdd:cd00180   80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL---DSDGTVKLADFGLAKDLDSDDSLLKTTGGtt 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 -PAYLAPEVLRNKGYNRSLDMWSVGVIIYvslsgtfpfnededihdqiqnaafmyppnpwkEIShEAIDLINNLLQVKMR 668
Cdd:cd00180  157 pPYYAPPELLGGRYYGPKVDIWSLGVILY--------------------------------ELE-ELKDLIRRMLQYDPK 203
                        250
                 ....*....|..
gi 568979055 669 KRYSVDKTLSHP 680
Cdd:cd00180  204 KRPSAKELLEHL 215
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
428-682 1.06e-55

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 192.18  E-value: 1.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQES------QLRNEVAILQNLH-HPGVVNLECMFETPERVFV 500
Cdd:cd14093    7 PKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEaeelreATRREIEILRQVSgHPNIIELHDVFESPTFIFL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEK 580
Cdd:cd14093   87 VFELCRKGELFDYLT-EVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL---DDNLNVKISDFGFATRLDEG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLR------NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIH--DQIQNAAFMYPPNPWKEIS 652
Cdd:cd14093  163 EKLRELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVmlRNIMEGKYEFGSPEWDDIS 242
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 653 HEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14093  243 DTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
430-682 1.28e-55

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 191.19  E-value: 1.28e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-- 507
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGgs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 --DMLEMilsseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS---F 582
Cdd:cd06606   86 laSLLKK-----FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG---VVKLADFGCAKRLAEIAtgeG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDihdqiqNAAFMY-------PPNPWKEISHEA 655
Cdd:cd06606  158 TKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGN------PVAALFkigssgePPPIPEHLSEEA 231
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06606  232 KDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
430-681 2.26e-55

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 191.27  E-value: 2.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQ--ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-H 506
Cdd:cd05581    7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDK-RHIIKEkkVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYApN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS----- 581
Cdd:cd05581   86 GDLLEYIR--KYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDM---HIKITDFGTAKVLGPDSspest 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 -------------FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEdIHDQIQNAAFMYPP 645
Cdd:cd05581  161 kgdadsqiaynqaRAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFrgsNEYL-TFQKIVKLEYEFPE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568979055 646 NpwkeISHEAIDLINNLLQVKMRKRYSVDKT------LSHPW 681
Cdd:cd05581  240 N----FPPDAKDLIQKLLVLDPSKRLGVNENggydelKAHPF 277
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
432-688 3.43e-54

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 187.43  E-value: 3.43e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLR-FPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHiVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVGTP 590
Cdd:cd05572   81 WTILR-DRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL---DSNGYVKLVDFGFAKKLGSGRKTWTFCGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED----IHDQI--QNAAFMYPPNpwkeISHEAIDLINNLLQ 664
Cdd:cd05572  157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEdpmkIYNIIlkGIDKIEFPKY----IDKNAKNLIKQLLR 232
                        250       260
                 ....*....|....*....|....*....
gi 568979055 665 VKMRKRY-----SVDKTLSHPWLQDYQtW 688
Cdd:cd05572  233 RNPEERLgylkgGIRDIKKHKWFEGFD-W 260
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
430-681 3.84e-54

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 187.55  E-value: 3.84e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14184    7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGK-EHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGgD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAS-ADPFPQVKLCDFGFARIIGEKSFrrSVV 587
Cdd:cd14184   86 LFDAITSSTK--YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEyPDGTKSLKLGDFGLATVVEGPLY--TVC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF----NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLL 663
Cdd:cd14184  162 GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrsenNLQEDLFDQILLGKLEFPSPYWDNITDSAKELISHML 241
                        250
                 ....*....|....*...
gi 568979055 664 QVKMRKRYSVDKTLSHPW 681
Cdd:cd14184  242 QVNVEARYTAEQILSHPW 259
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
430-682 1.19e-53

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 185.87  E-value: 1.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESqLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05122    6 EKIGKGGFGVVYKARHKKTGQIVAIKKI-NLESKEKKES-ILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSVVGT 589
Cdd:cd05122   84 LKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG---EVKLIDFGLSAQLSDGKTRNTFVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEdihdqIQNAAFMYPPNPWKEI------SHEAIDLINNLL 663
Cdd:cd05122  161 PYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELP-----PMKALFLIATNGPPGLrnpkkwSKEFKDFLKKCL 235
                        250
                 ....*....|....*....
gi 568979055 664 QVKMRKRYSVDKTLSHPWL 682
Cdd:cd05122  236 QKDPEKRPTAEQLLKHPFI 254
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
432-682 1.37e-53

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 185.51  E-value: 1.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESqLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-DML 510
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFI-KCRKAKDRED-VRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGgELF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARIIGEKSFRRSVVGTP 590
Cdd:cd14103   79 ERVVD-DDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGN-QIKIIDFGLARKYDPDKKLKVLFGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIH--DQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMR 668
Cdd:cd14103  157 EFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAEtlANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPR 236
                        250
                 ....*....|....
gi 568979055 669 KRYSVDKTLSHPWL 682
Cdd:cd14103  237 KRMSAAQCLQHPWL 250
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
430-680 4.12e-53

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 184.59  E-value: 4.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVN-LECmFETPERVFVVMEKL-HG 507
Cdd:cd08215    6 RVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKyYES-FEENGKLCIVMEYAdGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMIL--SSEKGRLPEH-ITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS-FR 583
Cdd:cd08215   85 DLAQKIKkqKKKGQPFPEEqILDWFV-QICLALKYLHSRKILHRDLKTQNIFLTKDG---VVKLGDFGISKVLESTTdLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIH---DQIQNAAfmYPPNPwKEISHEAIDLIN 660
Cdd:cd08215  161 KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPF-EANNLPalvYKIVKGQ--YPPIP-SQYSSELRDLVN 236
                        250       260
                 ....*....|....*....|
gi 568979055 661 NLLQVKMRKRYSVDKTLSHP 680
Cdd:cd08215  237 SMLQKDPEKRPSANEILSSP 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
424-682 4.12e-53

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 184.39  E-value: 4.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPT-KQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd14079    4 YIL--GKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSlDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKL-HGDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKS 581
Cdd:cd14079   82 EYVsGGELFDYI--VQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL---DSNMNVKIADFGLSNIMRDGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRS-LDMWSVGVIIYVSLSGTFPFnEDEDIHD---QIQNAAFMYPpnpwKEISHEAID 657
Cdd:cd14079  157 FLKTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPF-DDEHIPNlfkKIKSGIYTIP----SHLSPGARD 231
                        250       260
                 ....*....|....*....|....*
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14079  232 LIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
431-682 4.93e-53

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 184.27  E-value: 4.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-KLHGDM 509
Cdd:cd14087    8 LIGRGSFSRVVRVEHRVTRQPYAIKMIETKC---RGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMElATGGEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFA--RIIGEKSFRRSVV 587
Cdd:cd14087   85 FDRIIA--KGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLAstRKKGPNCLMKTTC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQV 665
Cdd:cd14087  163 GTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRtrLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLLTV 242
                        250
                 ....*....|....*..
gi 568979055 666 KMRKRYSVDKTLSHPWL 682
Cdd:cd14087  243 NPGERLSATQALKHPWI 259
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
420-682 1.63e-52

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 183.55  E-value: 1.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVF 499
Cdd:cd14169    1 INSVYEL--KEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGK-EAMVENEIAVLRRINHENIVSLEDIYESPTHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG-DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASadPFPQVKL--CDFGFARI 576
Cdd:cd14169   78 LAMELVTGgELFDRII--ERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAT--PFEDSKImiSDFGLSKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 iGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKEISHE 654
Cdd:cd14169  154 -EAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDseLFNQILKAEYEFDSPYWDDISES 232
                        250       260
                 ....*....|....*....|....*...
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14169  233 AKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
422-684 1.64e-52

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 184.81  E-value: 1.64e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 422 TVYQIFPDE-VLGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQEsqlrneVAILQNLH-HPGVVNLECMFETPERVF 499
Cdd:cd14092    3 QNYELDLREeALGDGSFSVCRKCVHKKTGQEFAVKIVSR-RLDTSRE------VQLLRLCQgHPNIVKLHEVFQDELHTY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG-DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIG 578
Cdd:cd14092   76 LVMELLRGgELLERI--RKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFARLKP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNK----GYNRSLDMWSVGVIIYVSLSGTFPF------NEDEDIHDQIQNAAFMYPPNPW 648
Cdd:cd14092  154 ENQPLKTPCFTLPYAAPEVLKQAlstqGYDESCDLWSLGVILYTMLSGQVPFqspsrnESAAEIMKRIKSGDFSFDGEEW 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 649 KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14092  234 KNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
424-672 1.78e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 189.45  E-value: 1.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:COG0515    9 YRI--LRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSF 582
Cdd:COG0515   87 EYVEGESLADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL---TPDGRVKLIDFGIARALGGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRS--VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPPNPWKEISHEAIDL 658
Cdd:COG0515  163 TQTgtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSpaELLRAHLREPPPPPSELRPDLPPALDAI 242
                        250
                 ....*....|....
gi 568979055 659 INNLLQVKMRKRYS 672
Cdd:COG0515  243 VLRALAKDPEERYQ 256
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
431-681 2.46e-52

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 182.22  E-value: 2.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFP-TKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14663    7 TLGEGTFAKVKFARNTKTGESVAIKIIDKEQVArEGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI---IGEKSFRRSV 586
Cdd:cd14663   87 LFSKIAK-NGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDG---NLKISDFGLSALseqFRQDGLLHTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSL-DMWSVGVIIYVSLSGTFPFnEDEDI---HDQIQNAAFMYPpnPWkeISHEAIDLINNL 662
Cdd:cd14663  163 CGTPNYVAPEVLARRGYDGAKaDIWSCGVILFVLLAGYLPF-DDENLmalYRKIMKGEFEYP--RW--FSPGAKSLIKRI 237
                        250
                 ....*....|....*....
gi 568979055 663 LQVKMRKRYSVDKTLSHPW 681
Cdd:cd14663  238 LDPNPSTRITVEQIMASPW 256
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
430-682 3.99e-52

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 181.60  E-value: 3.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK--LRFPtKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH- 506
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKssLTKP-KQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSn 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARII---GEKsfR 583
Cdd:cd14099   86 GSLMELL--KRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL---DENMNVKIGDFGLAARLeydGER--K 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPwkEISHEAIDLIN 660
Cdd:cd14099  159 KTLCGTPNYIAPEVLeKKKGHSFEVDIWSLGVILYTLLVGKPPFETSdvKETYKRIKKNEYSFPSHL--SISDEAKDLIR 236
                        250       260
                 ....*....|....*....|..
gi 568979055 661 NLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14099  237 SMLQPDPTKRPSLDEILSHPFF 258
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
432-682 1.32e-50

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 178.78  E-value: 1.32e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRK-TGRDVAIKIIDKLRF-----PTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd14096    9 IGEGAFSNVYKAVPLRnTGKPVAIKVVRKADLssdnlKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HG-DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFP-------------------- 564
Cdd:cd14096   89 DGgEIFHQIV--RLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIPFIPsivklrkadddetkvdegef 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 565 ----------QVKLCDFGFARIIGEKSfRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIH- 633
Cdd:cd14096  167 ipgvggggigIVKLADFGLSKQVWDSN-TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF-YDESIEt 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 634 --DQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14096  245 ltEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
420-682 1.65e-50

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 177.84  E-value: 1.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNE----VAILQNLHHPGVVNLECMFETP 495
Cdd:cd14196    3 VEDFYDI--GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEiereVSILRQVLHPNIITLHDVYENR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 496 ERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFlITQILVALRHLHFKNIVHCDLKPENVLLASAD-PFPQVKLCDFGFA 574
Cdd:cd14196   81 TDVVLILELVSGGELFDFLAQKESLSEEEATSF-IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 RIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEIS 652
Cdd:cd14196  160 HEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANITAVSYDFDEEFFSHTS 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 653 HEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14196  240 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
430-681 1.75e-50

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 177.10  E-value: 1.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRD-VAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14121    1 EKLGSGTYATVYKAYRKSGAREvVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd14121   81 DLSRFIRS-RRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSR-YNPVLKLADFGFAQHLKPNDEAHSLRG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQ-NAAFMYPPNPwkEISHEAIDLINNLLQV 665
Cdd:cd14121  159 SPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRsfEELEEKIRsSKPIEIPTRP--ELSADCRDLLLRLLQR 236
                        250
                 ....*....|....*.
gi 568979055 666 KMRKRYSVDKTLSHPW 681
Cdd:cd14121  237 DPDRRISFEEFFAHPF 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
432-682 3.29e-50

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 176.97  E-value: 3.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDK--LR-------FPTKQESQL---RNEVAILQNLHHPGVVNL-ECMfETPER- 497
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKsrLRkrregknDRGKIKNALddvRREIAIMKKLDHPNIVRLyEVI-DDPESd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 -VFVVMEKL-HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR 575
Cdd:cd14008   80 kLYLVLEYCeGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG---TVKISDFGVSE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 II--GEKSFRRSvVGTPAYLAPEVLR--NKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPPNPw 648
Cdd:cd14008  157 MFedGNDTLQKT-AGTPAFLAPELCDgdSKTYSgKAADIWALGVTLYCLVFGRLPFNGDNilELYEAIQNQNDEFPIPP- 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 649 kEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14008  235 -ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
430-682 3.44e-50

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 177.29  E-value: 3.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd07829    5 EKLGEGTYGVVYKAKDKKTGEIVALK---KIRLDNEEEgipsTALR-EISLLKELKHPNIVKLLDVIHTENKLYLVFEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIG--EKSFR 583
Cdd:cd07829   81 DQD-LKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRD---GVLKLADFGLARAFGipLRTYT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVgTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQIQ-----------------------NA 639
Cdd:cd07829  157 HEVV-TLWYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEI-DQLFkifqilgtpteeswpgvtklpdyKP 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 640 AFM-YPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07829  235 TFPkWPKNDLEKVlprlDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
430-687 5.23e-50

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 177.06  E-value: 5.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFptkqesQLRNEVAILQNL-HHPGVVNLECMFETPERVFVVMEKLHG- 507
Cdd:cd14091    6 EEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKR------DPSEEIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLRGg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQ-VKLCDFGFAriigeKSFRRS- 585
Cdd:cd14091   80 ELLDRIL--RQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPEsLRICDFGFA-----KQLRAEn 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 -VVGTPAY----LAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NED--EDIHDQIQNAAF-MYPPNpWKEISHE 654
Cdd:cd14091  153 gLLMTPCYtanfVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFasgPNDtpEVILARIGSGKIdLSGGN-WDHVSDS 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQT 687
Cdd:cd14091  232 AKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDS 264
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
432-682 7.41e-50

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 175.60  E-value: 7.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGELY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSVVGTPA 591
Cdd:cd14075   90 TKISTE-GKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNN---CVKVGDFGFSTHAKRGETLNTFCGSPP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 592 YLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQVKMR 668
Cdd:cd14075  166 YAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETvaKLKKCILEGTYTIPSY----VSEPCQELIRGILQPVPS 241
                        250
                 ....*....|....
gi 568979055 669 KRYSVDKTLSHPWL 682
Cdd:cd14075  242 DRYSIDEIKNSEWL 255
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
432-682 8.52e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 176.55  E-value: 8.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-DML 510
Cdd:cd14085   11 LGRGATSVVYRCRQKGTQKPYAVKKLKK----TVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGgELF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTP 590
Cdd:cd14085   87 DRIV--EKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTMKTVCGTP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE---DEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKM 667
Cdd:cd14085  165 GYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDergDQYMFKRILNCDYDFVSPWWDDVSLNAKDLVKKLIVLDP 244
                        250
                 ....*....|....*
gi 568979055 668 RKRYSVDKTLSHPWL 682
Cdd:cd14085  245 KKRLTTQQALQHPWV 259
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
419-682 1.05e-49

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 176.78  E-value: 1.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERV 498
Cdd:cd14168    7 DIKKIFEF--KEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGK-ESSIENEIAVLRKIKHENIVALEDIYESPNHL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 499 FVVMEKLHG-DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARII 577
Cdd:cd14168   84 YLVMQLVSGgELFDRIV--EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKME 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKEISHEA 655
Cdd:cd14168  162 GKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDskLFEQILKADYEFDSPYWDDISDSA 241
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14168  242 KDFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
431-682 2.88e-49

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 173.98  E-value: 2.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05578    7 VIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRnVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVGT 589
Cdd:cd05578   87 LRYHLQ-QKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---DEQGHVHITDFNIATKLTDGTLATSTSGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN-----EDEDIHDQIQNAAFMYPPNpWkeiSHEAIDLINNLLQ 664
Cdd:cd05578  163 KPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEihsrtSIEEIRAKFETASVLYPAG-W---SEEAIDLINKLLE 238
                        250
                 ....*....|....*....
gi 568979055 665 VKMRKRYSVDKTLS-HPWL 682
Cdd:cd05578  239 RDPQKRLGDLSDLKnHPYF 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
432-682 3.76e-49

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 173.89  E-value: 3.76e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQ----VKLCDFGFARI---IGEKSFRR 584
Cdd:cd14097   89 ELL-LRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLSVQkygLGEDMLQE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SvVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNL 662
Cdd:cd14097  168 T-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFvaKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNVLQQL 246
                        250       260
                 ....*....|....*....|
gi 568979055 663 LQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14097  247 LKVDPAHRMTASELLDNPWI 266
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
103-181 4.21e-49

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 167.07  E-value: 4.21e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 103 DKLLMSKVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLGEVTINGELLSPGAESD 181
Cdd:cd20843    1 DKMLLSKVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCKFNCHKRCATRVPNDCLGETLFNGDLVPMEAASD 79
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
423-681 5.79e-49

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 174.14  E-value: 5.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 423 VYQIfPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLrfPTKQESQLRNEVAIL-QNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14090    2 LYKL-TGELLGEGAYASVQTCINLYTGKEYAVKIIEKH--PGHSRSRVFREVETLhQCQGHPNILQLIEYFEDDERFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHG-DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEK 580
Cdd:cd14090   79 FEKMRGgPLLSHI--EKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIKLS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTP---------AYLAPEVL-----RNKGYNRSLDMWSVGVIIYVSLSGTFPF----NED------------- 629
Cdd:cd14090  157 STSMTPVTTPelltpvgsaEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFygrcGEDcgwdrgeacqdcq 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 630 EDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14090  237 ELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
424-681 7.70e-49

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 172.86  E-value: 7.70e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfptKQESQLRNEVailqNLH-----HPGVVNL----ECMFET 494
Cdd:cd14089    2 YTI-SKQVLGLGINGKVLECFHKKTGEKFALKVL-------RDNPKARREV----ELHwrasgCPHIVRIidvyENTYQG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PERVFVVMEKLHG-DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGF 573
Cdd:cd14089   70 RKCLLVVMECMEGgELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 ARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE------DIHDQIQNAAFMYPPNP 647
Cdd:cd14089  150 AKETTTKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaispGMKKRIRNGQYEFPNPE 229
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 648 WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14089  230 WSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
430-684 3.44e-48

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 172.34  E-value: 3.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF---PTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd14094    9 EVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFtssPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDML--EMILSSEKGRL-PEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGE-KSF 582
Cdd:cd14094   89 GADLcfEIVKRADAGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGEsGLV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINN 661
Cdd:cd14094  169 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFyGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRR 248
                        250       260
                 ....*....|....*....|...
gi 568979055 662 LLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14094  249 MLMLDPAERITVYEALNHPWIKE 271
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
424-682 3.68e-48

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 171.03  E-value: 3.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF----PtkqesQLRNEVAILQNLHHPGVVNLECMFETPERVF 499
Cdd:cd14078    5 YELH--ETIGSGGFAKVKLATHILTGEKVAIKIMDKKALgddlP-----RVKTEIEALKNLSHQHICRLYHVIETDNKIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLH-GDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARII- 577
Cdd:cd14078   78 MVLEYCPgGELFDYIV--AKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLL---DEDQNLKLIDFGLCAKPk 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 -GEKSFRRSVVGTPAYLAPEVLRNKGYNRS-LDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPnpWkeISH 653
Cdd:cd14078  153 gGMDHHLETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPFDDDnvMALYRKIQSGKYEEPE--W--LSP 228
                        250       260
                 ....*....|....*....|....*....
gi 568979055 654 EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14078  229 SSKLLLDQMLQVDPKKRITVKELLNHPWV 257
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
431-686 4.16e-48

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 170.85  E-value: 4.16e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd06623    8 VLGQGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSeKGRLPEHITKFLITQILVALRHLH-FKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSF-RRSVVG 588
Cdd:cd06623   87 ADLLKK-VGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKG---EVKIADFGISKVLENTLDqCNTFVG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPN-PWKEISHEAIDLINNLLQV 665
Cdd:cd06623  163 TVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFlpPGQPSFFELMQAICDGPPPSlPAEEFSPEFRDFISACLQK 242
                        250       260
                 ....*....|....*....|.
gi 568979055 666 KMRKRYSVDKTLSHPWLQDYQ 686
Cdd:cd06623  243 DPKKRPSAAELLQHPFIKKAD 263
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
419-682 1.23e-47

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 169.72  E-value: 1.23e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQIFPDEvLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQ-NLHHPGVVNLECMFETPER 497
Cdd:cd14198    4 NFNNFYILTSKE-LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLElAKSNPRVVNLHEVYETTSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 VFVVME-KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARI 576
Cdd:cd14198   83 IILILEyAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHE 654
Cdd:cd14198  163 IGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFvgEDNQETFLNISQVNVDYSEETFSSVSQL 242
                        250       260
                 ....*....|....*....|....*...
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14198  243 ATDFIQKLLVKNPEKRPTAEICLSHSWL 270
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
430-670 2.13e-47

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 171.15  E-value: 2.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:PTZ00263  24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKreiLKM--KQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFrrSV 586
Cdd:PTZ00263 102 GGELFTHLRK-AGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL---DNKGHVKVTDFGFAKKVPDRTF--TL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnPWKEisHEAIDLINNLLQ 664
Cdd:PTZ00263 176 CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTpfRIYEKILAGRLKFP--NWFD--GRARDLVKGLLQ 251

                 ....*.
gi 568979055 665 VKMRKR 670
Cdd:PTZ00263 252 TDHTKR 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
432-670 4.49e-47

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 167.33  E-value: 4.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRktGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLP-EHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKS-FRRSVVGT 589
Cdd:cd13999   79 DLLHKKKIPLSwSLRLKIAL-DIARGMNYLHSPPIIHRDLKSLNILLDEN---FTVKIADFGLSRIKNSTTeKMTGVVGT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRK 669
Cdd:cd13999  155 PRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEK 234

                 .
gi 568979055 670 R 670
Cdd:cd13999  235 R 235
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
432-682 4.88e-47

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 168.04  E-value: 4.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-QESQLRNEVAILQNLHHPGVVNLECMFETPE-RVFVVME-KLHGD 508
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfVEKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVMElGVQGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARII-----GEKSFR 583
Cdd:cd14165   89 LLEFIKL--RGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDFNIKLTDFGFSKRClrdenGRIVLS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFnEDEDIHD--QIQNAAFMYPPnPWKEISHEAIDLIN 660
Cdd:cd14165  164 KTFCGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPY-DDSNVKKmlKIQKEHRVRFP-RSKNLTSECKDLIY 241
                        250       260
                 ....*....|....*....|..
gi 568979055 661 NLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14165  242 RLLQPDVSQRLCIDEVLSHPWL 263
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
432-680 7.37e-47

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 167.16  E-value: 7.37e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRK-TGRDVAIKIIDKLRFpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNL-SKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLA-SADPFP-----QVKLCDFGFARIIGEKSFRR 584
Cdd:cd14120   80 ADYLQA-KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShNSGRKPspndiRLKIADFGFARFLQDGMMAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPwKEISHEAIDLINNL 662
Cdd:cd14120  159 TLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFqaQTPQELKAFYEKNANLRPNIP-SGTSPALKDLLLGL 237
                        250
                 ....*....|....*...
gi 568979055 663 LQVKMRKRYSVDKTLSHP 680
Cdd:cd14120  238 LKRNPKDRIDFEDFFSHP 255
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
424-685 7.43e-47

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 169.63  E-value: 7.43e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQ----LRnEVAILQNLHHPGVVNLECMFETPER-- 497
Cdd:cd07834    2 YEL--LKPIGSGAYGVVCSAYDKRTGRKVAIK---KISNVFDDLIDakriLR-EIKILRHLKHENIIGLLDILRPPSPee 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 ---VFVVMEKLHGDmLEMILSSEKGRLPEHItKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA 574
Cdd:cd07834   76 fndVYIVTELMETD-LHKVIKSPQPLTDDHI-QYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC---DLKICDFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 RIIGE---KSFRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVI---------------------IYVSLSGTFPfneD 629
Cdd:cd07834  151 RGVDPdedKGFLTEYVVTRWYRAPELLLSsKKYTKAIDIWSVGCIfaelltrkplfpgrdyidqlnLIVEVLGTPS---E 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 630 EDIhDQIQNAAFM--------YPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd07834  228 EDL-KFISSEKARnylkslpkKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
423-682 1.37e-46

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 166.25  E-value: 1.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 423 VYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd06627    1 NYQL--GDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA-RIIGEKS 581
Cdd:cd06627   79 EYVENGSLASIIKK-FGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG---LVKLADFGVAtKLNEVEK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnedediHDQIQNAAfMY-------PPNPwKEISHE 654
Cdd:cd06627  155 DENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY------YDLQPMAA-LFrivqddhPPLP-ENISPE 226
                        250       260
                 ....*....|....*....|....*...
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06627  227 LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
431-684 2.87e-46

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 166.81  E-value: 2.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF-PTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDm 509
Cdd:cd14209    8 TLGTGSFGRVMLVRHKETGNYYAMKILDKQKVvKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEYVPGG- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 lEMI-LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFrrSVVG 588
Cdd:cd14209   87 -EMFsHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI---DQQGYIKVTDFGFAKRVKGRTW--TLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQVK 666
Cdd:cd14209  161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQpiQIYEKIVSGKVRFP----SHFSSDLKDLLRNLLQVD 236
                        250       260
                 ....*....|....*....|...
gi 568979055 667 MRKRY-----SVDKTLSHPWLQD 684
Cdd:cd14209  237 LTKRFgnlknGVNDIKNHKWFAT 259
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
431-670 3.14e-46

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 167.39  E-value: 3.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ-LRNEVAIL-QNLHHPGVVNLECMFETPERVFVVMEKLHG- 507
Cdd:cd05570    2 VLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVEcTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNGg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05570   82 DLMFHIQRA--RRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL---DAEGHIKIADFGMCKEgIWGGNTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQ 664
Cdd:cd05570  157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDdeDELFEAILNDEVLYPRW----LSREAVSILKGLLT 232

                 ....*.
gi 568979055 665 VKMRKR 670
Cdd:cd05570  233 KDPARR 238
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
416-682 4.60e-46

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 165.58  E-value: 4.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 416 ENVDisTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ----ESQLRNEVAILQNLHHPGVVNLECM 491
Cdd:cd14194    1 ENVD--DYYDT--GEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrgvsREDIEREVSILKEIQHPNVITLHEV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 492 FETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASAD-PFPQVKLCD 570
Cdd:cd14194   77 YENKTDVILILELVAGGELFDFLAEKESLTEEEATEFL-KQILNGVYYLHSLQIAHFDLKPENIMLLDRNvPKPRIKIID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 571 FGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEDIHDqIQNAAFMYPPNP 647
Cdd:cd14194  156 FGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLAN-VSAVNYEFEDEY 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 648 WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14194  235 FSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
430-682 8.20e-46

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 164.10  E-value: 8.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQES-QLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-KLHG 507
Cdd:cd14073    7 ETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMvRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEyASGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVV 587
Cdd:cd14073   87 ELYDYI--SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL---DQNGNAKIADFGLSNLYSKDKLLQTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDEDIH--DQIQNAAFMYPPNPwkeisHEAIDLINNLLQ 664
Cdd:cd14073  162 GSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKRlvKQISSGDYREPTQP-----SDASGLIRWMLT 236
                        250
                 ....*....|....*...
gi 568979055 665 VKMRKRYSVDKTLSHPWL 682
Cdd:cd14073  237 VNPKRRATIEDIANHWWV 254
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
424-682 8.30e-46

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 164.72  E-value: 8.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVVM 502
Cdd:cd14197    9 YSLSPGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 E-KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKS 581
Cdd:cd14197   89 EyAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLI 659
Cdd:cd14197  169 ELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFlgDDKQETFLNISQMNVSYSEEEFEHLSESAIDFI 248
                        250       260
                 ....*....|....*....|...
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14197  249 KTLLIKKPENRATAEDCLKHPWL 271
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
429-684 1.05e-45

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 165.98  E-value: 1.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfptKQESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd14179   12 DKPLGEGSFSICRKCLHKKTNQEYAVKIVSK-----RMEANTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 -DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIigeKSFRRSV 586
Cdd:cd14179   87 gELLERI--KKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARL---KPPDNQP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPA----YLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN---------EDEDIHDQIQNAAFMYPPNPWKEISH 653
Cdd:cd14179  162 LKTPCftlhYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQchdksltctSAEEIMKKIKQGDFSFEGEAWKNVSQ 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 654 EAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14179  242 EAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD 272
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
420-684 2.30e-45

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 163.63  E-value: 2.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVF 499
Cdd:cd14183    4 ISERYKV--GRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGK-EHMIQNEVSILRRVKHPNIVLLIEEMDMPTELY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG-DMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL-ASADPFPQVKLCDFGFARII 577
Cdd:cd14183   81 LVMELVKGgDLFDAITSTN--KYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLATVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFrrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF----NEDEDIHDQIQNAAFMYPPNPWKEISH 653
Cdd:cd14183  159 DGPLY--TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrgsgDDQEVLFDQILMGQVDFPSPYWDNVSD 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 654 EAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14183  237 SAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
430-683 2.51e-45

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 163.64  E-value: 2.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE----SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd14195   11 EELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRgvsrEEIEREVNILREIQHPNIITLHDIFENKTDVVLILELV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRLPEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASAD-PFPQVKLCDFGFARIIGEKSFRR 584
Cdd:cd14195   91 SGGELFDFLAEKESLTEEEATQFL-KQILDGVHYLHSKRIAHFDLKPENIMLLDKNvPNPRIKLIDFGIAHKIEAGNEFK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNL 662
Cdd:cd14195  170 NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRL 249
                        250       260
                 ....*....|....*....|.
gi 568979055 663 LQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14195  250 LVKDPKKRMTIAQSLEHSWIK 270
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
429-682 2.80e-45

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 162.97  E-value: 2.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-KLHG 507
Cdd:cd14074    8 EETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILElGDGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasadpFPQ---VKLCDFGFAR--IIGEKsf 582
Cdd:cd14074   88 DMYDYIMKHENG-LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVF-----FEKqglVKLTDFGFSNkfQPGEK-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNR-SLDMWSVGVIIYVSLSGTFPFNE--DEDIHDQIQNAAFMYPPNpwkeISHEAIDLI 659
Cdd:cd14074  160 LETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEanDSETLTMIMDCKYTVPAH----VSPECKDLI 235
                        250       260
                 ....*....|....*....|...
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14074  236 RRMLIRDPKKRASLEEIENHPWL 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
430-683 2.85e-45

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 162.77  E-value: 2.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06614    6 EKIGEGASGEVYKATDRATGKEVAIK---KMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG-EKSFRRSVVG 588
Cdd:cd06614   83 LTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG---SVKLADFGFAAQLTkEKSKRNSVVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP-FNE----------DEDIHDqiqnaafmyPPNPWKeISHEAID 657
Cdd:cd06614  160 TPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPyLEEpplralflitTKGIPP---------LKNPEK-WSPEFKD 229
                        250       260
                 ....*....|....*....|....*.
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06614  230 FLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
430-683 2.90e-45

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 163.26  E-value: 2.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHR-KTGRDVAIKIIDKLRFpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14201   12 DLVGHGAFAVVFKGRHRkKTDWEVAIKSINKKNL-SKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFP------QVKLCDFGFARIIGEKSF 582
Cdd:cd14201   91 DLADYLQA-KGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKssvsgiRIKIADFGFARYLQSNMM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPwKEISHEAIDLIN 660
Cdd:cd14201  170 AATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFqaNSPQDLRMFYEKNKNLQPSIP-RETSPYLADLLL 248
                        250       260
                 ....*....|....*....|...
gi 568979055 661 NLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14201  249 GLLQRNQKDRMDFEAFFSHPFLE 271
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
431-695 2.91e-45

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 165.92  E-value: 2.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRfpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05573    8 VIGRGAFGEVWLVRDKDTGQVYAMKILRKsdmLK--REQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 -DMleMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA-RII-------- 577
Cdd:cd05573   86 gDL--MNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL---DADGHIKLADFGLCtKMNksgdresy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 -----------GEKSFRR----------SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED----- 631
Cdd:cd05573  161 lndsvntlfqdNVLARRRphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLvetys 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 632 --IHDQIqnaAFMYPPNPwkEISHEAIDLINNLLqVKMRKRY-SVDKTLSHPWLQDYQtWLDLRELE 695
Cdd:cd05573  241 kiMNWKE---SLVFPDDP--DVSPEAIDLIRRLL-CDPEDRLgSAEEIKAHPFFKGID-WENLRESP 300
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
421-682 3.06e-45

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 162.78  E-value: 3.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPtKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFV 500
Cdd:cd14193    1 NSYYNVNKEEILGGGRFGQVHKCEEKSSGLKLAAKII-KARSQ-KEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARIIGEK 580
Cdd:cd14193   79 VMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAN-QVKIIDFGLARRYKPR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDL 658
Cdd:cd14193  158 EKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFlgEDDNETLNNILACQWDFEDEEFADISEEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 568979055 659 INNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14193  238 ISKLLIKEKSWRMSASEALKHPWL 261
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
416-682 3.84e-45

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 163.04  E-value: 3.84e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 416 ENVDisTVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ----ESQLRNEVAILQNLHHPGVVNLECM 491
Cdd:cd14105    1 ENVE--DFYDI--GEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRrgvsREDIEREVSILRQVLHPNIITLHDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 492 FETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASAD-PFPQVKLCD 570
Cdd:cd14105   77 FENKTDVVLILELVAGGELFDFLAEKESLSEEEATEFL-KQILDGVNYLHTKNIAHFDLKPENIMLLDKNvPIPRIKLID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 571 FGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPW 648
Cdd:cd14105  156 FGLAHKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANITAVNYDFDDEYF 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 649 KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14105  236 SNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
421-682 4.47e-45

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 162.48  E-value: 4.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlrFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFV 500
Cdd:cd14191    1 SDFYDI--EERLGSGKFGQVFRLVEKKTKKVWAGKFFKA--YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHG-DMLEMILSSEKGRLPEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARIIGE 579
Cdd:cd14191   77 VLEMVSGgELFERIIDEDFELTERECIKYMR-QISEGVEYIHKQGIVHLDLKPENIMCVNKTG-TKIKLIDFGLARRLEN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd14191  155 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmgDNDNETLANVTSATWDFDDEAFDEISDDAKD 234
                        250       260
                 ....*....|....*....|....*
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14191  235 FISNLLKKDMKARLTCTQCLQHPWL 259
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
432-681 5.60e-45

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 161.67  E-value: 5.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-GDML 510
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSK---KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDdGRLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTP 590
Cdd:cd14115   78 DYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMR 668
Cdd:cd14115  156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDEskEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPR 235
                        250
                 ....*....|...
gi 568979055 669 KRYSVDKTLSHPW 681
Cdd:cd14115  236 RRPTAATCLQHPW 248
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
424-682 1.10e-44

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 161.25  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPdeVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfpTKQESQLRN------EVAIL---QNLHHPGVVNLECMFET 494
Cdd:cd14005    2 YEVGD--LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSR--VTEWAMINGpvpvplEIALLlkaSKPGVPGVIRLLDWYER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PERVFVVMEKLHG--DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASadPFPQVKLCDFG 572
Cdd:cd14005   78 PDGFLLIMERPEPcqDLFDFI--TERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINL--RTGEVKLIDFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 573 FARIIgEKSFRRSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDEDIHDqiqnaafmypPNPWKE- 650
Cdd:cd14005  154 CGALL-KDSVYTDFDGTRVYSPPEWIRHGRYHgRPATVWSLGILLYDMLCGDIPFENDEQILR----------GNVLFRp 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568979055 651 -ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14005  223 rLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
430-682 5.16e-44

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 159.38  E-value: 5.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFP----TKQesqLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-K 504
Cdd:cd14162    6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPedylQKF---LPREIEVIKGLKHPNLICFYEAIETTSRVYIIMElA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR-----IIGE 579
Cdd:cd14162   83 ENGDLLDYI--RKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL---DKNNNLKITDFGFARgvmktKDGK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRSVVGTPAYLAPEVLRNKGYNRSL-DMWSVGVIIYVSLSGTFPFnEDEDIH---DQIQNAAfMYPPNPwkEISHEA 655
Cdd:cd14162  158 PKLSETYCGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPF-DDSNLKvllKQVQRRV-VFPKNP--TVSEEC 233
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLqVKMRKRYSVDKTLSHPWL 682
Cdd:cd14162  234 KDLILRML-SPVKKRITIEEIKRDPWF 259
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
432-681 8.15e-44

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 158.64  E-value: 8.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfpTKQESQLRnEVAILQNL-HHPGVVN-LECMFETPERVFVVME-KLHGD 508
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPS--TKLKDFLR-EYNISLELsVHPHIIKtYDVAFETEDYYVFAQEyAPYGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMIlSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpFPQVKLCDFGFARIIGekSFRRSVVG 588
Cdd:cd13987   78 LFSII-PPQVG-LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKD-CRRVKLCDFGLTRRVG--STVKRVSG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVL---RNKGY--NRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQI-------QNAAFMYPPNPWKEISHEAI 656
Cdd:cd13987  153 TIPYTAPEVCeakKNEGFvvDPSIDVWAFGVLLFCCLTGNFPW-EKADSDDQFyeefvrwQKRKNTAVPSQWRRFTPKAL 231
                        250       260
                 ....*....|....*....|....*...
gi 568979055 657 DLINNLLQVKMRKRYSVD---KTLSHPW 681
Cdd:cd13987  232 RMFKKLLAPEPERRCSIKevfKYLGDRW 259
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
435-684 1.24e-43

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 158.41  E-value: 1.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-QESQLRNEVAILQNL-HHPGVVNLECMFETPERVFVVMEKLHGDMLEM 512
Cdd:cd05611    7 GAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKnQVTNVKAERAIMMIQgESPYVAKLYYSFQSKDYLYLVMEYLNGGDCAS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 513 ILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVGTPAY 592
Cdd:cd05611   87 LIKT-LGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFGLSRNGLEKRHNKKFVGTPDY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 593 LAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKR 670
Cdd:cd05611  163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAEtpDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKR 242
                        250
                 ....*....|....*..
gi 568979055 671 YS---VDKTLSHPWLQD 684
Cdd:cd05611  243 LGangYQEIKSHPFFKS 259
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
421-682 1.68e-43

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 158.16  E-value: 1.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQESQLrNEVAILQNLHHPGVVNLECMFETPERVFV 500
Cdd:cd14190    1 SSTFSIHSKEVLGGGKFGKVHTCTEKRTGLKLAAKVINK-QNSKDKEMVL-LEIQVMNQLNHRNLIQLYEAIETPNEIVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHG-DMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARIIGE 579
Cdd:cd14190   79 FMEYVEGgELFERIVD-EDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH-QVKIIDFGLARRYNP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIH--DQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd14190  157 REKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTEtlNNVLMGNWYFDEETFEHVSDEAKD 236
                        250       260
                 ....*....|....*....|....*
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14190  237 FVSNLIIKERSARMSATQCLKHPWL 261
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
424-682 1.73e-43

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 158.21  E-value: 1.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDEV--LGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14113    5 FDSFYSEVaeLGRGRFSVVKKCDQRGTKRAVATKFVNK---KLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKL-HGDMLEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEK 580
Cdd:cd14113   82 LEMAdQGRLLDYVVRW--GNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQIQNAA---FMYPPNPWKEISHEAID 657
Cdd:cd14113  160 YYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPF-LDESVEETCLNICrldFSFPDDYFKGVSQKAKD 238
                        250       260
                 ....*....|....*....|....*
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14113  239 FVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
428-685 3.13e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 157.77  E-value: 3.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKL---RFPTKQESQLRN----EVAILQNLH-HPGVVNLECMFETPERVF 499
Cdd:cd14182    7 PKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITgggSFSPEEVQELREatlkEIDILRKVSgHPNIIQLKDTYETNTFFF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLH-GDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIG 578
Cdd:cd14182   87 LVFDLMKkGELFDYL--TEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILL---DDDMNIKLTDFGFSCQLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLR------NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED--IHDQIQNAAFMYPPNPWKE 650
Cdd:cd14182  162 PGEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQmlMLRMIMSGNYQFGSPEWDD 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 651 ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd14182  242 RSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQY 276
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
430-680 3.94e-43

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 156.93  E-value: 3.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPE--RVFVVMEKL-H 506
Cdd:cd08217    6 ETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRAntTLYIVMEYCeG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMI--LSSEKGRLPEHITKFLITQILVALRHLHFKN-----IVHCDLKPENVLLaSADPFpqVKLCDFGFARIIGE 579
Cdd:cd08217   86 GDLAQLIkkCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFL-DSDNN--VKLGDFGLARVLSH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KS-FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEdiHDQ----IQNAAFmyPPNPwKEISHE 654
Cdd:cd08217  163 DSsFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAAN--QLElakkIKEGKF--PRIP-SRYSSE 237
                        250       260
                 ....*....|....*....|....*.
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd08217  238 LNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
430-682 3.95e-43

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 156.98  E-value: 3.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfPTKQESQ---LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd14114    8 EELGTGAFGVVHRCTERATGNNFAAKFI-----MTPHESDketVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARIIGEKSFRRSV 586
Cdd:cd14114   83 GGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRS-NEVKLIDFGLATHLDPKESVKVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEDIHDqIQNAAFMYPPNPWKEISHEAIDLINNLL 663
Cdd:cd14114  162 TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFageNDDETLRN-VKSCDWNFDDSAFSGISEEAKDFIRKLL 240
                        250
                 ....*....|....*....
gi 568979055 664 QVKMRKRYSVDKTLSHPWL 682
Cdd:cd14114  241 LADPNKRMTIHQALEHPWL 259
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
431-682 6.18e-43

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 155.86  E-value: 6.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTkQESQLRnEVAILQNL----HHPGVVNLECMFETPE--RVFVVMEK 504
Cdd:cd05118    6 KIGEGAFGTVWLARDKVTGEKVAIKKI-KNDFRH-PKAALR-EIKLLKHLndveGHPNIVKLLDVFEHRGgnHLCLVFEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfPQVKLCDFGFARIIGEKSFRR 584
Cdd:cd05118   83 MGMNLYELIKDYPRG-LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLEL--GQLKLADFGLARSFTSPPYTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVgTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIQN-AAFMYPPnpwkeishEAIDLINNL 662
Cdd:cd05118  160 YVA-TRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTG-RPLFPGDSEVDQLAKiVRLLGTP--------EALDLLSKM 229
                        250       260
                 ....*....|....*....|
gi 568979055 663 LQVKMRKRYSVDKTLSHPWL 682
Cdd:cd05118  230 LKYDPAKRITASQALAHPYF 249
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
424-682 1.63e-42

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 154.86  E-value: 1.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd14071    2 YDI--ERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KL-HGDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSF 582
Cdd:cd14071   80 YAsNGEIFDYL--AQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL---DANMNIKIADFGFSNFFKPGEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPpnpwKEISHEAIDLI 659
Cdd:cd14071  155 LKTWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGStlQTLRDRVLSGRFRIP----FFMSTDCEHLI 230
                        250       260
                 ....*....|....*....|...
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14071  231 RRMLVLDPSKRLTIEQIKKHKWM 253
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
424-683 1.80e-42

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 155.17  E-value: 1.80e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDEVLGSGQFGIVYGGKHR-KTGRDVAIKIIDKLRFpTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd14202    2 FEFSRKDLIGHGAFAVVFKGRHKeKHDLEVAVKCINKKNL-AKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLA-----SADPFP-QVKLCDFGFARI 576
Cdd:cd14202   81 EYCNGGDLADYLHT-MRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrKSNPNNiRIKIADFGFARY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPwKEISHE 654
Cdd:cd14202  160 LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASspQDLRLFYEKNKSLSPNIP-RETSSH 238
                        250       260
                 ....*....|....*....|....*....
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14202  239 LRQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
432-684 2.66e-42

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 156.18  E-value: 2.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfptKQESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVVMEKLHG-DM 509
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISR-----RMEANTQREVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGgEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSfrrSVVGT 589
Cdd:cd14180   89 LDRI--KKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARLRPQGS---RPLQT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PA----YLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---------NEDEDIHDQIQNAAFMYPPNPWKEISHEAI 656
Cdd:cd14180  164 PCftlqYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFqskrgkmfhNHAADIMHKIKEGDFSLEGEAWKGVSEEAK 243
                        250       260
                 ....*....|....*....|....*...
gi 568979055 657 DLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14180  244 DLVRGLLTVDPAKRLKLSELRESDWLQG 271
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
421-682 2.74e-42

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 154.73  E-value: 2.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFV 500
Cdd:cd14192    1 NSYYAVCPHEVLGGGRFGQVHKCTELSTGLTLAAKII-KVK-GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARIIGEK 580
Cdd:cd14192   79 IMEYVDGGELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTG-NQIKIIDFGLARRYKPR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDL 658
Cdd:cd14192  158 EKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFlgETDAETMNNIVNCKWDFDAEAFENLSEEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 568979055 659 INNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14192  238 ISRLLVKEKSCRMSATQCLKHEWL 261
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
429-681 3.07e-42

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 154.76  E-value: 3.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVlGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14010    6 DEI-GRGKHSVVYKGRRKGTIEFVAIKCVDK-----SKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGE--------- 579
Cdd:cd14010   80 DLETLLRQD-GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL---DGNGTLKLSDFGLARREGEilkelfgqf 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 --------KSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWK 649
Cdd:cd14010  156 sdegnvnkVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFvaESFTELVEKILNEDPPPPPPKVS 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 650 -EISHEAIDLINNLLQVKMRKRYSVDKTLSHP-W 681
Cdd:cd14010  236 sKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
424-682 3.30e-42

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 155.13  E-value: 3.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIF-PDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKL--RFPTKQESQLRN----EVAILQNLH-HPGVVNLECMFETP 495
Cdd:cd14181    9 YQKYdPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTaeRLSPEQLEEVRSstlkEIHILRQVSgHPSIITLIDSYESS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 496 ERVFVVMEKLH-GDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA 574
Cdd:cd14181   89 TFIFLVFDLMRrGELFDYL--TEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---DDQLHIKLSDFGFS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 RIIGEKSFRRSVVGTPAYLAPEVLR------NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDI--HDQIQNAAFMYPPN 646
Cdd:cd14181  164 CHLEPGEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMlmLRMIMEGRYQFSSP 243
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 647 PWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14181  244 EWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
432-682 9.70e-42

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 152.80  E-value: 9.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIID--KLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPE--RVFVVMEKLHG 507
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKkrKLRRIPNGEANVKREIQILRRLNHRNVIKLVDVLYNEEkqKLYMVMEYCVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA----RIIGEKSFR 583
Cdd:cd14119   81 GLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDG---TLKISDFGVAealdLFAEDDTCT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSvVGTPAYLAPEVLRNKGY--NRSLDMWSVGVIIYVSLSGTFPFnEDEDIHD---QIQNAAFMYPPNpwkeISHEAIDL 658
Cdd:cd14119  158 TS-QGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPF-EGDNIYKlfeNIGKGEYTIPDD----VDPDLQDL 231
                        250       260
                 ....*....|....*....|....
gi 568979055 659 INNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14119  232 LRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
430-682 1.21e-41

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 153.63  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidklRFPTKQESQ------LRnEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd07833    7 GVVGEGAYGVVLKCRNKATGEIVAIK-----KFKESEDDEdvkktaLR-EVKVLRQLRHENIVNLKEAFRRKGRLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFR 583
Cdd:cd07833   81 YVERTLLELLEASPGG-LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG---VLKLCDFGFARALTARPAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 R--SVVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQ---IQNA------------------ 639
Cdd:cd07833  157 PltDYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDI-DQlylIQKClgplppshqelfssnprf 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 640 ---AF--MYPPNPWKE-----ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07833  236 agvAFpePSQPESLERrypgkVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
430-682 1.75e-41

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 152.60  E-value: 1.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKII-------------DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPE 496
Cdd:cd14077    7 KTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkereKRLEKEISRDIRTIREAALSSLLNHPHICRLRDFLRTPN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHG-DMLEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR 575
Cdd:cd14077   87 HYYMLFEYVDGgQLLDYIISH--GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSG---NIKIIDFGLSN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFRRSVVGTPAYLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPFnEDED---IHDQIQNAAFMYPpnpwKEI 651
Cdd:cd14077  162 LYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPF-DDENmpaLHAKIKKGKVEYP----SYL 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14077  237 SSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
432-682 5.08e-41

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 150.94  E-value: 5.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-DML 510
Cdd:cd14069    9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGgELF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMIlSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA---RIIGEKSFRRSVV 587
Cdd:cd14069   89 DKI-EPDVG-MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEND---NLKISDFGLAtvfRYKGKERLLNKMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRS-LDMWSVGVIIYVSLSGTFPFneDEDIHDQIQNAAFMYPPN----PWKEISHEAIDLINNL 662
Cdd:cd14069  164 GTLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAGELPW--DQPSDSCQEYSDWKENKKtyltPWKKIDTAALSLLRKI 241
                        250       260
                 ....*....|....*....|
gi 568979055 663 LQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14069  242 LTENPNKRITIEDIKKHPWY 261
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
432-681 5.96e-41

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 151.96  E-value: 5.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd07841    8 LGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDginfTALR-EIKLLQELKHPNIIGLLDVFGHKSNINLVFEFMET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DmLEMILSSEKGRL-PEHItKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRS- 585
Cdd:cd07841   87 D-LEKVIKDKSIVLtPADI-KSYMLMTLRGLEYLHSNWILHRDLKPNNLLI---ASDGVLKLADFGLARSFGSPNRKMTh 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 -VVgTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI------------QNAAFM--------- 642
Cdd:cd07841  162 qVV-TRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRVPFLPGDSDI-DQLgkifealgtpteENWPGVtslpdyvef 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568979055 643 --YPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07841  240 kpFPPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
432-682 6.76e-41

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 151.66  E-value: 6.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAIL---QNLHHPGVVNLECMFETPER-----VF 499
Cdd:cd07838    7 IGEGAYGTVYKARDLQDGRFVALK---KVRVPLSEEgiplSTIR-EIALLkqlESFEHPNVVRLLDVCHGPRTdrelkLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHGDmLEMILS--SEKGRLPEHItKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII 577
Cdd:cd07838   83 LVFEHVDQD-LATYLDkcPKPGLPPETI-KDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG---QVKLADFGLARIY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGTFPFNEDEDIHDQI-------------QNAAFM 642
Cdd:cd07838  158 SFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAelFNRRPLFRGSSEADQLGKIfdviglpseeewpRNSALP 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 643 ---YPPNP-------WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07838  238 rssFPSYTprpfksfVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
424-682 7.71e-41

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 151.15  E-value: 7.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQES-QLRnEVAILQNL-HHPGVVNLECMFETPERVFVV 501
Cdd:cd07830    1 YKVI--KQLGDGTFGSVYLARNKETGELVAIKKM-KKKFYSWEECmNLR-EVKSLRKLnEHPNIVKLKEVFRENDELYFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS 581
Cdd:cd07830   77 FEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLAREIRSRP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEV-LRNKGYNRSLDMWSVGVIIY--VSLSGTFPFNEDEDIHDQI-------------------QNA 639
Cdd:cd07830  154 PYTDYVSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAelYTLRPLFPGSSEIDQLYKIcsvlgtptkqdwpegyklaSKL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 640 AFMYP---PNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07830  234 GFRFPqfaPTSLHQLipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
424-682 1.46e-40

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 149.58  E-value: 1.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFptkqesqLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd14109    5 YEI-GEEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF-------LMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLH--GDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAsadpFPQVKLCDFGFARIIGEKS 581
Cdd:cd14109   77 NLAstIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ----DDKLKLADFGQSRRLLRGK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHD--QIQNAAFMYPPNPWKEISHEAIDLI 659
Cdd:cd14109  153 LTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETltNVRSGKWSFDSSPLGNISDDARDFI 232
                        250       260
                 ....*....|....*....|...
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14109  233 KKLLVYIPESRLTVDEALNHPWF 255
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
109-177 2.25e-40

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 142.46  E-value: 2.25e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 109 KVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLGEVTINGELLSPG 177
Cdd:cd20844    1 RVKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCRFNCHKRCASKVPRDCLGEVTFNGEPASPG 69
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
430-682 3.12e-40

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 148.56  E-value: 3.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRkTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-KLHG 507
Cdd:cd14161    9 ETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDlLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEyASRG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVV 587
Cdd:cd14161   88 DLYDYI--SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL---DANGNIKIADFGLSNLYNQDKFLQTYC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPFnedeDIHD------QIQNAAFMYPPNPwkeisHEAIDLIN 660
Cdd:cd14161  163 GSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPF----DGHDykilvkQISSGAYREPTKP-----SDACGLIR 233
                        250       260
                 ....*....|....*....|..
gi 568979055 661 NLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14161  234 WLLMVNPERRATLEDVASHWWV 255
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
430-682 3.29e-40

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 148.47  E-value: 3.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK--QESQLRnEVAILQNLHHPGVVNL-ECMFETPERVFVVMEKLH 506
Cdd:cd14164    6 TTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfvQKFLPR-ELSILRRVNHPNIVQMfECIEVANGRLYIVMEAAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfPQVKLCDFGFARII-GEKSFRRS 585
Cdd:cd14164   85 TDLLQKI--QEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADD--RKIKIADFGFARFVeDYPELSTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNpwKEISHEAIDLINNLLQ 664
Cdd:cd14164  161 FCGSRAYTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSG--VALEEPCRALIRTLLQ 238
                        250
                 ....*....|....*...
gi 568979055 665 VKMRKRYSVDKTLSHPWL 682
Cdd:cd14164  239 FNPSTRPSIQQVAGNSWL 256
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
432-715 4.41e-40

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 149.51  E-value: 4.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKII---DKLRFptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05612    9 IGTGTFGRVHLVRDRISEHYYALKVMaipEVIRL--KQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFrrSVVG 588
Cdd:cd05612   87 ELFSYLRN-SGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL---DKEGHIKLTDFGFAKKLRDRTW--TLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQVK 666
Cdd:cd05612  161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNpfGIYEKILAGKLEFP----RHLDLYAKDLIKKLLVVD 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568979055 667 MRKRY-----SVDKTLSHPWLQDYQtWLD--LRELECRIGERyITHESDDSRWEQY 715
Cdd:cd05612  237 RTRRLgnmknGADDVKNHRWFKSVD-WDDvpQRKLKPPIVPK-VSHDGDTSNFDDY 290
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
430-693 4.53e-40

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 150.46  E-value: 4.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-QESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG- 507
Cdd:cd05599    7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKeQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMleMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVV 587
Cdd:cd05599   87 DM--MTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLL---DARGHIKLSDFGLCTGLKKSHLAYSTV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQN--AAFMYPPNPwkEISHEAIDLINNLL 663
Cdd:cd05599  162 GTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDpqETCRKIMNwrETLVFPPEV--PISPEAKDLIERLL 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568979055 664 QVKMRK--RYSVDKTLSHPWLQDYQtWLDLRE 693
Cdd:cd05599  240 CDAEHRlgANGVEEIKSHPFFKGVD-WDHIRE 270
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
431-670 6.08e-40

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 149.77  E-value: 6.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQL----RNevAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHimaeRN--VLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRS 585
Cdd:cd05575   80 GGELFFHLQRER-HFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILL---DSQGHVVLTDFGLCKEgIEPSDTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEdIHDQIQNAAFMYPPNpwkeISHEAIDLINNL 662
Cdd:cd05575  156 FCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFysrDTAE-MYDNILHKPLRLRTN----VSPSARDLLEGL 230

                 ....*...
gi 568979055 663 LQVKMRKR 670
Cdd:cd05575  231 LQKDRTKR 238
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
424-682 3.08e-39

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 146.84  E-value: 3.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKI-IDKLRfptkqesqLRNEVailqNLH-----HPGVVNL------ECM 491
Cdd:cd14171    6 YEVNWTQKLGTGISGPVRVCVKKSTGERFALKIlLDRPK--------ARTEV----RLHmmcsgHPNIVQIydvyanSVQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 492 F----ETPERVFVVMEKLHGDMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVK 567
Cdd:cd14171   74 FpgesSPRARLLIVMELMEGGELFDRISQHRH-FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 568 LCDFGFARIigEKSFRRSVVGTPAYLAPEVL--------RNKG---------YNRSLDMWSVGVIIYVSLSGTFPF---- 626
Cdd:cd14171  153 LCDFGFAKV--DQGDLMTPQFTPYYVAPQVLeaqrrhrkERSGiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFyseh 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 627 ---NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14171  231 psrTITKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
430-691 4.28e-39

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 147.50  E-value: 4.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEvAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARiiGEKSF---RRS 585
Cdd:cd05571   81 ELFFHLSRER-VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL---DKDGHIKITDFGLCK--EEISYgatTKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDEDI-HDQIQNAAFMYPPNpwkeISHEAIDLINNLL 663
Cdd:cd05571  155 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNRDHEVlFELILMEEVRFPST----LSPEAKSLLAGLL 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568979055 664 QVKMRKRY-----SVDKTLSHPWLQDYqTWLDL 691
Cdd:cd05571  231 KKDPKKRLgggprDAKEIMEHPFFASI-NWDDL 262
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
430-695 4.31e-39

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 147.38  E-value: 4.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfptkQESQLRNEVA-------ILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd05574    7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDK------EEMIKRNKVKrvltereILATLDHPFLPTLYASFQTSTHLCFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKG-RLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL--------------ASADPFPQVK 567
Cdd:cd05574   81 DYCPGGELFRLLQKQPGkRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfdlsKQSSVTPPPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 568 LCDFGFAR------------IIGEKSFR-RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDED 631
Cdd:cd05574  161 RKSLRKGSrrssvksieketFVAEPSARsNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFkgsNRDET 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 632 IHdQIQNAAFMYPPNPwkEISHEAIDLINNLLQVKMRKR----YSVDKTLSHPWLQDYQtWLDLRELE 695
Cdd:cd05574  241 FS-NILKKELTFPESP--PVSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFRGVN-WALIRNMT 304
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
431-695 5.30e-39

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 147.17  E-value: 5.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKH---RKTGRDVAIKIIDKLRFPTKQE--SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd05584    3 VLGKGGYGKVFQVRKttgSDKGKIFAMKVLKKASIVRNQKdtAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR-IIGEKSFRR 584
Cdd:cd05584   83 SGGELFMHLERE-GIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL---DAQGHVKLTDFGLCKeSIHDGTVTH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEDIhDQIQNAAFMYPPNpwkeISHEAIDLINN 661
Cdd:cd05584  159 TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFtaeNRKKTI-DKILKGKLNLPPY----LTNEARDLLKK 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 662 LLqvkmrKRYSVDKTLS----------HPWLQDYQtWLDL--RELE 695
Cdd:cd05584  234 LL-----KRNVSSRLGSgpgdaeeikaHPFFRHIN-WDDLlaKKVE 273
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
432-682 5.65e-39

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 145.10  E-value: 5.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-----KL 505
Cdd:cd14116   13 LGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGvEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEyaplgTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMilssekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFArIIGEKSFRRS 585
Cdd:cd14116   93 YRELQKL------SKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAG---ELKIADFGWS-VHAPSSRRTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLL 663
Cdd:cd14116  163 LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANtyQETYKRISRVEFTFPDF----VTEGARDLISRLL 238
                        250
                 ....*....|....*....
gi 568979055 664 QVKMRKRYSVDKTLSHPWL 682
Cdd:cd14116  239 KHNPSQRPMLREVLEHPWI 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
424-681 5.84e-39

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 145.13  E-value: 5.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd14665    2 YELVKD--IGSGNFGVARLMRDKQTKELVAVKYIER---GEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHG-DMLEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLaSADPFPQVKLCDFGFARIIGEKSF 582
Cdd:cd14665   77 YAAGgELFERICNA--GRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL-DGSPAPRLKICDFGYSKSSVLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNRSL-DMWSVGVIIYVSLSGTFPFNEDEDIHD------QIQNAAFMYPpnPWKEISHEA 655
Cdd:cd14665  154 PKSTVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRNfrktiqRILSVQYSIP--DYVHISPEC 231
                        250       260
                 ....*....|....*....|....*.
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14665  232 RHLISRIFVADPATRITIPEIRNHEW 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
431-680 8.76e-39

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 144.46  E-value: 8.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-GD 508
Cdd:cd08530    7 KLGKGSYGSVYKVKRLSDNQVYALKEVN-LGSLSQKEREdSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPfGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLP---EHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIgEKSFRRS 585
Cdd:cd08530   86 LSKLISKRKKKRRLfpeDDIWRIFI-QMLRGLKALHDQKILHRDLKSANILLSAGD---LVKIGDLGISKVL-KKNLAKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWkeiSHEAIDLINNLL 663
Cdd:cd08530  161 QIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARtmQELRYKVCRGKFPPIPPVY---SQDLQQIIRSLL 237
                        250
                 ....*....|....*..
gi 568979055 664 QVKMRKRYSVDKTLSHP 680
Cdd:cd08530  238 QVNPKKRPSCDKLLQSP 254
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
432-682 1.08e-38

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 144.09  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGDML 510
Cdd:cd08529    8 LGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAeNGDLH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKGRLPEH-ITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS-FRRSVVG 588
Cdd:cd08529   88 SLIKSQRGRPLPEDqIWKFFI-QTLLGLSHLHSKKILHRDIKSMNIFLDKGD---NVKIGDLGVAKILSDTTnFAQTIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKeISHEAIDLINNLLQVKMR 668
Cdd:cd08529  164 TPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISAS-YSQDLSQLIDSCLTKDYR 242
                        250
                 ....*....|....
gi 568979055 669 KRYSVDKTLSHPWL 682
Cdd:cd08529  243 QRPDTTELLRNPSL 256
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
113-166 1.32e-38

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 136.65  E-value: 1.32e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLGE 166
Cdd:cd20796    1 PHTFVVHTYTKPTVCQHCKKLLKGLFRQGLQCKDCKFNCHKKCAEKVPKDCTGE 54
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
430-685 2.10e-38

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 144.15  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQESQLRNEVAILQNLHHPGVVNL----ECMFETPeRVFVVMEKL 505
Cdd:cd06917    7 ELVGRGSYGAVYRGYHVKTGRVVALKVLN-LDTDDDDVSDIQKEVALLSQLKLGQPKNIikyyGSYLKGP-SLWIIMDYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRS 585
Cdd:cd06917   85 EGGSIRTLM--RAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTG---NVKLCDFGVAASLNQNSSKRS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 V-VGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNeDEDIHDQIQNAAFMYPPN-PWKEISHEAIDLINNL 662
Cdd:cd06917  160 TfVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYS-DVDALRAVMLIPKSKPPRlEGNGYSPLLKEFVAAC 238
                        250       260
                 ....*....|....*....|...
gi 568979055 663 LQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd06917  239 LDEEPKDRLSADELLKSKWIKQH 261
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
424-681 2.12e-38

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 143.37  E-value: 2.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfptKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd14662    2 YELVKD--IGSGNFGVARLMRNKETKELVAVKYIERGL---KIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 -KLHGDMLEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLaSADPFPQVKLCDFGFARIIGEKSF 582
Cdd:cd14662   77 yAAGGELFERICNA--GRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL-DGSPAPRLKICDFGYSKSSVLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDED---IHDQIQN-AAFMYPPNPWKEISHEAID 657
Cdd:cd14662  154 PKSTVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDDpknFRKTIQRiMSVQYKIPDYVRVSQDCRH 233
                        250       260
                 ....*....|....*....|....
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14662  234 LLSRIFVANPAKRITIPEIKNHPW 257
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
430-680 2.33e-38

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 144.57  E-value: 2.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKlrfpTKQESQLRN-EVAILQNLHHPGVVNLECMF----ETPERVF--VVM 502
Cdd:cd14137   10 KVIGSGSFGVVYQAKLLETGEVVAIK---K----VLQDKRYKNrELQIMRRLKHPNIVKLKYFFyssgEKKDEVYlnLVM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMI--LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQV-KLCDFGFARII-- 577
Cdd:cd14137   83 EYMPETLYRVIrhYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV---DPETGVlKLCDFGSAKRLvp 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSfrRSVVGTPAYLAPE-VLRNKGYNRSLDMWSVGVIIYVSLSGT--FPFNEDED-----IH-------DQIQNAAFM 642
Cdd:cd14137  160 GEPN--VSYICSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQplFPGESSVDqlveiIKvlgtptrEQIKAMNPN 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 643 Y--------PPNPWKEI-----SHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd14137  238 YtefkfpqiKPHPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
433-682 3.20e-38

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 143.21  E-value: 3.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 433 GSGQFGIVYGGKHRKTGRDVAIKIIdklRFPTKQES---QLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06626    9 GEGTFGKVYTAVNLDTGELMAMKEI---RFQDNDPKtikEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILssEKGR-LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfpqVKLCDFGFARIIGEKSFR----- 583
Cdd:cd06626   86 LEELL--RHGRiLDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL---IKLGDFGSAVKLKNNTTTmapge 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 -RSVVGTPAYLAPEVLRN---KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEdihdqiQNAAFMY-------PPNPWK-EI 651
Cdd:cd06626  161 vNSLVGTPAYMAPEVITGnkgEGHGRAADIWSLGCVVLEMATGKRPWSELD------NEWAIMYhvgmghkPPIPDSlQL 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06626  235 SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
431-695 3.73e-38

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 144.84  E-value: 3.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFPTKQESQLRNEVAILQNlHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05592    2 VLGKGSFGKVMLAELKGTNQYFAIKALKKdvvLEDDDVECTMIERRVLALAS-QHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA--RIIGEKSfRRS 585
Cdd:cd05592   81 GDL-MFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL---DREGHIKIADFGMCkeNIYGENK-AST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN-EDED-IHDQIQNAAFMYPpnpwKEISHEAIDLINNLL 663
Cdd:cd05592  156 FCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHgEDEDeLFWSICNDTPHYP----RWLTKEAASCLSLLL 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568979055 664 QVKMRKRYSVDKTL-----SHPWLQ--DYQTwLDLRELE 695
Cdd:cd05592  232 ERNPEKRLGVPECPagdirDHPFFKtiDWDK-LERREID 269
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
432-682 6.27e-38

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 141.89  E-value: 6.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-GDML 510
Cdd:cd14072    8 IGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASgGEVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVGTP 590
Cdd:cd14072   88 DYLVA--HGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL---DADMNIKIADFGFSNEFTPGNKLDTFCGSP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQVKM 667
Cdd:cd14072  163 PYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQnlKELRERVLRGKYRIP----FYMSTDCENLLKKFLVLNP 238
                        250
                 ....*....|....*
gi 568979055 668 RKRYSVDKTLSHPWL 682
Cdd:cd14072  239 SKRGTLEQIMKDRWM 253
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
432-682 6.32e-38

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 143.24  E-value: 6.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTK----QESQLRnEVAILQNL-HHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALK---KVALRKLeggiPNQALR-EIKALQACqGHPYVVKLRDVFPHGTGFVLVFEYML 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRR-- 584
Cdd:cd07832   84 SSLSEVLRDEERP-LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG---VLKIADFGLARLFSEEDPRLys 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNK-GYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI---------QNA--------------- 639
Cdd:cd07832  160 HQVATRWYRAPELLYGSrKYDEGVDLWAVGCIFAELLNGSPLFPGENDI-EQLaivlrtlgtPNEktwpeltslpdynki 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 640 AFMY-PPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07832  239 TFPEsKGIRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
424-682 1.38e-37

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 141.28  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-QESQLRNEVAILQNLHHPGVVNLECMFETPE-RVFVV 501
Cdd:cd14163    2 YQL--GKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEfIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLH-GDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpqVKLCDFGFARII--G 578
Cdd:cd14163   80 MELAEdGDVFDCVL--HGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQLpkG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQI--QNAAFMYPPNpwKEISHEA 655
Cdd:cd14163  154 GRELSQTFCGSTAYAAPEVLQGVPHDsRKGDIWSMGVVLYVMLCAQLPF-DDTDIPKMLcqQQKGVSLPGH--LGVSRTC 230
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14163  231 QDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
430-683 1.64e-37

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 141.54  E-value: 1.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdklRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14104    6 EELGRGQFGIVHRCVETSSKKTYMAKFV---KVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGvD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMIlSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARII--GEKsFRRSV 586
Cdd:cd14104   83 IFERI-TTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGS-YIKIIEFGQSRQLkpGDK-FRLQY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VgTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQ 664
Cdd:cd14104  160 T-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFeaETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLV 238
                        250
                 ....*....|....*....
gi 568979055 665 VKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14104  239 KERKSRMTAQEALNHPWLK 257
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
430-682 2.94e-37

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 140.21  E-value: 2.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF------PTKQESQLRNEVAILQNLH---HPGVVNLECMFETPERVFV 500
Cdd:cd14004    6 KEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvdtwvRDRKLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDEFYYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKlHG---DMLEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII 577
Cdd:cd14004   86 VMEK-HGsgmDLFDFIER--KPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNG---TIKLIDFGSAAYI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFrRSVVGTPAYLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDqiqnaAFMYPPnpwKEISHEAI 656
Cdd:cd14004  160 KSGPF-DTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIEEILE-----ADLRIP---YAVSEDLI 230
                        250       260
                 ....*....|....*....|....*.
gi 568979055 657 DLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14004  231 DLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
430-682 3.30e-37

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 140.09  E-value: 3.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd08225    6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRL--PEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADPFpqVKLCDFGFARIIGEK-SFRRSV 586
Cdd:cd08225   86 LMKRINRQRGVLfsEDQILSWFV-QISLGLKHIHDRKILHRDIKSQNIFLSKNGMV--AKLGDFGIARQLNDSmELAYTC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQIQN--AAFMYPPNPwkEISHEAIDLINNLLQ 664
Cdd:cd08225  163 VGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF-EGNNLHQLVLKicQGYFAPISP--NFSRDLRSLISQLFK 239
                        250
                 ....*....|....*...
gi 568979055 665 VKMRKRYSVDKTLSHPWL 682
Cdd:cd08225  240 VSPRDRPSITSILKRPFL 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
430-682 3.85e-37

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 140.93  E-value: 3.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLrnevaILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14175    7 ETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEI-----LLRYGQHPNIITLKDVYDDGKHVYLVTELMRGgE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQ-VKLCDFGFARII-GEKSFRRSV 586
Cdd:cd14175   82 LLDKILRQK--FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPEsLRICDFGFAKQLrAENGLLMTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINN 661
Cdd:cd14175  160 CYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangpsDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSK 239
                        250       260
                 ....*....|....*....|.
gi 568979055 662 LLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14175  240 MLHVDPHQRLTAKQVLQHPWI 260
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
432-682 4.26e-37

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 139.95  E-value: 4.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfpTKQES----QLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEK-LH 506
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKK--AKKDSyvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELcPG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF---ARIIGEKSFR 583
Cdd:cd14070   88 GNLMHRIY--DKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEND---NIKLIDFGLsncAGILGYSDPF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPW-KEISHEAIDLINNL 662
Cdd:cd14070  163 STQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEMNPLpTDLSPGAISFLRSL 242
                        250       260
                 ....*....|....*....|
gi 568979055 663 LQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14070  243 LEPDPLKRPNIKQALANRWL 262
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
430-682 5.03e-37

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 142.08  E-value: 5.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLrnevaILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14176   25 EDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI-----LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGgE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQ-VKLCDFGFARII-GEKSFRRSV 586
Cdd:cd14176  100 LLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQLrAENGLLMTP 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN---ED--EDIHDQIQNAAFMYPPNPWKEISHEAIDLINN 661
Cdd:cd14176  178 CYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDtpEEILARIGSGKFSLSGGYWNSVSDTAKDLVSK 257
                        250       260
                 ....*....|....*....|.
gi 568979055 662 LLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14176  258 MLHVDPHQRLTAALVLRHPWI 278
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
419-685 5.73e-37

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 141.67  E-value: 5.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECM-----FE 493
Cdd:cd07849    2 DVGPRYQNL--SYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTLR-EIKILLRFKHENIIGILDIqrpptFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 494 TPERVFVVMEKLHGDMLEMILSSekgRLP-EHITKFlITQILVALRHLHFKNIVHCDLKPENVLL-ASADpfpqVKLCDF 571
Cdd:cd07849   79 SFKDVYIVQELMETDLYKLIKTQ---HLSnDHIQYF-LYQILRGLKYIHSANVLHRDLKPSNLLLnTNCD----LKICDF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 572 GFARII----GEKSFRRSVVGTPAYLAPEV-LRNKGYNRSLDMWSVGVIIYVSLSGT--FPFNE---------------- 628
Cdd:cd07849  151 GLARIAdpehDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRplFPGKDylhqlnlilgilgtps 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 629 DEDIHDQIQNAAF-------MYPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd07849  231 QEDLNCIISLKARnyikslpFKPKVPWNKLfpnaDPKALDLLDKMLTFNPHKRITVEEALAHPYLEQY 298
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
430-682 7.50e-37

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 139.39  E-value: 7.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd14088    7 QVIKTEEFCEIFRAKDKTTGKLYTCKKFLK-RDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGrE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIigEKSFRRSVVG 588
Cdd:cd14088   86 VFDWIL--DQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKL--ENGLIKEPCG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF----------NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDL 658
Cdd:cd14088  162 TPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFydeaeeddyeNHDKNLFRKILAGDYEFDSPYWDDISQAAKDL 241
                        250       260
                 ....*....|....*....|....
gi 568979055 659 INNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14088  242 VTRLMEVEQDQRITAEEAISHEWI 265
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
430-682 1.61e-36

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 138.30  E-value: 1.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIK---IIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSV 586
Cdd:cd06632   86 GGSIHKLLQ-RYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV---DTNGVVKLADFGMAKHVEAFSFAKSF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLR--NKGYNRSLDMWSVGVIIYVSLSGTFPFNededihdQIQNAAFMY--------PPNPwKEISHEAI 656
Cdd:cd06632  162 KGSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWS-------QYEGVAAIFkignsgelPPIP-DHLSPDAK 233
                        250       260
                 ....*....|....*....|....*.
gi 568979055 657 DLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06632  234 DFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
429-683 2.26e-36

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 138.62  E-value: 2.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqeSQLRNEVAIL-QNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd14174    7 DELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSR--SRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVV 587
Cdd:cd14174   85 GSILAHIQKRK-HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACTPIT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 --------GTPAYLAPEVL-----RNKGYNRSLDMWSVGVIIYVSLSGTFPFNED-----------------EDIHDQIQ 637
Cdd:cd14174  164 tpelttpcGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvcqNKLFESIQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 638 NAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14174  244 EGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
430-670 4.92e-36

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 138.60  E-value: 4.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEvAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSVV 587
Cdd:cd05595   81 ELFFHLSRER-VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLCKEgITDGATMKTFC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NED-EDIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQV 665
Cdd:cd05595  157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDhERLFELILMEEIRFP----RTLSPEAKSLLAGLLKK 232

                 ....*
gi 568979055 666 KMRKR 670
Cdd:cd05595  233 DPKQR 237
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
424-682 6.12e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 137.45  E-value: 6.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLrnevaILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd14178    5 YEIKED--IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEI-----LLRYGQHPNIITLKDVYDDGKFVYLVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHG-DMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQ-VKLCDFGFARII-GEK 580
Cdd:cd14178   78 LMRGgELLDRILRQKC--FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPEsIRICDFGFAKQLrAEN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDIHDQIQNAAFMYPPNPWKEISHEA 655
Cdd:cd14178  156 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFangpdDTPEEILARIGSGKYALSGGNWDSISDAA 235
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14178  236 KDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
435-684 7.48e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 136.77  E-value: 7.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGGKHRKTGRDVAIKIIdklrfpTKQESQLRNEVA-------ILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05609   11 GAYGAVYLVRHRETRQRFAMKKI------NKQNLILRNQIQqvfverdILTFAENPFVVSMYCSFETKRHLCMVMEYVEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDFGFARIiG--------- 578
Cdd:cd05609   85 GDCATLLKN-IGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITS---MGHIKLTDFGLSKI-Glmslttnly 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 ----EKSFR----RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPw 648
Cdd:cd05609  160 eghiEKDTRefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDtpEELFGQVISDEIEWPEGD- 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568979055 649 KEISHEAIDLINNLLQVKMRKRY---SVDKTLSHPWLQD 684
Cdd:cd05609  239 DALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQD 277
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
421-682 8.01e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 137.45  E-value: 8.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLrnevaILQNLHHPGVVNLECMFETPERVFV 500
Cdd:cd14177    3 TDVYELKED--IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEI-----LMRYGQHPNIITLKDVYDDGRYVYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHG-DMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL----ASADpfpQVKLCDFGFAR 575
Cdd:cd14177   76 VTELMKGgELLDRILRQK--FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmddsANAD---SIRICDFGFAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 II-GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDIHDQIQNAAFMYPPNPWK 649
Cdd:cd14177  151 QLrGENGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFangpnDTPEEILLRIGSGKFSLSGGNWD 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568979055 650 EISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14177  231 TVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
424-673 1.08e-35

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 135.86  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIK------IIDKlrfptKQESQLRNEVAILQNLHHPGVVN-LECMFETPE 496
Cdd:cd08224    2 YEI--EKKIGKGQFSVVYRARCLLDGRLVALKkvqifeMMDA-----KARQDCLKEIDLLQQLNHPNIIKyLASFIENNE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMILSSEKGR--LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA 574
Cdd:cd08224   75 LNIVLELADAGDLSRLIKHFKKQKrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANG---VVKLGDLGLG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 RIIGEKSFR-RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGtfPFNEDE----DIHDQIQNAAfmYPPNP 647
Cdd:cd08224  152 RFFSSKTTAaHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYemAALQS--PFYGEKmnlySLCKKIEKCE--YPPLP 227
                        250       260
                 ....*....|....*....|....*.
gi 568979055 648 WKEISHEAIDLINNLLQVKMRKRYSV 673
Cdd:cd08224  228 ADLYSQELRDLVAACIQPDPEKRPDI 253
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
431-693 1.24e-35

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 138.28  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfpTKQESQLRNEVA-------ILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd05596   33 VIGRGAFGEVQLVRHKSTKKVYAMKLL------SKFEMIKRSDSAffweerdIMAHANSEWIVQLHYAFQDDKYLYMVMD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFR 583
Cdd:cd05596  107 YMPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL---DASGHLKLADFGTCMKMDKDGLV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RS--VVGTPAYLAPEVLRNKG----YNRSLDMWSVGVIIYVSLSGTFPFNED------EDIHDQIQNAAFmyPPNPwkEI 651
Cdd:cd05596  182 RSdtAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADslvgtyGKIMNHKNSLQF--PDDV--EI 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568979055 652 SHEAIDLINNLLQVKMRK--RYSVDKTLSHPWLQDYQ-TWLDLRE 693
Cdd:cd05596  258 SKDAKSLICAFLTDREVRlgRNGIEEIKAHPFFKNDQwTWDNIRE 302
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
423-682 3.64e-35

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 135.15  E-value: 3.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 423 VYQIfPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLrfPTKQESQLRNEVAIL-QNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14173    2 VYQL-QEEVLGEGAYARVQTCINLITNKEYAVKIIEKR--PGHSRSRVFREVEMLyQCQGHRNVLELIEFFEEEDKFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHG-DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEK 580
Cdd:cd14173   79 FEKMRGgSILSHI--HRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SfRRSVVGTP---------AYLAPEVLRNKG-----YNRSLDMWSVGVIIYVSLSGTFPF----------NEDED----- 631
Cdd:cd14173  157 S-DCSPISTPelltpcgsaEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgwDRGEAcpacq 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 632 --IHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14173  236 nmLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
432-695 4.11e-35

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 134.58  E-value: 4.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLR-NEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMAlNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKGR-LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVGT 589
Cdd:cd05577   81 KYHIYNVGTRgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL---DDHGHVRISDLGLAVEFKGGKKIKGRVGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNK-GYNRSLDMWSVGVIIYVSLSGTFPFN------EDEDIHDQIQNAAFMYPpnpwKEISHEAIDLINNL 662
Cdd:cd05577  158 HGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRqrkekvDKEELKRRTLEMAVEYP----DSFSPEARSLCEGL 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568979055 663 LQVKMRKRY-----SVDKTLSHPWLQDyqtwLDLRELE 695
Cdd:cd05577  234 LQKDPERRLgcrggSADEVKEHPFFRS----LNWQRLE 267
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
430-682 4.82e-35

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 134.35  E-value: 4.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfptKQESQLRNEVAilqnlHH------PGVVNLECMFETPER----VF 499
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALKLL-------YDSPKARREVE-----HHwrasggPHIVHILDVYENMHHgkrcLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG-DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIG 578
Cdd:cd14172   78 IIMECMEGgELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDI----HDQIQNAAFMYPPNPWKEIS 652
Cdd:cd14172  158 VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFysNTGQAIspgmKRRIRMGQYGFPNPEWAEVS 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 653 HEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14172  238 EEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
430-670 5.10e-35

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 134.01  E-value: 5.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-----QESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVVME 503
Cdd:cd13993    6 SPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKdgndfQKLPQLREIDLHRRVSrHPNIITLHDVFETEVAIYIVLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KL-HGDMLEMILSSEKGRL-PEHITKFlITQILVALRHLHFKNIVHCDLKPENVLLasADPFPQVKLCDFGFAriIGEKS 581
Cdd:cd13993   86 YCpNGDLFEAITENRIYVGkTELIKNV-FLQLIDAVKHCHSLGIYHRDIKPENILL--SQDEGTVKLCDFGLA--TTEKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKG------YNRSLDMWSVGVIIYVSLSGTFPF---NEDEDIHdqiqNAAFMYPPNPWKEI- 651
Cdd:cd13993  161 SMDFGVGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWkiaSESDPIF----YDYYLNSPNLFDVIl 236
                        250       260
                 ....*....|....*....|.
gi 568979055 652 --SHEAIDLINNLLQVKMRKR 670
Cdd:cd13993  237 pmSDDFYNLLRQIFTVNPNNR 257
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
431-684 5.48e-35

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 135.39  E-value: 5.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEvTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFR-RSVVG 588
Cdd:cd05585   81 LFHHLQRE-GRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL---DYTGHIALCDFGLCKLNMKDDDKtNTFCG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHD---QIQNAAFMYPPNpwkeISHEAIDLINNLLQV 665
Cdd:cd05585  157 TPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPF-YDENTNEmyrKILQEPLRFPDG----FDRDAKDLLIGLLNR 231
                        250       260
                 ....*....|....*....|..
gi 568979055 666 KMRKRYSV---DKTLSHPWLQD 684
Cdd:cd05585  232 DPTKRLGYngaQEIKNHPFFDQ 253
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
428-685 5.75e-35

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 135.96  E-value: 5.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDK-LRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPER------VFV 500
Cdd:cd07855    9 PIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNaFDVVTTAKRTLR-ELKILRHFKHDNIIAIRDILRPKVPyadfkdVYV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSSEKGRLpEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEK 580
Cdd:cd07855   88 VLDLMESDLHHIIHSDQPLTL-EHIRYFLY-QLLRGLKYIHSANVIHRDLKPSNLLVNEN---CELKIGDFGMARGLCTS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 S-----FRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVI---------------------IYVSLSGTFPFN-----E 628
Cdd:cd07855  163 PeehkyFMTEYVATRWYRAPELMLSlPEYTQAIDMWSVGCIfaemlgrrqlfpgknyvhqlqLILTVLGTPSQAvinaiG 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 629 DEDIHDQIQNAAfMYPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd07855  243 ADRVRRYIQNLP-NKQPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFLAKY 302
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
421-682 7.59e-35

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 133.16  E-value: 7.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPERVF 499
Cdd:cd06612    2 EEVFDI--LEKLGEGSYGSVYKAIHKETGQVVAIKVV-----PVEEDLQeIIKEISILKQCDSPYIVKYYGSYFKNTDLW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG----DMLEMILSSekgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR 575
Cdd:cd06612   75 IVMEYCGAgsvsDIMKITNKT----LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL---NEEGQAKLADFGVSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFRR-SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIHDqiQNAAFMYPPNP------W 648
Cdd:cd06612  148 QLTDTMAKRnTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYS---DIHP--MRAIFMIPNKPpptlsdP 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 649 KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06612  223 EKWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
431-687 1.96e-34

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 132.47  E-value: 1.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd06605    8 ELGEGNGGVVSKVRHRPSGQIMAVKVI-RLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSsEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLASADpfpQVKLCDFGfarIIGE--KSFRRSVV 587
Cdd:cd06605   87 DKILK-EVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRG---QVKLCDFG---VSGQlvDSLAKTFV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDED----IHDQIQNAAFMYPPN-PWKEISHEAIDLINN 661
Cdd:cd06605  160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpPPNAKpsmmIFELLSYIVDEPPPLlPSGKFSPDFQDFVSQ 239
                        250       260
                 ....*....|....*....|....*.
gi 568979055 662 LLQVKMRKRYSVDKTLSHPWLQDYQT 687
Cdd:cd06605  240 CLQKDPTERPSYKELMEHPFIKRYEY 265
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
431-683 2.10e-34

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 132.52  E-value: 2.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVY-----GGKHrkTGRDVAIKIIDKLRFPTKQESQ--LRNEVAILQNLHH-PGVVNLECMFETPERVFVVM 502
Cdd:cd05583    1 VLGTGAYGKVFlvrkvGGHD--AGKLYAMKVLKKATIVQKAKTAehTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSF 582
Cdd:cd05583   79 DYVNGGELFTHLYQ-REHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSEGHVVLTDFGLSKEFLPGEN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RR--SVVGTPAYLAPEVLRNK--GYNRSLDMWSVGVIIYVSLSGTFPF------NEDEDIHDQIQNAAfmyPPNPwKEIS 652
Cdd:cd05583  155 DRaySFCGTIEYMAPEVVRGGsdGHDKAVDWWSLGVLTYELLTGASPFtvdgerNSQSEISKRILKSH---PPIP-KTFS 230
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 653 HEAIDLINNLLQVKMRKR-----YSVDKTLSHPWLQ 683
Cdd:cd05583  231 AEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFK 266
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
431-681 2.29e-34

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 132.09  E-value: 2.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKI--IDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEvKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 ----DMLEMIlssekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA-RI--IGEK 580
Cdd:cd06625   87 gsvkDEIKAY-----GALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNG---NVKLGDFGASkRLqtICSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhdqiqnAAF----MYPPNPW--KEISHE 654
Cdd:cd06625  159 TGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPM------AAIfkiaTQPTNPQlpPHVSED 232
                        250       260
                 ....*....|....*....|....*..
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd06625  233 ARDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
430-693 2.40e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 133.93  E-value: 2.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ--LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKhiMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05604   82 GELFFHLQRER-SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILL---DSQGHIVLTDFGLCKEgISNSDTTTTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQIQNaAFMYPPNPWKEISHEAIDLINNLLQVK 666
Cdd:cd05604  158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPF-YCRDTAEMYEN-ILHKPLVLRPGISLTAWSILEELLEKD 235
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 667 MRKRYSVDKTL----SHPWLQDYqTWLDLRE 693
Cdd:cd05604  236 RQLRLGAKEDFleikNHPFFESI-NWTDLVQ 265
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
431-682 2.45e-34

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 131.91  E-value: 2.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK-LRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14186    8 LLGKGSFACVYRARSLHTGLEVAIKMIDKkAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA---RIIGEKSFrrSV 586
Cdd:cd14186   88 MSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRN---MNIKIADFGLAtqlKMPHEKHF--TM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQ 664
Cdd:cd14186  163 CGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDtvKNTLNKVVLADYEMPAF----LSREAQDLIHQLLR 238
                        250
                 ....*....|....*...
gi 568979055 665 VKMRKRYSVDKTLSHPWL 682
Cdd:cd14186  239 KNPADRLSLSSVLDHPFM 256
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
424-682 8.30e-34

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 130.47  E-value: 8.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFPTkqesQLRNEVAILQNLH------HPGVVNLECMFETPE 496
Cdd:cd14133    1 YEV--LEVLGKGTFGQVVKCYDLLTGEEVALKIIkNNKDYLD----QSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARI 576
Cdd:cd14133   75 HLCIVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRC-QIKIIDFGSSCF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEKSFrrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSG--TFPfneDEDIHDQIQNAAFMYPPNPWKEISH- 653
Cdd:cd14133  154 LTQRLY--SYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGepLFP---GASEVDQLARIIGTIGIPPAHMLDQg 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 654 -----EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14133  229 kaddeLFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
431-693 1.22e-33

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 132.05  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05601    8 VIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEvSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFG-FARIIGEKS-FRRSVV 587
Cdd:cd05601   88 LLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI---DRTGHIKLADFGsAAKLSSDKTvTSKMPV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVL------RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDI--HDQIQN--AAFMYPPNPwkEISHEAID 657
Cdd:cd05601  165 GTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIktYSNIMNfkKFLKFPEDP--KVSESAVD 242
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 658 LINNLLQVKmRKRYSVDKTLSHPWLQDYQtWLDLRE 693
Cdd:cd05601  243 LIKGLLTDA-KERLGYEGLCCHPFFSGID-WNNLRQ 276
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
430-670 1.32e-33

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 131.63  E-value: 1.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ--LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhiMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05603   81 GELFFHLQRER-CFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL---DCQGHVVLTDFGLCKEgMEPEETTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPPNPwkeiSHEAIDLINNLLQ 664
Cdd:cd05603  157 CGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDvsQMYDNILHKPLHLPGGK----TVAACDLLQGLLH 232

                 ....*.
gi 568979055 665 VKMRKR 670
Cdd:cd05603  233 KDQRRR 238
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
430-670 1.61e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 132.06  E-value: 1.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ--LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05602   13 KVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKhiMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYING 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKGRLpEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05602   93 GELFYHLQRERCFL-EPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQG---HIVLTDFGLCKEnIEPNGTTSTF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQ 664
Cdd:cd05602  169 CGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFysRNTAEMYDNILNKPLQLKPN----ITNSARHLLEGLLQ 244

                 ....*.
gi 568979055 665 VKMRKR 670
Cdd:cd05602  245 KDRTKR 250
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
431-680 2.02e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 129.08  E-value: 2.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd08220    7 VVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKGRL--PEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASADPFpqVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd08220   87 FEYIQQRKGSLlsEEEILHFF-VQILLALHHVHSKQILHRDLKTQNILLNKKRTV--VKIGDFGISKILSSKSKAYTVVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWkeiSHEAIDLINNLLQVK 666
Cdd:cd08220  164 TPCYISPELCEGKPYNQKSDIWALGCVLYelASLKRAFEAANLPALVLKIMRGTFAPISDRY---SEELRHLILSMLHLD 240
                        250
                 ....*....|....
gi 568979055 667 MRKRYSVDKTLSHP 680
Cdd:cd08220  241 PNKRPTLSEIMAQP 254
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
435-681 2.03e-33

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 130.42  E-value: 2.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLE--CMFETPERVFVVMEKLHGD 508
Cdd:cd07843   16 GTYGVVYRARDKKTGEIVALK---KLKMEKEKEgfpiTSLR-EINILLKLQHPNIVTVKevVVGSNLDKIYMVMEYVEHD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 mLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE--KSFRRSV 586
Cdd:cd07843   92 -LKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRG---ILKICDFGLAREYGSplKPYTQLV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VgTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQIQ------------------------NAAF 641
Cdd:cd07843  168 V-TLWYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEI-DQLNkifkllgtptekiwpgfselpgakKKTF 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 642 MYPPN-------PWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07843  246 TKYPYnqlrkkfPALSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
430-698 2.38e-33

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 129.67  E-value: 2.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-- 507
Cdd:cd06609    7 ERIGKGSFGEVYKGIDKRTNQVVAIKVID-LEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGgs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 --DMLEMilssekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL-ASADpfpqVKLCDFGFAriiGEKSF-- 582
Cdd:cd06609   86 vlDLLKP------GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLsEEGD----VKLADFGVS---GQLTStm 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 --RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIHDqiQNAAFMYPPNPWK-----EISHEA 655
Cdd:cd06609  153 skRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLS---DLHP--MRVLFLIPKNNPPslegnKFSKPF 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELECRI 698
Cdd:cd06609  228 KDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSYLTLLIERI 270
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
431-670 2.43e-33

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 130.88  E-value: 2.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQ---NLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd05589    6 VLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEvESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFVMEYAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLaSADPFpqVKLCDFGFARI-IGEKSFRRS 585
Cdd:cd05589   86 GGDLMMHIHEDV--FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLL-DTEGY--VKIADFGLCKEgMGFGDRTST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPpnpwKEISHEAIDLINNLL 663
Cdd:cd05589  161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFpgDDEEEVFDSIVNDEVRYP----RFLSTEAISIMRRLL 236

                 ....*..
gi 568979055 664 QVKMRKR 670
Cdd:cd05589  237 RKNPERR 243
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
432-682 2.59e-33

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 128.96  E-value: 2.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIV--YGGKHRKTGRDVAIKIIDKLRFPTKQE---SQLRNEVAILQNLHHPGVVNLECMFETPERVFV-VMEKL 505
Cdd:cd13994    1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDESKRKdyvKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWClVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 -HGDMLEMIlssEKGRLPEHITKF-LITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA---RIIGEK 580
Cdd:cd13994   81 pGGDLFTLI---EKADSLSLEEKDcFFKQILRGVAYLHSHGIAHRDLKPENILL---DEDGVLKLTDFGTAevfGMPAEK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRS--VVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPF----NEDEDIHDQIQNAAFMYPPNPWKEISH 653
Cdd:cd13994  155 ESPMSagLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIENLL 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 654 --EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd13994  235 psECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
432-682 2.76e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 128.78  E-value: 2.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd08218    8 IGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRL-PEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEK-SFRRSVVGT 589
Cdd:cd08218   88 KRINAQRGVLfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDG---IIKLGDFGIARVLNSTvELARTCIGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEDIHDQIQNAafmYPPNPwKEISHEAIDLINNLLQVK 666
Cdd:cd08218  165 PYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFeagNMKNLVLKIIRGS---YPPVP-SRYSYDLRSLVSQLFKRN 240
                        250
                 ....*....|....*.
gi 568979055 667 MRKRYSVDKTLSHPWL 682
Cdd:cd08218  241 PRDRPSINSILEKPFI 256
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
431-683 3.03e-33

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 128.81  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF----PTKQESQLRNEVAILQNL----HHPGVVNLECMFETPERVFVVM 502
Cdd:cd14101    7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EK-LHG-DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVL--LASADpfpqVKLCDFGFARIIG 578
Cdd:cd14101   87 ERpQHCqDLFDYI--TERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILvdLRTGD----IKLIDFGSGATLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFrRSVVGTPAYLAPE-VLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDihdqIQNAAFMYPpnpwKEISHEAID 657
Cdd:cd14101  161 DSMY-TDFDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPFERDTD----ILKAKPSFN----KRVSNDCRS 231
                        250       260
                 ....*....|....*....|....*.
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14101  232 LIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
430-683 6.11e-33

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 128.12  E-value: 6.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQesQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06647   13 EKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVVG 588
Cdd:cd06647   91 LTDVVT--ETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDG---SVKLTDFGFcAQITPEQSKRSTMVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDEdihdqiQNAAFMYPPNPWKEISHEAI------DLINN 661
Cdd:cd06647  166 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENP------LRALYLIATNGTPELQNPEKlsaifrDFLNR 239
                        250       260
                 ....*....|....*....|..
gi 568979055 662 LLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06647  240 CLEMDVEKRGSAKELLQHPFLK 261
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
432-682 7.90e-33

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 127.56  E-value: 7.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDkLRfptKQESQ--LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMD-LR---KQQRRelLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVVG 588
Cdd:cd06648   91 LTDIVT--HTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG---RVKLSDFGFcAQVSKEVPRRKSLVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHdQIQNAAFMYPP---NPWKeISHEAIDLINNLLQV 665
Cdd:cd06648  166 TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQ-AMKRIRDNEPPklkNLHK-VSPRLRSFLDRMLVR 243
                        250
                 ....*....|....*..
gi 568979055 666 KMRKRYSVDKTLSHPWL 682
Cdd:cd06648  244 DPAQRATAAELLNHPFL 260
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
410-682 1.30e-32

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 127.28  E-value: 1.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 410 SNCQIQENVDIStvyqifpdevlgSGQFGIVYGGKHRKTGRDVAIKIIDKLRFptkqeSQLRNEVAILQNlHHPGVVNLE 489
Cdd:PHA03390  14 KNCEIVKKLKLI------------DGKFGKVSVLKHKPTQKLFVQKIIKAKNF-----NAIEPMVHQLMK-DNPNFIKLY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 490 CMFETPERVFVVMEKLH-GDMLEMILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfpQVKL 568
Cdd:PHA03390  76 YSVTTLKGHVLIMDYIKdGDLFDLLKK--EGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKD--RIYL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 569 CDFGFARIIGEKSFRRsvvGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDI-----HDQIQNaaf 641
Cdd:PHA03390 152 CDYGLCKIIGTPSCYD---GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFkeDEDEELdleslLKRQQK--- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568979055 642 myPPNPWKEISHEAIDLINNLLQVKMRKR-YSVDKTLSHPWL 682
Cdd:PHA03390 226 --KLPFIKNVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFL 265
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
430-682 1.87e-32

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 126.56  E-value: 1.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14108    8 KEIGRGAFSYLRRVKEKSSDLSFAAKFIPV---RAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARIIGEKSFRRSVVGT 589
Cdd:cd14108   85 LERI--TKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKT-DQVRICDFGNAQELTPNEPQYCKYGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLqVKM 667
Cdd:cd14108  162 PEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFvgENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVL-VSD 240
                        250
                 ....*....|....*
gi 568979055 668 RKRYSVDKTLSHPWL 682
Cdd:cd14108  241 RLRPDAEETLEHPWF 255
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
422-682 1.95e-32

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 126.54  E-value: 1.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 422 TVYQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKqeSQLRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd14107    2 SVYEVK--EEIGRGTFGFVKRVTHKGNGECCAAKFI-PLRSSTR--ARAFQERDILARLSHRRLTCLLDQFETRKTLILI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEklhgdmlemILSSE--------KGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGF 573
Cdd:cd14107   77 LE---------LCSSEelldrlflKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTR-EDIKICDFGF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 ARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHD--QIQNAAFMYPPNPWKEI 651
Cdd:cd14107  147 AQEITPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATllNVAEGVVSWDTPEITHL 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14107  227 SEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
432-686 2.43e-32

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 128.44  E-value: 2.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIK-IIDKLRFPTKQESQLRnEVAILQNL-HHPGVVNLECMF--ETPERVFVVMEKLHG 507
Cdd:cd07852   15 LGKGAYGIVWKAIDKKTGEVVALKkIFDAFRNATDAQRTFR-EIMFLQELnDHPNIIKLLNVIraENDKDIYLVFEYMET 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMIlssEKGRLPE-HItKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKSFRRSV 586
Cdd:cd07852   94 DLHAVI---RANILEDiHK-QYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSD---CRVKLADFGLARSLSQLEEDDEN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 ------VGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGT--FP----FNE------------DEDIhDQIQN--A 639
Cdd:cd07852  167 pvltdyVATRWYRAPEILlGSTRYTKGVDMWSVGCILGEMLLGKplFPgtstLNQlekiievigrpsAEDI-ESIQSpfA 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 640 AFMY------PPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQ 686
Cdd:cd07852  246 ATMLeslppsRPKSLDELfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFH 302
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
424-682 2.83e-32

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 127.66  E-value: 2.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFptkqESQLRNEVAILQNL------HHPGVVNLECMFETPE 496
Cdd:cd14210   15 YEV--LSVLGKGSFGQVVKCLDHKTGQLVAIKIIrNKKRF----HQQALVEVKILKHLndndpdDKHNIVRYKDSFIFRG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARI 576
Cdd:cd14210   89 HLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKS-SIKVIDFGSSCF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEKSF-----RrsvvgtpAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT--FP-FNEDEDI-----------HDQIQ 637
Cdd:cd14210  168 EGEKVYtyiqsR-------FYRAPEVILGLPYDTAIDMWSLGCILAELYTGYplFPgENEEEQLacimevlgvppKSLID 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 638 NAAF-------MYPPNP----WKEI---------------SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14210  241 KASRrkkffdsNGKPRPttnsKGKKrrpgskslaqvlkcdDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
432-682 4.01e-32

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 126.06  E-value: 4.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHR-----KTGRDVAIKII--DKLRFPTkQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd14076    9 LGEGEFGKVKLGWPLpkanhRSGVQVAIKLIrrDTQQENC-QTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHG-DMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKS-- 581
Cdd:cd14076   88 VSGgELFDYILARR--RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL---DKNRNLVITDFGFANTFDHFNgd 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPE-VLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDED---------IHDQIQNAAFMYPpnpwKE 650
Cdd:cd14076  163 LMSTSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGYLPFDDDPHnpngdnvprLYRYICNTPLIFP----EY 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568979055 651 ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14076  239 VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
429-682 4.01e-32

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 127.07  E-value: 4.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIID---------KLRFPTKQESQLRNEVAILQNLHHpgvvNLECMFetpervf 499
Cdd:cd14170    7 SQVLGLGINGKVLQIFNKRTQEKFALKMLQdcpkarrevELHWRASQCPHIVRIVDVYENLYA----GRKCLL------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG-DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIG 578
Cdd:cd14170   76 IVMECLDGgELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE------DIHDQIQNAAFMYPPNPWKEIS 652
Cdd:cd14170  156 SHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaispGMKTRIRMGQYEFPNPEWSEVS 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 653 HEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14170  236 EEVKMLIRNLLKTEPTQRMTITEFMNHPWI 265
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
430-615 4.14e-32

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 125.87  E-value: 4.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNL-ECMFETPErVFVVMEKLHG- 507
Cdd:cd13996   12 ELLGSGGFGSVYKVRNKVDGVTYAIKKI-RLTEKSSASEKVLREVKALAKLNHPNIVRYyTAWVEEPP-LYIQMELCEGg 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 ---DMLEMILSSEKGRLPEHITKFLitQILVALRHLHFKNIVHCDLKPENVLLASadPFPQVKLCDFGFARIIGEK---- 580
Cdd:cd13996   90 tlrDWIDRRNSSSKNDRKLALELFK--QILKGVSYIHSKGIVHRDLKPSNIFLDN--DDLQVKIGDFGLATSIGNQkrel 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 581 -----------SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVI 615
Cdd:cd13996  166 nnlnnnnngntSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGII 211
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
431-695 4.26e-32

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 126.32  E-value: 4.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPT-KQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd05605    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKrKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGgD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd05605   87 LKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILL---DDHGHVRISDLGLAVEIPEGETIRGRVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN------EDEDIHDQIQNAAFMYPpnpwKEISHEAIDLINNL 662
Cdd:cd05605  164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRarkekvKREEVDRRVKEDQEEYS----EKFSEEAKSICSQL 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568979055 663 LQ--VKMR---KRYSVDKTLSHPWLQDyqtwLDLRELE 695
Cdd:cd05605  240 LQkdPKTRlgcRGEGAEDVKSHPFFKS----INFKRLE 273
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
430-710 5.80e-32

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 127.08  E-value: 5.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-KLHG 507
Cdd:cd05597    7 KVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAEtACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDyYCGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMiLSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRS-- 585
Cdd:cd05597   87 DLLTL-LSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRNGHIRLADFGSCLKLREDGTVQSsv 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLR----NKG-YNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQN--AAFMYPPNPwKEISHEAI 656
Cdd:cd05597  163 AVGTPDYISPEILQamedGKGrYGPECDWWSLGVCMYEMLYGETPFYAESlvETYGKIMNhkEHFSFPDDE-DDVSEEAK 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 657 DLINNLLQVKMRK--RYSVDKTLSHPWLQDYQtWLDLRELEC-RIGEryITHESDDS 710
Cdd:cd05597  242 DLIRRLICSRERRlgQNGIDDFKKHPFFEGID-WDNIRDSTPpYIPE--VTSPTDTS 295
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
432-681 6.76e-32

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 125.55  E-value: 6.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF--------------PTKQESQLRN-------EVAILQNLHHPGVVNLEC 490
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrKPGALGKPLDpldrvyrEIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 491 MFETPER-----VFVVMEKlhGDMLEMILSSEkgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQ 565
Cdd:cd14118   82 VLDDPNEdnlymVFELVDK--GAVMEVPTDNP---LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLL---GDDGH 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 566 VKLCDFGFARII-GEKSFRRSVVGTPAYLAPEVL---RNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDI---HDQIQN 638
Cdd:cd14118  154 VKIADFGVSNEFeGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPF-EDDHIlglHEKIKT 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568979055 639 AAFMYPPNPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14118  233 DPVVFPDDP--VVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
432-683 8.46e-32

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 124.98  E-value: 8.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGDM 509
Cdd:cd14117   14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGvEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYApRGEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAriIGEKSFRR-SVVG 588
Cdd:cd14117   94 YKELQKH--GRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKG---ELKIADFGWS--VHAPSLRRrTMCG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN--EDEDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQVK 666
Cdd:cd14117  167 TLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFEsaSHTETYRRIVKVDLKFPPF----LSDGSRDLISKLLRYH 242
                        250
                 ....*....|....*..
gi 568979055 667 MRKRYSVDKTLSHPWLQ 683
Cdd:cd14117  243 PSERLPLKGVMEHPWVK 259
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
432-684 8.53e-32

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 126.53  E-value: 8.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNL---HHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEvAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEkGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05586   81 GELFWHLQKE-GRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL---DANGHIALCDFGLSKAdLTDNKTTNTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEV-LRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEdEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQV 665
Cdd:cd05586  157 CGTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYA-EDTQQMYRNIAFGKVRFPKDVLSDEGRSFVKGLLNR 235
                        250       260
                 ....*....|....*....|...
gi 568979055 666 KMRKRY-SVDKTL---SHPWLQD 684
Cdd:cd05586  236 NPKHRLgAHDDAVelkEHPFFAD 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
432-682 8.58e-32

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 125.87  E-value: 8.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQEsQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMD-LRKQQRRE-LLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDFGF-ARIIGEKSFRRSVVGTP 590
Cdd:cd06659  107 DIVS--QTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL---DGRVKLSDFGFcAQISKDVPKRKSLVGTP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhdQIQNAAFMYPPnPWKEISHEAI----DLINNLLQVK 666
Cdd:cd06659  182 YWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPV--QAMKRLRDSPP-PKLKNSHKASpvlrDFLERMLVRD 258
                        250
                 ....*....|....*.
gi 568979055 667 MRKRYSVDKTLSHPWL 682
Cdd:cd06659  259 PQERATAQELLDHPFL 274
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
430-695 9.52e-32

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 126.18  E-value: 9.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLR-NEVAILQNLH-HPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTmTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 -DMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRS 585
Cdd:cd05590   81 gDLMFHIQKSR--RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMCKEgIFNGKTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDeDIHDQIQNAAFMYPpnPWkeISHEAIDLINNL 662
Cdd:cd05590  156 FCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFeaeNED-DLFEAILNDEVVYP--TW--LSQDAVDILKAF 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568979055 663 LQVKMRKRY-SVDK-----TLSHPWLQDYQtW--LDLRELE 695
Cdd:cd05590  231 MTKNPTMRLgSLTLggeeaILRHPFFKELD-WekLNRRQIE 270
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
432-721 9.74e-32

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 127.84  E-value: 9.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDK-LRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMKKkVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGDF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR-IIGEK--------- 580
Cdd:cd05600   99 RTLLNN-SGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLI---DSSGHIKLTDFGLASgTLSPKkiesmkirl 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 -------------SFRR---------------SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--E 630
Cdd:cd05600  175 eevkntafleltaKERRniyramrkedqnyanSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGStpN 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 631 DIHDQIQNaafmyppnpWKE---------------ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQtWLDLRE-- 693
Cdd:cd05600  255 ETWANLYH---------WKKtlqrpvytdpdlefnLSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKNID-WDRLREgs 324
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 568979055 694 -------LECRIGERYI---THESDDSR-WEQYAGEQGL 721
Cdd:cd05600  325 kppfipeLESEIDTSYFddfNDEADMAKyKDVHEKQKSL 363
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
430-695 1.21e-31

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 126.19  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK--LRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05619   11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKdvVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVMEYLNG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 -DMLEMILSSEKGRLPEhiTKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR--IIGEKSfRR 584
Cdd:cd05619   91 gDLMFHIQSCHKFDLPR--ATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGHIKIADFGMCKenMLGDAK-TS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN--EDEDIHDQIQNAAFMYPpnpwKEISHEAIDLINNL 662
Cdd:cd05619  165 TFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHgqDEEELFQSIRMDNPFYP----RWLEKEAKDILVKL 240
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 663 LQVKMRKRYSVDKTL-SHPWLQDYQtW--LDLRELE 695
Cdd:cd05619  241 FVREPERRLGVRGDIrQHPFFREIN-WeaLEEREIE 275
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
431-695 1.29e-31

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 124.99  E-value: 1.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd05608    8 VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEgAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGgD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMI--LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFR-RS 585
Cdd:cd05608   88 LRYHIynVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL---DDDGNVRISDLGLAVELKDGQTKtKG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN------EDEDIHDQIQNAAFMYPpnpwKEISHEAIDLI 659
Cdd:cd05608  165 YAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRargekvENKELKQRILNDSVTYS----EKFSPASKSIC 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568979055 660 NNLLQVKMRKRY-----SVDKTLSHPWLQDyqtwLDLRELE 695
Cdd:cd05608  241 EALLAKDPEKRLgfrdgNCDGLRTHPFFRD----INWRKLE 277
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
430-682 1.81e-31

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 124.32  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd07835    5 EKIGEGTYGVVYKARDKLTGEIVALK---KIRLETEDEgvpsTAIR-EISLLKELNHPNIVRLLDVVHSENKLYLVFEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIG--EKSFR 583
Cdd:cd07835   81 DLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLI---DTEGALKLADFGLARAFGvpVRTYT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVgTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI------------------------QN 638
Cdd:cd07835  158 HEVV-TLWYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEI-DQLfrifrtlgtpdedvwpgvtslpdyKP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 639 AAFMYPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07835  236 TFPKWARQDLSKVvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
431-682 1.99e-31

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 123.80  E-value: 1.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIK--IIDKLRFPTKQE-----SQLRNEVAILQNLHHPGVVN-LECMFETpERVFVVM 502
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENKDRkksmlDALQREIALLRELQHENIVQyLGSSSDA-NHLNIFL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR------- 575
Cdd:cd06628   86 EYVPGGSVATLLNN-YGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILV---DNKGGIKISDFGISKkleansl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEdediHDQIQnAAF----MYPPNPWKEI 651
Cdd:cd06628  162 STKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPD----CTQMQ-AIFkigeNASPTIPSNI 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06628  237 SSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
430-681 2.41e-31

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 124.15  E-value: 2.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE---SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd07860    6 EKIGEGTYGVVYKARNKLTGEVVALK---KIRLDTETEgvpSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG--EKSFRR 584
Cdd:cd07860   83 QDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEG---AIKLADFGLARAFGvpVRTYTH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVgTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI-----------------------QNAA 640
Cdd:cd07860  160 EVV-TLWYRAPEILLGcKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEI-DQLfrifrtlgtpdevvwpgvtsmpdYKPS 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 641 F-MYPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07860  238 FpKWARQDFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
432-720 2.57e-31

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 125.12  E-value: 2.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIidkLRfptKQESQLRNEVA-------ILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd05598    9 IGVGAFGEVSLVRKKDTNALYAMKT---LR---KKDVLKRNQVAhvkaerdILAEADNEWVVKLYYSFQDKENLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 L-HGDMleMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAriigeKSFR 583
Cdd:cd05598   83 IpGGDL--MSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLC-----TGFR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 ----------RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQ----NAAFMYPPNPwk 649
Cdd:cd05598  153 wthdskyylaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKvinwRTTLKIPHEA-- 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 650 EISHEAIDLINNLL-QVKMR-KRYSVDKTLSHPWLQDYqTWLDLRELECrIGERYITHESDDSRWEQYAGEQG 720
Cdd:cd05598  231 NLSPEAKDLILRLCcDAEDRlGRNGADEIKAHPFFAGI-DWEKLRKQKA-PYIPTIRHPTDTSNFDPVDPEKL 301
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
431-626 3.62e-31

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 124.43  E-value: 3.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKhRKTGRDV----AIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd05582    2 VLGQGSFGKVFLVR-KITGPDAgtlyAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR-IIGEKSFRRS 585
Cdd:cd05582   81 GGDLFTRLSKEV-MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEDGHIKLTDFGLSKeSIDHEKKAYS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd05582  157 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPF 197
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
423-682 3.86e-31

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 122.77  E-value: 3.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 423 VYQIFPdeVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE----SQLRNEVAILQNLHH--PGVVNLECMFETPE 496
Cdd:cd14100    1 QYQVGP--LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGElpngTRVPMEIVLLKKVGSgfRGVIRLLDWFERPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLH--GDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVL--LASADpfpqVKLCDFG 572
Cdd:cd14100   79 SFVLVLERPEpvQDLFDFI--TERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILidLNTGE----LKLIDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 573 FARIIGEKSFrRSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDEDIhdqIQNAAFMYppnpwKEI 651
Cdd:cd14100  153 SGALLKDTVY-TDFDGTRVYSPPEWIRFHRYHgRSAAVWSLGILLYDMVCGDIPFEHDEEI---IRGQVFFR-----QRV 223
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14100  224 SSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
430-693 4.52e-31

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 125.88  E-value: 4.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQL-RNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05621   58 KVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGG 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRR--SV 586
Cdd:cd05621  138 DLVNLMSNYD--VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADFGTCMKMDETGMVHcdTA 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKG----YNRSLDMWSVGVIIYVSLSGTFPFNEDEDI--HDQIQN--AAFMYPPNpwKEISHEAIDL 658
Cdd:cd05621  213 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVgtYSKIMDhkNSLNFPDD--VEISKHAKNL 290
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568979055 659 INNLL---QVKMrKRYSVDKTLSHPWLQDYQ-TWLDLRE 693
Cdd:cd05621  291 ICAFLtdrEVRL-GRNGVEEIKQHPFFRNDQwNWDNIRE 328
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
432-681 5.08e-31

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 123.44  E-value: 5.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECMFETPER------VFVV 501
Cdd:cd07840    7 IGEGTYGQVYKARNKKTGELVALK---KIRMENEKEgfpiTAIR-EIKLLQKLDHPNVVRLKEIVTSKGSakykgsIYMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDmLEMILSSEKGRL-PEHItKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEK 580
Cdd:cd07840   83 FEYMDHD-LTGLLDNPEVKFtESQI-KCYMKQLLEGLQYLHSNGILHRDIKGSNILI---NNDGVLKLADFGLARPYTKE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRR--SVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIH--DQIqnAAFMYPPNP--W----- 648
Cdd:cd07840  158 NNADytNRVITLWYRPPELLLGaTRYGPEVDMWSVGCILAELFTGKPIFQGKTELEqlEKI--FELCGSPTEenWpgvsd 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 649 ----------------------KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07840  236 lpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
430-681 6.37e-31

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 122.97  E-value: 6.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd07836    6 EKLGEGTYATVYKGRNRTTGEIVALKEI-HLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LE-MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG--EKSFRRSV 586
Cdd:cd07836   85 KKyMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRG---ELKLADFGLARAFGipVNTFSNEV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VgTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGT--FPFNEDEDIHDQI---------------------QNAAFM 642
Cdd:cd07836  162 V-TLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRplFPGTNNEDQLLKIfrimgtptestwpgisqlpeyKPTFPR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568979055 643 YPPNPWKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07836  241 YPPQDLQQLfphaDPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
432-626 7.73e-31

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 122.56  E-value: 7.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPT----KQESQLRNEVAILQNLHHPGVVNL-----ECMFETPERV-FVV 501
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIK---KCRQELspsdKNRERWCLEVQIMKKLNHPNVVSArdvppELEKLSPNDLpLLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSEKGR--LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGE 579
Cdd:cd13989   78 MEYCSGGDLRKVLNQPENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELDQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 580 KSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd13989  158 GSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
424-680 8.37e-31

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 122.08  E-value: 8.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESqLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd06610    3 YELI--EVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSMDE-LRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLH-GDMLEMILSS-EKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE-- 579
Cdd:cd06610   80 LLSgGSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDG---SVKIADFGVSASLATgg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 ---KSFRRSVVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFnedediHDQ---------IQNAAFMYPPN 646
Cdd:cd06610  157 drtRKVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPY------SKYppmkvlmltLQNDPPSLETG 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 647 -PWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd06610  231 aDYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
419-683 9.48e-31

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 123.63  E-value: 9.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQifPDEVLGSGQFGIVYGGKHRKTGRDVAIK--------IIDKLRfptkqesQLRnEVAILQNLHHPGVVNLEC 490
Cdd:cd07858    2 EVDTKYV--PIKPIGRGAYGIVCSAKNSETNEKVAIKkianafdnRIDAKR-------TLR-EIKLLRHLDHENVIAIKD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 491 MFETPER-----VFVVMEKLHGDMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL-ASADpfp 564
Cdd:cd07858   72 IMPPPHReafndVYIVYELMDTDLHQIIRSSQT--LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLnANCD--- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 565 qVKLCDFGFARIIGEKS-FRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVI---------------------IYVSLS 621
Cdd:cd07858  147 -LKICDFGLARTTSEKGdFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIfaellgrkplfpgkdyvhqlkLITELL 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979055 622 GTfPFNEDED-IHDQI-------------QNAAFMYPpnpwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd07858  226 GS-PSEEDLGfIRNEKarryirslpytprQSFARLFP-----HANPLAIDLLEKMLVFDPSKRITVEEALAHPYLA 295
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
429-645 9.81e-31

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 121.50  E-value: 9.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   429 DEVLGSGQFGIVYGGKHR----KTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLE--CMfeTPERVFVVM 502
Cdd:smart00221   4 GKKLGEGAFGEVYKGTLKgkgdGKEVEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLgvCT--EEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   503 EKL-HGDMLEMILSSEKGRLPeHITKFLI-TQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDFGFARIIGEK 580
Cdd:smart00221  81 EYMpGGDLLDYLRKNRPKELS-LSDLLSFaLQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSRDLYDD 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   581 SFRRSVVGT-P-AYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGTFPFN-EDEDIHDQIQNAAFMYPP 645
Cdd:smart00221 157 DYYKVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWeiFTLGEEPYPGmSNAEVLEYLKKGYRLPKP 226
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
429-645 1.12e-30

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 121.10  E-value: 1.12e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   429 DEVLGSGQFGIVYGGKHR----KTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLE--CMfeTPERVFVVM 502
Cdd:smart00219   4 GKKLGEGAFGEVYKGKLKgkggKKKVEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLgvCT--EEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   503 EKL-HGDMLEmILSSEKGRLPeHITKFLI-TQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDFGFARIIGEK 580
Cdd:smart00219  81 EYMeGGDLLS-YLRKNRPKLS-LSDLLSFaLQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSRDLYDD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   581 SFRRSVVGT-P-AYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGTFPFN-EDEDIHDQIQNAAFMYPP 645
Cdd:smart00219 156 DYYRKRGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWeiFTLGEQPYPGmSNEEVLEYLKNGYRLPQP 225
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
430-629 1.16e-30

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 121.34  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRktGRDVAIKIIDKLRFPTKQESQLRNEVAILqNLHHPGVVNL---ECMFETPERVFVVMEKLH 506
Cdd:cd13979    9 EPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAA-RLRHENIVRVlaaETGTDFASLGLIIMEYCG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGRLP-EHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE---KSF 582
Cdd:cd13979   86 NGTLQQLIYEGSEPLPlAHRILISL-DIARALRFCHSHGIVHLDVKPANILISEQG---VCKLCDFGCSVKLGEgneVGT 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 583 RRSVV-GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED 629
Cdd:cd13979  162 PRSHIgGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL 209
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
431-680 1.17e-30

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 122.03  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd07848    8 VVGEGAYGVVLKCRHKETKEIVAIKKFkDSEENEEVKETTLR-ELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFlITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRR--SVV 587
Cdd:cd07848   87 LELLEEMPNGVPPEKVRSY-IYQLIKAIHWCHKNDIVHRDIKPENLLISHND---VLKLCDFGFARNLSEGSNANytEYV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYvSLSGTFPFNEDEDIHDQ---IQNAAFMYPP--------NP------WKE 650
Cdd:cd07848  163 ATRWYRSPELLLGAPYGKAVDMWSVGCILG-ELSDGQPLFPGESEIDQlftIQKVLGPLPAeqmklfysNPrfhglrFPA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568979055 651 ISHEA--------------IDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd07848  242 VNHPQslerrylgilsgvlLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
432-680 1.26e-30

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 121.26  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06613    8 IGSGTYGDVYKARNIATGELAAVKVI-KLE-PGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGSLQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRR-SVVGTP 590
Cdd:cd06613   86 DIY-QVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDG---DVKLADFGVSAQLTATIAKRkSFIGTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVL---RNKGYNRSLDMWSVGvIIYVSLSGTFP--FnedeDIHdqIQNAAFM-----YPP------NPWKEISHe 654
Cdd:cd06613  162 YWMAPEVAaveRKGGYDGKCDIWALG-ITAIELAELQPpmF----DLH--PMRALFLipksnFDPpklkdkEKWSPDFH- 233
                        250       260
                 ....*....|....*....|....*.
gi 568979055 655 aiDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd06613  234 --DFIKKCLTKNPKKRPTATKLLQHP 257
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
430-683 1.29e-30

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 122.14  E-value: 1.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQesQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06655   25 EKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKE--LIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVVG 588
Cdd:cd06655  103 LTDVVTETC--MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDG---SVKLTDFGFcAQITPEQSKRSTMVG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPP--NPWKeISHEAIDLINNLLQVK 666
Cdd:cd06655  178 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPElqNPEK-LSPIFRDFLNRCLEMD 256
                        250
                 ....*....|....*..
gi 568979055 667 MRKRYSVDKTLSHPWLQ 683
Cdd:cd06655  257 VEKRGSAKELLQHPFLK 273
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
424-670 1.34e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 121.46  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTGRDV-AIKIID--KLRF-PTKQESQ-----LRNEVAIL-QNLHHPGVVNLECMFE 493
Cdd:cd08528    2 YAVL--ELLGSGAFGCVYKVRKKSNGQTLlALKEINmtNPAFgRTEQERDksvgdIISEVNIIkEQLRHPNIVRYYKTFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 494 TPERVFVVMEKLHGDMLEMILSSEK---GRLPEHITKFLITQILVALRHLHF-KNIVHCDLKPENVLLASADpfpQVKLC 569
Cdd:cd08528   80 ENDRLYIVMELIEGAPLGEHFSSLKeknEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDD---KVTIT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 570 DFGFARIIG-EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAfmYPPN 646
Cdd:cd08528  157 DFGLAKQKGpESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNmlTLATKIVEAE--YEPL 234
                        250       260
                 ....*....|....*....|....
gi 568979055 647 PWKEISHEAIDLINNLLQVKMRKR 670
Cdd:cd08528  235 PEGMYSDDITFVIRSCLTPDPEAR 258
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
430-670 1.37e-30

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 123.65  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05593   21 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSVV 587
Cdd:cd05593  101 ELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEgITDAATMKTFC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NED-EDIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQV 665
Cdd:cd05593  177 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDhEKLFELILMEDIKFP----RTLSADAKSLLSGLLIK 252

                 ....*
gi 568979055 666 KMRKR 670
Cdd:cd05593  253 DPNKR 257
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
430-695 1.49e-30

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 122.75  E-value: 1.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK--LRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKdvVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR--IIGEKSfRRS 585
Cdd:cd05620   81 GDL-MFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFGMCKenVFGDNR-AST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDihDQIQNAAFMYPPNPWKEISHEAIDLINNLLQV 665
Cdd:cd05620  156 FCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDE--DELFESIRVDTPHYPRWITKESKDILEKLFER 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568979055 666 KMRKRYSVDKTLS-HPWLQDYQ-TWLDLRELE 695
Cdd:cd05620  234 DPTRRLGVVGNIRgHPFFKTINwTALEKRELD 265
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
424-682 1.66e-30

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 121.17  E-value: 1.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYggKHRKTGRDV-AIKIIDKLRFPTKQESQLRNEVAILQNL-HHPGVVNL---EcMFETPERV 498
Cdd:cd14131    3 YEIL--KQLGKGGSSKVY--KVLNPKKKIyALKRVDLEGADEQTLQSYKNEIELLKKLkGSDRIIQLydyE-VTDEDDYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 499 FVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfpQVKLCDFGFARIIG 578
Cdd:cd14131   78 YMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG----RLKLIDFGIAKAIQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKS---FRRSVVGTPAYLAPEVLRNKGYN----------RSLDMWSVGVIIYVSLSGTFPFNedediHDQIQNAAFMYPP 645
Cdd:cd14131  154 NDTtsiVRDSQVGTLNYMSPEAIKDTSASgegkpkskigRPSDVWSLGCILYQMVYGKTPFQ-----HITNPIAKLQAII 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568979055 646 NPWKEISH------EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14131  229 DPNHEIEFpdipnpDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
431-670 2.01e-30

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 122.50  E-value: 2.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFPTKQESQLRNEVAILQNlHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05587    3 VLGKGSFGKVMLAERKGTDELYAIKILKKdviIQDDDVECTMVEKRVLALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFAR--IIGEKSfRRS 585
Cdd:cd05587   82 GDL-MYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---DAEGHIKIADFGMCKegIFGGKT-TRT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN-EDED-IHDQIQNAAFMYPpnpwKEISHEAIDLINNLL 663
Cdd:cd05587  157 FCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDgEDEDeLFQSIMEHNVSYP----KSLSKEAVSICKGLL 232

                 ....*..
gi 568979055 664 QVKMRKR 670
Cdd:cd05587  233 TKHPAKR 239
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
432-681 2.14e-30

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 121.32  E-value: 2.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidklRF------PTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIK-----KFveseddPVIKKIALR-EIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII-GEKSFRR 584
Cdd:cd07847   83 DHTVLNELEKNPRG-VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQG---QIKLCDFGFARILtGPGDDYT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGT--FPFNEDEDI--------------HDQI--QNAAF--MY 643
Cdd:cd07847  159 DYVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQplWPGKSDVDQlylirktlgdliprHQQIfsTNQFFkgLS 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 644 PPNP---------WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07847  239 IPEPetrepleskFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
432-691 3.16e-30

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 122.40  E-value: 3.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTG-RDVAIKIIDKLRF-PTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:PTZ00426  38 LGTGSFGRVILATYKNEDfPPVAIKRFEKSKIiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLaSADPFpqVKLCDFGFARIIGEKSFrrSVVGT 589
Cdd:PTZ00426 118 FFTFLRRNK-RFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL-DKDGF--IKMTDFGFAKVVDTRTY--TLCGT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQVKM 667
Cdd:PTZ00426 192 PEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFyaNEPLLIYQKILEGIIYFP----KFLDNNCKHLMKKLLSHDL 267
                        250       260
                 ....*....|....*....|....*....
gi 568979055 668 RKRY-----SVDKTLSHPWLQDYQtWLDL 691
Cdd:PTZ00426 268 TKRYgnlkkGAQNVKEHPWFGNID-WVSL 295
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
432-685 3.68e-30

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 121.74  E-value: 3.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRD--VAIKIIDKLrFPTK--QESQLRnEVAILQNLH-HPGVVNL---ECMFETPER-VFVVM 502
Cdd:cd07857    8 LGQGAYGIVCSARNAETSEEetVAIKKITNV-FSKKilAKRALR-ELKLLRHFRgHKNITCLydmDIVFPGNFNeLYLYE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENvLLASADPfpQVKLCDFGFARIIGEKSF 582
Cdd:cd07857   86 ELMEADLHQIIRSGQ--PLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGN-LLVNADC--ELKICDFGLARGFSENPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRS-----VVGTPAYLAPEV-LRNKGYNRSLDMWSVGVIIYVSLSGTfPFNEDEDIHDQI-------------------- 636
Cdd:cd07857  161 ENAgfmteYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRK-PVFKGKDYVDQLnqilqvlgtpdeetlsrigs 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 637 ---QNAAFMYPPNPWKEI-------SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd07857  240 pkaQNYIRSLPNIPKKPFesifpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYLAIW 298
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
430-670 3.84e-30

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 122.45  E-value: 3.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05594   31 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgRLPEHITKFLITQILVALRHLHF-KNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05594  111 ELFFHLSRER-VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLCKEgIKDGATMKTF 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NED-EDIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQ 664
Cdd:cd05594  187 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDhEKLFELILMEEIRFP----RTLSPEAKSLLSGLLK 262

                 ....*.
gi 568979055 665 VKMRKR 670
Cdd:cd05594  263 KDPKQR 268
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
423-682 3.92e-30

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 119.67  E-value: 3.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 423 VYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLR---FPTKQESQLRNEVAILQNLHHP--GVVNLECMFETPER 497
Cdd:cd14102    1 VYQV--GSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERvteWGTLNGVMVPLEIVLLKKVGSGfrGVIKLLDWYERPDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 VFVVMEK--LHGDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfPQVKLCDFGFAR 575
Cdd:cd14102   79 FLIVMERpePVKDLFDFI--TEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRT--GELKLIDFGSGA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFrRSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDEDIhdqIQNAAFMYppnpwKEISHE 654
Cdd:cd14102  155 LLKDTVY-TDFDGTRVYSPPEWIRYHRYHgRSATVWSLGVLLYDMVCGDIPFEQDEEI---LRGRLYFR-----RRVSPE 225
                        250       260
                 ....*....|....*....|....*...
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14102  226 CQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
429-682 4.89e-30

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 119.64  E-value: 4.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMeklhgd 508
Cdd:cd13983    6 NEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIF------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSsekGRLPEHITKF------LIT----QILVALRHLHFKN--IVHCDLKPENVLLASADpfPQVKLCDFGFARI 576
Cdd:cd13983   80 ITELMTS---GTLKQYLKRFkrlklkVIKswcrQILEGLNYLHTRDppIIHRDLKCDNIFINGNT--GEVKIGDLGLATL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IgEKSFRRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIYVSLSGTFPFNEdedihdqIQNAAFMY-------PPNPWK 649
Cdd:cd13983  155 L-RQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSE-------CTNAAQIYkkvtsgiKPESLS 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 650 EISHEAI-DLINNLLQVKmRKRYSVDKTLSHPWL 682
Cdd:cd13983  226 KVKDPELkDFIEKCLKPP-DERPSARELLEHPFF 258
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
432-681 4.94e-30

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 120.07  E-value: 4.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNL-HHPGVVNL-ECMFE-TPERVFVVMEKLHGD 508
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLEQVNNLREIQALRRLsPHPNILRLiEVLFDrKTGRLALVFELMDMN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMIlsseKGR---LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAsadpFPQVKLCDFGFARIIGEKSFRRS 585
Cdd:cd07831   86 LYELI----KGRkrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK----DDILKLADFGSCRGIYSKPPYTE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKG-YNRSLDMWSVGVIIY--VSLSGTFPFNEDED----IHD--------------QIQNAAFMYP 644
Cdd:cd07831  158 YISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFeiLSLFPLFPGTNELDqiakIHDvlgtpdaevlkkfrKSRHMNYNFP 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568979055 645 PNPWKEI-------SHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07831  238 SKKGTGLrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-691 7.39e-30

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 120.11  E-value: 7.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKH---RKTGRDVAIKIIDKLRFPTKQES--QLRNEVAILQNLHH-PGVVNLECMFETPERVFVVME 503
Cdd:cd05613    6 KVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKATIVQKAKTaeHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLHLILD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR--IIGEKS 581
Cdd:cd05613   86 YINGGELFTHLS-QRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSG---HVVLTDFGLSKefLLDENE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLR--NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMY---PPNPwKEISHEAI 656
Cdd:cd05613  162 RAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILksePPYP-QEMSALAK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568979055 657 DLINNLLQVKMRKRY-----SVDKTLSHPWLQDYQtWLDL 691
Cdd:cd05613  241 DIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQKIN-WDDL 279
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
430-695 7.91e-30

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 122.81  E-value: 7.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05624   78 KVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETAcFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA-RIIGEKSFRRSV- 586
Cdd:cd05624  158 DLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL---DMNGHIRLADFGSClKMNDDGTVQSSVa 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNK-----GYNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQN--AAFMYPPNPwKEISHEAID 657
Cdd:cd05624  235 VGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESlvETYGKIMNheERFQFPSHV-TDVSEEAKD 313
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568979055 658 LINNLLQVKMRK--RYSVDKTLSHPWLQDYQtWLDLRELE 695
Cdd:cd05624  314 LIQRLICSRERRlgQNGIEDFKKHAFFEGLN-WENIRNLE 352
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
430-682 8.14e-30

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 119.33  E-value: 8.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDklrfPTKQE-SQLRNEVAILQNL-HHPGVVNLECMFETP------ERVFVV 501
Cdd:cd06608   12 EVIGEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEeEEIKLEINILRKFsNHPNIATFYGAFIKKdppggdDQLWLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHG----DMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARII 577
Cdd:cd06608   88 MEYCGGgsvtDLVKGLRKKGK-RLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE---AEVKLVDFGVSAQL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRR-SVVGTPAYLAPEVL-----RNKGYNRSLDMWSVGvIIYVSLS-GTFPFNedeDIHDqiQNAAFMYPPNP--- 647
Cdd:cd06608  164 DSTLGRRnTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLG-ITAIELAdGKPPLC---DMHP--MRALFKIPRNPppt 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568979055 648 ------WkeiSHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06608  238 lkspekW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
430-682 8.39e-30

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 118.48  E-value: 8.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKT-------GRDVAIKIIdklrFPTKQESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVV 501
Cdd:cd14019    7 EKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHI----YPTSSPSRILNELECLERLGgSNNVSGLITAFRNEDQVVAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKL-HGDMLEMILSSEkgrlPEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQV-KLCDFGFARIIGE 579
Cdd:cd14019   83 LPYIeHDDFRDFYRKMS----LTDIRIYL-RNLFKALKHVHSFGIIHRDVKPGNFLY---NRETGKgVLVDFGLAQREED 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRR-SVVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFP-FNEDEDIHDQIQNAAFMYppnpwkeiSHEAI 656
Cdd:cd14019  155 RPEQRaPRAGTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRFPfFFSSDDIDALAEIATIFG--------SDEAY 226
                        250       260
                 ....*....|....*....|....*.
gi 568979055 657 DLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14019  227 DLLDKLLELDPSKRITAEEALKHPFF 252
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
432-684 1.70e-29

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 119.39  E-value: 1.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECMF--ETPERVFVVMEKL 505
Cdd:cd07845   15 IGEGTYGIVYRARDTTSGEIVALK---KVRMDNERDgipiSSLR-EITLLLNLRHPNIVELKEVVvgKHLDSIFLVMEYC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG--EKSFR 583
Cdd:cd07845   91 EQD-LASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG---CLKIADFGLARTYGlpAKPMT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVgTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGT--FPFN-EDEDI----------HDQI------------- 636
Cdd:cd07845  167 PKVV-TLWYRAPELLLGcTTYTTAIDMWAVGCILAELLAHKplLPGKsEIEQLdliiqllgtpNESIwpgfsdlplvgkf 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 637 ----QNAAFMYPPNPWkeISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd07845  246 tlpkQPYNNLKHKFPW--LSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE 295
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
430-693 1.88e-29

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 121.65  E-value: 1.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQL-RNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05622   79 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRR--SV 586
Cdd:cd05622  159 DLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKMNKEGMVRcdTA 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKG----YNRSLDMWSVGVIIYVSLSGTFPFNEDEDI--HDQIQN--AAFMYPPNpwKEISHEAIDL 658
Cdd:cd05622  234 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVgtYSKIMNhkNSLTFPDD--NDISKEAKNL 311
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568979055 659 INNLL---QVKMrKRYSVDKTLSHPWLQDYQ-TWLDLRE 693
Cdd:cd05622  312 ICAFLtdrEVRL-GRNGVEEIKRHLFFKNDQwAWETLRD 349
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
431-684 2.69e-29

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 118.92  E-value: 2.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd05632    9 VLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGgD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd05632   89 LKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILL---DDYGHIRISDLGLAVKIPEGESIRGRVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN------EDEDIHDQIQNAAFMYPpnpwKEISHEAIDLINNL 662
Cdd:cd05632  166 TVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRgrkekvKREEVDRRVLETEEVYS----AKFSEEAKSICKML 241
                        250       260
                 ....*....|....*....|....*..
gi 568979055 663 LQVKMRKR-----YSVDKTLSHPWLQD 684
Cdd:cd05632  242 LTKDPKQRlgcqeEGAGEVKRHPFFRN 268
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
435-682 3.27e-29

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 117.25  E-value: 3.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGG--KHRKTGRDVAIKIidklRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEM 512
Cdd:cd14112   14 GRFSVIVKAvdSTTETDAHCAVKI----FEVSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQEDVFTR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 513 ILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpQVKLCDFGFARIIGeKSFRRSVVGTPAY 592
Cdd:cd14112   90 FSSNDY--YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSW-QVKLVDFGRAQKVS-KLGKVPVDGDTDW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 593 LAPEVLRNKG--YNRSlDMWSVGVIIYVSLSGTFPFNEDEDIHDQI-QNAAFMY--PPNPWKEISHEAIDLINNLLQVKM 667
Cdd:cd14112  166 ASPEFHNPETpiTVQS-DIWGLGVLTFCLLSGFHPFTSEYDDEEETkENVIFVKcrPNLIFVEATQEALRFATWALKKSP 244
                        250
                 ....*....|....*
gi 568979055 668 RKRYSVDKTLSHPWL 682
Cdd:cd14112  245 TRRMRTDEALEHRWL 259
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
419-685 3.62e-29

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 119.32  E-value: 3.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFETP 495
Cdd:cd07851   12 EVPDRYQNL--SPVGSGAYGQVCSAFDTKTGRKVAIK---KLSRPFQSAIHAKRtyrELRLLKHMKHENVIGLLDVFTPA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 496 ER------VFVVMEkLHGDMLEMILSSEKgrLP-EHItKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKL 568
Cdd:cd07851   87 SSledfqdVYLVTH-LMGADLNNIVKCQK--LSdDHI-QFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNED---CELKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 569 CDFGFARIIGEKsfRRSVVGTPAYLAPEVLRNKG-YNRSLDMWSVGVIIYVSLSGT--FPFNE---------------DE 630
Cdd:cd07851  160 LDFGLARHTDDE--MTGYVATRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLTGKtlFPGSDhidqlkrimnlvgtpDE 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 631 DIHDQIQNAAF-----MYPPNPWKEISH-------EAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd07851  238 ELLKKISSESArnyiqSLPQMPKKDFKEvfsganpLAIDLLEKMLVLDPDKRITAAEALAHPYLAEY 304
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
431-678 5.30e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 116.61  E-value: 5.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQES--QLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-G 507
Cdd:cd08219    7 VVGEGSFGRALLVQHVNSDQKYAMK---EIRLPKSSSAveDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDgG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMIlSSEKGRL-PEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEK-SFRRS 585
Cdd:cd08219   84 DLMQKI-KLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNG---KVKLGDFGSARLLTSPgAYACT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPwKEISHEAIDLINNLLQV 665
Cdd:cd08219  160 YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLP-SHYSYELRSLIKQMFKR 238
                        250
                 ....*....|...
gi 568979055 666 KMRKRYSVDKTLS 678
Cdd:cd08219  239 NPRSRPSATTILS 251
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
431-670 5.52e-29

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 116.94  E-value: 5.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYggKHRKTGRDVAIKIIDKLRF-------------------PTKQESQLRNEVAILQNLHHPGVVNLECM 491
Cdd:cd14000    1 LLGDGGFGSVY--RASYKGEPVAVKIFNKHTSsnfanvpadtmlrhlratdAMKNFRLLRQELTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 492 FETPerVFVVMEKLHGDMLEMILSSEKGR---LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQV-- 566
Cdd:cd14000   79 GIHP--LMLVLELAPLGSLDHLLQQDSRSfasLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAIii 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 567 KLCDFGFARiigeKSFR---RSVVGTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE------DIHDQI 636
Cdd:cd14000  157 KIADYGISR----QCCRmgaKGSEGTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLkfpnefDIHGGL 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 637 QNAAFMYPPNPWKEIsheaIDLINNLLQVKMRKR 670
Cdd:cd14000  233 RPPLKQYECAPWPEV----EVLMKKCWKENPQQR 262
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
426-686 5.79e-29

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 117.26  E-value: 5.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 426 IFPDEvLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd06622    4 EVLDE-LGKGNYGSVYKVLHRPTGVTMAMKEI-RLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMIL--SSEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLASADpfpQVKLCDFGFARIIgEKSF 582
Cdd:cd06622   82 DAGSLDKLYagGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNG---QVKLCDFGVSGNL-VASL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKG------YNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNPWKEISHE 654
Cdd:cd06622  158 AKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYPPEtyANIFAQLSAIVDGDPPTLPSGYSDD 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQ 686
Cdd:cd06622  238 AQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYK 269
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
432-682 6.39e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 118.77  E-value: 6.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKII-----DKLRfptkqeSQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVR------RQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGRLPEhitkfLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFR-RS 585
Cdd:PLN00034 156 GGSLEGTHIADEQFLAD-----VARQILSGIAYLHRRHIVHRDIKPSNLLINSAK---NVKIADFGVSRILAQTMDPcNS 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLrNKGYNRSL------DMWSVGVIIYVSLSGTFPFNededIHDQIQNAAFM------YPPNPWKEISH 653
Cdd:PLN00034 228 SVGTIAYMSPERI-NTDLNHGAydgyagDIWSLGVSILEFYLGRFPFG----VGRQGDWASLMcaicmsQPPEAPATASR 302
                        250       260
                 ....*....|....*....|....*....
gi 568979055 654 EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:PLN00034 303 EFRHFISCCLQREPAKRWSAMQLLQHPFI 331
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
430-645 6.63e-29

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 116.48  E-value: 6.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHR---KTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL- 505
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKggdGKTVDVAVKTL-KEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMe 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMiLSSEKGRLPEHITKFLITQILVA--------LRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARII 577
Cdd:cd00192   80 GGDLLDF-LRKSRPVFPSPEPSTLSLKDLLSfaiqiakgMEYLASKKFVHRDLAARNCLVGED---LVVKISDFGLSRDI 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 578 GEKSFRRSVVGTP---AYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGTfPFNE--DEDIHDQIQNAAFMYPP 645
Cdd:cd00192  156 YDDDYYRKKTGGKlpiRWMAPESLKDGIFTSKSDVWSFGVLLWeiFTLGAT-PYPGlsNEEVLEYLRKGYRLPKP 229
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
430-680 8.46e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 116.37  E-value: 8.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLR-FPTKQES---QLRNEVAILQNLHHPGVVnlECMFETPE--RVFVVME 503
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRnSSSEQEEvveAIREEIRMMARLNHPNIV--RMLGATQHksHFNIFVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfpQVKLCDFGFA-----RIIG 578
Cdd:cd06630   84 WMAGGSVASLLS-KYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQ--RLRIADFGAAarlasKGTG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEdihdqIQN--------AAFMYPPNPWKE 650
Cdd:cd06630  161 AGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEK-----ISNhlalifkiASATTPPPIPEH 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 651 ISHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd06630  236 LSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
431-679 1.50e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 115.02  E-value: 1.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPT-KQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14189    8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKpHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRL-PEhiTKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA-RIIGEKSFRRSVV 587
Cdd:cd14189   88 LAHIWKARHTLLePE--VRYYLKQIISGLKYLHLKGILHRDLKLGNFFINEN---MELKVGDFGLAaRLEPPEQRKKTIC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQ---IQNAAFMYPPNpwkeISHEAIDLINNLLQ 664
Cdd:cd14189  163 GTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPF-ETLDLKETyrcIKQVKYTLPAS----LSLPARHLLAGILK 237
                        250
                 ....*....|....*
gi 568979055 665 VKMRKRYSVDKTLSH 679
Cdd:cd14189  238 RNPGDRLTLDQILEH 252
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
429-680 1.96e-28

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 119.97  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMF-----ETPERVFVVME 503
Cdd:PTZ00283  37 SRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKCHEDFakkdpRNPENVLMIAL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLH----GDMLEMILSSEKGRLP--EHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII 577
Cdd:PTZ00283 117 VLDyanaGDLRQEIKSRAKTNRTfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG---LVKLGDFGFSKMY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 G---EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQIQNA-AFMYPPNPwKEISH 653
Cdd:PTZ00283 194 AatvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPF-DGENMEEVMHKTlAGRYDPLP-PSISP 271
                        250       260
                 ....*....|....*....|....*..
gi 568979055 654 EAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:PTZ00283 272 EMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
431-682 2.54e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 114.46  E-value: 2.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPE-RVFVVMEKLHGDM 509
Cdd:cd08223    7 VIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGFCEGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGR-LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfpqVKLCDFGFARII-GEKSFRRSVV 587
Cdd:cd08223   87 LYTRLKEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNI---IKVGDLGIARVLeSSSDMATTLI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEdEDIHD---QIQNAAFmyPPNPwKEISHEAIDLINNLLQ 664
Cdd:cd08223  164 GTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNA-KDMNSlvyKILEGKL--PPMP-KQYSPELGELIKAMLH 239
                        250
                 ....*....|....*...
gi 568979055 665 VKMRKRYSVDKTLSHPWL 682
Cdd:cd08223  240 QDPEKRPSVKRILRQPYI 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-682 2.69e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 114.45  E-value: 2.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFG--IVYggkhRKTGRD--VAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd08221    4 PVRVLGRGAFGeaVLY----RKTEDNslVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRL-PEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII-GEKS 581
Cdd:cd08221   80 YCNGGNLHDKIAQQKNQLfPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGISKVLdSESS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSGTFpfnedeDIHDQIQNAAFMYPPNpWKEI----SHEA 655
Cdd:cd08221  157 MAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYelLTLKRTF------DATNPLRLAVKIVQGE-YEDIdeqySEEI 229
                        250       260
                 ....*....|....*....|....*..
gi 568979055 656 IDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd08221  230 IQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
431-628 3.19e-28

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 115.12  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd05630    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGgD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd05630   87 LKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL---DDHGHIRISDLGLAVHVPEGQTIKGRVG 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE 628
Cdd:cd05630  164 TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQ 203
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
430-682 3.87e-28

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 114.82  E-value: 3.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE---SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd07861    6 EKIGEGTYGVVYKGRNKKTGQIVAMK---KIRLESEEEgvpSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGR-LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIG--EKSFR 583
Cdd:cd07861   83 MDLKKYLDSLPKGKyMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLI---DNKGVIKLADFGLARAFGipVRVYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVgTPAYLAPEVLRNKG-YNRSLDMWSVGViIYVSLSGTFP-FNEDEDIhDQ---------------------IQNAA 640
Cdd:cd07861  160 HEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGT-IFAEMATKKPlFHGDSEI-DQlfrifrilgtptediwpgvtsLPDYK 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 641 FMYPpnPWKE---------ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07861  237 NTFP--KWKKgslrtavknLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
418-696 4.24e-28

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 114.45  E-value: 4.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 418 VDISTVYQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKIIDklrfpTKQESQLRN---EVAILQNLHHPGVVNLECMFET 494
Cdd:cd06611    1 VNPNDIWEIIGE--LGDGAFGKVYKAQHKETGLFAAAKIIQ-----IESEEELEDfmvEIDILSECKHPNIVGLYEAYFY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PERVFVVMEKLHGDMLE-MILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF 573
Cdd:cd06611   74 ENKLWILIEFCDGGALDsIMLELERG-LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDG---DVKLADFGV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 -ARIIGEKSFRRSVVGTPAYLAPEVL-----RNKGYNRSLDMWSVGvIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPP-- 645
Cdd:cd06611  150 sAKNKSTLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLG-ITLIELAQMEPPHHELNPMRVLLKILKSEPPtl 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 646 ---NPWkeiSHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELEC 696
Cdd:cd06611  229 dqpSKW---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLLA 279
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
429-683 4.77e-28

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 114.68  E-value: 4.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVlGSGQFGIVYGGKHRKTGRDVAIKIIDKLR------FPTKQE------------------SQLRNEVAILQNLHHPG 484
Cdd:cd14199    8 DEI-GKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagFPRRPPprgaraapegctqprgpiERVYQEIAILKKLDHPN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 485 VVNLECMFETP--ERVFVVMEKL-HGDMLEMILSSEkgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAD 561
Cdd:cd14199   87 VVKLVEVLDDPseDHLYMVFELVkQGPVMEVPTLKP---LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 562 pfpQVKLCDFGFARII-GEKSFRRSVVGTPAYLAPEVL---RNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDI---HD 634
Cdd:cd14199  164 ---HIKIADFGVSNEFeGSDALLTNTVGTPAFMAPETLsetRKIFSGKALDVWAMGVTLYCFVFGQCPF-MDERIlslHS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 635 QIQNAAFMYPPNPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd14199  240 KIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
431-709 6.04e-28

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 115.59  E-value: 6.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFP----TKQESQLRnEVAILQNLHHPGVVNLECMFeTPER-------VF 499
Cdd:cd07850    7 PIGSGAQGIVCAAYDTVTGQNVAIK---KLSRPfqnvTHAKRAYR-ELVLMKLVNHKNIIGLLNVF-TPQKsleefqdVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHGDMLEMI---LSSEKgrlpehiTKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARI 576
Cdd:cd07850   82 LVMELMDANLCQVIqmdLDHER-------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLART 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEkSFRRS--VVgTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT--FPFNE---------------DEDIHDQIQ 637
Cdd:cd07850  152 AGT-SFMMTpyVV-TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTvlFPGTDhidqwnkiieqlgtpSDEFMSRLQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 638 NAAFMY-------PPNPWKEI-----------------SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLqdyQTWLDLRE 693
Cdd:cd07850  230 PTVRNYvenrpkyAGYSFEELfpdvlfppdseehnklkASQARDLLSKMLVIDPEKRISVDDALQHPYI---NVWYDPSE 306
                        330
                 ....*....|....*.
gi 568979055 694 LECRIGERYiTHESDD 709
Cdd:cd07850  307 VEAPPPAPY-DHSIDE 321
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
432-682 7.80e-28

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 113.89  E-value: 7.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLR------FP---------------TKQESQLR---NEVAILQNLHHPGVVN 487
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygFPrrppprgskaaqgeqAKPLAPLErvyQEIAILKKLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 488 LECMFETPER-----VFVVMEKlhGDMLEmiLSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADp 562
Cdd:cd14200   88 LIEVLDDPAEdnlymVFDLLRK--GPVME--VPSDKP-FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDG- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 563 fpQVKLCDFGFA-RIIGEKSFRRSVVGTPAYLAPEVLRNKGYN---RSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQI 636
Cdd:cd14200  162 --HVKIADFGVSnQFEGNDALLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPFIDEFilALHNKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 637 QNAAFMYPPNPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14200  240 KNKPVEFPEEP--EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
430-683 9.13e-28

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 114.05  E-value: 9.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQesQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06656   25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSS---EKGRLPEhitkfLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRS 585
Cdd:cd06656  103 LTDVVTEtcmDEGQIAA-----VCRECLQALDFLHSNQVIHRDIKSDNILLGMDG---SVKLTDFGFcAQITPEQSKRST 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPP--NPwKEISHEAIDLINNLL 663
Cdd:cd06656  175 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPElqNP-ERLSAVFRDFLNRCL 253
                        250       260
                 ....*....|....*....|
gi 568979055 664 QVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06656  254 EMDVDRRGSAKELLQHPFLK 273
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
430-682 9.37e-28

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 113.30  E-value: 9.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKhRKTGRDVAIKII-----DKLRfPTKQESQLRNEVAILQNLHHPGVVNL--ECMFETPERVFvvM 502
Cdd:cd06631    7 NVLGKGAYGTVYCGL-TSTGQLIAVKQVeldtsDKEK-AEKEYEKLQEEVDLLKTLKHVNIVGYlgTCLEDNVVSIF--M 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAsadPFPQVKLCDFGFARII----- 577
Cdd:cd06631   83 EFVPGGSIASILA-RFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLM---PNGVIKLIDFGCAKRLcinls 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 --GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhdqiqnAAFMY--------PPNP 647
Cdd:cd06631  159 sgSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPM------AAIFAigsgrkpvPRLP 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 648 WKeISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06631  233 DK-FSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
430-681 9.46e-28

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 113.68  E-value: 9.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd07839    6 EKIGEGTYGTVFKAKNRETHEIVALK---RVRLDDDDEgvpsSALR-EICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG--EKSFR 583
Cdd:cd07839   82 DQD-LKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNG---ELKLADFGLARAFGipVRCYS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVgTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQ-----------------------NA 639
Cdd:cd07839  158 AEVV-TLWYRPPDVLFGaKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKrifrllgtpteeswpgvsklpdyKP 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 640 AFMYPPNP-WKEI----SHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07839  237 YPMYPATTsLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
432-681 9.54e-28

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 113.57  E-value: 9.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIiDKLrfpTKQESQLR---------NEVAILQNLHHPGVVNLECMFETPERVFV-V 501
Cdd:cd13990    8 LGKGGFSEVYKAFDLVEQRYVACKI-HQL---NKDWSEEKkqnyikhalREYEIHKSLDHPRIVKLYDVFEIDTDSFCtV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHL--HFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGE 579
Cdd:cd13990   84 LEYCDGNDLDFYLK-QHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIMDD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFR-------RSVVGTPAYLAPEV-LRNKGYNR---SLDMWSVGVIIYVSLSGTFPFNED---EDIHDQ--IQNA-AFM 642
Cdd:cd13990  163 ESYNsdgmeltSQGAGTYWYLPPECfVVGKTPPKissKVDVWSVGVIFYQMLYGRKPFGHNqsqEAILEEntILKAtEVE 242
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568979055 643 YPPNPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd13990  243 FPSKP--VVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
431-684 9.85e-28

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 113.30  E-value: 9.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHH----PGVVNLECMFETPERVFVVMEKL 505
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgETLALNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRS 585
Cdd:cd05606   81 NGGDLHYHLS-QHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLACDFSKKKPHAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 vVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYPPNPwKEISHEAIDLINNL 662
Cdd:cd05606  157 -VGTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFrqHKTKDKHEIDRMTLTMNVELP-DSFSPELKSLLEGL 234
                        250       260
                 ....*....|....*....|....*..
gi 568979055 663 LQVKMRKRY-----SVDKTLSHPWLQD 684
Cdd:cd05606  235 LQRDVSKRLgclgrGATEVKEHPFFKG 261
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
413-694 9.89e-28

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 113.97  E-value: 9.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 413 QIQENVDISTVYQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKIIDklrfpTKQESQLRN---EVAILQNLHHPGVVNLE 489
Cdd:cd06644    3 HVRRDLDPNEVWEIIGE--LGDGAFGKVYKAKNKETGALAAAKVIE-----TKSEEELEDymvEIEILATCNHPYIVKLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 490 CMFETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLC 569
Cdd:cd06644   76 GAFYWDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDG---DIKLA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 570 DFGF-ARIIGEKSFRRSVVGTPAYLAPEV-----LRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMY 643
Cdd:cd06644  153 DFGVsAKNVKTLQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEP 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 644 P----PNPWkeiSHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLREL 694
Cdd:cd06644  233 PtlsqPSKW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPLREL 284
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
427-682 1.01e-27

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 112.61  E-value: 1.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 427 FPDEVlGSGQFGIVYGGKHRKTGRDVAIKIIdklrfPTKQESQLR--NEVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd14111    7 FLDEK-ARGRFGVIRRCRENATGKNFPAKIV-----PYQAEEKQGvlQEYEILKSLHHERIMALHEAYITPRYLVLIAEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDmlEMILS-SEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAsadPFPQVKLCDFGFARIIGEKSFR 583
Cdd:cd14111   81 CSGK--ELLHSlIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT---NLNAIKIVDFGSAQSFNPLSLR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 R--SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDED---IHDQIQNAAF----MYPpnpwkEISHE 654
Cdd:cd14111  156 QlgRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPF-EDQDpqeTEAKILVAKFdafkLYP-----NVSQS 229
                        250       260
                 ....*....|....*....|....*...
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14111  230 ASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
432-685 1.03e-27

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 113.69  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdklrfPTKQESQLRN----EVAILQNLHHPGVVNL--ECMFETPErVFVVMEKL 505
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVI-----HIDAKSSVRKqilrELQILHECHSPYIVSFygAFLNENNN-IIICMEYM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLASADpfpQVKLCDFGFAriiGE--KSF 582
Cdd:cd06620   87 DCGSLDKILK-KKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG---QIKLCDFGVS---GEliNSI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED----------IHDQIQNAAFMYPPNPWKEI- 651
Cdd:cd06620  160 ADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDdddgyngpmgILDLLQRIVNEPPPRLPKDRi 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 652 -SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd06620  240 fPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQA 274
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
432-657 1.32e-27

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 112.75  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGkHRKTGRDVAIKIIDKLRFPTKqESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14066    1 IGSGGFGTVYKG-VLENGTVVAVKRLNEMNCAAS-KKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGR--LPEHITKFLITQILVALRHLH---FKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKSFRRS- 585
Cdd:cd14066   79 DRLHCHKGSppLPWPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDED---FEPKLTDFGLARLIPPSESVSKt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 --VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE------DIHDQIQNAafmyppnpWKEISHEAID 657
Cdd:cd14066  156 saVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRenasrkDLVEWVESK--------GKEELEDILD 227
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
429-617 1.39e-27

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 112.20  E-value: 1.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  429 DEVLGSGQFGIVYGGK----HRKTGRDVAIKIIDKlrFPTKQESQ-LRNEVAILQNLHHPGVVNLE--CMFETPerVFVV 501
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLKE--GADEEEREdFLEEASIMKKLDHPNIVKLLgvCTQGEP--LYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  502 MEKL-HGDMLEmILSSEKGRLP-EHITKFlITQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDFGFARIIGE 579
Cdd:pfam07714  80 TEYMpGGDLLD-FLRKHKRKLTlKDLLSM-ALQIAKGMEYLESKNFVHRDLAARNCLVSE---NLVVKISDFGLSRDIYD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568979055  580 KSFRRSVVGTP---AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:pfam07714 155 DDYYRKRGGGKlpiKWMAPESLKDGKFTSKSDVWSFGVLLW 195
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
430-682 1.41e-27

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 113.24  E-value: 1.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdklRFptKQE-----SQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd07844    6 DKLGEGSYATVYKGRSKLTGQLVALKEI---RL--EHEegapfTAIR-EASLLKDLKHANIVTLHDIIHTKKTLTLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSF 582
Cdd:cd07844   80 LDTD-LKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERG---ELKLADFGLARAksVPSKTY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVgTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQ-------------------NAAF- 641
Cdd:cd07844  156 SNEVV-TLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQLHkifrvlgtpteetwpgvssNPEFk 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 642 -----MYPPNP----WKEISH--EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07844  235 pysfpFYPPRPlinhAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
430-682 1.72e-27

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 112.79  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDklrFPTKQESQLRNEVAILQNL-HHPGVVNLECMF--ETP----ERVFVVM 502
Cdd:cd06636   22 EVVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKLEINMLKKYsHHRNIATYYGAFikKSPpghdDQLWLVM 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKL-HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA----RII 577
Cdd:cd06636   99 EFCgAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSaqldRTV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEksfRRSVVGTPAYLAPEVLR-----NKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIHDqiQNAAFMYPPNP----- 647
Cdd:cd06636  176 GR---RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLC---DMHP--MRALFLIPRNPppklk 247
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 648 WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06636  248 SKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
430-679 1.77e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 112.44  E-value: 1.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRF------PTKQESQLRNEVAILQNLHHPGVVNLE-CMFETPERVF-VV 501
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVK---QVQFdpespeTSKEVNALECEIQLLKNLLHERIVQYYgCLRDPQERTLsIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR----II 577
Cdd:cd06652   85 MEYMPGGSIKDQLKS-YGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVG---NVKLGDFGASKrlqtIC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAfmYPPNPW--KEISHEA 655
Cdd:cd06652  161 LSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIAT--QPTNPQlpAHVSDHC 238
                        250       260
                 ....*....|....*....|....
gi 568979055 656 IDLINNLLqVKMRKRYSVDKTLSH 679
Cdd:cd06652  239 RDFLKRIF-VEAKLRPSADELLRH 261
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
432-626 3.09e-27

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 112.32  E-value: 3.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNL-----ECMFETPERVFVVMEKLH 506
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSC-RLELSVKNKDRWCHEIQIMKKLNHPNVVKAcdvpeEMNFLVNDVPLLAMEYCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKG--RLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRR 584
Cdd:cd14039   80 GGDLRKLLNKPENccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQGSLCT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14039  160 SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
430-683 3.60e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 112.13  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQesQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06654   26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSS---EKGRLPEhitkfLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRS 585
Cdd:cd06654  104 LTDVVTEtcmDEGQIAA-----VCRECLQALEFLHSNQVIHRDIKSDNILLGMDG---SVKLTDFGFcAQITPEQSKRST 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnededIHDQIQNAAFMYPPNPWKEISH----EAI--DLI 659
Cdd:cd06654  176 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY-----LNENPLRALYLIATNGTPELQNpeklSAIfrDFL 250
                        250       260
                 ....*....|....*....|....
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06654  251 NRCLEMDVEKRGSAKELLQHQFLK 274
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
428-682 4.28e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 111.98  E-value: 4.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLH---HPGVVNLE--CMFETPER- 497
Cdd:cd07863    4 PVAEIGVGAYGTVYKARDPHSGHFVALK---SVRVQTNEDglplSTVR-EVALLKRLEafdHPNIVRLMdvCATSRTDRe 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 --VFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR 575
Cdd:cd07863   80 tkVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGG---QVKLADFGLAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGViIYVSLSGTFPF---NEDEDIHDQIQNAAFMYPPNPW---- 648
Cdd:cd07863  157 IYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGC-IFAEMFRRKPLfcgNSEADQLGKIFDLIGLPPEDDWprdv 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 649 -------------------KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07863  236 tlprgafsprgprpvqsvvPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
430-636 5.56e-27

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 111.36  E-value: 5.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidklRFPTKQESQLRN-----EVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd07846    7 GLVGEGSYGMVMKCRHKETGQIVAIK-----KFLESEDDKMVKkiamrEIKMLKQLRHENLVNLIEVFRRKKRWYLVFEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAsadPFPQVKLCDFGFARII-GEKSFR 583
Cdd:cd07846   82 VDHTVLDDLEKYPNG-LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLaAPGEVY 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 584 RSVVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI 636
Cdd:cd07846  158 TDYVATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDI-DQL 210
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
432-626 5.78e-27

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 112.20  E-value: 5.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNL---ECMFETPERVfVVMEKLHGD 508
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMR-EFEVLKKLNHKNIVKLfaiEEELTTRHKV-LVMELCPCG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILS--SEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVL-LASADPFPQVKLCDFGFARIIGEKSFRRS 585
Cdd:cd13988   79 SLYTVLEepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQSVYKLTDFGAARELEDDEQFVS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 586 VVGTPAYLAPE-----VLR---NKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd13988  159 LYGTEEYLHPDmyeraVLRkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
419-690 5.97e-27

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 112.56  E-value: 5.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQ-IFPdevLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRnEVAILQNLHHPGVVNL-ECMFETPE 496
Cdd:cd07854    2 DLGSRYMdLRP---LGCGSNGLVFSAVDSDCDKRVAVKKI-VLTDPQSVKHALR-EIKIIRRLDHDNIVKVyEVLGPSGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 R-------------VFVVMEKLHGDMLEMIlssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPF 563
Cdd:cd07854   77 DltedvgsltelnsVYIVQEYMETDLANVL---EQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 564 pqVKLCDFGFARII----GEKSFRRSVVGTPAYLAPE-VLRNKGYNRSLDMWSVGVIIYVSLSG---------------- 622
Cdd:cd07854  154 --LKIGDFGLARIVdphySHKGYLSEGLVTKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGkplfagaheleqmqli 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 623 --TFPFNEDEDiHDQIQN--AAFM-----YPPNPWK----EISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWL 689
Cdd:cd07854  232 leSVPVVREED-RNELLNviPSFVrndggEPRRPLRdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCYSCPF 310

                 .
gi 568979055 690 D 690
Cdd:cd07854  311 D 311
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1-46 8.45e-27

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 103.95  E-value: 8.45e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTG 46
Cdd:cd20839   27 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLTG 72
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
432-626 9.77e-27

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 110.24  E-value: 9.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLH--FKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIG------EKSFR 583
Cdd:cd13978   81 SLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILL---DNHFHVKISDFGLSKLGMksisanRRRGT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568979055 584 RSVVGTPAYLAPEVLR--NKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd13978  158 ENLGGTPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLTRKEPF 202
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
430-697 1.24e-26

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 111.43  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFPTKQESQLRNEVAILQNlHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKdviLQDDDVDCTMTEKRILALAA-KHPFLTALHSCFQTKDRLFFVMEYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 G-DMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRR 584
Cdd:cd05591   80 GgDLMFQIQRARK--FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEgILNGKTTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDeDIHDQIQNAAFMYPpnPWkeISHEAIDLINN 661
Cdd:cd05591  155 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeadNED-DLFESILHDDVLYP--VW--LSKEAVSILKA 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568979055 662 LLQVKMRKRYSV-------DKTLSHPWLQDyqtwLDLRELECR 697
Cdd:cd05591  230 FMTKNPAKRLGCvasqggeDAIRQHPFFRE----IDWEALEQR 268
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
430-679 1.25e-26

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 109.72  E-value: 1.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPT-KQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKpHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA-RIIGEKSFRRSVV 587
Cdd:cd14188   87 SMAHILKARK-VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEN---MELKVGDFGLAaRLEPLEHRRRTIC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQV 665
Cdd:cd14188  163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTnlKETYRCIREARYSLPSS----LLAPAKHLIASMLSK 238
                        250
                 ....*....|....
gi 568979055 666 KMRKRYSVDKTLSH 679
Cdd:cd14188  239 NPEDRPSLDEIIRH 252
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
432-684 1.57e-26

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 110.20  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMF--ETPERVFVVMEKLHGDM 509
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILR-ELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYCEGGS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMI---LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAriiGE--KSFRR 584
Cdd:cd06621   88 LDSIykkVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKG---QVKLCDFGVS---GElvNSLAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnededIHDQIQNAA-------FMYPPNP---------- 647
Cdd:cd06621  162 TFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF-----PPEGEPPLGpiellsyIVNMPNPelkdepengi 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568979055 648 -WkeiSHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd06621  237 kW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKA 271
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
431-670 1.73e-26

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 110.86  E-value: 1.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFPTKQESQLRNEVAILQNlHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05616    7 VLGKGSFGKVMLAERKGTDELYAVKILKKdvvIQDDDVECTMVEKRVLALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 -DMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRS 585
Cdd:cd05616   86 gDLMYHI--QQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML---DSEGHIKIADFGMCKEnIWDGVTTKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN-EDED-IHDQIQNAAFMYPpnpwKEISHEAIDLINNLL 663
Cdd:cd05616  161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEgEDEDeLFQSIMEHNVAYP----KSMSKEAVAICKGLM 236

                 ....*..
gi 568979055 664 QVKMRKR 670
Cdd:cd05616  237 TKHPGKR 243
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
430-684 1.86e-26

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 110.55  E-value: 1.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd07869   11 EKLGEGSYATVYKGKSKVNGKLVALKVI-RLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSFRRSVV 587
Cdd:cd07869   90 CQYMDKHPGGLHPENVKLFLF-QLLRGLSYIHQRYILHRDLKPQNLLISDTG---ELKLADFGLARAksVPSHTYSNEVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 gTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMY-PPN------------------- 646
Cdd:cd07869  166 -TLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLgTPNedtwpgvhslphfkperft 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 647 ---------PWKEISH--EAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd07869  245 lyspknlrqAWNKLSYvnHAEDLASKLLQCFPKNRLSAQAALSHEYFSD 293
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
432-683 1.92e-26

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 110.13  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQEsQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMD-LRKQQRRE-LLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVVGTP 590
Cdd:cd06658  108 DIVTHT--RMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDG---RIKLSDFGFcAQVSKEVPKRKSLVGTP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP-FNED-----EDIHDQIqnaafmyPPNpWKEiSHEAIDLINNLLQ 664
Cdd:cd06658  183 YWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPyFNEPplqamRRIRDNL-------PPR-VKD-SHKVSSVLRGFLD 253
                        250       260
                 ....*....|....*....|...
gi 568979055 665 VKM----RKRYSVDKTLSHPWLQ 683
Cdd:cd06658  254 LMLvrepSQRATAQELLQHPFLK 276
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
432-694 1.98e-26

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 109.73  E-value: 1.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDklrfpTKQESQLRN---EVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVID-----TKSEEELEDymvEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVV 587
Cdd:cd06643   88 AVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG---DIKLADFGVsAKNTRTLQRRDSFI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVL-----RNKGYNRSLDMWSVGVIIyVSLSGTFPFNEDEDIHDQIQNAAFMYP-----PNPWkeiSHEAID 657
Cdd:cd06643  165 GTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTL-IEMAQIEPPHHELNPMRVLLKIAKSEPptlaqPSRW---SPEFKD 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLREL 694
Cdd:cd06643  241 FLRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLREL 277
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
432-686 2.03e-26

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 110.74  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIK-IIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETP-ERVFVVMEkLHGDM 509
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKkIMKPFSTPVLAKRTYR-ELKLLKHLRHENIISLSDIFISPlEDIYFVTE-LLGTD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL-ASADpfpqVKLCDFGFARIigEKSFRRSVVG 588
Cdd:cd07856   96 LHRLLTSR--PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVnENCD----LKICDFGLARI--QDPQMTGYVS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEV-LRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIH--------------DQIQNAA------FMYP--- 644
Cdd:cd07856  168 TRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNqfsiitellgtppdDVINTICsentlrFVQSlpk 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 645 --PNPWKE----ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQ 686
Cdd:cd07856  248 reRVPFSEkfknADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYH 295
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
421-687 2.03e-26

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 110.16  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIFPDEV-----LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETP 495
Cdd:cd06618    7 GKKYKADLNDLenlgeIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 496 ERVFVVMEKLhGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLasaDPFPQVKLCDFGFA 574
Cdd:cd06618   87 SDVFICMELM-STCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILL---DESGNVKLCDFGIS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 -RIIGEKSFRRSVvGTPAYLAPEVL---RNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDEDIHDQIQNAAfmyPP-- 645
Cdd:cd06618  163 gRLVDSKAKTRSA-GCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYrncKTEFEVLTKILNEE---PPsl 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568979055 646 NPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQT 687
Cdd:cd06618  239 PPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYET 280
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
427-680 2.08e-26

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 109.28  E-value: 2.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 427 FPDEVLGSGQFG-IVYGGKHRktGRDVAIK--IIDKLRFPTKqesqlrnEVAILQNL-HHPGVVNLECMFETPERVFVVM 502
Cdd:cd13982    4 FSPKVLGYGSEGtIVFRGTFD--GRPVAVKrlLPEFFDFADR-------EVQLLRESdEHPNVIRYFCTEKDRQFLYIAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKGRLPEHIT---KFLITQILVALRHLHFKNIVHCDLKPENVLLA--SADPFPQVKLCDFGFAR-- 575
Cdd:cd13982   75 ELCAASLQDLVESPRESKLFLRPGlepVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpNAHGNVRAMISDFGLCKkl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFRR--SVVGTPAYLAPEVLR---NKGYNRSLDMWSVGVIIYVSLS-GTFPFNE----DEDIhdqIQNAAFMYPP 645
Cdd:cd13982  155 DVGRSSFSRrsGVAGTSGWIAPEMLSgstKRRQTRAVDIFSLGCVFYYVLSgGSHPFGDklerEANI---LKGKYSLDKL 231
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 646 NPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd13982  232 LSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
418-678 2.47e-26

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 108.87  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 418 VDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDK-LRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPE 496
Cdd:cd14187    1 VDPRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKsLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARI 576
Cdd:cd14187   81 FVYVVLELCRRRSL-LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDD---MEVKIGDFGLATK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 I---GEKsfRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYPpnpwKEI 651
Cdd:cd14187  157 VeydGER--KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSclKETYLRIKKNEYSIP----KHI 230
                        250       260
                 ....*....|....*....|....*..
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLS 678
Cdd:cd14187  231 NPVAASLIQKMLQTDPTARPTINELLN 257
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
431-651 2.52e-26

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 108.50  E-value: 2.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRktGRDVAIKIIDK---LRFptkqesqLRNEVAILQNLHHPGVVNLECMFETPErvFVVMEKLHG 507
Cdd:cd14068    1 LLGDGGFGSVYRAVYR--GEDVAVKIFNKhtsFRL-------LRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQV--KLCDFGFARIIGEKSFRRS 585
Cdd:cd14068   70 GSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQYCCRMGIKTS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979055 586 vVGTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSG--------TFPFNEDE-DIHDQIQNAAFMYPPNPWKEI 651
Cdd:cd14068  150 -EGTPGFRAPEVARgNVIYNQQADVYSFGLLLYDILTCgeriveglKFPNEFDElAIQGKLPDPVKEYGCAPWPGV 224
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
431-670 3.28e-26

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 109.31  E-value: 3.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd05631    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGgD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd05631   87 LKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL---DDRGHIRISDLGLAVQIPEGETVRGRVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED------EDIHDQIQNAAFMYPpnpwKEISHEAIDLINNL 662
Cdd:cd05631  164 TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkervkrEEVDRRVKEDQEEYS----EKFSEDAKSICRML 239

                 ....*...
gi 568979055 663 LQVKMRKR 670
Cdd:cd05631  240 LTKNPKER 247
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
430-683 5.38e-26

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 108.25  E-value: 5.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRF------PTKQESQLRNEVAILQNLHHPGVVNLE-CMFETPERVFVV- 501
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAK---QVQFdpespeTSKEVSALECEIQLLKNLQHERIVQYYgCLRDRAEKTLTIf 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR----II 577
Cdd:cd06651   90 MEYMPGGSVKDQLKA-YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG---NVKLGDFGASKrlqtIC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAfmYPPNPW--KEISHEA 655
Cdd:cd06651  166 MSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTNPQlpSHISEHA 243
                        250       260
                 ....*....|....*....|....*...
gi 568979055 656 IDLINNLLqVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06651  244 RDFLGCIF-VEARHRPSAEELLRHPFAQ 270
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
432-679 5.63e-26

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 114.45  E-value: 5.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMF--ETPERVFVVMEKLH-GD 508
Cdd:PTZ00266   21 IGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKLYILMEFCDaGD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  509 MLEMILSSEK--GRLPEHITKFLITQILVALRHLHF-------KNIVHCDLKPENVLLASA--------------DPFPQ 565
Cdd:PTZ00266  101 LSRNIQKCYKmfGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGirhigkitaqannlNGRPI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055  566 VKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVL--RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQIQNAAFMY 643
Cdd:PTZ00266  181 AKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANNF-SQLISELKRG 259
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568979055  644 PPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSH 679
Cdd:PTZ00266  260 PDLPIKGKSKELNILIKNLLNLSAKERPSALQCLGY 295
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
432-682 6.20e-26

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 108.56  E-value: 6.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDmLE 511
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDSD-LK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSFRRSVVgT 589
Cdd:cd07871   91 QYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKG---ELKLADFGLARAksVPTKTYSNEVV-T 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSG--TFPFNE-DEDIH--------------------DQIQNAAF-MYP 644
Cdd:cd07871  167 LWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGrpMFPGSTvKEELHlifrllgtpteetwpgvtsnEEFRSYLFpQYR 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568979055 645 PNPWK----EISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07871  247 AQPLInhapRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
432-626 6.74e-26

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 108.51  E-value: 6.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidklrfPTKQESQLRN------EVAILQNLHHPGVVNLEcmfETPERvfvvMEKL 505
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIK-------QCRQELSPKNrerwclEIQIMKRLNHPNVVAAR---DVPEG----LQKL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSS--EKGRLPEHITKF-------------LITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCD 570
Cdd:cd14038   68 APNDLPLLAMEycQGGDLRKYLNQFenccglregailtLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIID 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568979055 571 FGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14038  148 LGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
421-682 7.68e-26

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 108.17  E-value: 7.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 421 STVYQIFPD--------EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfptKQESQLRNEVAILQNLH-HPGVVNLECM 491
Cdd:cd06638    7 TIIFDSFPDpsdtweiiETIGKGTYGKVFKVLNKKNGSKAAVKILDPIH---DIDEEIEAEYNILKALSdHPNVVKFYGM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 492 F-----ETPERVFVVMEKLHG----DMLEMILssEKG-RLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAD 561
Cdd:cd06638   84 YykkdvKNGDQLWLVLELCNGgsvtDLVKGFL--KRGeRMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 562 pfpQVKLCDFGF-ARIIGEKSFRRSVVGTPAYLAPEVLR-----NKGYNRSLDMWSVGVIIYVSLSGTFPFnedEDIHDq 635
Cdd:cd06638  162 ---GVKLVDFGVsAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPL---ADLHP- 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 636 iQNAAFMYPPNPWKEI------SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06638  235 -MRALFKIPRNPPPTLhqpelwSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
432-680 9.76e-26

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 106.70  E-value: 9.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFP---TKQESQLRNEVAILQNL-HHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVK---KSKKPfrgPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELCEN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILS--SEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpqvKLCDFGFARIIgEKSFRRS 585
Cdd:cd13997   85 GSLQDALEelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTC---KIGDFGLATRL-ETSGDVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 vVGTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIQNAAFMYPPNPwkEISHEAIDLINNLLQ 664
Cdd:cd13997  161 -EGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATG-EPLPRNGQQWQQLRQGKLPLPPGL--VLSQELTRLLKVMLD 236
                        250
                 ....*....|....*.
gi 568979055 665 VKMRKRYSVDKTLSHP 680
Cdd:cd13997  237 PDPTRRPTADQLLAHD 252
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
432-687 1.17e-25

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 107.84  E-value: 1.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEV-AILQNLHHPGVVN-----------LECMfetpERVF 499
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKRI-RSTVDEKEQKRLLMDLdVVMRSSDCPYIVKfygalfregdcWICM----ELMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHgdmlEMILSSEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLasaDPFPQVKLCDFGfarIIG 578
Cdd:cd06616   89 ISLDKFY----KYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILL---DRNGNIKLCDFG---ISG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 --EKSFRRSV-VGTPAYLAPEVL----RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPP----NP 647
Cdd:cd06616  159 qlVDSIAKTRdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGDPPilsnSE 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568979055 648 WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQT 687
Cdd:cd06616  239 EREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEE 278
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
1-46 1.57e-25

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 100.50  E-value: 1.57e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTG 46
Cdd:cd20841   30 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLPG 75
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
430-684 1.70e-25

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 107.50  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDklrFPTKQESQLRNEVAILQNL-HHPGVVNLECMF--ETP----ERVFVVM 502
Cdd:cd06637   12 ELVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTGDEEEEIKQEINMLKKYsHHRNIATYYGAFikKNPpgmdDQLWLVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKL-HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA----RII 577
Cdd:cd06637   89 EFCgAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSaqldRTV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEksfRRSVVGTPAYLAPEVLR-----NKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIHDqiQNAAFMYPPNPW---- 648
Cdd:cd06637  166 GR---RNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLC---DMHP--MRALFLIPRNPAprlk 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568979055 649 -KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd06637  238 sKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRD 274
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
432-616 1.73e-25

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 106.04  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIidkLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKE---LKRFDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARII-------GEKSFRR 584
Cdd:cd14065   77 ELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMpdektkkPDRKKRL 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14065  157 TVVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
424-682 1.95e-25

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 106.31  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKII-----DKLRFPTKQES---QLRNEVAILQNLHHPGVVnlECM-FET 494
Cdd:cd06629    1 FKWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVelpktSSDRADSRQKTvvdALKSEIDTLKDLDHPNIV--QYLgFEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PERVF-VVMEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGF 573
Cdd:cd06629   79 TEDYFsIFLEYVPGGSIGSCLR-KYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILV---DLEGICKISDFGI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 AR----IIGEKSfRRSVVGTPAYLAPEVLRN--KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhdqiqnaAFMY---- 643
Cdd:cd06629  155 SKksddIYGNNG-ATSMQGSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAI-------AAMFklgn 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568979055 644 ----PPNPWK-EISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06629  227 krsaPPVPEDvNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
431-673 1.99e-25

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 106.65  E-value: 1.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdkLRFPTKQESQLRNEVAILQNL-HHPGVVNL---ECMFETPERVFV-VMEKL 505
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALKRM--YFNDEEQLRVAIKEIEIMKRLcGHPNIVQYydsAILSSEGRKEVLlLMEYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKN--IVHCDLKPENVLLASADPFpqvKLCDFGFARIIGEKSFR 583
Cdd:cd13985   85 PGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRF---KLCDFGSATTEHYPLER 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVG----------TPAYLAPEVL---RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhdQIQNAAFMYPPNPwkE 650
Cdd:cd13985  162 AEEVNiieeeiqkntTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKL--AIVAGKYSIPEQP--R 237
                        250       260
                 ....*....|....*....|...
gi 568979055 651 ISHEAIDLINNLLQVKMRKRYSV 673
Cdd:cd13985  238 YSPELHDLIRHMLTPDPAERPDI 260
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
431-670 2.04e-25

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 108.16  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK---LRFPTKQESQLRNEVAILQNlHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05615   17 VLGKGSFGKVMLAERKGSDELYAIKILKKdvvIQDDDVECTMVEKRVLALQD-KPPFLTQLHSCFQTVDRLYFVMEYVNG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 -DMLEMILSSEKGRLPEHItkFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRS 585
Cdd:cd05615   96 gDLMYHIQQVGKFKEPQAV--FYAAEISVGLFFLHKKGIIYRDLKLDNVML---DSEGHIKIADFGMCKEhMVEGVTTRT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN-EDED-IHDQIQNAAFMYPpnpwKEISHEAIDLINNLL 663
Cdd:cd05615  171 FCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDgEDEDeLFQSIMEHNVSYP----KSLSKEAVSICKGLM 246

                 ....*..
gi 568979055 664 QVKMRKR 670
Cdd:cd05615  247 TKHPAKR 253
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-693 2.14e-25

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 108.08  E-value: 2.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVY-----GGkhRKTGRDVAIKIIDKLRFPTKQESQ--LRNEVAILQNLHH-PGVVNLECMFETPERVFVV 501
Cdd:cd05614    6 KVLGTGAYGKVFlvrkvSG--HDANKLYAMKVLRKAALVQKAKTVehTRTERNVLEHVRQsPFLVTLHYAFQTDAKLHLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR--IIGE 579
Cdd:cd05614   84 LDYVSGGELFTHLY-QRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEG---HVVLTDFGLSKefLTEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRSVVGTPAYLAPEVLRNK-GYNRSLDMWSVGVIIYVSLSGTFPF------NEDEDIHDQIQNaafMYPPNPwKEIS 652
Cdd:cd05614  160 KERTYSFCGTIEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFtlegekNTQSEVSRRILK---CDPPFP-SFIG 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 653 HEAIDLINNLLQVKMRKR-----YSVDKTLSHPWLQDYQtWLDLRE 693
Cdd:cd05614  236 PVARDLLQKLLCKDPKKRlgagpQGAQEIKEHPFFKGLD-WEALAL 280
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
431-682 2.33e-25

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 106.34  E-value: 2.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfPTKQESQ---LRNEVAILQNLHHPGVVN-LECMFEtpERVF-VVMEKL 505
Cdd:cd06624   15 VLGKGTFGVVYAARDLSTQVRIAIKEI-----PERDSREvqpLHEEIALHSRLSHKNIVQyLGSVSE--DGFFkIFMEQV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRLP--EHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfPQVKLCDFGFA-RIIGEKSF 582
Cdd:cd06624   88 PGGSLSALLRSKWGPLKdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYS--GVVKISDFGTSkRLAGINPC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRN--KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAF--MYPPNPwKEISHEAIDL 658
Cdd:cd06624  166 TETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMfkIHPEIP-ESLSEEAKSF 244
                        250       260
                 ....*....|....*....|....
gi 568979055 659 INNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06624  245 ILRCFEPDPDKRATASDLLQDPFL 268
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
431-634 2.41e-25

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 107.51  E-value: 2.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE---SQLRNEVaILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd05588    2 VIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDidwVQTEKHV-FETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSV 586
Cdd:cd05588   81 GDL-MFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLL---DSEGHIKLTDYGMCKEgLRPGDTTSTF 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-------NEDEDIHD 634
Cdd:cd05588  157 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdNPDQNTED 211
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
432-660 2.43e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 106.27  E-value: 2.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF-PTKQESQLRNEVAILQNLHHPGVVN-LECMFETPERVFVVMEKLHGDM 509
Cdd:cd08228   10 IGRGQFSEVYRATCLLDRKPVALKKVQIFEMmDAKARQDCVKEIDLLKQLNHPNVIKyLDSFIEDNELNIVLELADAGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGR--LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFR-RSV 586
Cdd:cd08228   90 SQMIKYFKKQKrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATG---VVKLGDLGLGRFFSSKTTAaHSL 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE----DIHDQIQNAAfmYPPNPWKEISHEAIDLIN 660
Cdd:cd08228  167 VGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmnlfSLCQKIEQCD--YPPLPTEHYSEKLRELVS 242
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
430-683 2.44e-25

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 106.62  E-value: 2.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLrfpTKQESQLRNEVAILQNL-HHPGVVNLECMFETPER-----VFVVME 503
Cdd:cd06639   28 ETIGKGTYGKVYKVTNKKDGSLAAVKILDPI---SDVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQyvggqLWLVLE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHG----DMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE 579
Cdd:cd06639  105 LCNGgsvtELVKGLLKCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG---GVKLVDFGVSAQLTS 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRSV-VGTPAYLAPEVLR-----NKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIHDqiQNAAFMYPPNP------ 647
Cdd:cd06639  181 ARLRRNTsVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLF---DMHP--VKALFKIPRNPpptlln 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568979055 648 ---W-KEISHeaidLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06639  256 pekWcRGFSH----FISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
433-681 3.16e-25

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 106.99  E-value: 3.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 433 GSGQFGIVYG--GKHRKTGRDVAIKII--DKLRFPTKQESQLRnEVAILQNLHHPGVVNL-ECMFETPER-VFVVMEKLH 506
Cdd:cd07842    9 GRGTYGRVYKakRKNGKDGKEYAIKKFkgDKEQYTGISQSACR-EIALLRELKHENVVSLvEVFLEHADKsVYLLFDYAE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMI---LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFP-QVKLCDFGFARIIGE--K 580
Cdd:cd07842   88 HDLWQIIkfhRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERgVVKIGDLGLARLFNAplK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRS--VVGTPAYLAPEVLRN-KGYNRSLDMWSVGVII--YVSLSGTF-----------PFNED--------------- 629
Cdd:cd07842  168 PLADLdpVVVTIWYRAPELLLGaRHYTKAIDIWAIGCIFaeLLTLEPIFkgreakikksnPFQRDqlerifevlgtptek 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 630 --EDI-----HDQIQNAAFM--YPPN---PW----KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07842  248 dwPDIkkmpeYDTLKSDTKAstYPNSllaKWmhkhKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
430-695 4.69e-25

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 108.56  E-value: 4.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05623   78 KVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETAcFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA-RIIGEKSFRRSV- 586
Cdd:cd05623  158 DLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM---DMNGHIRLADFGSClKLMEDGTVQSSVa 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLR----NKG-YNRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQN--AAFMYPPNpWKEISHEAID 657
Cdd:cd05623  235 VGTPDYISPEILQamedGKGkYGPECDWWSLGVCMYEMLYGETPFYAESlvETYGKIMNhkERFQFPTQ-VTDVSENAKD 313
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568979055 658 LINNLLQVKMRK--RYSVDKTLSHPWLQDYQtWLDLRELE 695
Cdd:cd05623  314 LIRRLICSREHRlgQNGIEDFKNHPFFVGID-WDNIRNCE 352
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
432-617 4.75e-25

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 106.88  E-value: 4.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKII---DKLRfptkqESQLRnEVAILQNLHHPGVVNL-ECM-----FETPERVFVVM 502
Cdd:cd14134   20 LGEGTFGKVLECWDRKRKRYVAVKIIrnvEKYR-----EAAKI-EIDVLETLAEKDPNGKsHCVqlrdwFDYRGHMCIVF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKGRLP-EHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASAD----PFP------------Q 565
Cdd:cd14134   94 ELLGPSLYDFLKKNNYGPFPlEHVQHIAK-QLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvYNPkkkrqirvpkstD 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 566 VKLCDFGFAriIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd14134  173 IKLIDFGSA--TFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILV 222
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
432-683 5.25e-25

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 105.86  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDmLE 511
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALKEI-RLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKD-LK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSFRRSVVgT 589
Cdd:cd07873   88 QYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERG---ELKLADFGLARAksIPTKTYSNEVV-T 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 590 PAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGT--FPFNE-DEDIH---------------DQIQNAAFM---YP--- 644
Cdd:cd07873  164 LWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRplFPGSTvEEQLHfifrilgtpteetwpGILSNEEFKsynYPkyr 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568979055 645 PNPWKE----ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd07873  244 ADALHNhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFH 286
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
428-684 6.24e-25

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 107.52  E-value: 6.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETP-----ERVFVVM 502
Cdd:cd07853    4 PDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPhidpfEEIYVVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEkgRL-PEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIigeKS 581
Cdd:cd07853   84 ELMQSDLHKIIVSPQ--PLsSDHVKVFLY-QILRGLKYLHSAGILHRDIKPGNLLVNSN---CVLKICDFGLARV---EE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSV-----VGTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIH--DQIQN--------------- 638
Cdd:cd07853  155 PDESKhmtqeVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQqlDLITDllgtpsleamrsace 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 639 --AAFMY--PPNP---------WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd07853  235 gaRAHILrgPHKPpslpvlytlSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
431-626 6.59e-25

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 104.78  E-value: 6.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRktGRDVAIKI--IDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14061    1 VIGVGGFGKVYRGIWR--GEEVAVKAarQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSseKGRLPEHITKFLITQILVALRHLHFKN---IVHCDLKPENVLLASA-----DPFPQVKLCDFGFARIIgEK 580
Cdd:cd14061   79 ALNRVLA--GRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienedLENKTLKITDFGLAREW-HK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14061  156 TTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
424-663 9.90e-25

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 106.02  E-value: 9.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPER-----V 498
Cdd:cd07859    2 YKI--QEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 499 FVVMEKLHGDMLEMILSSEKgRLPEHiTKFLITQILVALRHLHFKNIVHCDLKPENVlLASADpfPQVKLCDFGFARIIG 578
Cdd:cd07859   80 YVVFELMESDLHQVIKANDD-LTPEH-HQFFLYQLLRALKYIHTANVFHRDLKPKNI-LANAD--CKLKICDFGLARVAF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKS----FRRSVVGTPAYLAPEVLRN--KGYNRSLDMWSVGVIIYVSLSGTfpfnededihdqiqnaafmyPPNPWKEIS 652
Cdd:cd07859  155 NDTptaiFWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGK--------------------PLFPGKNVV 214
                        250
                 ....*....|.
gi 568979055 653 HEaIDLINNLL 663
Cdd:cd07859  215 HQ-LDLITDLL 224
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
431-628 1.06e-24

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 104.60  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05607    9 VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSgEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSS--EKGRLPEHITkFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSVV 587
Cdd:cd05607   89 LKYHIYNvgERGIEMERVI-FYSAQITCGILHLHSLKIVYRDMKPENVLL---DDNGNCRLSDLGLAVEVKEGKPITQRA 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE 628
Cdd:cd05607  165 GTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
431-628 1.35e-24

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 103.91  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRktGRDVAIKII--DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14148    1 IIGVGGFGKVYKGLWR--GEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgrLPEHITKFLITQILVALRHLH---FKNIVHCDLKPENVLLASA----DPFPQV-KLCDFGFARIiGEK 580
Cdd:cd14148   79 ALNRALAGKK--VPPHVLVNWAVQIARGMNYLHneaIVPIIHRDLKSSNILILEPiendDLSGKTlKITDFGLARE-WHK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE 628
Cdd:cd14148  156 TTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYRE 203
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
432-626 1.38e-24

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 102.96  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRktGRDVAIKIIDKLRfptkqESQLRNevaiLQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14059    1 LGSGAQGAVFLGKFR--GEEVAVKKVRDEK-----ETDIKH----LRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFlITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSVVGTPA 591
Cdd:cd14059   70 EVLRAGREITPSLLVDW-SKQIASGMNYLHLHKIIHRDLKSPNVLVTYND---VLKISDFGTSKELSEKSTKMSFAGTVA 145
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568979055 592 YLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14059  146 WMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
426-694 1.67e-24

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 105.23  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 426 IFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRN------------EVAILQNLHHPGVVNLECMFE 493
Cdd:PTZ00024  11 IQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 494 TPERVFVVMEKLHGDMLEMIlsSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGF 573
Cdd:PTZ00024  91 EGDFINLVMDIMASDLKKVV--DRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFI---NSKGICKIADFGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 ARIIG-----------EKSFRR----SVVGTPAYLAPEVL--RNKgYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI 636
Cdd:PTZ00024 166 ARRYGyppysdtlskdETMQRReemtSKVVTLWYRAPELLmgAEK-YHFAVDMWSVGCIFAELLTGKPLFPGENEI-DQL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 637 QNAAFMY-PPNP--WKEISH------------------------EAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWL 689
Cdd:PTZ00024 244 GRIFELLgTPNEdnWPQAKKlplyteftprkpkdlktifpnasdDAIDLLQSLLKLNPLERISAKEALKHEYFKSDPLPC 323

                 ....*
gi 568979055 690 DLREL 694
Cdd:PTZ00024 324 DPSQL 328
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
435-680 1.75e-24

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 105.73  E-value: 1.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQ-ESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMI 513
Cdd:cd05610   15 GAFGKVYLGRKKNNSKLYAVKVVKKADMINKNmVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 514 LSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFG--------------------- 572
Cdd:cd05610   95 LHI-YGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEG---HIKLTDFGlskvtlnrelnmmdilttpsm 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 573 ------FARIIGE-------------------KSFRRS--------VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVS 619
Cdd:cd05610  171 akpkndYSRTPGQvlslisslgfntptpyrtpKSVRRGaarvegerILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEF 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 620 LSGTFPFNED--EDIHDQIQNAAFMYPPNPwKEISHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd05610  251 LTGIPPFNDEtpQQVFQNILNRDIPWPEGE-EELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
424-629 1.78e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 108.34  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIidkLR--FPTKQESQLR--NEVailQN---LHHPGVVNlecMFETPE 496
Cdd:NF033483   9 YEI--GERIGRGGMAEVYLAKDTRLDRDVAVKV---LRpdLARDPEFVARfrREA---QSaasLSHPNIVS---VYDVGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 ---RVFVVMEKLHGDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGF 573
Cdd:NF033483  78 dggIPYIVMEYVDGRTLKDYIR-EHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI---TKDGRVKVTDFGI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 ARIIGEKSFRR--SVVGTPAYLAPEVLRNkGY--NRSlDMWSVGVIIYVSLSGTFPFNED 629
Cdd:NF033483 154 ARALSSTTMTQtnSVLGTVHYLSPEQARG-GTvdARS-DIYSLGIVLYEMLTGRPPFDGD 211
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
430-616 1.82e-24

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 105.02  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLrnEVAILQNL---------HHpgVVNLECMFETPERVFV 500
Cdd:cd14212    5 DLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKPAYFRQAML--EIAILTLLntkydpedkHH--IVRLLDHFMHHGHLCI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFAriigek 580
Cdd:cd14212   80 VFELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDS-PEIKLIDFGSA------ 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGT----PAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14212  153 CFENYTLYTyiqsRFYRSPEVLLGLPYSTAIDMWSLGCIA 192
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
419-695 1.89e-24

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 106.09  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVyqifpdEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLR-FPTKQESQLRNEVAILQNLHHPGVVNLECMFETPER 497
Cdd:cd05629    2 DFHTV------KVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEmFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 VFVVMEKL-HGDMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGF--- 573
Cdd:cd05629   76 LYLIMEFLpGGDLMTMLIKYDT--FSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI---DRGGHIKLSDFGLstg 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 -----------------------------------------ARIIGEKSFRR----SVVGTPAYLAPEVLRNKGYNRSLD 608
Cdd:cd05629  151 fhkqhdsayyqkllqgksnknridnrnsvavdsinltmsskDQIATWKKNRRlmaySTVGTPDYIAPEIFLQQGYGQECD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 609 MWSVGVIIYVSLSGTFPFNEdEDIHD---QIQNaafmyppnpWKE---------ISHEAIDLINNLLQVKMRK--RYSVD 674
Cdd:cd05629  231 WWSLGAIMFECLIGWPPFCS-ENSHEtyrKIIN---------WREtlyfpddihLSVEAEDLIRRLITNAENRlgRGGAH 300
                        330       340
                 ....*....|....*....|.
gi 568979055 675 KTLSHPWLQDYQtWLDLRELE 695
Cdd:cd05629  301 EIKSHPFFRGVD-WDTIRQIR 320
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
430-693 2.40e-24

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 105.53  E-value: 2.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HG 507
Cdd:cd05627    8 KVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQvAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLpGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFG------------FAR 575
Cdd:cd05627   88 DMMTLLM--KKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLL---DAKGHVKLSDFGlctglkkahrteFYR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGE--------------------KSFRR----SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED-- 629
Cdd:cd05627  163 NLTHnppsdfsfqnmnskrkaetwKKNRRqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSEtp 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 630 EDIHDQIQN--AAFMYPPNpwKEISHEAIDLINNLLQVKMRK--RYSVDKTLSHPWLQDYQtWLDLRE 693
Cdd:cd05627  243 QETYRKVMNwkETLVFPPE--VPISEKAKDLILRFCTDAENRigSNGVEEIKSHPFFEGVD-WEHIRE 307
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
112-165 3.66e-24

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 95.83  E-value: 3.66e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 112 VPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20795    2 RPHSLFVHSYKSPTFCDFCGEMLFGLVRQGLKCEGCGLNFHKRCAYKIPNNCTG 55
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
430-681 3.91e-24

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 102.41  E-value: 3.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRF-PTKQESQ-----LRNEVAILQNLHHPGVVNLECMFETPE--RVFVV 501
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVK---QVPFdPDSQETSkevnaLECEIQLLKNLRHDRIVQYYGCLRDPEekKLSIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR----II 577
Cdd:cd06653   85 VEYMPGGSVKDQLKA-YGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAG---NVKLGDFGASKriqtIC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 578 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd06653  161 MSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPQLPDGVSDACRD 240
                        250       260
                 ....*....|....*....|....
gi 568979055 658 LINNLLqVKMRKRYSVDKTLSHPW 681
Cdd:cd06653  241 FLRQIF-VEEKRRPTAEFLLRHPF 263
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
432-617 4.66e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 102.12  E-value: 4.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQES---QLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG- 507
Cdd:cd08222    8 LGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDetvDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 ---DMLEMILSSEKGRLPEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASAdpfpQVKLCDFGFARII-GEKSFR 583
Cdd:cd08222   88 dldDKISEYKKSGTTIDENQILDWFI-QLLLAVQYMHERRILHRDLKAKNIFLKNN----VIKVGDFGISRILmGTSDLA 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568979055 584 RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd08222  163 TTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILY 196
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
448-622 5.86e-24

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 108.39  E-value: 5.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   448 TGRDVAIKIIDKLRfPT--KQESQLRNEVAILQNLHHPGVVNLECMFET-PERVFVVMEKLHGDMLEMILSSEkGRLPEH 524
Cdd:TIGR03903    2 TGHEVAIKLLRTDA-PEeeHQRARFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAAD-GALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055   525 ITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGF------ARIIGEKSFRRS--VVGTPAYLAPE 596
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIgtllpgVRDADVATLTRTteVLGTPTYCAPE 159
                          170       180
                   ....*....|....*....|....*.
gi 568979055   597 VLRNKGYNRSLDMWSVGVIIYVSLSG 622
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTG 185
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
431-670 6.81e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 103.99  E-value: 6.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQL----RNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd05633   12 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLalneRIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSv 586
Cdd:cd05633   92 GGDLHYHLS-QHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHVRISDLGLACDFSKKKPHAS- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFNE--DEDIH--DQIQNAAFMYPPNPWkeiSHEAIDLINN 661
Cdd:cd05633  167 VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHeiDRMTLTVNVELPDSF---SPELKSLLEG 243

                 ....*....
gi 568979055 662 LLQVKMRKR 670
Cdd:cd05633  244 LLQRDVSKR 252
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
431-670 7.75e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 103.20  E-value: 7.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQL----RNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd14223    7 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLalneRIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSv 586
Cdd:cd14223   87 GGDLHYHLS-QHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL---DEFGHVRISDLGLACDFSKKKPHAS- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPFNE--DEDIHDQIQNAAFMYPPNPwKEISHEAIDLINNLL 663
Cdd:cd14223  162 VGTHGYMAPEVLqKGVAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHEIDRMTLTMAVELP-DSFSPELRSLLEGLL 240

                 ....*..
gi 568979055 664 QVKMRKR 670
Cdd:cd14223  241 QRDVNRR 247
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
418-681 8.40e-24

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 102.78  E-value: 8.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 418 VDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKII----DKLRFPTkqeSQLRnEVAILQNLHHPGVVNLECMF- 492
Cdd:cd07866    2 YGCSKLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKIlmhnEKDGFPI---TALR-EIKILKKLKHPNVVPLIDMAv 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 493 -------ETPERVFVVMEKLHGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQ 565
Cdd:cd07866   78 erpdkskRKRGSVYMVTPYMDHD-LSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILI---DNQGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 566 VKLCDFGFARII----------GEKSFRR--SVVGTPAYLAPE-VLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDI 632
Cdd:cd07866  154 LKIADFGLARPYdgpppnpkggGGGGTRKytNLVVTRWYRPPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDI 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 633 HDQIQNAAFMYPPNP----------------------------WKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07866  234 DQLHLIFKLCGTPTEetwpgwrslpgcegvhsftnyprtleerFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
425-685 8.86e-24

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 101.88  E-value: 8.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 425 QIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd06619    2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVI-PLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMIlssekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIgEKSFRR 584
Cdd:cd06619   81 MDGGSLDVY-----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRG---QVKLCDFGVSTQL-VNSIAK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnededihDQIQ-NAAFMYPPNPWKEISHEA-------- 655
Cdd:cd06619  152 TYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPY-------PQIQkNQGSLMPLQLLQCIVDEDppvlpvgq 224
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 656 -----IDLINNLLQVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd06619  225 fsekfVHFITQCMRKQPKERPAPENLMDHPFIVQY 259
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
432-681 1.05e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 102.03  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTG-RDVAIKiidKLRFPTKQE----SQLRnEVAILQNLH---HPGVVNL--ECMFETPER---V 498
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGgRFVALK---RVRVQTGEEgmplSTIR-EVAVLRHLEtfeHPNVVRLfdVCTVSRTDRetkL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 499 FVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG 578
Cdd:cd07862   85 TLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSG---QIKLADFGLARIYS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 579 EKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQI---------------------- 636
Cdd:cd07862  162 FQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDV-DQLgkildviglpgeedwprdvalp 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 637 QNAAFMYPPNPWK----EISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07862  241 RQAFHSKSAQPIEkfvtDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
430-684 1.12e-23

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 101.82  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE---SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:PLN00009   8 EKIGEGTYGVVYKARDRVTNETIALK---KIRLEQEDEgvpSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfPQVKLCDFGFARIIG--EKSFRR 584
Cdd:PLN00009  85 LDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRT--NALKLADFGLARAFGipVRTFTH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVgTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPN----------------- 646
Cdd:PLN00009 163 EVV-TLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNeetwpgvtslpdyksaf 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 647 -PWKE---------ISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:PLN00009 242 pKWPPkdlatvvptLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
432-686 1.51e-23

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 102.81  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTK---QESQLRNEVAILQNLHHPGVVNLECMFeTPERVF------VVM 502
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVK---KLSRPFQsiiHAKRTYRELRLLKHMKHENVIGLLDVF-TPARSLeefndvYLV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENvLLASADpfPQVKLCDFGFARIIGEKsf 582
Cdd:cd07877  101 THLMGADLNNIVKCQK--LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN-LAVNED--CELKILDFGLARHTDDE-- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGT--FPFNEDEDIHDQIQNAAFMYPPNPWKEISHE----- 654
Cdd:cd07877  174 MTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRtlFPGTDHIDQLKLILRLVGTPGAELLKKISSEsarny 253
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 655 ----------------------AIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQ 686
Cdd:cd07877  254 iqsltqmpkmnfanvfiganplAVDLLEKMLVLDSDKRITAAQALAHAYFAQYH 307
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
430-679 1.62e-23

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 100.91  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVN-LECMFETPErVFVVMEKLHGD 508
Cdd:cd14046   12 QVLGKGAFGQVVKVRNKLDGRYYAIKKI-KLRSESKNNSRILREVMLLSRLNHQHVVRyYQAWIERAN-LYIQMEYCEKS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKfLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR------------- 575
Cdd:cd14046   90 TLRDLIDSGLFQDTDRLWR-LFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNG---NVKIGDFGLATsnklnvelatqdi 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 ------IIGEKSFRRSVVGTPAYLAPEVLRNKG--YNRSLDMWSVGVIIYvslSGTFPFN---EDEDIHDQIQNAAFMYP 644
Cdd:cd14046  166 nkstsaALGSSGDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFF---EMCYPFStgmERVQILTALRSVSIEFP 242
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 645 PN-PWKEISHEAiDLINNLLQVKMRKRYSVDKTLSH 679
Cdd:cd14046  243 PDfDDNKHSKQA-KLIRWLLNHDPAKRPSAQELLKS 277
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
430-683 1.65e-23

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 101.99  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDm 509
Cdd:cd07872   12 EKLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKD- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSFRRSVV 587
Cdd:cd07872   90 LKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERG---ELKLADFGLARAksVPTKTYSNEVV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 gTPAYLAPEVLRNKG-YNRSLDMWSVGVIIYVSLSGT--FPFNEDED-IH--------------------DQIQNAAF-M 642
Cdd:cd07872  167 -TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRplFPGSTVEDeLHlifrllgtpteetwpgissnDEFKNYNFpK 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 643 YPPNPWkeISH------EAIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd07872  246 YKPQPL--INHaprldtEGIELLTKFLQYESKKRISAEEAMKHAYFR 290
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
431-670 2.86e-23

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 102.02  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDK-LRFPTKQESQLRNEVAIL-QNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05617   22 VIGRGSYAKVLLVRLKKNDQIYAMKVVKKeLVHDDEDIDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLFLVIEYVNGG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARI-IGEKSFRRSVV 587
Cdd:cd05617  102 DL-MFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTDYGMCKEgLGPGDTTSTFC 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNL 662
Cdd:cd05617  178 GTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGF 257

                 ....*...
gi 568979055 663 LQVKMRKR 670
Cdd:cd05617  258 LNKDPKER 265
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
112-163 3.16e-23

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 93.11  E-value: 3.16e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 112 VPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20838    1 VPHRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNC 52
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
430-682 3.22e-23

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 100.42  E-value: 3.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDFGFARI--IGEKSFRRSVV 587
Cdd:cd07870   85 AQYMIQHPGGLHPYNVRLFMF-QLLRGLAYIHGQHILHRDLKPQNLLISY---LGELKLADFGLARAksIPSQTYSSEVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 gTPAYLAPEVLRNK-GYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQ-----------------------NAAFMY 643
Cdd:cd07870  161 -TLWYRPPDVLLGAtDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEkiwtvlgvptedtwpgvsklpnyKPEWFL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 644 PPNP------WKEISH--EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07870  240 PCKPqqlrvvWKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
431-634 4.39e-23

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 101.65  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAIL-QNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05618   27 VIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDiDWVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVIEYVNGG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLeMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI-IGEKSFRRSVV 587
Cdd:cd05618  107 DL-MFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEG---HIKLTDYGMCKEgLRPGDTTSTFC 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-------NEDEDIHD 634
Cdd:cd05618  183 GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdNPDQNTED 236
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
432-670 5.02e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 100.11  E-value: 5.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRF-PTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-GDM 509
Cdd:cd08229   32 IGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADaGDL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGR--LPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFR-RSV 586
Cdd:cd08229  112 SRMIKHFKKQKrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG---VVKLGDLGLGRFFSSKTTAaHSL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDE----DIHDQIQNAAfmYPPNPWKEISHEAIDLINNL 662
Cdd:cd08229  189 VGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmnlySLCKKIEQCD--YPPLPSDHYSEELRQLVNMC 266

                 ....*...
gi 568979055 663 LQVKMRKR 670
Cdd:cd08229  267 INPDPEKR 274
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
430-659 5.46e-23

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 101.65  E-value: 5.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQE-SQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HG 507
Cdd:cd05628    7 KVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQvGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLpGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFG------------FAR 575
Cdd:cd05628   87 DMMTLLM--KKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLL---DSKGHVKLSDFGlctglkkahrteFYR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGE--------------------KSFRR----SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED-- 629
Cdd:cd05628  162 NLNHslpsdftfqnmnskrkaetwKRNRRqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSEtp 241
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568979055 630 EDIHDQIQN--AAFMYPPNpwKEISHEAIDLI 659
Cdd:cd05628  242 QETYKKVMNwkETLIFPPE--VPISEKAKDLI 271
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
432-682 5.61e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 99.71  E-value: 5.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQEsQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMD-LRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVVGTP 590
Cdd:cd06657  106 DIVTHT--RMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG---RVKLSDFGFcAQVSKEVPRRKSLVGTP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP-FNED-----EDIHDQIqnaafmyPP--NPWKEISHEAIDLINNL 662
Cdd:cd06657  181 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPplkamKMIRDNL-------PPklKNLHKVSPSLKGFLDRL 253
                        250       260
                 ....*....|....*....|
gi 568979055 663 LQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06657  254 LVRDPAQRATAAELLKHPFL 273
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
432-695 6.51e-23

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 100.89  E-value: 6.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFeTP-------ERVFVV 501
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVK---KLSRPFQSLIHARRtyrELRLLKHMKHENVIGLLDVF-TPatsienfNEVYLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MeKLHGDMLEMILSSEKgRLPEHItKFLITQILVALRHLHFKNIVHCDLKPENVllaSADPFPQVKLCDFGFARIIGEKs 581
Cdd:cd07878   99 T-NLMGADLNNIVKCQK-LSDEHV-QFLIYQLLRGLKYIHSAGIIHRDLKPSNV---AVNEDCELRILDFGLARQADDE- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 fRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGT--FPFNEDEDIHDQIQNAAFMYPPNPWKEISHE---- 654
Cdd:cd07878  172 -MTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKalFPGNDYIDQLKRIMEVVGTPSPEVLKKISSEhark 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979055 655 -----------------------AIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELE 695
Cdd:cd07878  251 yiqslphmpqqdlkkifrganplAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPEDEPEAE 314
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
432-682 1.06e-22

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 99.57  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKII---DKLRFPTKQESQLRNEVaILQNLHHPGVVNLECMFETPE-------RVFVV 501
Cdd:cd14136   18 LGWGHFSTVWLCWDLQNKRFVALKVVksaQHYTEAALDEIKLLKCV-READPKDPGREHVVQLLDDFKhtgpngtHVCMV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSSE-KGrLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLASADPfpQVKLCDFGFARIIgE 579
Cdd:cd14136   97 FEVLGPNLLKLIKRYNyRG-IPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKI--EVKIADLGNACWT-D 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN--------EDEDIHDQIQNAAFMYPPN----- 646
Cdd:cd14136  173 KHFT-EDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDphsgedysRDEDHLALIIELLGRIPRSiilsg 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 647 --------------------PWK---------EISHEAIDLINN----LLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14136  252 kysreffnrkgelrhisklkPWPledvlvekyKWSKEEAKEFASfllpMLEYDPEKRATAAQCLQHPWL 320
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
432-680 1.10e-22

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 99.15  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRfptkqESQLRNEVAILQNLH-HPGVVNLECMFETP-ERVFV-VMEKL-HG 507
Cdd:cd14132   26 IGRGKYSEVFEGINIGNNEKVVIKVLKPVK-----KKKIKREIKILQNLRgGPNIVKLLDVVKDPqSKTPSlIFEYVnNT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMI--LSSEKGRlpehitkFLITQILVALRHLHFKNIVHCDLKPENVLLasaDP-FPQVKLCDFGFARIIGEKSFRR 584
Cdd:cd14132  101 DFKTLYptLTDYDIR-------YYMYELLKALDYCHSKGIMHRDVKPHNIMI---DHeKRKLRLIDWGLAEFYHPGQEYN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQI--------------------------- 636
Cdd:cd14132  171 VRVASRYYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLvkiakvlgtddlyayldkygielpprl 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 637 QNAAFMYPPNPWKE---------ISHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd14132  251 NDILGRHSKKPWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
430-628 1.53e-22

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 98.22  E-value: 1.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd06641   10 EKIGKGSFGEVFKGIDNRTQKVVAIKIID-LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGgS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMIlssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSV-V 587
Cdd:cd06641   89 ALDLL---EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHG---EVKLADFGVAGQLTDTQIKRN*fV 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE 628
Cdd:cd06641  163 GTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSE 203
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
430-681 1.65e-22

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 98.37  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHH-PGVVNLECMFETPER----VFV 500
Cdd:cd07837    7 EKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEgvpsTALR-EVSLLQMLSQsIYIVRLLDVEHVEENgkplLYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSSEKG---RLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFpqVKLCDFGFAR-- 575
Cdd:cd07837   83 VFEYLDTDLKKFIDSYGRGphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGL--LKIADLGLGRaf 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 IIGEKSFRRSVVgTPAYLAPEVLRNKG-YNRSLDMWSVGVIiYVSLSGTFP-FNEDEDIHDQIQNAAFMYPPNP------ 647
Cdd:cd07837  161 TIPIKSYTHEIV-TLWYRAPEVLLGSThYSTPVDMWSVGCI-FAEMSRKQPlFPGDSELQQLLHIFRLLGTPNEevwpgv 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 648 -----------WK---------EISHEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd07837  239 sklrdwheypqWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
432-686 1.85e-22

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 99.59  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE---SQLRNEVAILQNLHHPGVVNLECMFeTPERVFVVMEKLHGD 508
Cdd:cd07879   23 VGSGAYGSVCSAIDKRTGEKVAIK---KLSRPFQSEifaKRAYRELTLLKHMQHENVIGLLDVF-TSAVSGDEFQDFYLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGR---LPEHITKFLITQILVALRHLHFKNIVHCDLKPENvLLASADpfPQVKLCDFGFARiiGEKSFRRS 585
Cdd:cd07879   99 MPYMQTDLQKIMghpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN-LAVNED--CELKILDFGLAR--HADAEMTG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQIQN-------------------AAFMY-- 643
Cdd:cd07879  174 YVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLF-KGKDYLDQLTQilkvtgvpgpefvqkledkAAKSYik 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 644 --PPNPWKEISH-------EAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQ 686
Cdd:cd07879  253 slPKYPRKDFSTlfpkaspQAVDLLEKMLELDVDKRLTATEALEHPYFDSFR 304
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
432-695 2.09e-22

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 99.39  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFeTPER-------VFVV 501
Cdd:cd07874   25 IGSGAQGIVCAAYDAVLDRNVAIK---KLSRPFQNQTHAKRayrELVLMKCVNHKNIISLLNVF-TPQKsleefqdVYLV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMIlsseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKS 581
Cdd:cd07874  101 MELMDANLCQVI----QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLARTAGTSF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII--YVSLSGTFPFNEDED-----------------------IHDQI 636
Cdd:cd07874  174 MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgeMVRHKILFPGRDYIDqwnkvieqlgtpcpefmkklqptVRNYV 253
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979055 637 QN----AAFMYP---PNPW--------KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLqdyQTWLDLRELE 695
Cdd:cd07874  254 ENrpkyAGLTFPklfPDSLfpadsehnKLKASQARDLLSKMLVIDPAKRISVDEALQHPYI---NVWYDPAEVE 324
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
430-720 3.22e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 99.32  E-value: 3.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTK-QESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HG 507
Cdd:cd05626    7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRnQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIpGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGF-------------- 573
Cdd:cd05626   87 DMMSLLIRMEV--FPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI---DLDGHIKLTDFGLctgfrwthnskyyq 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 574 ----------------------------------ARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVS 619
Cdd:cd05626  162 kgshirqdsmepsdlwddvsncrcgdrlktleqrATKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEM 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 620 LSGTFPFNEDEDIHDQIQ----NAAFMYPPNpwKEISHEAIDLINNLLQVKMRK--RYSVDKTLSHPWLQDYQTWLDLRE 693
Cdd:cd05626  242 LVGQPPFLAPTPTETQLKvinwENTLHIPPQ--VKLSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFSEVDFSSDIRT 319
                        330       340
                 ....*....|....*....|....*..
gi 568979055 694 LECRIGERyITHESDDSRWEQYAGEQG 720
Cdd:cd05626  320 QPAPYVPK-ISHPMDTSNFDPVEEESP 345
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
1-34 6.50e-22

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 89.28  E-value: 6.50e-22
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGV 34
Cdd:cd20795   23 MLFGLVRQGLKCEGCGLNFHKRCAYKIPNNCTGS 56
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
113-163 6.74e-22

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 89.10  E-value: 6.74e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20798    1 PHTLAEHNYKKPTVCKVCDKLLVGLVRQGLKCRDCGVNVHKKCASLLPSNC 51
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
449-626 6.87e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 99.71  E-value: 6.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 449 GRDVAIKIIDKLRFPT--KQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME-KLHGDMLEMILSSEKGRLP--E 523
Cdd:PTZ00267  89 GSDPKEKVVAKFVMLNdeRQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEyGSGGDLNKQIKQRLKEHLPfqE 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 524 HITKFLITQILVALRHLHFKNIVHCDLKPENVLLAsadPFPQVKLCDFGFARIIGEK---SFRRSVVGTPAYLAPEVLRN 600
Cdd:PTZ00267 169 YEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM---PTGIIKLGDFGFSKQYSDSvslDVASSFCGTPYYLAPELWER 245
                        170       180
                 ....*....|....*....|....*.
gi 568979055 601 KGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:PTZ00267 246 KRYSKKADMWSLGVILYELLTLHRPF 271
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
430-685 7.70e-22

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 96.28  E-value: 7.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG-D 508
Cdd:cd06642   10 ERIGKGSFGEVYKGIDNRTKEVVAIKIID-LEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGgS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMIlssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSV-V 587
Cdd:cd06642   89 ALDLL---KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQG---DVKLADFGVAGQLTDTQIKRNTfV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIHDqiQNAAFMYPPN--PWKEISHEA--IDLINNLL 663
Cdd:cd06642  163 GTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNS---DLHP--MRVLFLIPKNspPTLEGQHSKpfKEFVEACL 237
                        250       260
                 ....*....|....*....|..
gi 568979055 664 QVKMRKRYSVDKTLSHPWLQDY 685
Cdd:cd06642  238 NKDPRFRPTAKELLKHKFITRY 259
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
431-684 8.72e-22

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 98.95  E-value: 8.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfptKQESQLRN-EVAILQNLHHPGVVNL------ECMFETPERVF--VV 501
Cdd:PTZ00036  73 IIGNGSFGVVYEAICIDTSEKVAIKKV-------LQDPQYKNrELLIMKNLNHINIIFLkdyyytECFKKNEKNIFlnVV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 ME----KLHGDMLEMilSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQ-VKLCDFGFAR- 575
Cdd:PTZ00036 146 MEfipqTVHKYMKHY--ARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI---DPNTHtLKLCDFGSAKn 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 576 -IIGEKSFrrSVVGTPAYLAPEV-LRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQI------------QNAAF 641
Cdd:PTZ00036 221 lLAGQRSV--SYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILG-YPIFSGQSSVDQLvriiqvlgtpteDQLKE 297
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 642 MYP-----------PNPWKEI-----SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:PTZ00036 298 MNPnyadikfpdvkPKDLKKVfpkgtPDDAINFISQFLKYEPLKRLNPIEALADPFFDD 356
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
432-695 8.76e-22

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 97.79  E-value: 8.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFeTPER-------VFVV 501
Cdd:cd07876   29 IGSGAQGIVCAAFDTVLGINVAVK---KLSRPFQNQTHAKRayrELVLLKCVNHKNIISLLNVF-TPQKsleefqdVYLV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMIlsseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKS 581
Cdd:cd07876  105 MELMDANLCQVI----HMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLARTACTNF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhDQ---------IQNAAFM---------- 642
Cdd:cd07876  178 MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHI-DQwnkvieqlgTPSAEFMnrlqptvrny 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 643 ------YPPNPWKEI----------------SHEAIDLINNLLQVKMRKRYSVDKTLSHPWLqdyQTWLDLRELE 695
Cdd:cd07876  257 venrpqYPGISFEELfpdwifpseserdklkTSQARDLLSKMLVIDPDKRISVDEALRHPYI---TVWYDPAEAE 328
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
425-683 9.70e-22

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 95.21  E-value: 9.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 425 QIFPD-EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQ----LRNEVAILQNLHHPGVVNLECMFETPERVF 499
Cdd:cd06607    1 KIFEDlREIGHGSFGAVYYARNKRTSEVVAIK---KMSYSGKQSTEkwqdIIKEVKFLRQLRHPNTIEYKGCYLREHTAW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHG---DMLEMilssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI 576
Cdd:cd06607   78 LVMEYCLGsasDIVEV----HKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPG---TVKLADFGSASL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IgekSFRRSVVGTPAYLAPEVL--RNKG-YNRSLDMWSVGvIIYVSLSGTFP--FNED--EDIHDQIQNAAFMYPPNPWk 649
Cdd:cd06607  151 V---CPANSFVGTPYWMAPEVIlaMDEGqYDGKVDVWSLG-ITCIELAERKPplFNMNamSALYHIAQNDSPTLSSGEW- 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568979055 650 eiSHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06607  226 --SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
431-626 1.01e-21

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 95.49  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRktGRDVAIKII--DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd14146    1 IIGVGGFGKVYRATWK--GQEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKG--------RLPEHITKFLITQILVALRHLH---FKNIVHCDLKPENVLLASADPFPQV-----KLCDFG 572
Cdd:cd14146   79 TLNRALAAANAapgprrarRIPPHILVNWAVQIARGMLYLHeeaVVPILHRDLKSSNILLLEKIEHDDIcnktlKITDFG 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568979055 573 FARIiGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14146  159 LARE-WHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
432-625 1.24e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 96.66  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06650   13 LGAGNGGVVFKVSHKPSGLVMARKLI-HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSsEKGRLPEHITKFLITQILVALRHLHFKN-IVHCDLKPENVLLASADpfpQVKLCDFGFA-RIIgeKSFRRSVVGT 589
Cdd:cd06650   92 QVLK-KAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRG---EIKLCDFGVSgQLI--DSMANSFVGT 165
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568979055 590 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP 625
Cdd:cd06650  166 RSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
432-614 3.12e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 94.33  E-value: 3.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06646   17 VGSGTYGDVYKARNLHTGELAAVKII-KLE-PGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA-RIIGEKSFRRSVVGTP 590
Cdd:cd06646   95 DIYHV-TGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNG---DVKLADFGVAaKITATIAKRKSFIGTP 170
                        170       180
                 ....*....|....*....|....*..
gi 568979055 591 AYLAPEVL---RNKGYNRSLDMWSVGV 614
Cdd:cd06646  171 YWMAPEVAaveKNGGYNQLCDIWAVGI 197
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
432-616 3.21e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 95.13  E-value: 3.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKII----DKLRFPTkqeSQLRnEVAILQNLHHPGVVNLECMFETPER--------VF 499
Cdd:cd07865   20 IGQGTFGEVFKARHRKTGQIVALKKVlmenEKEGFPI---TALR-EIKILQLLKHENVVNLIEICRTKATpynrykgsIY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR---- 575
Cdd:cd07865   96 LVFEFCEHD-LAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG---VLKLADFGLARafsl 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568979055 576 -IIGEKSFRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVII 616
Cdd:cd07865  172 aKNSQPNRYTNRVVTLWYRPPELLLGeRDYGPPIDMWGAGCIM 214
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
426-638 3.27e-21

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 94.03  E-value: 3.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 426 IFPDEVLGSGQFGIVYGGKHRKTGRD---VAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPErVFVVM 502
Cdd:cd05056    8 ITLGRCIGEGQFGDVYQGVYMSPENEkiaVAVKTCKNCTSPSVREKFLQ-EAYIMRQFDHPHIVKLIGVITENP-VWIVM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSF 582
Cdd:cd05056   86 ELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPD---CVKLGDFGLSRYMEDESY 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 583 RRSVVGT-P-AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN--EDEDIHDQIQN 638
Cdd:cd05056  163 YKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQgvKNNDVIGRIEN 223
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
432-695 3.61e-21

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 95.88  E-value: 3.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFeTPER-------VFVV 501
Cdd:cd07875   32 IGSGAQGIVCAAYDAILERNVAIK---KLSRPFQNQTHAKRayrELVLMKCVNHKNIIGLLNVF-TPQKsleefqdVYIV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMIlsseKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKS 581
Cdd:cd07875  108 MELMDANLCQVI----QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLARTAGTSF 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 582 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT--FPFNEDED---------------------------I 632
Cdd:cd07875  181 MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGvlFPGTDHIDqwnkvieqlgtpcpefmkklqptvrtyV 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979055 633 HDQIQNAAF---------MYPPNPW--KEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLqdyQTWLDLRELE 695
Cdd:cd07875  261 ENRPKYAGYsfeklfpdvLFPADSEhnKLKASQARDLLSKMLVIDASKRISVDEALQHPYI---NVWYDPSEAE 331
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
1-44 4.88e-21

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 87.42  E-value: 4.88e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSL 44
Cdd:cd20840   30 MLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSGARKRRLSSTSL 73
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
430-647 5.46e-21

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 93.58  E-value: 5.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDkLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd06640   10 ERIGKGSFGEVFKGIDNRTQQVVAIKIID-LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRR-SVVG 588
Cdd:cd06640   89 ALDLLRA--GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQG---DVKLADFGVAGQLTDTQIKRnTFVG 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 589 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPfneDEDIHDqiQNAAFMYPPNP 647
Cdd:cd06640  164 TPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP---NSDMHP--MRVLFLIPKNN 217
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
430-713 5.73e-21

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 95.88  E-value: 5.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdklrfpTKQESQLRNEVA-------ILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd05625    7 KTLGIGAFGEVCLARKVDTKALYATKTL------RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKL-HGDMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFG--------- 572
Cdd:cd05625   81 DYIpGGDMMSLLI--RMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGlctgfrwth 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 573 -----------------FARIIGEKSFRR----------------------SVVGTPAYLAPEVLRNKGYNRSLDMWSVG 613
Cdd:cd05625  156 dskyyqsgdhlrqdsmdFSNEWGDPENCRcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 614 VIIYVSLSGTFPFNEDEDIHDQIQ----NAAFMYPPNpwKEISHEAIDLINNLLQVKMRK--RYSVDKTLSHPWLQDYQT 687
Cdd:cd05625  236 VILFEMLVGQPPFLAQTPLETQMKvinwQTSLHIPPQ--AKLSPEASDLIIKLCRGPEDRlgKNGADEIKAHPFFKTIDF 313
                        330       340
                 ....*....|....*....|....*.
gi 568979055 688 WLDLRELECRIGERyITHESDDSRWE 713
Cdd:cd05625  314 SSDLRQQSAPYIPK-ITHPTDTSNFD 338
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
429-626 5.88e-21

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 93.57  E-value: 5.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYggKHRKTGRDVAIKIidKLRFPTKQESQ----LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEK 504
Cdd:cd14145   11 EEIIGIGGFGKVY--RAIWIGDEVAVKA--ARHDPDEDISQtienVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIV---HCDLKPENVLL----ASADPFPQV-KLCDFGFARI 576
Cdd:cd14145   87 ARGGPLNRVLSGK--RIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvENGDLSNKIlKITDFGLARE 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 iGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14145  165 -WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
432-682 1.16e-20

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 92.80  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRfPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06645   19 IGSGTYGDVYKARNVNTGELAAIKVI-KLE-PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSeKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF-ARIIGEKSFRRSVVGTP 590
Cdd:cd06645   97 DIYHV-TGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNG---HVKLADFGVsAQITATIAKRKSFIGTP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 591 AYLAPEVL---RNKGYNRSLDMWSVGvIIYVSLSGTFPfnEDEDIHDQ----IQNAAFMYPPN-----PWKEISHEAIDL 658
Cdd:cd06645  173 YWMAPEVAaveRKGGYNQLCDIWAVG-ITAIELAELQP--PMFDLHPMralfLMTKSNFQPPKlkdkmKWSNSFHHFVKM 249
                        250       260
                 ....*....|....*....|....
gi 568979055 659 InnlLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd06645  250 A---LTKNPKKRPTAEKLLQHPFV 270
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
435-682 2.24e-20

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 91.52  E-value: 2.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGGKHRKTGRDVAIKIIDklRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMIL 514
Cdd:cd14110   14 GRFSVVRQCEEKRSGQMLAAKIIP--YKPEDKQLVLR-EYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 515 SSEKGRLPEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR-------IIGEKsfRRSVV 587
Cdd:cd14110   91 AERNSYSEAEVTDYL-WQILSAVDYLHSRRILHLDLRSENMIITEKN---LLKIVDLGNAQpfnqgkvLMTDK--KGDYV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GTpayLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDIHDQIQNAAFMYpPNPWKEISHEAIDLINNLLQV 665
Cdd:cd14110  165 ET---MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDlnWERDRNIRKGKVQL-SRCYAGLSGGAVNFLKSTLCA 240
                        250
                 ....*....|....*..
gi 568979055 666 KMRKRYSVDKTLSHPWL 682
Cdd:cd14110  241 KPWGRPTASECLQNPWL 257
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
424-592 2.37e-20

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 91.36  E-value: 2.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfpTKQESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVVM 502
Cdd:cd14016    2 YKL--VKKIGSGSFGEVYLGIDLKTGEEVAIKIEKK----DSKHPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLhGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARI------ 576
Cdd:cd14016   76 DLL-GPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAKKyrdprt 154
                        170
                 ....*....|....*....
gi 568979055 577 ---IGEKSfRRSVVGTPAY 592
Cdd:cd14016  155 gkhIPYRE-GKSLTGTARY 172
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
432-616 3.84e-20

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 90.66  E-value: 3.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKlrfPTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKN---DVDQHKIVR-EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGE-----KSFRRSV 586
Cdd:cd14156   77 ELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVGEmpandPERKLSL 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14156  157 VGSAFWMAPEMLRGEPYDRKVDVFSFGIVL 186
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
431-682 3.90e-20

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 92.05  E-value: 3.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKI--IDKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFETPERVF-VVMEK 504
Cdd:cd14041   13 LLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKENYHKHacrEYRIHKELDHPRIVKLYDYFSLDTDSFcTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKgRLPEHITKFLITQILVALRHLH--FKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSF 582
Cdd:cd14041   93 CEGNDLDFYLKQHK-LMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RR--------SVVGTPAYLAPEVL----RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFM------YP 644
Cdd:cd14041  172 NSvdgmeltsQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILkatevqFP 251
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568979055 645 PNPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14041  252 PKP--VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
429-684 4.62e-20

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 90.94  E-value: 4.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNL----ECMFETPERVFVVMEK 504
Cdd:cd14031   15 DIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFydswESVLKGKKCIVLVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKGRLPEhITKFLITQILVALRHLHFKN--IVHCDLKPENVLLASadPFPQVKLCDFGFARIIgEKSF 582
Cdd:cd14031   95 MTSGTLKTYLKRFKVMKPK-VLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG--PTGSVKIGDLGLATLM-RTSF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEvLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEdedihdqIQNAAFMY--------PPNPWKEISHE 654
Cdd:cd14031  171 AKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSE-------CQNAAQIYrkvtsgikPASFNKVTDPE 242
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14031  243 VKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
416-614 5.59e-20

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 91.64  E-value: 5.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 416 ENVDIstVYQIFPDEV------LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQ----LRNEVAILQNLHHPGV 485
Cdd:cd06633    9 EIADL--FYKDDPEEIfvdlheIGHGSFGAVYFATNSHTNEVVAIK---KMSYSGKQTNEkwqdIIKEVKFLQQLKHPNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 486 VNLECMFETPERVFVVMEKLHG---DMLEMilssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADp 562
Cdd:cd06633   84 IEYKGCYLKDHTAWLVMEYCLGsasDLLEV----HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 563 fpQVKLCDFGFARIIgekSFRRSVVGTPAYLAPEVL--RNKG-YNRSLDMWSVGV 614
Cdd:cd06633  159 --QVKLADFGSASIA---SPANSFVGTPYWMAPEVIlaMDEGqYDGKVDIWSLGI 208
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
114-163 8.41e-20

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 83.34  E-value: 8.41e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd00029    1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
431-682 1.63e-19

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 89.73  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKI--IDKLRFPTKQESQLRN---EVAILQNLHHPGVVNLECMFETPERVF-VVMEK 504
Cdd:cd14040   13 LLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHacrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKN--IVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSF 582
Cdd:cd14040   93 CEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 -------RRSVVGTPAYLAPEVL----RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFM------YPP 645
Cdd:cd14040  172 gvdgmdlTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILkatevqFPV 251
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568979055 646 NPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14040  252 KP--VVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
431-625 1.67e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 89.80  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd06615    8 ELGAGNGGVVTKVLHRPSGLIMARKLI-HLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSsEKGRLPEHIT-KFLITQI--LVALRHLHfkNIVHCDLKPENVLLASADpfpQVKLCDFGFAriiGE--KSFRRS 585
Cdd:cd06615   87 DQVLK-KAGRIPENILgKISIAVLrgLTYLREKH--KIMHRDVKPSNILVNSRG---EIKLCDFGVS---GQliDSMANS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP 625
Cdd:cd06615  158 FVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYP 197
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
431-682 1.71e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 89.86  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE----SQLRnEVAILQNLHHPGVVNLECM---------FETPER 497
Cdd:cd07864   14 IIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEgfpiTAIR-EIKILRQLNHRSVVNLKEIvtdkqdaldFKKDKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 VF-VVMEKLHGDMLEMILSSEKGRLPEHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI 576
Cdd:cd07864   90 AFyLVFEYMDHDLMGLLESGLVHFSEDHIKSFM-KQLLEGLNYCHKKNFLHRDIKCSNILLNNKG---QIKLADFGLARL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEKSFR--RSVVGTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNP--W--- 648
Cdd:cd07864  166 YNSEESRpyTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPavWpdv 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 649 --------------------KEISH---EAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd07864  246 iklpyfntmkpkkqyrrrlrEEFSFiptPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
429-626 2.62e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 88.55  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRktGRDVAIKII--DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH 506
Cdd:cd14147    8 EEVIGIGGFGKVYRGSWR--GELVAVKAArqDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIV---HCDLKPENVLLAsadpFPQV---------KLCDFGFA 574
Cdd:cd14147   86 GGPLSRALAGR--RVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLL----QPIEnddmehktlKITDFGLA 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 575 RIiGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14147  160 RE-WHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
432-679 3.03e-19

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 88.14  E-value: 3.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPER----VFVVMEKLHG 507
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTELMTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKGRLPEHITKFlITQILVALRHLHFKN--IVHCDLKPENVLLASadPFPQVKLCDFGFArIIGEKSFRRS 585
Cdd:cd14033   89 GTLKTYLKRFREMKLKLLQRW-SRQILKGLHFLHSRCppILHRDLKCDNIFITG--PTGSVKIGDLGLA-TLKRASFAKS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 586 VVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIYVSLSGTFPFNEdedihdqIQNAAFMY--------PPNPWKEISHEAID 657
Cdd:cd14033  165 VIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSE-------CQNAAQIYrkvtsgikPDSFYKVKVPELKE 236
                        250       260
                 ....*....|....*....|..
gi 568979055 658 LINNLLQVKMRKRYSVDKTLSH 679
Cdd:cd14033  237 IIEGCIRTDKDERFTIQDLLEH 258
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
432-643 3.26e-19

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 87.88  E-value: 3.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRktGRDVAIKIIDklrFPTKQESqLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIE---SESEKKA-FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSeKGRLPEHITKFLIT---QILVALRHLHF---KNIVHCDLKPENVLLASADPFpqVKLCDFGFARIIgeKSFRRS 585
Cdd:cd14058   75 NVLHG-KEPKPIYTAAHAMSwalQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTV--LKICDFGTACDI--STHMTN 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnededihDQIQNAAFMY 643
Cdd:cd14058  150 NKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF-------DHIGGPAFRI 200
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
432-617 3.59e-19

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 87.88  E-value: 3.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHrKTGRDVAIKIIDKLRFPTKQESQLrnEVAILQNLHHPGVVNLECMFETPERVFVV---MEKlhGD 508
Cdd:cd05148   14 LGSGYFGEVWEGLW-KNRVRVAIKILKSDDLLKQQDFQK--EVQALKRLRHKHLISLFAVCSVGEPVYIItelMEK--GS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKSFRRSVVG 588
Cdd:cd05148   89 LLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED---LVCKVADFGLARLIKEDVYLSSDKK 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 568979055 589 TP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05148  166 IPyKWTAPEAASHGTFSTKSDVWSFGILLY 195
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
432-625 3.89e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 89.34  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd06649   13 LGAGNGGVVTKVQHKPSGLIMARKLI-HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKgRLPEHITKFLITQILVALRHLHFKN-IVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEkSFRRSVVGTP 590
Cdd:cd06649   92 QVLKEAK-RIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRG---EIKLCDFGVSGQLID-SMANSFVGTR 166
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568979055 591 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP 625
Cdd:cd06649  167 SYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
497-682 4.38e-19

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 87.41  E-value: 4.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARI 576
Cdd:cd14023   59 KAYVFFEKDFGDMHSYVRSCK--RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEER-TQLRLESLEDTHI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 I-GEKSFRRSVVGTPAYLAPEVLRNKGY--NRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnpwKEI 651
Cdd:cd14023  136 MkGEDDALSDKHGCPAYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDpsALFSKIRRGQFCIP----DHV 211
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568979055 652 SHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14023  212 SPKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
432-636 4.67e-19

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 89.24  E-value: 4.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQE---SQLRNEVAILQNLHHPGVVNLECMFeTPER-------VFVV 501
Cdd:cd07880   23 VGSGAYGTVCSALDRRTGAKVAIK---KLYRPFQSElfaKRAYRELRLLKHMKHENVIGLLDVF-TPDLsldrfhdFYLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDmLEMILSSEKgrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVllaSADPFPQVKLCDFGFARiiGEKS 581
Cdd:cd07880   99 MPFMGTD-LGKLMKHEK--LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL---AVNEDCELKILDFGLAR--QTDS 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568979055 582 FRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTfPFNEDEDIHDQI 636
Cdd:cd07880  171 EMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGK-PLFKGHDHLDQL 225
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
431-617 5.48e-19

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 87.86  E-value: 5.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGR----DVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLE--CMFETPERVFVVMEk 504
Cdd:cd05057   14 VLGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREETGPKANEEILD-EAYVMASVDHPHLVRLLgiCLSSQVQLITQLMP- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 lHGDMLEMiLSSEKGRL-PEHITKFlITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII--GEKS 581
Cdd:cd05057   92 -LGCLLDY-VRNHRDNIgSQLLLNW-CVQIAKGMSYLEEKRLVHRDLAARNVLVKTPN---HVKITDFGLAKLLdvDEKE 165
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568979055 582 FRRSVVGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05057  166 YHAEGGKVPiKWMALESIQYRIYTHKSDVWSYGVTVW 202
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
432-669 6.04e-19

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 87.57  E-value: 6.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKqesqlrnEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAE-------ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSsEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLAS--ADPFpqvkLCDFGFARII-----GEKSFRR 584
Cdd:cd13991   87 QLIK-EQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSdgSDAF----LCDFGHAECLdpdglGKSLFTG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVV-GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE--DEDIHDQIQNAafmyPPnPWKEISHEAIDLINN 661
Cdd:cd13991  162 DYIpGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQyySGPLCLKIANE----PP-PLREIPPSCAPLTAQ 236

                 ....*...
gi 568979055 662 LLQVKMRK 669
Cdd:cd13991  237 AIQAGLRK 244
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
432-616 7.17e-19

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 86.76  E-value: 7.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIiDKLrfPTKQESQLRnEVAILQNLHHPGVVNLE--CMFETpeRVFVVMEKLHGDM 509
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM-NTL--SSNRANMLR-EVQLMNRLSHPNILRFMgvCVHQG--QLHALTEYINGGN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARII---GEKSFRRSV 586
Cdd:cd14155   75 LEQLLDSNE-PLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEKIpdySDGKEKLAV 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14155  154 VGSPYWMAPEVLRGEPYNEKADVFSYGIIL 183
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
425-680 8.51e-19

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 86.59  E-value: 8.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 425 QIFP-DEVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLR-NEVAILQNLH-HPGVVNLECMFETPERVFVV 501
Cdd:cd14050    1 QCFTiLSKLGEGSFGEVFKVRSREDGKLYAVKRS-RSRFRGEKDRKRKlEEVERHEKLGeHPNCVRFIKAWEEKGILYIQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMilSSEKGRLPE-HITKFLItQILVALRHLHFKNIVHCDLKPENVLLaSADPFpqVKLCDFGFARIIGEK 580
Cdd:cd14050   80 TELCDTSLQQY--CEETHSLPEsEVWNILL-DLLKGLKHLHDHGLIHLDIKPANIFL-SKDGV--CKLGDFGLVVELDKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGV-IIYVSLSGTFPFNEDeDIHdQIQNAafMYPPNPWKEISHEAIDLI 659
Cdd:cd14050  154 DIHDAQEGDPRYMAPELLQGS-FTKAADIFSLGItILELACNLELPSGGD-GWH-QLRQG--YLPEEFTAGLSPELRSII 228
                        250       260
                 ....*....|....*....|.
gi 568979055 660 NNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd14050  229 KLMMDPDPERRPTAEDLLALP 249
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
424-626 8.97e-19

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 88.05  E-value: 8.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTG-RDVAIKIIDklRFPTKQESQLRnEVAILQ--NLHHPG----VVNLECMFETPE 496
Cdd:cd14135    2 YRVY--GYLGKGVFSNVVRARDLARGnQEVAIKIIR--NNELMHKAGLK-ELEILKklNDADPDdkkhCIRLLRHFEHKN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMIlsSEKGR---LpeHIT--KFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpFPQVKLCDF 571
Cdd:cd14135   77 HLCLVFESLSMNLREVL--KKYGKnvgL--NIKavRSYAQQLFLALKHLKKCNILHADIKPDNILVNEK--KNTLKLCDF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 572 GFARIIGEKSFrrsvvgTPaYL------APEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14135  151 GSASDIGENEI------TP-YLvsrfyrAPEIILGLPYDYPIDMWSVGCTLYELYTGKILF 204
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
429-684 9.69e-19

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 86.67  E-value: 9.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPER----VFVVMEK 504
Cdd:cd14032    6 DIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKGRLPEhITKFLITQILVALRHLHFKN--IVHCDLKPENVLLASadPFPQVKLCDFGFArIIGEKSF 582
Cdd:cd14032   86 MTSGTLKTYLKRFKVMKPK-VLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITG--PTGSVKIGDLGLA-TLKRASF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEvLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEdedihdqIQNAAFMY-------PPNPWKEISHEA 655
Cdd:cd14032  162 AKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSE-------CQNAAQIYrkvtcgiKPASFEKVTDPE 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 656 I-DLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14032  234 IkEIIGECICKNKEERYEIKDLLSHAFFAE 263
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
430-616 9.88e-19

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 87.09  E-value: 9.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRK-TGRDVAIKIIDK-LRFPTKQESQLRnEVAILQNLH---HPGVVNLECMFETPERVFVVMEK 504
Cdd:cd14052    6 ELIGSGEFSQVYKVSERVpTGKVYAVKKLKPnYAGAKDRLRRLE-EVSILRELTldgHDNIVQLIDSWEYHGHLYIQTEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILS--SEKGRLPEhitkFLITQILV----ALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG 578
Cdd:cd14052   85 CENGSLDVFLSelGLLGRLDE----FRVWKILVelslGLRFIHDHHFVHLDLKPANVLITFEG---TLKIGDFGMATVWP 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568979055 579 -EKSFRRSvvGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14052  158 lIRGIERE--GDREYIAPEILSEHMYDKPADIFSLGLIL 194
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
440-684 1.05e-18

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 86.99  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 440 VYGGKHRKTGRDVAIKIIDKLRFP--TKQESQ-----LRNEVAILQNLHHPGVVNL--------ECM-FETpERVFVVME 503
Cdd:cd14011   12 IYNGSKKSTKQEVSVFVFEKKQLEeySKRDREqilelLKRGVKQLTRLRHPRILTVqhpleesrESLaFAT-EPVFASLA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMilSSEKGRLPEH-----ITKFLITQILVALRHLHF-KNIVHCDLKPENVLLASADPFpqvKLCDFGFA--- 574
Cdd:cd14011   91 NVLGERDNM--PSPPPELQDYklydvEIKYGLLQISEALSFLHNdVKLVHGNICPESVVINSNGEW---KLAGFDFCiss 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 --RIIGEKSFRRSVVGTPA-------YLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPFNEDED---------IHDQ 635
Cdd:cd14011  166 eqATDQFPYFREYDPNLPPlaqpnlnYLAPEYILSKTCDPASDMFSLGVLIYaIYNKGKPLFDCVNNllsykknsnQLRQ 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 636 IQNAAFMYPPNPWKeisheaiDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14011  246 LSLSLLEKVPEELR-------DHVKTLLNVTPEVRPDAEQLSKIPFFDD 287
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
431-673 1.56e-18

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 86.41  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKiidklRFPTKQESQLR---NEVAILQNLH-HPGVVNLECMFETPERvfvvmEKLH 506
Cdd:cd14036    7 VIAEGGFAFVYEAQDVGTGKEYALK-----RLLSNEEEKNKaiiQEINFMKKLSgHPNIVQFCSAASIGKE-----ESDQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GdMLEMILSSE--KGRLPEHITK------FLITQIL-------VALRHLHFKN--IVHCDLKPENVLLASADpfpQVKLC 569
Cdd:cd14036   77 G-QAEYLLLTElcKGQLVDFVKKveapgpFSPDTVLkifyqtcRAVQHMHKQSppIIHRDLKIENLLIGNQG---QIKLC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 570 DFGFARIIGE------KSFRRSVV-------GTPAYLAPEVL---RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIh 633
Cdd:cd14036  153 DFGSATTEAHypdyswSAQKRSLVedeitrnTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKL- 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568979055 634 dQIQNAAFMYPPNPWK-EISHeaiDLINNLLQVKMRKRYSV 673
Cdd:cd14036  232 -RIINAKYTIPPNDTQyTVFH---DLIRSTLKVNPEERLSI 268
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
114-163 1.68e-18

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 79.43  E-value: 1.68e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568979055   114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
pknD PRK13184
serine/threonine-protein kinase PknD;
424-696 1.84e-18

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 90.21  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKII--DKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:PRK13184   4 YDII--RLIGKGGMGEVYLAYDPVCSRRVALKKIreDLSENPLLKKRFLR-EAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKLHGDMLEMILSS--EKGRLP------EHITKFL--ITQILVALRHLHFKNIVHCDLKPENVLLASadpFPQVKLCDF 571
Cdd:PRK13184  81 MPYIEGYTLKSLLKSvwQKESLSkelaekTSVGAFLsiFHKICATIEYVHSKGVLHRDLKPDNILLGL---FGEVVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 572 GFARII-GEKSFRRS------------------VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE---- 628
Cdd:PRK13184 158 GAAIFKkLEEEDLLDidvdernicyssmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRkkgr 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 629 ----DEDIHDQIQNAafmyppnPWKEISHEAIDLINNLLQVKMRKRYSVDKTLS---HPWLQDYQTW-----LDLRELEC 696
Cdd:PRK13184 238 kisyRDVILSPIEVA-------PYREIPPFLSQIAMKALAVDPAERYSSVQELKqdlEPHLQGSPEWtvkatLMTKKKSC 310
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
429-684 2.15e-18

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 86.26  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPER----VFVVMEK 504
Cdd:cd14030   30 DIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKgRLPEHITKFLITQILVALRHLHFKN--IVHCDLKPENVLLASadPFPQVKLCDFGFArIIGEKSF 582
Cdd:cd14030  110 MTSGTLKTYLKRFK-VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG--PTGSVKIGDLGLA-TLKRASF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIYVSLSGTFPFNEdedihdqIQNAAFMY-------PPNPWKEIS-HE 654
Cdd:cd14030  186 AKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSE-------CQNAAQIYrrvtsgvKPASFDKVAiPE 257
                        250       260       270
                 ....*....|....*....|....*....|
gi 568979055 655 AIDLINNLLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd14030  258 VKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
114-163 2.38e-18

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 78.86  E-value: 2.38e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20793    1 HKFKVHTYYSPTFCDHCGSLLYGLVRQGLKCKDCGMNVHHRCKENVPHLC 50
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
432-683 2.46e-18

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 86.62  E-value: 2.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQ----LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd06634   23 IGHGSFGAVYFARDVRNNEVVAIK---KMSYSGKQSNEkwqdIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 ---DMLEMilssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSfrr 584
Cdd:cd06634  100 sasDLLEV----HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPG---LVKLGDFGSASIMAPAN--- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVL--RNKG-YNRSLDMWSVGvIIYVSLSGTFP----FNEDEDIHDQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd06634  170 SFVGTPYWMAPEVIlaMDEGqYDGKVDVWSLG-ITCIELAERKPplfnMNAMSALYHIAQNESPALQSGHWSEYFRNFVD 248
                        250       260
                 ....*....|....*....|....*.
gi 568979055 658 linNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06634  249 ---SCLQKIPQDRPTSDVLLKHRFLL 271
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
432-683 2.78e-18

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 86.64  E-value: 2.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQ----LRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHG 507
Cdd:cd06635   33 IGHGSFGAVYFARDVRTSEVVAIK---KMSYSGKQSNEkwqdIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 ---DMLEMilssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIgekSFRR 584
Cdd:cd06635  110 sasDLLEV----HKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG---QVKLADFGSASIA---SPAN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTPAYLAPEVL--RNKG-YNRSLDMWSVGvIIYVSLSGTFP----FNEDEDIHDQIQNAAFMYPPNPWKEISHEAID 657
Cdd:cd06635  180 SFVGTPYWMAPEVIlaMDEGqYDGKVDVWSLG-ITCIELAERKPplfnMNAMSALYHIAQNESPTLQSNEWSDYFRNFVD 258
                        250       260
                 ....*....|....*....|....*.
gi 568979055 658 linNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06635  259 ---SCLQKIPQDRPTSEELLKHMFVL 281
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
430-670 4.11e-18

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 84.85  E-value: 4.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFptkQESQLRNEVAILQNLHHPGVVNLECMFETP-------------- 495
Cdd:cd14047   12 ELIGSGGFGQVFKAKHRIDGKTYAIK---RVKL---NNEKAEREVKALAKLDHPNIVRYNGCWDGFdydpetsssnssrs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 496 --ERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLI-TQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFG 572
Cdd:cd14047   86 ktKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIfEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG---KVKIGDFG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 573 FARII---GEKSFRRsvvGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFmyPPNpWK 649
Cdd:cd14047  163 LVTSLkndGKRTKSK---GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLRNGIL--PDI-FD 236
                        250       260
                 ....*....|....*....|.
gi 568979055 650 EISHEAIDLINNLLQVKMRKR 670
Cdd:cd14047  237 KRYKIEKTIIKKMLSKKPEDR 257
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
114-163 4.14e-18

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 78.64  E-value: 4.14e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568979055  114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPEC 50
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
430-616 6.10e-18

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 85.58  E-value: 6.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIidkLRFPTKQESQLRNEVAILQNL------HHPGVVNLECmFETPERVFVVME 503
Cdd:cd14211    5 EFLGRGTFGQVVKCWKRGTNEIVAIKI---LKNHPSYARQGQIEVSILSRLsqenadEFNFVRAYEC-FQHKNHTCLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFP-QVKLCDFGFARIIgEKSF 582
Cdd:cd14211   81 MLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHV-SKAV 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568979055 583 RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14211  160 CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVI 193
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
420-674 6.36e-18

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 85.91  E-value: 6.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFptkqESQLRNEVAIL--------QNLHHpgVVNLEC 490
Cdd:cd14225   41 IAYRYEIL--EVIGKGSFGQVVKALDHKTNEHVAIKIIrNKKRF----HHQALVEVKILdalrrkdrDNSHN--VIHMKE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 491 MFETPERVFVVMEKLHGDMLEMILSSE-KGRLPEHITKFLITqILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLC 569
Cdd:cd14225  113 YFYFRNHLCITFELLGMNLYELIKKNNfQGFSLSLIRRFAIS-LLQCLRLLYRERIIHCDLKPENILLRQRGQ-SSIKVI 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 570 DFGFARIIGEKSFrrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIqnAAFM----YPP 645
Cdd:cd14225  191 DFGSSCYEHQRVY--TYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTG-YPLFPGENEVEQL--ACIMevlgLPP 265
                        250       260
                 ....*....|....*....|....*....
gi 568979055 646 npwkeisheaidliNNLLQVKMRKRYSVD 674
Cdd:cd14225  266 --------------PELIENAQRRRLFFD 280
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
430-683 6.45e-18

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 84.78  E-value: 6.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAI-LQNLHHPGVVNLE-CMFETPErVFVVMEKLHG 507
Cdd:cd06617    7 EELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYgALFREGD-VWICMEVMDT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 --DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLASADpfpQVKLCDFGfarIIGE--KSF 582
Cdd:cd06617   85 slDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNG---QVKLCDFG---ISGYlvDSV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 RRSV-VGTPAYLAPE----VLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPN-PWKEISHEAI 656
Cdd:cd06617  159 AKTIdAGCKPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQVVEEPSPQlPAEKFSPEFQ 238
                        250       260
                 ....*....|....*....|....*..
gi 568979055 657 DLINNLLQVKMRKRYSVDKTLSHPWLQ 683
Cdd:cd06617  239 DFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
465-625 7.45e-18

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 84.63  E-value: 7.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 465 KQESQLRNEVAILQNLHHPGVVNLECMFETPeRVFVVMEKLHGDMLEMILSSEKGR----LPEHITKFLITQILVALRHL 540
Cdd:cd14067   52 KNFSEFRQEASMLHSLQHPCIVYLIGISIHP-LCFALELAPLGSLNTVLEENHKGSsfmpLGHMLTFKIAYQIAAGLAYL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 541 HFKNIVHCDLKPENVLLASAD--PFPQVKLCDFGFARiigeKSFRRSVVG---TPAYLAPEVLRNKGYNRSLDMWSVGVI 615
Cdd:cd14067  131 HKKNIIFCDLKSDNILVWSLDvqEHINIKLSDYGISR----QSFHEGALGvegTPGYQAPEIRPRIVYDEKVDMFSYGMV 206
                        170
                 ....*....|
gi 568979055 616 IYVSLSGTFP 625
Cdd:cd14067  207 LYELLSGQRP 216
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
419-636 8.14e-18

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 84.31  E-value: 8.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 419 DISTVYQIFPDEVL-----GSGQFGIVYGGKHRKtgrDVAIKIIdKLRFPTKQESQ-LRNEVAILQNLHHPGVVnLECMF 492
Cdd:cd14149    2 DSSYYWEIEASEVMlstriGSGSFGTVYKGKWHG---DVAVKIL-KVVDPTPEQFQaFRNEVAVLRKTRHVNIL-LFMGY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 493 ETPERVFVVMEKLHGDMLEMILSSEKgrlpehiTKFLITQILVALR-------HLHFKNIVHCDLKPENVLLASAdpfPQ 565
Cdd:cd14149   77 MTKDNLAIVTQWCEGSSLYKHLHVQE-------TKFQMFQLIDIARqtaqgmdYLHAKNIIHRDMKSNNIFLHEG---LT 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 566 VKLCDFGFARIIGEKSFRRSV---VGTPAYLAPEVLR---NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDiHDQI 636
Cdd:cd14149  147 VKIGDFGLATVKSRWSGSQQVeqpTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGELPYSHINN-RDQI 222
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
424-671 9.91e-18

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 85.06  E-value: 9.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFptkqESQLRNEVAILQNL-HHPG-----VVNLECMFETPE 496
Cdd:cd14226   15 YEI--DSLIGKGSFGQVVKAYDHVEQEWVAIKIIkNKKAF----LNQAQIEVRLLELMnKHDTenkyyIVRLKRHFMFRN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFK--NIVHCDLKPENVLLASADPfPQVKLCDFGFA 574
Cdd:cd14226   89 HLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKR-SAIKIIDFGSS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 RIIGEKSFRrsVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIyVSLSGTFPFNEDEDIHDQIQN--AAFMYPPNPWKEIS 652
Cdd:cd14226  168 CQLGQRIYQ--YIQSRFYRSPEVLLGLPYDLAIDMWSLGCIL-VEMHTGEPLFSGANEVDQMNKivEVLGMPPVHMLDQA 244
                        250       260
                 ....*....|....*....|....*.
gi 568979055 653 HEA-------IDLINNLLQVKMRKRY 671
Cdd:cd14226  245 PKArkffeklPDGTYYLKKTKDGKKY 270
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
432-634 1.14e-17

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 84.09  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGkhRKTGRDVAIKIIDKLRFPTKQE--SQLRNEVAILQNLHHPGVVNL---ECMFETPERVFVVMekLH 506
Cdd:cd14158   23 LGEGGFGVVFKG--YINDKNVAVKKLAAMVDISTEDltKQFEQEIQVMAKCQHENLVELlgySCDGPQLCLVYTYM--PN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMiLSSEKGRLPehITKFLITQILVA----LRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKS- 581
Cdd:cd14158   99 GSLLDR-LACLNDTPP--LSWHMRCKIAQGtangINYLHENNHIHRDIKSANILL---DETFVPKISDFGLARASEKFSq 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 582 --FRRSVVGTPAYLAPEVLRNKGYNRSlDMWSVGVIIYVSLSGTFPFNEDEDIHD 634
Cdd:cd14158  173 tiMTERIVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPVDENRDPQL 226
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
453-634 1.20e-17

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 83.99  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 453 AIKIIDKLRFPTKQ---ESQLRNEVAILQNLHHPGVVNLECMFETPE-RVFVVMEKLH---GDMLEMILSSEKGRLPEHI 525
Cdd:cd14001   32 AVKKINSKCDKGQRslyQERLKEEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYGGkslNDLIEERYEAGLGPFPAAT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 526 TKFLITQILVALRHLHF-KNIVHCDLKPENVLLASadPFPQVKLCDFGFARIIGEKSFRRS-----VVGTPAYLAPEVLR 599
Cdd:cd14001  112 ILKVALSIARALEYLHNeKKILHGDIKSGNVLIKG--DFESVKLCDFGVSLPLTENLEVDSdpkaqYVGTEPWKAKEALE 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 600 NKG-YNRSLDMWSVGVIIY--VSLSG--TFPFNEDEDIHD 634
Cdd:cd14001  190 EGGvITDKADIFAYGLVLWemMTLSVphLNLLDIEDDDED 229
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
428-617 1.34e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 83.77  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 428 PDEVLGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLR--NEVAILQNLHHPGVVN-LECMFETPER------- 497
Cdd:cd14048   10 PIQCLGRGGFGVVFEAKNKVDDCNYAVK---RIRLPNNELAREKvlREVRALAKLDHPGIVRyFNAWLERPPEgwqekmd 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 498 ---VFVVMEKLHGDMLE--MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFG 572
Cdd:cd14048   87 evyLYIQMQLCRKENLKdwMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDD---VVKVGDFG 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 573 FARIIGEKSFRRSV-------------VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd14048  164 LVTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILF 221
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
432-636 1.58e-17

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 82.83  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKtgrDVAIKIIdKLRFPTKQESQ-LRNEVAILQNLHHPGVVN-LECMfeTPERVFVVMEKLHGdm 509
Cdd:cd14062    1 IGSGSFGTVYKGRWHG---DVAVKKL-NVTDPTPSQLQaFKNEVAVLRKTRHVNILLfMGYM--TKPQLAIVTQWCEG-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 lemilSSEKGRLPEHITKFLITQILVALR-------HLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA----RIIG 578
Cdd:cd14062   73 -----SSLYKHLHVLETKFEMLQLIDIARqtaqgmdYLHAKNIIHRDLKSNNIFLHED---LTVKIGDFGLAtvktRWSG 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 579 EKSFRRSvVGTPAYLAPEVLRNKG---YNRSLDMWSVGVIIYVSLSGTFPFnEDEDIHDQI 636
Cdd:cd14062  145 SQQFEQP-TGSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPY-SHINNRDQI 203
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
113-163 1.77e-17

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 76.59  E-value: 1.77e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20824    1 PHNFKPHSFSIPTKCDYCGEKIWGLSKKGLSCKDCGFNCHIKCELKVPPEC 51
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
114-163 2.06e-17

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 76.32  E-value: 2.06e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20837    1 HRFKVYNYMSPTFCDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
432-617 2.14e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 83.20  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHR----KTGRDVAIKiidKLRFPTKQESQ--LRNEVAILQNLHHPGVVNLECMFETPER--VFVVME 503
Cdd:cd05038   12 LGEGHFGSVELCRYDplgdNTGEQVAVK---SLQPSGEEQHMsdFKREIEILRTLDHEYIVKYKGVCESPGRrsLRLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRLpEHITKFLIT-QILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS- 581
Cdd:cd05038   89 YLPSGSLRDYLQRHRDQI-DLKRLLLFAsQICKGMEYLGSQRYIHRDLAARNILVESED---LVKISDFGLAKVLPEDKe 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568979055 582 --FRRSVVGTPAY-LAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05038  165 yyYVKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLY 203
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
440-682 2.25e-17

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 82.39  E-value: 2.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 440 VYGGKHRKTGRDVAIKIIDKLRFptkQESqLRNEVAILQNLHHPGVVNLeCMFETpeRVFVVMEKLHGDMLEMILSSEKg 519
Cdd:cd14022    9 VFRAVHLHSGEELVCKVFDIGCY---QES-LAPCFCLPAHSNINQITEI-ILGET--KAYVFFERSYGDMHSFVRTCKK- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 520 rLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARII-GEKSFRRSVVGTPAYLAPEVL 598
Cdd:cd14022   81 -LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER-TRVKLESLEDAYILrGHDDSLSDKHGCPAYVSPEIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 599 RNKGY--NRSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQVKMRKRYSVD 674
Cdd:cd14022  159 NTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEpsSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQ 234

                 ....*...
gi 568979055 675 KTLSHPWL 682
Cdd:cd14022  235 EILDHPWF 242
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
429-626 2.85e-17

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 82.69  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEV-LGSGQFGIVYGG--KHRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETpERVFVVMEKL 505
Cdd:cd05115    8 DEVeLGSGNFGCVKKGvyKMRKKQIDVAIKVLKQGNEKAVRDEMMR-EAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG-EKSFRR 584
Cdd:cd05115   86 SGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQH---YAKISDFGLSKALGaDDSYYK 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 585 SVVGTP---AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPF 626
Cdd:cd05115  163 ARSAGKwplKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
432-616 3.18e-17

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 82.31  E-value: 3.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiiDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMK--ELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSF--------- 582
Cdd:cd14221   79 GIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENK---SVVVADFGLARLMVDEKTqpeglrslk 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 583 ------RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14221  156 kpdrkkRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
426-645 3.74e-17

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 81.92  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 426 IFPDEV-----LGSGQFGIVYGGkHRKTGRDVAIKIIdklRFPTKQESQLRNEVAILQNLHHPGVVNLE--CMFETPerV 498
Cdd:cd05112    1 IDPSELtfvqeIGSGQFGLVHLG-YWLNKDKVAIKTI---REGAMSEEDFIEEAEVMMKLSHPKLVQLYgvCLEQAP--I 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 499 FVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG 578
Cdd:cd05112   75 CLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQ---VVKVSDFGMTRFVL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 579 EKSFRRSVvGTP---AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFNE--DEDIHDQIQNAAFMYPP 645
Cdd:cd05112  152 DDQYTSST-GTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENrsNSEVVEDINAGFRLYKP 223
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
113-165 3.98e-17

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 76.62  E-value: 3.98e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20841   10 PHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 62
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
473-631 4.94e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 83.39  E-value: 4.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 473 EVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKP 552
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSD-LYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKT 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 553 ENVLLASADpfpQVKLCDFGFARI-IGEKSFrRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED 631
Cdd:PHA03209 186 ENIFINDVD---QVCIGDLGAAQFpVVAPAF-LGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPP 261
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
430-617 5.71e-17

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 81.23  E-value: 5.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVY-GGKHRKTGR--DVAIKII--DKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPErVFVVMEK 504
Cdd:cd05040    1 EKLGDGSFGVVRrGEWTTPSGKviQVAVKCLksDVLSQPNAMDDFLK-EVNAMHSLDHPNLIRLYGVVLSSP-LMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEK---- 580
Cdd:cd05040   79 APLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKD---KVKIGDFGLMRALPQNedhy 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 581 --SFRRSVvgtP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05040  156 vmQEHRKV---PfAWCAPESLKTRKFSHASDVWMFGVTLW 192
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
432-636 6.62e-17

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 81.60  E-value: 6.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKtgrDVAIKIIdKLRFPTKQESQ-LRNEVAILQNLHHPGVVnLECMFETPERVFVVMEKLHGDML 510
Cdd:cd14150    8 IGTGSFGTVFRGKWHG---DVAVKIL-KVTEPTPEQLQaFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGSSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILssekgrlpeHI--TKFLITQILVALR-------HLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKS 581
Cdd:cd14150   83 YRHL---------HVteTRFDTMQLIDVARqtaqgmdYLHAKNIIHRDLKSNNIFLHEG---LTVKIGDFGLATVKTRWS 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 582 FRRSV---VGTPAYLAPEVLR---NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDiHDQI 636
Cdd:cd14150  151 GSQQVeqpSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSGTLPYSNINN-RDQI 210
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
430-637 7.58e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 82.38  E-value: 7.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIidkLRFPTKQESQLRNEVAILQNL------HHPGVVNLECmFETPERVFVVME 503
Cdd:cd14229    6 DFLGRGTFGQVVKCWKRGTNEIVAVKI---LKNHPSYARQGQIEVGILARLsnenadEFNFVRAYEC-FQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasADPFPQ---VKLCDFGFARIIgEK 580
Cdd:cd14229   82 MLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIML--VDPVRQpyrVKVIDFGSASHV-SK 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 581 SFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIQ 637
Cdd:cd14229  159 TVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGALEYDQIR 214
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
113-163 8.39e-17

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 74.82  E-value: 8.39e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20797    3 PHVVEVEQYMTPTFCDYCGEMLTGLMKQGVKCKNCRCNFHKRCANAPRNNC 53
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
432-651 8.44e-17

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 82.04  E-value: 8.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKhRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMF--ETPERVFVVMEKLHGDM 509
Cdd:cd07867   10 VGRGTYGHVYKAK-RKDGKDEKEYALKQIEGTGISMSACR-EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMI-------LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADP-FPQVKLCDFGFARIIGEK- 580
Cdd:cd07867   88 WHIIkfhraskANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPeRGRVKIADMGFARLFNSPl 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 581 ---SFRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFN-EDEDI-------HDQIQN--AAFMYPPN 646
Cdd:cd07867  168 kplADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPIFHcRQEDIktsnpfhHDQLDRifSVMGFPAD 247

                 ....*.
gi 568979055 647 P-WKEI 651
Cdd:cd07867  248 KdWEDI 253
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
113-163 9.73e-17

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 74.37  E-value: 9.73e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20827    1 PHRFEKHNFTTPTYCDYCSSLLWGLVKTGMRCADCGYSCHEKCLEHVPKNC 51
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
432-616 9.75e-17

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 81.01  E-value: 9.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiiDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMK--ELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSF--------- 582
Cdd:cd14154   79 DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDK---TVVVADFGLARLIVEERLpsgnmspse 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 583 ------------RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14154  156 tlrhlkspdrkkRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
424-670 1.22e-16

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 80.79  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKiidklRFPTKQESQL---RNEVAILQNLH-HPGVVNL-----ECMFET 494
Cdd:cd14037    3 HHVTIEKYLAEGGFAHVYLVKTSNGGNRAALK-----RVYVNDEHDLnvcKREIEIMKRLSgHKNIVGYidssaNRSGNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PERVFVVMEKLHGDMLEMILSSekgRLPEHITKFLITQIL------VALRHlHFKN-IVHCDLKPENVLLASADPFpqvK 567
Cdd:cd14037   78 VYEVLLLMEYCKGGGVIDLMNQ---RLQTGLTESEILKIFcdvceaVAAMH-YLKPpLIHRDLKVENVLISDSGNY---K 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 568 LCDFG---FARIIGEKSFRRSVV-------GTPAYLAPEVL---RNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIhd 634
Cdd:cd14037  151 LCDFGsatTKILPPQTKQGVTYVeedikkyTTLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPFEESGQL-- 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568979055 635 QIQNAAFMYPPNPwkEISHEAIDLINNLLQVKMRKR 670
Cdd:cd14037  229 AILNGNFTFPDNS--RYSKRLHKLIRYMLEEDPEKR 262
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
114-163 1.28e-16

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 74.23  E-value: 1.28e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20809    1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVC 50
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
432-626 1.29e-16

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 80.18  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTgRDVAIKIIdklRFPTKQESQLRNEVAILQNLHHPGVVNLE--CMFETPerVFVVMEKLHGDM 509
Cdd:cd05059   12 LGSGQFGVVHLGKWRGK-IDVAIKMI---KEGSMSEDDFIEEAKVMMKLSHPKLVQLYgvCTKQRP--IFIVTEYMANGC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSvVGT 589
Cdd:cd05059   86 LLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQN---VVKVSDFGLARYVLDDEYTSS-VGT 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568979055 590 P---AYLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPF 626
Cdd:cd05059  162 KfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWeVFSEGKMPY 202
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
432-679 1.34e-16

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 80.80  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTK-QESQLRNEVAILQNLHHPGVVNLE---CMFETPER--VFVVME-K 504
Cdd:cd13986    8 LGEGGFSFVYLVEDLSTGRLYALK---KILCHSKeDVKEAMREIENYRLFNHPNILRLLdsqIVKEAGGKkeVYLLLPyY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMI--LSSEKGRLPEHITKFLITQILVALRHLH---FKNIVHCDLKPENVLLasaDPFPQVKLCDFGF---ARI 576
Cdd:cd13986   85 KRGSLQDEIerRLVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLL---SEDDEPILMDLGSmnpARI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 577 IGEKSFRRSVV-------GTPAYLAPEVLRNKGY---NRSLDMWSVGVIIYVSLSGTFPFNEDED----IHDQIQNAAFM 642
Cdd:cd13986  162 EIEGRREALALqdwaaehCTMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPFERIFQkgdsLALAVLSGNYS 241
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568979055 643 YPPNPwkEISHEAIDLINNLLQVKMRKRYSVDKTLSH 679
Cdd:cd13986  242 FPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
432-636 1.40e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 81.64  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKhRKTGRDVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMF--ETPERVFVVMEKLHGDM 509
Cdd:cd07868   25 VGRGTYGHVYKAK-RKDGKDDKDYALKQIEGTGISMSACR-EIALLRELKHPNVISLQKVFlsHADRKVWLLFDYAEHDL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMI-------LSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADP-FPQVKLCDFGFARIIGEK- 580
Cdd:cd07868  103 WHIIkfhraskANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPeRGRVKIADMGFARLFNSPl 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 581 ---SFRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFN-EDEDI-------HDQI 636
Cdd:cd07868  183 kplADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPIFHcRQEDIktsnpyhHDQL 250
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
440-682 1.44e-16

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 79.78  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 440 VYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRnevaiLQNlhHPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSEkg 519
Cdd:cd13976    9 LYRCVDIHTGEELVCKVVPVPECHAVLRAYFR-----LPS--HPNISGVHEVIAGETKAYVFFERDHGDLHSYVRSRK-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 520 RLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARII-GEKSFRRSVVGTPAYLAPEVL 598
Cdd:cd13976   80 RLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER-TKLRLESLEDAVILeGEDDSLSDKHGCPAYVSPEIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 599 RNKG-YN-RSLDMWSVGVIIYVSLSGTFPFNEDE--DIHDQIQNAAFMYPpnpwKEISHEAIDLINNLLQVKMRKRYSVD 674
Cdd:cd13976  159 NSGAtYSgKAADVWSLGVILYTMLVGRYPFHDSEpaSLFAKIRRGQFAIP----ETLSPRARCLIRSLLRREPSERLTAE 234

                 ....*...
gi 568979055 675 KTLSHPWL 682
Cdd:cd13976  235 DILLHPWL 242
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
425-617 1.91e-16

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 80.11  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 425 QIFPDEVLGSGQFGIVYGGKHRKTGR---DVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVV 501
Cdd:cd05033    5 YVTIEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTL-KSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKlhgdmleMILSSEKGRLPEHITKFLITQILVALR-------HLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA 574
Cdd:cd05033   84 TEY-------MENGSLDKFLRENDGKFTVTQLVGMLRgiasgmkYLSEMNYVHRDLAARNILVNSDL---VCKVSDFGLS 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 575 RIIGEKSFRRSVVG--TPA-YLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05033  154 RRLEDSEATYTTKGgkIPIrWTAPEAIAYRKFTSASDVWSFGIVMW 199
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
114-161 1.97e-16

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410360  Cd Length: 52  Bit Score: 73.45  E-value: 1.97e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPN 161
Cdd:cd20810    3 HSFELTTFKEPTTCSVCKKLLKGLFFQGYKCSVCGAAVHKECIAKVKR 50
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
432-626 2.74e-16

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 79.70  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRdVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGDML 510
Cdd:cd05072   15 LGAGQFGEVWMGYYNNSTK-VAVK---TLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMaKGSLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKGR--LPEHITkfLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKSF--RRSV 586
Cdd:cd05072   91 DFLKSDEGGKvlLPKLID--FSAQIAEGMAYIERKNYIHRDLRAANVLVSES---LMCKIADFGLARVIEDNEYtaREGA 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568979055 587 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPF 626
Cdd:cd05072  166 KFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY 206
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
432-617 4.29e-16

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 78.99  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTgRDVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNLE--CMFETPerVFVVMEKL-HGD 508
Cdd:cd05068   16 LGSGQFGEVWEGLWNNT-TPVAVK---TLKPGTMDPEDFLREAQIMKKLRHPKLIQLYavCTLEEP--IYIITELMkHGS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMiLSSEKG--RLPEHITkfLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSV 586
Cdd:cd05068   90 LLEY-LQGKGRslQLPQLID--MAAQVASGMAYLESQNYIHRDLAARNVLVGENN---ICKVADFGLARVIKVEDEYEAR 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568979055 587 VGTP---AYLAPEVLRnkgYNR---SLDMWSVGVIIY 617
Cdd:cd05068  164 EGAKfpiKWTAPEAAN---YNRfsiKSDVWSFGILLT 197
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
435-626 4.61e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 78.90  E-value: 4.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 435 GQFGIVYGGKHRKTGRDVAIKIIDKLRF-PTKQESQLRnevailqnLHHPGVVNLECMFETPERVFVVMEKLHG-DMLEM 512
Cdd:cd13995   15 GAFGKVYLAQDTKTKKRMACKLIPVEQFkPSDVEIQAC--------FRHENIAELYGALLWEETVHLFMEAGEGgSVLEK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 513 ILSSekGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfpQVKLCDFGFA-RIIGEKSFRRSVVGTPA 591
Cdd:cd13995   87 LESC--GPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMST----KAVLVDFGLSvQMTEDVYVPKDLRGTEI 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568979055 592 YLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd13995  161 YMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPW 195
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
432-617 4.66e-16

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 78.48  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTgRDVAIKIidkLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGDML 510
Cdd:cd05034    3 LGAGQFGEVWMGVWNGT-TKVAVKT---LKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMsKGSLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMiLSSEKGR---LPEHITkfLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKSFR-RSV 586
Cdd:cd05034   79 DY-LRTGEGRalrLPQLID--MAAQIASGMAYLESRNYIHRDLAARNILVGEN---NVCKVADFGLARLIEDDEYTaREG 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568979055 587 VGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05034  153 AKFPiKWTAPEAALYGRFTIKSDVWSFGILLY 184
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
430-678 4.74e-16

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 80.56  E-value: 4.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKII-DKLRFptkqESQLRNEVAILQNLHHP---GVVNLECMFET---PERVFVVM 502
Cdd:cd14224   71 KVIGKGSFGQVVKAYDHKTHQHVALKMVrNEKRF----HRQAAEEIRILEHLKKQdkdNTMNVIHMLESftfRNHICMTF 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfPQVKLCDFGFARIIGEKSF 582
Cdd:cd14224  147 ELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGR-SGIKVIDFGSSCYEHQRIY 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 583 rrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIqnAAFM----YPPNPWKEISHEAIDL 658
Cdd:cd14224  226 --TYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG-YPLFPGEDEGDQL--ACMIellgMPPQKLLETSKRAKNF 300
                        250       260
                 ....*....|....*....|
gi 568979055 659 INNllqvKMRKRYSVDKTLS 678
Cdd:cd14224  301 ISS----KGYPRYCTVTTLP 316
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
113-163 5.54e-16

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 72.48  E-value: 5.54e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20828    5 PHNFEPHSFVTPTNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQC 55
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
425-636 9.69e-16

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 78.18  E-value: 9.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 425 QIFPDEVLGSGQFGIVYGGKHRKtgrDVAIKIIDkLRFPTKQESQ-LRNEVAILQNLHHPGVVnLECMFETPERVFVVME 503
Cdd:cd14151    9 QITVGQRIGSGSFGTVYKGKWHG---DVAVKMLN-VTAPTPQQLQaFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFA----RIIGE 579
Cdd:cd14151   84 WCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLAtvksRWSGS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRsVVGTPAYLAPEVLR---NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDiHDQI 636
Cdd:cd14151  161 HQFEQ-LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN-RDQI 218
PTZ00284 PTZ00284
protein kinase; Provisional
416-685 1.31e-15

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 80.01  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 416 ENVDISTV-YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKII---DKLRFPTKQESQLRNEVAILQNLHHPGVVNLECM 491
Cdd:PTZ00284 122 EDIDVSTQrFKIL--SLLGEGTFGKVVEAWDRKRKEYCAVKIVrnvPKYTRDAKIEIQFMEKVRQADPADRFPLMKIQRY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 492 FETPE-RVFVVMEKLHGDMLEMILssEKGRLPEHITKFLITQILVALRHLHFK-NIVHCDLKPENVLLASAD-------- 561
Cdd:PTZ00284 200 FQNETgHMCIVMPKYGPCLLDWIM--KHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETSDtvvdpvtn 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 562 ----PFP-QVKLCDFGFAriIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnedeDIHDQI 636
Cdd:PTZ00284 278 ralpPDPcRVRICDLGGC--CDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLY----DTHDNL 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 637 QNAAFMYP-----PNPW----------------------KEISHEA-----------------IDLINNLLQVKMRKRYS 672
Cdd:PTZ00284 352 EHLHLMEKtlgrlPSEWagrcgteearllynsagqlrpcTDPKHLAriararpvrevirddllCDLIYGLLHYDRQKRLN 431
                        330
                 ....*....|...
gi 568979055 673 VDKTLSHPWLQDY 685
Cdd:PTZ00284 432 ARQMTTHPYVLKY 444
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
418-645 1.31e-15

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 77.60  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 418 VDISTVyQIfpDEVLGSGQFGIVYGGKHRKTGRD---VAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFET 494
Cdd:cd05065    1 IDVSCV-KI--EEVIGAGEFGEVCRGRLKLPGKReifVAIKTL-KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA 574
Cdd:cd05065   77 SRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSN---LVCKVSDFGLS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 575 RIIGEKS----FRRSVVGT-PA-YLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFNE--DEDIHDQIQNAAFMYPP 645
Cdd:cd05065  154 RFLEDDTsdptYTSSLGGKiPIrWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDmsNQDVINAIEQDYRLPPP 233
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
114-163 1.63e-15

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 71.22  E-value: 1.63e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20836    1 HKFKVHTYSSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
113-165 1.71e-15

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 71.59  E-value: 1.71e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20839    7 PHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 59
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
430-675 2.26e-15

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 76.71  E-value: 2.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKTC-RETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPehiTKFLITQILVA---LRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFAR--IIGEKSFRR 584
Cdd:cd05041   80 LLTFLRKKGARLT---VKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLVGENN---VLKISDFGMSReeEDGEYTVSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 585 SVVGTP-AYLAPEVLRNKGYNRSLDMWSVGVI---IYVSLSGTFPFNEDEDIHDQIQNAAFMYPPnpwKEISHEAIDLIN 660
Cdd:cd05041  154 GLKQIPiKWTAPEALNYGRYTSESDVWSFGILlweIFSLGATPYPGMSNQQTREQIESGYRMPAP---ELCPEAVYRLML 230
                        250
                 ....*....|....*
gi 568979055 661 NLLQVKMRKRYSVDK 675
Cdd:cd05041  231 QCWAYDPENRPSFSE 245
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
432-682 2.45e-15

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 77.75  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFG-IVYGGKHRKTGRDVAIKIIDKLRfptKQESQLRNEVAILQNLHH--PGVVNLeCM-----FETPERVFVVME 503
Cdd:cd14215   20 LGEGTFGrVVQCIDHRRGGARVALKIIKNVE---KYKEAARLEINVLEKINEkdPENKNL-CVqmfdwFDYHGHMCISFE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAD----------------PFPQVK 567
Cdd:cd14215   96 LLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyeltynlekkrdersvKSTAIR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 568 LCDFGFARIigEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNededIHDQIQNAAFM---YP 644
Cdd:cd14215  176 VVDFGSATF--DHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQ----THDNREHLAMMeriLG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 645 PNP-------------------WKEIS------------------------HEAIDLINNLLQVKMRKRYSVDKTLSHPW 681
Cdd:cd14215  250 PIPsrmirktrkqkyfyhgrldWDENTsagryvrenckplrryltseaeehHQLFDLIESMLEYEPSKRLTLAAALKHPF 329

                 .
gi 568979055 682 L 682
Cdd:cd14215  330 F 330
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
113-163 2.83e-15

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 70.42  E-value: 2.83e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20806    1 PHNFKVHTFKGPHWCDYCGNFMWGLIAQGVKCEDCGFNAHKQCSKLVPHDC 51
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
432-617 3.10e-15

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 77.60  E-value: 3.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRnEVAILQNL--HHPGVVNLE-C------------------ 490
Cdd:cd13977    8 VGRGSYGVVYEAVVRRTGARVAVKKI-RCNAPENVELALR-EFWALSSIqrQHPNVIQLEeCvlqrdglaqrmshgssks 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 491 -----MFETP---ERVF---------VVMEKLHG-DMLEMILSsekgRLPEHIT-KFLITQILVALRHLHFKNIVHCDLK 551
Cdd:cd13977   86 dlyllLVETSlkgERCFdprsacylwFVMEFCDGgDMNEYLLS----RRPDRQTnTSFMLQLSSALAFLHRNQIVHRDLK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 552 PENVLLASADPFPQVKLCDFGFARIIG------------EKSFRRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIY 617
Cdd:cd13977  162 PDNILISHKRGEPILKVADFGLSKVCSgsglnpeepanvNKHFLSSACGSDFYMAPEVWEGH-YTAKADIFALGIIIW 238
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
433-626 4.27e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 75.76  E-value: 4.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 433 GSGQFGIVYGGKHRKTGRDVAIKiidKLrfptkqeSQLRNEVAILQNLHHPGVVNLE-CMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK---KL-------LKIEKEAEILSVLSHRNIIQFYgAILEAPNYGIVTEYASYGSLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLP-EHITKFlITQILVALRHLHFK---NIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEkSFRRSVV 587
Cdd:cd14060   72 YLNSNESEEMDmDQIMTW-ATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADG---VLKICDFGASRFHSH-TTHMSLV 146
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568979055 588 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14060  147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
432-617 4.43e-15

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 75.92  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNL--ECMFETPerVFVVMEKL-HGD 508
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVK---TLKEDTMEVEEFLKEAAVMKEIKHPNLVQLlgVCTREPP--FYIITEFMpYGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFR-RSVV 587
Cdd:cd05052   89 LLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENH---LVKVADFGLSRLMTGDTYTaHAGA 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568979055 588 GTP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05052  166 KFPiKWTAPESLAYNKFSIKSDVWAFGVLLW 196
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
432-616 4.65e-15

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 76.39  E-value: 4.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPER--VFVVMEKLHGDM 509
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQlmLYIQMQLCELSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMIlsSEKGRLP---------------EHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASADpfPQVKLCDFGFA 574
Cdd:cd14049   94 WDWI--VERNKRPceeefksapytpvdvDVTTKIL-QQLLEGVTYIHSMGIVHRDLKPRNIFLHGSD--IHVRIGDFGLA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 575 --RII--GEKSFRRSV---------VGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14049  169 cpDILqdGNDSTTMSRlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVIL 223
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
113-165 4.74e-15

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 70.47  E-value: 4.74e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20840   10 PHALNVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSG 62
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
420-637 5.20e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 77.44  E-value: 5.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIidkLRFPTKQESQLRNEVAILQNLHHPG------VVNLECmFE 493
Cdd:cd14228   13 MTNSYEVL--EFLGRGTFGQVAKCWKRSTKEIVAIKI---LKNHPSYARQGQIEVSILSRLSSENadeynfVRSYEC-FQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 494 TPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasADPFPQ---VKLCD 570
Cdd:cd14228   87 HKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIML--VDPVRQpyrVKVID 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 571 FGFARIIgEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIQ 637
Cdd:cd14228  165 FGSASHV-SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASEYDQIR 229
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
432-628 5.93e-15

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 75.46  E-value: 5.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHR-KTGR--DVAIKIIDKLRFPTKQESQLRnEVAILQNLHHPGVVNLECMFETPErVFVVMEKL-HG 507
Cdd:cd05060    3 LGHGNFGSVRKGVYLmKSGKevEVAVKTLKQEHEKAGKKEFLR-EASVMAQLDHPCIVRLIGVCKGEP-LMLVMELApLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKS--FRRS 585
Cdd:cd05060   81 PLLKYLK--KRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH---QAKISDFGMSRALGAGSdyYRAT 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 586 VVGT-P-AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFNE 628
Cdd:cd05060  156 TAGRwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGE 201
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
430-670 6.45e-15

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 75.61  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPerVFVVMEKLHGDM 509
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKgrLPEHITKFLITQILVALRHLHFKN--IVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKS----FR 583
Cdd:cd14025   80 LEKLLASEP--LPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILL---DAHYHVKISDFGLAKWNGLSHshdlSR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 584 RSVVGTPAYLAPEVLR--NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDI-HDQIQNAAFMYP-----PNPWKEISHEA 655
Cdd:cd14025  155 DGLRGTIAYLPPERFKekNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNIlHIMVKVVKGHRPslspiPRQRPSECQQM 234
                        250
                 ....*....|....*
gi 568979055 656 IDLINNLLQVKMRKR 670
Cdd:cd14025  235 ICLMKRCWDQDPRKR 249
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
420-637 8.04e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 76.67  E-value: 8.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 420 ISTVYQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKIidkLRFPTKQESQLRNEVAILQNLHHPG------VVNLECmFE 493
Cdd:cd14227   13 MTNTYEVL--EFLGRGTFGQVVKCWKRGTNEIVAIKI---LKNHPSYARQGQIEVSILARLSTESaddynfVRAYEC-FQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 494 TPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFP-QVKLCDFG 572
Cdd:cd14227   87 HKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPyRVKVIDFG 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 573 FARIIgEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGtFPFNEDEDIHDQIQ 637
Cdd:cd14227  167 SASHV-SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASEYDQIR 229
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
432-633 8.28e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 75.23  E-value: 8.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRdVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLH-GDML 510
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQGL-VVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEkGNLM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMIlssEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFA------RIIGEKSFRR 584
Cdd:cd14027   80 HVL---KKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLAsfkmwsKLTKEEHNEQ 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979055 585 SVV--------GTPAYLAPEVLRN---KGYNRSlDMWSVGVIIYVSLSGTFPF----NEDEDIH 633
Cdd:cd14027  154 REVdgtakknaGTLYYMAPEHLNDvnaKPTEKS-DVYSFAIVLWAIFANKEPYenaiNEDQIIM 216
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
465-680 9.39e-15

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 74.70  E-value: 9.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 465 KQESQLRNEVAILQNLHHPGVVNLECMFETPE------RVFVVMEKLHGDMLEMILSSEkGRLPEHITKFLITQILVALR 538
Cdd:cd14012   40 KQIQLLEKELESLKKLRHPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSELLDSV-GSVPLDTARRWTLQLLEALE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 539 HLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRS--VVGTPAYLAPEVLR-NKGYNRSLDMWSVGVI 615
Cdd:cd14012  119 YLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLDMCSRGSldEFKQTYWLPPELAQgSKSPTRKTDVWDLGLL 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 616 IYVSLSGTFPFNEDEDIHdqiqnaAFMYPPnpwkEISHEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd14012  199 FLQMLFGLDVLEKYTSPN------PVLVSL----DLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
430-617 1.05e-14

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 74.69  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRktGRDVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGD 508
Cdd:cd05039   12 ELIGKGEFGDVMLGDYR--GQKVAVK---CLKDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMaKGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSseKGRLpeHITKflITQILVAL------RHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARiigEKSF 582
Cdd:cd05039   87 LVDYLRS--RGRA--VITR--KDQLGFALdvcegmEYLESKKFVHRDLAARNVLVSEDN---VAKVSDFGLAK---EASS 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568979055 583 RRSVVGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05039  155 NQDGGKLPiKWTAPEALREKKFSTKSDVWSFGILLW 190
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
430-629 1.12e-14

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 75.08  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGK-HRktgrDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNL--ECMfeTPERVFVVMEKLH 506
Cdd:cd14063    6 EVIGKGRFGRVHRGRwHG----DVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFmgACM--DPPHLAIVTSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 507 GDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfpQVKLCDFGFARIIGEKSFRRS- 585
Cdd:cd14063   80 GRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG----RVVITDFGLFSLSGLLQPGRRe 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 586 -----VVGTPAYLAPEVLRN----------KGYNRSLDMWSVGVIIYVSLSGTFPFNED 629
Cdd:cd14063  156 dtlviPNGWLCYLAPEIIRAlspdldfeesLPFTKASDVYAFGTVWYELLAGRWPFKEQ 214
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
432-616 1.18e-14

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 74.98  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiiDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLE 511
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 512 MILSSEKGRLPEHITKFlITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE------------ 579
Cdd:cd14222   79 DFLRADDPFPWQQKVSF-AKGIASGMAYLHSMSIIHRDLNSHNCLIKLDK---TVVVADFGLSRLIVEekkkpppdkptt 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 580 --KSFRR-------SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd14222  155 kkRTLRKndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVL 200
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
429-627 1.27e-14

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 75.44  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRDVAIKI-IDKLRFPT--KQESQLRNEVAILQNLHHPGVVNLE--CMFETPERVFVVME 503
Cdd:cd05108   12 IKVLGSGAFGTVYKGLWIPEGEKVKIPVaIKELREATspKANKEILDEAYVMASVDNPHVCRLLgiCLTSTVQLITQLMP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 klHGDMLEMILSSEKGRLPEHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASadpfPQ-VKLCDFGFARIIG--EK 580
Cdd:cd05108   92 --FGCLLDYVREHKDNIGSQYLLNWCV-QIAKGMNYLEDRRLVHRDLAARNVLVKT----PQhVKITDFGLAKLLGaeEK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 581 SFRRSVVGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN 627
Cdd:cd05108  165 EYHAEGGKVPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYD 213
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
113-165 1.29e-14

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 68.43  E-value: 1.29e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20792    1 GHKFVATFFKQPTFCSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKCPG 53
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
432-611 1.35e-14

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 74.60  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRDVAIKiidkLRFPTKQESQLRNEVAILQNLH-HPGVVNLECMFETPERVFVVMEKLHGDML 510
Cdd:cd14017    8 IGGGGFGEIYKVRDVVDGEEVAMK----VESKSQPKQVLKMEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMTLLGPNLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL--ASADPFpQVKLCDFGFARIIGEKS------- 581
Cdd:cd14017   84 ELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrGPSDER-TVYILDFGLARQYTNKDgeverpp 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568979055 582 -----FRrsvvGTPAYLAPEVLRNKGYNRSLDMWS 611
Cdd:cd14017  163 rnaagFR----GTVRYASVNAHRNKEQGRRDDLWS 193
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
482-682 1.53e-14

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 73.76  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 482 HPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSEkgRLPEHITKFLITQILVALRHLHFKNIVHCDLKpenvllasad 561
Cdd:cd14024   44 HEGVCSVLEVVIGQDRAYAFFSRHYGDMHSHVRRRR--RLSEDEARGLFTQMARAVAHCHQHGVILRDLK---------- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 562 pfpqvkLCDFGFARIIGEK----SFRRSVVGT------------PAYLAPEVLRNK-GYN-RSLDMWSVGVIIYVSLSGT 623
Cdd:cd14024  112 ------LRRFVFTDELRTKlvlvNLEDSCPLNgdddsltdkhgcPAYVGPEILSSRrSYSgKAADVWSLGVCLYTMLLGR 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 624 FPFNEDED--IHDQIQNAAFMYPPNpwkeISHEAIDLINNLLQVKMRKRYSVDKTLSHPWL 682
Cdd:cd14024  186 YPFQDTEPaaLFAKIRRGAFSLPAW----LSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
432-645 1.58e-14

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 74.15  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTgRDVAIKIIdklRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL-HGDML 510
Cdd:cd05113   12 LGTGQFGVVKYGKWRGQ-YDVAIKMI---KEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMaNGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 511 EMILSSEKGRLPEHITKfLITQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARIIGEKSFRRSvVGTP 590
Cdd:cd05113   88 NYLREMRKRFQTQQLLE-MCKDVCEAMEYLESKQFLHRDLAARNCLV---NDQGVVKVSDFGLSRYVLDDEYTSS-VGSK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979055 591 ---AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN--EDEDIHDQIQNAAFMYPP 645
Cdd:cd05113  163 fpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYErfTNSETVEHVSQGLRLYRP 223
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
426-684 1.67e-14

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 74.24  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 426 IFPDEVLGSGQFGIVYGGKHRKTGRD---VAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVM 502
Cdd:cd05063    7 ITKQKVIGAGEFGEVFRGILKMPGRKevaVAIKTL-KPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIIT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIG---E 579
Cdd:cd05063   86 EYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSN---LECKVSDFGLSRVLEddpE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 580 KSFRRSVVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFnededihdqiqnaafmyppnpWKEISHEAID 657
Cdd:cd05063  163 GTYTTSGGKIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPY---------------------WDMSNHEVMK 221
                        250       260
                 ....*....|....*....|....*....
gi 568979055 658 LINN--LLQVKMRKRYSVDKTLSHPWLQD 684
Cdd:cd05063  222 AINDgfRLPAPMDCPSAVYQLMLQCWQQD 250
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
432-670 1.70e-14

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 74.23  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGG--KHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETpERVFVVMEKLHGDM 509
Cdd:cd05116    3 LGSGNFGTVKKGyyQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEA-ESWMLVMEMAELGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKfLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIG--EKSFRRSVV 587
Cdd:cd05116   82 LNKFLQKNRHVTEKNITE-LVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH---YAKISDFGLSKALRadENYYKAQTH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 588 GT-PA-YLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN--EDEDIHDQIQNAAFMYPPnpwKEISHEAIDLINNL 662
Cdd:cd05116  158 GKwPVkWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKgmKGNEVTQMIEKGERMECP---AGCPPEMYDLMKLC 234

                 ....*...
gi 568979055 663 LQVKMRKR 670
Cdd:cd05116  235 WTYDVDER 242
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
446-679 1.92e-14

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 74.75  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 446 RKTGRD--VAIKI--IDKLRFPTKQESQ----LRNEVAILQNLH-HPGVVNLECMF-----ETPE-------------RV 498
Cdd:cd13974   18 RKEGTDdfYTLKIltLEEKGEETQEDRQgkmlLHTEYSLLSLLHdQDGVVHHHGLFqdracEIKEdkssnvytgrvrkRL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 499 FVVMEKLH--------GDM--LEMILSSEKgRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPfpQVKL 568
Cdd:cd13974   98 CLVLDCLCahdfsdktADLinLQHYVIREK-RLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR--KITI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 569 CDFGFAR-IIGEKSFRRSVVGTPAYLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPF--NEDEDIHDQIQNAAFMYP 644
Cdd:cd13974  175 TNFCLGKhLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFydSIPQELFRKIKAAEYTIP 254
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568979055 645 PNpwKEISHEAIDLINNLLQVKMRKRYSVDKTLSH 679
Cdd:cd13974  255 ED--GRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
430-617 2.31e-14

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 74.72  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRD----VAIKIIDKLRFPtKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd05110   13 KVLGSGAFGTVYKGIWVPEGETvkipVAIKILNETTGP-KANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMIlSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARII--GEKSFR 583
Cdd:cd05110   92 HGCLLDYV-HEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPN---HVKITDFGLARLLegDEKEYN 167
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568979055 584 RSVVGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05110  168 ADGGKMPiKWMALECIHYRKFTHQSDVWSYGVTIW 202
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
430-646 2.85e-14

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 73.43  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVKSC-RETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARiiGEKSFRRSVVG- 588
Cdd:cd05084   81 FLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN---VLKISDFGMSR--EEEDGVYAATGg 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 589 ---TPA-YLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN--EDEDIHDQIQNAAFMYPPN 646
Cdd:cd05084  156 mkqIPVkWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYAnlSNQQTREAVEQGVRLPCPE 220
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
432-617 3.18e-14

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 73.53  E-value: 3.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGG-----KHRKTGRDVAIKIIdklrFPTKQESQLR---NEVAILQNLHHPGVVNLECMFETPERVFVVME 503
Cdd:cd05032   14 LGQGSFGMVYEGlakgvVKGEPETRVAIKTV----NENASMRERIeflNEASVMKEFNCHHVVRLLGVVSTGQPTLVVME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KL-HGDmLEMILSSEK-------GRLPEHITKFL--ITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGF 573
Cdd:cd05032   90 LMaKGD-LKSYLRSRRpeaennpGLGPPTLQKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDL---TVKIGDFGM 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 574 ARIIGEKSFRRSvvGTPAYL-----APEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05032  166 TRDIYETDYYRK--GGKGLLpvrwmAPESLKDGVFTTKSDVWSFGVVLW 212
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
430-616 3.28e-14

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 73.38  E-value: 3.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTgRDVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFeTPERVFVVMEKL-HGD 508
Cdd:cd05067   13 ERLGAGQFGEVWMGYYNGH-TKVAIK---SLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEYMeNGS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLPehITKFL--ITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARII--GEKSFRR 584
Cdd:cd05067   88 LVDFLKTPSGIKLT--INKLLdmAAQIAEGMAFIEERNYIHRDLRAANILVSDT---LSCKIADFGLARLIedNEYTARE 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568979055 585 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 616
Cdd:cd05067  163 GAKFPIKWTAPEAINYGTFTIKSDVWSFGILL 194
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
432-682 4.37e-14

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 74.12  E-value: 4.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFG-IVYGGKHRKTGRDVAIKIIDKLrfpTKQESQLRNEVAILQNLHHP------GVVNLECMFETPERVFVVMEK 504
Cdd:cd14213   20 LGEGAFGkVVECIDHKMGGMHVAVKIVKNV---DRYREAARSEIQVLEHLNTTdpnstfRCVQMLEWFDHHGHVCIVFEL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 LHGDMLEMIlsSEKGRLPEHI--TKFLITQILVALRHLHFKNIVHCDLKPENVLLASAD----------------PFPQV 566
Cdd:cd14213   97 LGLSTYDFI--KENSFLPFPIdhIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynpkmkrdertlKNPDI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 567 KLCDFGFARIigEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNededIHDQIQNAAFM---Y 643
Cdd:cd14213  175 KVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQ----THDSKEHLAMMeriL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 644 PPNP-------------------WKEIS------------------------HEAIDLINNLLQVKMRKRYSVDKTLSHP 680
Cdd:cd14213  249 GPLPkhmiqktrkrkyfhhdqldWDEHSsagryvrrrckplkefmlsqdvdhEQLFDLIQKMLEYDPAKRITLDEALKHP 328

                 ..
gi 568979055 681 WL 682
Cdd:cd14213  329 FF 330
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
113-163 4.68e-14

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410358  Cd Length: 52  Bit Score: 66.98  E-value: 4.68e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20808    1 KHNFQETTYFKPTFCDHCTGLLWGLIKQGYKCKDCGINCHKHCKDLVVVEC 51
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
430-645 4.85e-14

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 72.73  E-value: 4.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHR-KTgrDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGD 508
Cdd:cd05085    2 ELLGKGNFGEVYKGTLKdKT--PVAVKTC-KEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKGRLP-EHITKFLItQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRS-V 586
Cdd:cd05085   79 DFLSFLRKKKDELKtKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENN---ALKISDFGMSRQEDDGVYSSSgL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 587 VGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN--EDEDIHDQIQNAAFMYPP 645
Cdd:cd05085  155 KQIPiKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPgmTNQQAREQVEKGYRMSAP 217
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
432-626 8.00e-14

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 72.18  E-value: 8.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRktGRDVAIKIIDKLRFPTKQESQLR-NEVAILQNLHHPGVVNL--ECMfETPERVFVVMEKLHGD 508
Cdd:cd14064    1 IGSGSFGKVYKGRCR--NKIVAIKRYRANTYCSKSDVDMFcREVSILCRLNHPCVIQFvgACL-DDPSQFAIVTQYVSGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 509 MLEMILSSEKgRLPEHITKfLITQILVA--LRHLH--FKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARII---GEKS 581
Cdd:cd14064   78 SLFSLLHEQK-RVIDLQSK-LIIAVDVAkgMEYLHnlTQPIIHRDLNSHNILL---YEDGHAVVADFGESRFLqslDEDN 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568979055 582 FRRSvVGTPAYLAPEVL-RNKGYNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14064  153 MTKQ-PGNLRWMAPEVFtQCTRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
430-646 1.11e-13

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 72.27  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRK---TGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNL--ECMFETPERV---FVV 501
Cdd:cd14204   13 KVLGEGEFGSVMEGELQQpdgTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLlgVCLEVGSQRIpkpMVI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 502 MEKL-HGDMLEMILSSEKGRLPEHI-----TKFLItQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFAR 575
Cdd:cd14204   93 LPFMkYGDLHSFLLRSRLGSGPQHVplqtlLKFMI-DIALGMEYLSSRNFLHRDLAARNCMLRDD---MTVCVADFGLSK 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 576 IIGEKSFRRS--VVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPFN--EDEDIHDQIQNAAFMYPPN 646
Cdd:cd14204  169 KIYSGDYYRQgrIAKMPVkWIAVESLADRVYTVKSDVWAFGVTMWeIATRGMTPYPgvQNHEIYDYLLHGHRLKQPE 245
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
431-617 1.54e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 71.85  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIV----YGGKHRKTGRDVAIKiidKLRFPTKQESQ-LRNEVAILQNLHHPGVVNLECMFETPER--VFVVME 503
Cdd:cd05081   11 QLGKGNFGSVelcrYDPLGDNTGALVAVK---QLQHSGPDQQRdFQREIQILKALHSDFIVKYRGVSYGPGRrsLRLVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRLpEHITKFLI-TQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSf 582
Cdd:cd05081   88 YLPSGCLRDFLQRHRARL-DASRLLLYsSQICKGMEYLGSRRCVHRDLAARNILVESEA---HVKIADFGLAKLLPLDK- 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 583 RRSVVGTPA-----YLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05081  163 DYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLY 202
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
114-165 2.49e-13

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 64.66  E-value: 2.49e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPnNCLG 165
Cdd:cd20817    1 HSFQEHTFKKPTFCDVCKELLVGLSKQGLRCKNCKMNVHHKCQEGVP-DCSG 51
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
455-627 2.63e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 73.19  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 455 KIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSE---KGRLPEHITKFLIT 531
Cdd:PHA03210 195 LIAKRVKAGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMITQKYDFDLYSFMYDEAfdwKDRPLLKQTRAIMK 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 532 QILVALRHLHFKNIVHCDLKPENVLLaSADPfpQVKLCDFGFARIIGEK--SFRRSVVGTPAYLAPEVLRNKGYNRSLDM 609
Cdd:PHA03210 275 QLLCAVEYIHDKKLIHRDIKLENIFL-NCDG--KIVLGDFGTAMPFEKEreAFDYGWVGTVATNSPEILAGDGYCEITDI 351
                        170
                 ....*....|....*....
gi 568979055 610 WSVGVIIYVSLSGTF-PFN 627
Cdd:PHA03210 352 WSCGLILLDMLSHDFcPIG 370
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
429-626 2.71e-13

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 70.83  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTGRdVAIKiidKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFeTPERVFVVMEKLH-G 507
Cdd:cd05073   16 EKKLGAGQFGEVWMATYNKHTK-VAVK---TMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVV-TKEPIYIITEFMAkG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 508 DMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIGEKSF--RRS 585
Cdd:cd05073   91 SLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSAS---LVCKIADFGLARVIEDNEYtaREG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568979055 586 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPF 626
Cdd:cd05073  168 AKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY 209
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
430-617 4.11e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 70.43  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIV----YGGKHRKTGRDVAIKiidKLRFPTkqESQLRN---EVAILQNLHHPGVVNLE--CMFETPERVFV 500
Cdd:cd14205   10 QQLGKGNFGSVemcrYDPLQDNTGEVVAVK---KLQHST--EEHLRDferEIEILKSLQHDNIVKYKgvCYSAGRRNLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 501 VMEKLHGDMLEMILSSEKGRLpEHITKFLIT-QILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGE 579
Cdd:cd14205   85 IMEYLPYGSLRDYLQKHKERI-DHIKLLQYTsQICKGMEYLGTKRYIHRDLATRNILVENEN---RVKIGDFGLTKVLPQ 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568979055 580 -KSFRRsvVGTPA-----YLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd14205  161 dKEYYK--VKEPGespifWYAPESLTESKFSVASDVWSFGVVLY 202
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
432-617 4.61e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 70.34  E-value: 4.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIV----YGGKHRKTGRDVAIKIIDklrfPTKQESQ---LRNEVAILQNLHHPGVVNLE--CMFETPERVFVVM 502
Cdd:cd05079   12 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLK----PESGGNHiadLKKEIEILRNLYHENIVKYKgiCTEDGGNGIKLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 503 EKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSF 582
Cdd:cd05079   88 EFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGLTKAIETDKE 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568979055 583 RRSV---VGTPAY-LAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05079  165 YYTVkddLDSPVFwYAPECLIQSKFYIASDVWSFGVTLY 203
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
430-645 4.84e-13

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 69.90  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHrkTGRDVAIKIIdKLRFpTKQesQLRNEVAILQNLHHPGVVNLECMFeTPERVFVVMEKLHGDM 509
Cdd:cd05083   12 EIIGEGEFGAVLQGEY--MGQKVAVKNI-KCDV-TAQ--AFLEETAVMTKLQHKNLVRLLGVI-LHNGLYIVMELMSKGN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSeKGRLPEHITKFLITQILVA--LRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSFRRS 585
Cdd:cd05083   85 LVNFLRS-RGRALVPVIQLLQFSLDVAegMEYLESKKLVHRDLAARNILVSEDG---VAKISDFGLAKVgsMGVDNSRLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 586 VVGTpaylAPEVLRNKGYNRSLDMWSVGVIIYVSLS---GTFPFNEDEDIHDQIQNAAFMYPP 645
Cdd:cd05083  161 VKWT----APEALKNKKFSSKSDVWSYGVLLWEVFSygrAPYPKMSVKEVKEAVEKGYRMEPP 219
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
114-163 5.44e-13

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 64.27  E-value: 5.44e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20864    3 HQFVVKSFTTPTKCNQCTSLMVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
432-626 5.63e-13

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 69.51  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRdVAIKIIdklRFPTKQESQLRNEVAILQNLHHPGVVNLE--CMFETPerVFVVMEKLHGDM 509
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQYK-VAIKAI---REGAMSEEDFIEEAKVMMKLTHPKLVQLYgvCTQQKP--IYIVTEFMENGC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSFRRSVVGT 589
Cdd:cd05114   86 LLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTG---VVKVSDFGMTRYVLDDQYTSSSGAK 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568979055 590 -PA-YLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPF 626
Cdd:cd05114  163 fPVkWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPF 202
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
114-156 6.68e-13

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 63.42  E-value: 6.68e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCA 156
Cdd:cd20830    1 HRFVEQSFSTLQWCDKCGKFLFGLVHQGLQCQDCGLVCHRTCA 43
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
432-617 6.89e-13

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 70.00  E-value: 6.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRD-----VAIKIIDKlRFPTKQESQLRNEVAILQ--NLHHpgVVNLECMFETPERVFVVMEK 504
Cdd:cd05061   14 LGQGSFGMVYEGNARDIIKGeaetrVAVKTVNE-SASLRERIEFLNEASVMKgfTCHH--VVRLLGVVSKGQPTLVVMEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 505 L-HGDMLEMILS------SEKGRLPEHITKF--LITQILVALRHLHFKNIVHCDLKPENVLLAsaDPFpQVKLCDFGFAR 575
Cdd:cd05061   91 MaHGDLKSYLRSlrpeaeNNPGRPPPTLQEMiqMAAEIADGMAYLNAKKFVHRDLAARNCMVA--HDF-TVKIGDFGMTR 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568979055 576 IIGEKSF-RRSVVGT-PA-YLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05061  168 DIYETDYyRKGGKGLlPVrWMAPESLKDGVFTTSSDMWSFGVVLW 212
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
432-623 1.24e-12

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 68.67  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVY-----GGKHRktgrdVAIKIIdklrFPT--KQESQLRNEVAILQNL-HHPGVVNLE---------CMFET 494
Cdd:cd13975    8 LGRGQYGVVYacdswGGHFP-----CALKSV----VPPddKHWNDLALEFHYTRSLpKHERIVSLHgsvidysygGGSSI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 495 PerVFVVMEKLHGDMLEMIlsseKGRLPehitkfLITQILVAL------RHLHFKNIVHCDLKPENVLLASADpfpQVKL 568
Cdd:cd13975   79 A--VLLIMERLHRDLYTGI----KAGLS------LEERLQIALdvvegiRFLHSQGLVHRDIKLKNVLLDKKN---RAKI 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568979055 569 CDFGFARiiGEKSFRRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIYVSLSGT 623
Cdd:cd13975  144 TDLGFCK--PEAMMSGSIVGTPIHMAPELFSGK-YDNSVDVYAFGILFWYLCAGH 195
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
429-645 1.34e-12

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 68.74  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYGGKHRKTG-RD--VAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL 505
Cdd:cd05066    9 EKVIGAGEFGEVCSGRLKLPGkREipVAIKTL-KAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRlpehitkFLITQILVALR-------HLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFARIIG 578
Cdd:cd05066   88 ENGSLDAFLRKHDGQ-------FTVIQLVGMLRgiasgmkYLSDMGYVHRDLAARNILVNSN---LVCKVSDFGLSRVLE 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979055 579 ---EKSFRRSVVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFNE--DEDIHDQIQNAAFMYPP 645
Cdd:cd05066  158 ddpEAAYTTRGGKIPIrWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEmsNQDVIKAIEEGYRLPAP 231
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
114-163 1.35e-12

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 63.11  E-value: 1.35e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20800    5 HNWYACSHARPTYCNVCREALSGVTSHGLSCEVCKFKAHKRCAVKAPNNC 54
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
430-617 1.79e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 68.39  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIV----YGGKHRKTGRDVAIKIIdKLRFPTKQESQLRNEVAILQNLHHPGVVNLE-CMFETPER-VFVVME 503
Cdd:cd05080   10 RDLGEGHFGKVslycYDPTNDGTGEMVAVKAL-KADCGPQHRSGWKQEIDILKTLYHENIVKYKgCCSEQGGKsLQLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHgdmlemiLSSEKGRLPEH---ITKFLI--TQILVALRHLHFKNIVHCDLKPENVLLasaDPFPQVKLCDFGFARII- 577
Cdd:cd05080   89 YVP-------LGSLRDYLPKHsigLAQLLLfaQQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDFGLAKAVp 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568979055 578 -GEKSFRRSVVG-TPAY-LAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:cd05080  159 eGHEYYRVREDGdSPVFwYAPECLKEYKFYYASDVWSFGVTLY 201
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
431-645 1.90e-12

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 68.67  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFG-IVYGGKHRKTGRDVAIKIIDKLRFPTKQESQ---LRNEVAILQNL-HHPGVVNL--ECMFETPerVFVVME 503
Cdd:cd05055   42 TLGAGAFGkVVEATAYGLSKSDAVMKVAVKMLKPTAHSSEreaLMSELKIMSHLgNHENIVNLlgACTIGGP--ILVITE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 K-LHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARIIGEKSf 582
Cdd:cd05055  120 YcCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGK---IVKICDFGLARDIMNDS- 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 583 rRSVVGTPAYL-----APEVLRNKGYNRSLDMWSVGVIIY--VSLSGTfPFNE---DEDIHDQIQNAAFMYPP 645
Cdd:cd05055  196 -NYVVKGNARLpvkwmAPESIFNCVYTFESDVWSYGILLWeiFSLGSN-PYPGmpvDSKFYKLIKEGYRMAQP 266
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
429-628 1.91e-12

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 68.86  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 429 DEVLGSGQFGIVYG--GKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKL- 505
Cdd:cd08216    3 LYEIGKCFKGGGVVhlAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMa 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLaSADpfPQVKLCDFGFARIIGEKSFR-R 584
Cdd:cd08216   83 YGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILI-SGD--GKVVLSGLRYAYSMVKHGKRqR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568979055 585 SVVGTPAY-------LAPEVLRN--KGYNRSLDMWSVGVIIYVSLSGTFPFNE 628
Cdd:cd08216  160 VVHDFPKSseknlpwLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPFSD 212
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
121-163 2.17e-12

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 62.39  E-value: 2.17e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568979055 121 YTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20799   13 FNKPAYCNVCENMLVGLRKQGLCCTFCKYTVHERCVSRAPASC 55
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
119-163 2.17e-12

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 61.96  E-value: 2.17e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568979055 119 HSYTR----PTVCQFCKKLLkglfRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20812    3 HRFSKklfmRQTCDYCHKQM----FFGLKCKDCKYKCHKKCAKKAPPSC 47
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
430-645 3.12e-12

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 67.73  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKTGR--DVAIKIIdKLRFPTKQESQ-LRNEVAILQNLHHPGVVNL--ECMFET-----PERVF 499
Cdd:cd05075    6 KTLGEGEFGSVMEGQLNQDDSvlKVAVKTM-KIAICTRSEMEdFLSEAVCMKEFDHPNVMRLigVCLQNTesegyPSPVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 500 VVMEKLHGDMLEMILSSEKGRLP-----EHITKFLiTQILVALRHLHFKNIVHCDLKPENVLLASAdpfPQVKLCDFGFA 574
Cdd:cd05075   85 ILPFMKHGDLHSFLLYSRLGDCPvylptQMLVKFM-TDIASGMEYLSSKNFIHRDLAARNCMLNEN---MNVCVADFGLS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979055 575 RIIGEKSFRRS--VVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPFN--EDEDIHDQIQNAAFMYPP 645
Cdd:cd05075  161 KKIYNGDYYRQgrISKMPVkWIAIESLADRVYTTKSDVWSFGVTMWeIATRGQTPYPgvENSEIYDYLRQGNRLKQP 237
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
430-626 4.25e-12

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 67.34  E-value: 4.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 430 EVLGSGQFGIVYGGKHRKtgrDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDM 509
Cdd:cd14153    6 ELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 510 LEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASAdpfpQVKLCDFGFARIIG------EKSFR 583
Cdd:cd14153   83 LYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG----KVVITDFGLFTISGvlqagrREDKL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 584 RSVVGTPAYLAPEVLRNKG---------YNRSLDMWSVGVIIYVSLSGTFPF 626
Cdd:cd14153  159 RIQSGWLCHLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAREWPF 210
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
114-163 5.85e-12

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 61.20  E-value: 5.85e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLF-RQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20831    6 HTFVATHFKGGPSCAVCNKLIPGRFgKQGYQCRDCGLICHKRCHVKVETHC 56
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
432-646 5.98e-12

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 67.03  E-value: 5.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKHRKTGRD-----VAIKIIDKLrfPTKQ-ESQLRNEVAILQNLHHPGVVNL--ECMFETPErvFVVME 503
Cdd:cd05036   14 LGQGAFGEVYEGTVSGMPGDpsplqVAVKTLPEL--CSEQdEMDFLMEALIMSKFNHPNIVRCigVCFQRLPR--FILLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMILSSEKGRlPEHITKFLITQIL-----VAL--RHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARI 576
Cdd:cd05036   90 LMAGGDLKSFLRENRPR-PEQPSSLTMLDLLqlaqdVAKgcRYLEENHFIHRDIAARNCLLTCKGPGRVAKIGDFGMARD 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568979055 577 IGEKSFRRSvvGTPAYL-----APEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPF--NEDEDIHDQIQNAAFMYPPN 646
Cdd:cd05036  169 IYRADYYRK--GGKAMLpvkwmPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPYpgKSNQEVMEFVTSGGRMDPPK 244
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
431-651 6.44e-12

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 66.97  E-value: 6.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 431 VLGSGQFGIVYGGKHRKTGRDVAIKI-IDKLRFPT--KQESQLRNEVAILQNLHHPGVVNLE--CMFETPERVFVVMEkl 505
Cdd:cd05109   14 VLGSGAFGTVYKGIWIPDGENVKIPVaIKVLRENTspKANKEILDEAYVMAGVGSPYVCRLLgiCLTSTVQLVTQLMP-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 506 HGDMLEMIlSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADpfpQVKLCDFGFARI--IGEKSFR 583
Cdd:cd05109   92 YGCLLDYV-RENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPN---HVKITDFGLARLldIDETEYH 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979055 584 RSVVGTP-AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFN--EDEDIHDQIQNAAFM-YPPNPWKEI 651
Cdd:cd05109  168 ADGGKVPiKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDgiPAREIPDLLEKGERLpQPPICTIDV 240
C1_MRCKgamma cd20866
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
114-160 1.07e-11

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase gamma (MRCK gamma) and similar proteins; MRCK gamma (MRCKG), also called Cdc42-binding protein kinase gamma, DMPK-like gamma, myotonic dystrophy protein kinase-like gamma, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed in heart and skeletal muscles. It may act as a downstream effector of Cdc42 in cytoskeletal reorganization and contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410416  Cd Length: 52  Bit Score: 60.15  E-value: 1.07e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVP 160
Cdd:cd20866    1 HTFKPKTFTSPTKCLRCTSLMVGLVRQGLACEACNYVCHVSCAEGAP 47
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
424-707 1.10e-11

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 66.96  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 424 YQIFPDevLGSGQFG-IVYGGKHRKTGRDVAIKIIdklRFPTKQESQLRNEVAILQNLHHPGVVN------LECMFETPE 496
Cdd:cd14214   15 YEIVGD--LGEGTFGkVVECLDHARGKSQVALKII---RNVGKYREAARLEINVLKKIKEKDKENkflcvlMSDWFNFHG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 497 RVFVVMEKLHGDMLEMIlsSEKGRLPEHIT--KFLITQILVALRHLHFKNIVHCDLKPENVLLASAD------------- 561
Cdd:cd14214   90 HMCIAFELLGKNTFEFL--KENNFQPYPLPhiRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtlyneskscee 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 562 ---PFPQVKLCDFGFARIigEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDED------- 631
Cdd:cd14214  168 ksvKNTSIRVADFGSATF--DHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENrehlvmm 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 632 -----------IHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVkmrKRYSVDKTLSHPWLQDyqtwLDLRELECRIGE 700
Cdd:cd14214  246 ekilgpipshmIHRTRKQKYFYKGSLVWDENSSDGRYVSENCKPL---MSYMLGDSLEHTQLFD----LLRRMLEFDPAL 318

                 ....*..
gi 568979055 701 RYITHES 707
Cdd:cd14214  319 RITLKEA 325
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
113-164 1.22e-11

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 60.09  E-value: 1.22e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKGlfrQGLQCKDCRFNCHKRCAPKVPNNCL 164
Cdd:cd20826    2 SHSFKEKSFRKPRTCDVCKQIIWN---EGSSCRVCKYACHRKCEPKVTAACS 50
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
472-617 1.86e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 66.84  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 472 NEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDmLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLK 551
Cdd:PHA03211 209 HEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRSD-LYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIK 287
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568979055 552 PENVLLASADpfpQVKLCDFG---FARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 617
Cdd:PHA03211 288 TENVLVNGPE---DICLGDFGaacFARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1-31 1.87e-11

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 59.59  E-value: 1.87e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20838   22 LLYGLYKQGLQCKVCKMNVHKRCQKNVANNC 52
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
114-165 2.07e-11

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 59.64  E-value: 2.07e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20834    8 HEFIAKFFRQPTFCSVCKEFLWGFNKQGYQCRQCNAAVHKKCHDKILGKCPG 59
C1_alphaCHN cd20856
protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; ...
114-163 2.62e-11

protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; Alpha-chimaerin, also called A-chimaerin, N-chimaerin (CHN), alpha-chimerin, N-chimerin (NC), or Rho GTPase-activating protein 2 (ARHGAP2), is a GTPase-activating protein (GAP) for p21-rac and a phorbol ester receptor. It is involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance. Alpha-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410406  Cd Length: 57  Bit Score: 59.31  E-value: 2.62e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20856    6 HNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDC 55
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
114-163 3.55e-11

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410435  Cd Length: 54  Bit Score: 58.82  E-value: 3.55e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20885    4 HDFQPCSLTNPTWCDLCGDFIWGLYKQCLRCTHCKYTCHLRCRDLVTLDC 53
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
432-624 3.68e-11

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 64.68  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 432 LGSGQFGIVYGGKH---RKTGRDVAIKIIDKlrfPTKQE----SQLRNEVAILQNLH-HPGVVNLEcMFETpERVFVVME 503
Cdd:cd13981    8 LGEGGYASVYLAKDddeQSDGSLVALKVEKP---PSIWEfyicDQLHSRLKNSRLREsISGAHSAH-LFQD-ESILVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 504 KLHGDMLEMI----LSSEKGrLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLL------------ASADPFPQVK 567
Cdd:cd13981   83 SSQGTLLDVVnkmkNKTGGG-MDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegENGWLSKGLK 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979055 568 LCDFGFA---RIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTF 624
Cdd:cd13981  162 LIDFGRSidmSLFPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFGKY 221
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1-31 3.77e-11

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 58.60  E-value: 3.77e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20837   20 LLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
113-163 3.84e-11

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 58.57  E-value: 3.84e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568979055 113 PHTFVIHSYTRPTVCQFCKKLLKgLFRQGLQCKDCRFNCHKRCAPKVPNNC 163
Cdd:cd20821    2 PHRFVSKTVIKPETCVVCGKRIK-FGKKALKCKDCRVVCHPDCKDKLPLPC 51
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
114-165 4.59e-11

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 58.54  E-value: 4.59e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568979055 114 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLG 165
Cdd:cd20832    2 HQFVLQHYYQVTFCNHCSGLLWGIGYQGYQCSDCEFNIHKQCIEVIEESCPG 53
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
1-33 5.39e-11

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 58.45  E-value: 5.39e-11
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20796   21 LLKGLFRQGLQCKDCKFNCHKKCAEKVPKDCTG 53
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
2-32 5.86e-10

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 55.39  E-value: 5.86e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   2 LWGLVRQGLKCEGCGLNYHKRCAFKIPNNCS 32
Cdd:cd20806   22 MWGLIAQGVKCEDCGFNAHKQCSKLVPHDCQ 52
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1-31 7.83e-10

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 54.98  E-value: 7.83e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20793   20 LLYGLVRQGLKCKDCGMNVHHRCKENVPHLC 50
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
1-33 2.22e-09

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 54.60  E-value: 2.22e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20843   31 LLKGLFRQGLQCKDCKFNCHKRCATRVPNDCLG 63
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
1-32 3.19e-09

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 53.24  E-value: 3.19e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCS 32
Cdd:cd20797   23 MLTGLMKQGVKCKNCRCNFHKRCANAPRNNCA 54
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1-33 6.98e-09

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 53.48  E-value: 6.98e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20842   54 LLKGLFRQGLQCKDCKFNCHKRCAPKVPNNCLG 86
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1-31 9.70e-09

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 51.75  E-value: 9.70e-09
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd00029   20 LIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
1-31 1.11e-08

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 51.73  E-value: 1.11e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20798   21 LLVGLVRQGLKCRDCGVNVHKKCASLLPSNC 51
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1-31 2.55e-08

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 50.52  E-value: 2.55e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568979055    1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:pfam00130  20 FLWGLGKQGLKCSWCKLNVHKRCHEKVPPEC 50
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
1-32 3.29e-08

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 50.49  E-value: 3.29e-08
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCS 32
Cdd:cd20827   21 LLWGLVKTGMRCADCGYSCHEKCLEHVPKNCT 52
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
1-31 4.50e-08

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 50.03  E-value: 4.50e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20836   20 LLYGLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
1-33 4.59e-08

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 50.01  E-value: 4.59e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20824   21 KIWGLSKKGLSCKDCGFNCHIKCELKVPPECPG 53
C1_alphaCHN cd20856
protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; ...
2-31 1.50e-07

protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; Alpha-chimaerin, also called A-chimaerin, N-chimaerin (CHN), alpha-chimerin, N-chimerin (NC), or Rho GTPase-activating protein 2 (ARHGAP2), is a GTPase-activating protein (GAP) for p21-rac and a phorbol ester receptor. It is involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance. Alpha-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410406  Cd Length: 57  Bit Score: 48.53  E-value: 1.50e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 568979055   2 LWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20856   26 MWGLIAQGVKCADCGLNVHKQCSKMVPNDC 55
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1-33 1.56e-07

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 48.39  E-value: 1.56e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20792   21 FIWGLGKQGYQCQVCRFVVHKRCHEYVVFKCPG 53
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
1-33 4.62e-07

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 47.70  E-value: 4.62e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20844   25 LLKGLFRQGMQCKDCRFNCHKRCASKVPRDCLG 57
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
2-33 1.17e-06

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 46.09  E-value: 1.17e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979055   2 LWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20830   21 LFGLVHQGLQCQDCGLVCHRTCAATGLPKCEP 52
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
1-23 1.19e-06

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410358  Cd Length: 52  Bit Score: 45.79  E-value: 1.19e-06
                         10        20
                 ....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRC 23
Cdd:cd20808   21 LLWGLIKQGYKCKDCGINCHKHC 43
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
2-31 1.28e-06

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 45.73  E-value: 1.28e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 568979055   2 LWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20809   21 MVGLVRQGLVCEVCGYACHVSCADKAPQVC 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
1-32 1.34e-06

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 45.90  E-value: 1.34e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCS 32
Cdd:cd20828   25 ILWGIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1-31 4.98e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 44.00  E-value: 4.98e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568979055     1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:smart00109  20 SIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
1-33 2.65e-05

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 41.93  E-value: 2.65e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPnNCSG 33
Cdd:cd20817   20 LLVGLSKQGLRCKNCKMNVHHKCQEGVP-DCSG 51
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
2-33 5.60e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 41.54  E-value: 5.60e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979055   2 LWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20834   28 LWGFNKQGYQCRQCNAAVHKKCHDKILGKCPG 59
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
4-31 1.10e-04

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 40.77  E-value: 1.10e-04
                         10        20
                 ....*....|....*....|....*...
gi 568979055   4 GLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20800   27 GVTSHGLSCEVCKFKAHKRCAVKAPNNC 54
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
1-31 2.11e-04

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 40.00  E-value: 2.11e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20864   22 LMVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
6-32 4.77e-04

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 38.46  E-value: 4.77e-04
                         10        20
                 ....*....|....*....|....*..
gi 568979055   6 VRQGLKCEGCGLNYHKRCAFKIPNNCS 32
Cdd:cd20812   22 MFFGLKCKDCKYKCHKKCAKKAPPSCG 48
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
1-31 1.44e-03

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 37.35  E-value: 1.44e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568979055   1 MLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 31
Cdd:cd20799   25 MLVGLRKQGLCCTFCKYTVHERCVSRAPASC 55
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
2-33 2.55e-03

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 36.58  E-value: 2.55e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979055   2 LWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSG 33
Cdd:cd20832   22 LWGIGYQGYQCSDCEFNIHKQCIEVIEESCPG 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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