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Conserved domains on  [gi|332801047|ref|NP_113652|]
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ribosomal protein S6 kinase-like 1 isoform 2 [Homo sapiens]

Protein Classification

ribosomal protein S6 kinase-like 1( domain architecture ID 10119364)

ribosomal protein S6 kinase-like 1 is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 148-539 5.92e-156

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 445.84  E-value: 5.92e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 148 EQLRGCRVVGVIEKVQLVQDPATGGTFVVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFVSEDSIFLHLEHVQGGTLWS 227
Cdd:cd05576    1 EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 228 HLLSQAHsrhsglssgstqermkaqlnphlnlltparlpsghapgqdrialepprtspnlllageapstrpqreaegept 307
Cdd:cd05576   81 YLSKFLN------------------------------------------------------------------------- 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 308 artstsgssdlpkapgghlhlqarragqnsdagpprgltwvpegagpvlggcgrGMDQSCLSADGAGRGCGRATWSVREE 387
Cdd:cd05576   88 ------------------------------------------------------DKEIHQLFADLDERLAAASRFYIPEE 113

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDW 467
Cdd:cd05576  114 CIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDW 193

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 468 WSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFF 539
Cdd:cd05576  194 WSLGALLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 48-122 3.02e-36

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


:

Pssm-ID: 239140  Cd Length: 75  Bit Score: 129.39  E-value: 3.02e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047  48 DYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRPL 122
Cdd:cd02677    1 DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLHLSRSL 75
 
Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 148-539 5.92e-156

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 445.84  E-value: 5.92e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 148 EQLRGCRVVGVIEKVQLVQDPATGGTFVVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFVSEDSIFLHLEHVQGGTLWS 227
Cdd:cd05576    1 EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 228 HLLSQAHsrhsglssgstqermkaqlnphlnlltparlpsghapgqdrialepprtspnlllageapstrpqreaegept 307
Cdd:cd05576   81 YLSKFLN------------------------------------------------------------------------- 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 308 artstsgssdlpkapgghlhlqarragqnsdagpprgltwvpegagpvlggcgrGMDQSCLSADGAGRGCGRATWSVREE 387
Cdd:cd05576   88 ------------------------------------------------------DKEIHQLFADLDERLAAASRFYIPEE 113

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDW 467
Cdd:cd05576  114 CIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDW 193

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 468 WSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFF 539
Cdd:cd05576  194 WSLGALLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 48-122 3.02e-36

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 129.39  E-value: 3.02e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047  48 DYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRPL 122
Cdd:cd02677    1 DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLHLSRSL 75
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 390-549 5.26e-30

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 120.31  E-value: 5.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 390 KQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVdnlYSAPEVGGISELTEACD 466
Cdd:PTZ00263 121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTftlCGTPE---YLAPEVIQSKGHGKAVD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 467 WWSFGSLLYELLTGmalsqsHP-----SGIQAHTQ-----LQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSH 536
Cdd:PTZ00263 198 WWTMGVLLYEFIAG------YPpffddTPFRIYEKilagrLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNH 271

                        170
                 ....*....|...
gi 332801047 537 PFFSTIQWSKLVG 549
Cdd:PTZ00263 272 PYFHGANWDKLYA 284
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 386-539 2.76e-28

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 113.39  E-value: 2.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047   386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPEVggISE 460
Cdd:smart00220  96 EDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP---GEKLTTFvgtpeYMAPEV--LLG 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047   461 L--TEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEW--------LSRPAASLLTELLQFEPTRRLGMGEggv 530
Cdd:smart00220 171 KgyGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPpfpppewdISPEAKDLIRKLLVKDPEKRLTAEE--- 247


                   ....*....
gi 332801047   531 skLKSHPFF 539
Cdd:smart00220 248 --ALQHPFF 254
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
46-120 9.12e-25

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 97.76  E-value: 9.12e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047    46 KRDYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNCHLQR 120
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 50-115 4.80e-17

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 75.27  E-value: 4.80e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047   50 LVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFN 115
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
386-522 1.21e-14

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 76.20  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNL-YSAPEVGGISEL 461
Cdd:COG0515  106 PAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGiarALGGATLTQTGTVVGTPgYMAPEQARGEPV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332801047 462 TEACDWWSFGSLLYELLTGMAL--SQSHPSGIQAHTQ----------LQLPEWLSRpaasLLTELLQFEPTRR 522
Cdd:COG0515  186 DPRSDVYSLGVTLYELLTGRPPfdGDSPAELLRAHLRepppppselrPDLPPALDA----IVLRALAKDPEER 254
Pkinase pfam00069
Protein kinase domain;
450-539 6.64e-12

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.96  E-value: 6.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047  450 YSAPEVGGISELTEACDWWSFGSLLYELLTG-MALSQSHPSGIQAHTQLQ------LPEWLSRPAASLLTELLQFEPTRR 522
Cdd:pfam00069 126 YMAPEVLGGNPYGPKVDVWSLGCILYELLTGkPPFPGINGNEIYELIIDQpyafpeLPSNLSEEAKDLLKKLLKKDPSKR 205

                          90
                  ....*....|....*..
gi 332801047  523 LGMGEggvskLKSHPFF 539
Cdd:pfam00069 206 LTATQ-----ALQHPWF 217
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
387-480 1.44e-04

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----------QWSEV---------EpQCCGEAV 446
Cdd:NF033483 107 EEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaralssttmtQTNSVlgtvhylspE-QARGGTV 185

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332801047 447 DN---LYSApevgGIselteacdwwsfgsLLYELLTG 480
Cdd:NF033483 186 DArsdIYSL----GI--------------VLYEMLTG 204
 
Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 148-539 5.92e-156

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 445.84  E-value: 5.92e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 148 EQLRGCRVVGVIEKVQLVQDPATGGTFVVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFVSEDSIFLHLEHVQGGTLWS 227
Cdd:cd05576    1 EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 228 HLLSQAHsrhsglssgstqermkaqlnphlnlltparlpsghapgqdrialepprtspnlllageapstrpqreaegept 307
Cdd:cd05576   81 YLSKFLN------------------------------------------------------------------------- 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 308 artstsgssdlpkapgghlhlqarragqnsdagpprgltwvpegagpvlggcgrGMDQSCLSADGAGRGCGRATWSVREE 387
Cdd:cd05576   88 ------------------------------------------------------DKEIHQLFADLDERLAAASRFYIPEE 113

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDW 467
Cdd:cd05576  114 CIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDW 193

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 468 WSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFF 539
Cdd:cd05576  194 WSLGALLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 386-539 1.65e-47

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: 165.77  E-value: 1.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP---QC---CGEAVdnlYSAPEVGGIS 459
Cdd:cd05123   92 EERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSdgdRTytfCGTPE---YLAPEVLLGK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHT----QLQLPEWLSRPAASLLTELLQFEPTRRLgmGEGGVSKLKS 535
Cdd:cd05123  169 GYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKilksPLKFPEYVSPEAKSLISGLLQKDPTKRL--GSGGAEEIKA 246


                 ....
gi 332801047 536 HPFF 539
Cdd:cd05123  247 HPFF 250
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 386-547 9.25e-38

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: 141.38  E-value: 9.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL-----------YSAPE 454
Cdd:cd05582   96 EEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFG--------LSKESIDHEkkaysfcgtveYMAPE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 VGGISELTEACDWWSFGSLLYELLTGMALSQSHpSGIQAHTQ-----LQLPEWLSRPAASLLTELLQFEPTRRLGMGEGG 529
Cdd:cd05582  168 VVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGK-DRKETMTMilkakLGMPQFLSPEAQSLLRALFKRNPANRLGAGPDG 246

                        170
                 ....*....|....*...
gi 332801047 530 VSKLKSHPFFSTIQWSKL 547
Cdd:cd05582  247 VEEIKRHPFFATIDWNKL 264
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 48-122 3.02e-36

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 129.39  E-value: 3.02e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047  48 DYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRPL 122
Cdd:cd02677    1 DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLHLSRSL 75
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
 386-547 1.58e-35

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: 134.63  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVdnlYSAPEVggISEL- 461
Cdd:cd05580  100 NDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTytlCGTPE---YLAPEI--ILSKg 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 -TEACDWWSFGSLLYELLTG---------MALSQSHPSGIqahtqLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVS 531
Cdd:cd05580  175 hGKAVDWWALGILIYEMLAGyppffdenpMKIYEKILEGK-----IRFPSFFDPDAKDLIKRLLVVDLTKRLGNLKNGVE 249

                        170
                 ....*....|....*.
gi 332801047 532 KLKSHPFFSTIQWSKL 547
Cdd:cd05580  250 DIKNHPWFAGIDWDAL 265
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
 386-547 1.24e-34

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: 132.89  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwseVEPQCCGEAVDNL------YSAPEVGGIS 459
Cdd:cd05592   95 EDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGM---CKENIYGENKASTfcgtpdYIAPEILKGQ 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGmalsQSHPSGIQA--------HTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVS 531
Cdd:cd05592  172 KYNQSVDWWSFGVLLYEMLIG----QSPFHGEDEdelfwsicNDTPHYPRWLTKEAASCLSLLLERNPEKRLGVPECPAG 247

                        170
                 ....*....|....*.
gi 332801047 532 KLKSHPFFSTIQWSKL 547
Cdd:cd05592  248 DIRDHPFFKTIDWDKL 263
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 385-542 1.17e-32

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: 125.97  E-value: 1.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-------CG--EavdnlYSAPEV 455
Cdd:cd05583   97 TESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGEndraysfCGtiE-----YMAPEV 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 --GGISELTEACDWWSFGSLLYELLTGMA--------LSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGM 525
Cdd:cd05583  172 vrGGSDGHDKAVDWWSLGVLTYELLTGASpftvdgerNSQSEISKRILKSHPPIPKTFSAEAKDFILKLLEKDPKKRLGA 251

                        170
                 ....*....|....*..
gi 332801047 526 GEGGVSKLKSHPFFSTI 542
Cdd:cd05583  252 GPRGAHEIKEHPFFKGL 268
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
 386-547 6.56e-32

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: 125.40  E-value: 6.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwsevepqcCGEAV--DNL---------YSAPE 454
Cdd:cd05570   95 EERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGM--------CKEGIwgGNTtstfcgtpdYIAPE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 VggISEL--TEACDWWSFGSLLYELLTGMA---------LSQShpsgIQaHTQLQLPEWLSRPAASLLTELLQFEPTRRL 523
Cdd:cd05570  167 I--LREQdyGFSVDWWALGVLLYEMLAGQSpfegddedeLFEA----IL-NDEVLYPRWLSREAVSILKGLLTKDPARRL 239

                        170       180
                 ....*....|....*....|....
gi 332801047 524 GMGEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05570  240 GCGPKGEADIKAHPFFRNIDWDKL 263
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
 386-547 1.42e-31

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: 124.44  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDN-----------LYSAPE 454
Cdd:cd05584   99 EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFG--------LCKESIHDgtvthtfcgtiEYMAPE 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 VGGISELTEACDWWSFGSLLYELLTG----MALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGV 530
Cdd:cd05584  171 ILTRSGHGKAVDWWSLGALMYDMLTGappfTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSSRLGSGPGDA 250

                        170
                 ....*....|....*..
gi 332801047 531 SKLKSHPFFSTIQWSKL 547
Cdd:cd05584  251 EEIKAHPFFRHINWDDL 267
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 386-544 1.36e-30

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: 120.40  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSE---VEPQC--CGEAVDNL----------- 449
Cdd:cd05579   92 EDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFG-LSKvglVRRQIklSIQKKSNGapekedrrivg 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 ---YSAPEVGGISELTEACDWWSFGSLLYELLTGMA-LSQSHPSGIQAHTQLQLPEW-----LSRPAASLLTELLQFEPT 520
Cdd:cd05579  171 tpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPpFHAETPEEIFQNILNGKIEWpedpeVSDEAKDLISKLLTPDPE 250

                        170       180
                 ....*....|....*....|....
gi 332801047 521 RRLGMgeGGVSKLKSHPFFSTIQW 544
Cdd:cd05579  251 KRLGA--KGIEEIKNHPFFKGIDW 272
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
 386-548 2.59e-30

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: 120.88  E-value: 2.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE-VEPQ-----CCG--EavdnlYSAPEVGG 457
Cdd:cd05575   95 EPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEgIEPSdttstFCGtpE-----YLAPEVLR 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGMA--LSQSHP---SGIqAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGvSK 532
Cdd:cd05575  170 KQPYDRTVDWWCLGAVLYEMLYGLPpfYSRDTAemyDNI-LHKPLRLRTNVSPSARDLLEGLLQKDRTKRLGSGNDF-LE 247

                        170
                 ....*....|....*.
gi 332801047 533 LKSHPFFSTIQWSKLV 548
Cdd:cd05575  248 IKNHSFFRPINWDDLE 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 390-549 5.26e-30

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 120.31  E-value: 5.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 390 KQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVdnlYSAPEVGGISELTEACD 466
Cdd:PTZ00263 121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTftlCGTPE---YLAPEVIQSKGHGKAVD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 467 WWSFGSLLYELLTGmalsqsHP-----SGIQAHTQ-----LQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSH 536
Cdd:PTZ00263 198 WWTMGVLLYEFIAG------YPpffddTPFRIYEKilagrLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNH 271

                        170
                 ....*....|...
gi 332801047 537 PFFSTIQWSKLVG 549
Cdd:PTZ00263 272 PYFHGANWDKLYA 284
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 386-544 1.73e-28

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: 114.11  E-value: 1.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEV-----EPQCCGEAVDnlYSAPEVGGISE 460
Cdd:cd05611   96 EDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFG-LSRNglekrHNKKFVGTPD--YLAPETILGVG 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGM-ALSQSHPSGIQA---HTQLQLP----EWLSRPAASLLTELLQFEPTRRLgmGEGGVSK 532
Cdd:cd05611  173 DDKMSDWWSLGCVIFEFLFGYpPFHAETPDAVFDnilSRRINWPeevkEFCSPEAVDLINRLLCMDPAKRL--GANGYQE 250

                        170
                 ....*....|..
gi 332801047 533 LKSHPFFSTIQW 544
Cdd:cd05611  251 IKSHPFFKSINW 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 386-539 2.76e-28

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 113.39  E-value: 2.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047   386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPEVggISE 460
Cdd:smart00220  96 EDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP---GEKLTTFvgtpeYMAPEV--LLG 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047   461 L--TEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEW--------LSRPAASLLTELLQFEPTRRLGMGEggv 530
Cdd:smart00220 171 KgyGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPpfpppewdISPEAKDLIRKLLVKDPEKRLTAEE--- 247


                   ....*....
gi 332801047   531 skLKSHPFF 539
Cdd:smart00220 248 --ALQHPFF 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
 392-548 7.55e-28

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: 113.82  E-value: 7.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCGEAVdnlYSAPEVGGISELTEAC 465
Cdd:cd05585   99 YTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGlcklnmKDDDKTNTFCGTPE---YLAPELLLGHGYTKAV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 466 DWWSFGSLLYELLTGMA--LSQSHPSGIQAHTQ--LQLPEWLSRPAASLLTELLQFEPTRRLGMgeGGVSKLKSHPFFST 541
Cdd:cd05585  176 DWWTLGVLLYEMLTGLPpfYDENTNEMYRKILQepLRFPDGFDRDAKDLLIGLLNRDPTKRLGY--NGAQEIKNHPFFDQ 253


                 ....*..
gi 332801047 542 IQWSKLV 548
Cdd:cd05585  254 IDWKRLL 260
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
 386-548 8.15e-28

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: 113.61  E-value: 8.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCG--EavdnlYSAPEVGG 457
Cdd:cd05571   94 EDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGlckeeiSYGATTKTFCGtpE-----YLAPEVLE 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGMAlsqshPSGIQAHTQL---------QLPEWLSRPAASLLTELLQFEPTRRLGMGEG 528
Cdd:cd05571  169 DNDYGRAVDWWGLGVVMYEMMCGRL-----PFYNRDHEVLfelilmeevRFPSTLSPEAKSLLAGLLKKDPKKRLGGGPR 243

                        170       180
                 ....*....|....*....|
gi 332801047 529 GVSKLKSHPFFSTIQWSKLV 548
Cdd:cd05571  244 DAKEIMEHPFFASINWDDLY 263
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
 386-547 1.72e-27

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: 112.06  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPEVGGISE 460
Cdd:cd05605  101 EERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPE---GETIRGRvgtvgYMAPEVVKNER 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSQSHPSGIQ--------AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSK 532
Cdd:cd05605  178 YTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKreevdrrvKEDQEEYSEKFSEEAKSICSQLLQKDPKTRLGCRGEGAED 257

                        170
                 ....*....|....*
gi 332801047 533 LKSHPFFSTIQWSKL 547
Cdd:cd05605  258 VKSHPFFKSINFKRL 272
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 385-547 1.80e-27

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: 112.02  E-value: 1.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqcCGEAVDNLYS--------APEV- 455
Cdd:cd05613  103 TENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF----LLDENERAYSfcgtieymAPEIv 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 -GGISELTEACDWWSFGSLLYELLTGMAL--------SQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMG 526
Cdd:cd05613  179 rGGDSGHDKAVDWWSLGVLMYELLTGASPftvdgeknSQAEISRRILKSEPPYPQEMSALAKDIIQRLLMKDPKKRLGCG 258

                        170       180
                 ....*....|....*....|.
gi 332801047 527 EGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05613  259 PNGADEIKKHPFFQKINWDDL 279
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 386-547 4.35e-27

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: 111.93  E-value: 4.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQ-------CCGEAVdnlYSAPE-VGG 457
Cdd:cd05614  104 EDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEekertysFCGTIE---YMAPEiIRG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGMAL--------SQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGG 529
Cdd:cd05614  181 KSGHGKAVDWWSLGILMFELLTGASPftlegeknTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCKDPKKRLGAGPQG 260

                        170
                 ....*....|....*...
gi 332801047 530 VSKLKSHPFFSTIQWSKL 547
Cdd:cd05614  261 AQEIKEHPFFKGLDWEAL 278
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
 386-547 5.40e-27

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: 110.22  E-value: 5.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCgeAVDNLYSAPEV--GGISE 460
Cdd:cd05606   97 EAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGlacDFSKKKPHAS--VGTHGYMAPEVlqKGVAY 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEAcDWWSFGSLLYELLTGMALSQSHPSG----IQAHT---QLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKL 533
Cdd:cd05606  175 DSSA-DWFSLGCMLYKLLKGHSPFRQHKTKdkheIDRMTltmNVELPDSFSPELKSLLEGLLQRDVSKRLGCLGRGATEV 253

                        170
                 ....*....|....
gi 332801047 534 KSHPFFSTIQWSKL 547
Cdd:cd05606  254 KEHPFFKGVDWQQV 267
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
 386-547 2.31e-26

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: 108.77  E-value: 2.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQ--CCGEAVDNLYSAPEV--GGISeL 461
Cdd:cd05577   94 EARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGkkIKGRVGTHGYMAPEVlqKEVA-Y 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHPSGIQAH--------TQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKL 533
Cdd:cd05577  173 DFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEelkrrtleMAVEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSADEV 252

                        170
                 ....*....|....
gi 332801047 534 KSHPFFSTIQWSKL 547
Cdd:cd05577  253 KEHPFFRSLNWQRL 266
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 386-548 7.60e-26

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: 108.17  E-value: 7.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDN-----------LYSAPE 454
Cdd:cd05595   94 EDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG--------LCKEGITDgatmktfcgtpEYLAPE 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 VGGISELTEACDWWSFGSLLYELLTGMA--LSQSHPSGIQ--AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGV 530
Cdd:cd05595  166 VLEDNDYGRAVDWWGLGVVMYEMMCGRLpfYNQDHERLFEliLMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDA 245

                        170
                 ....*....|....*...
gi 332801047 531 SKLKSHPFFSTIQWSKLV 548
Cdd:cd05595  246 KEVMEHRFFLSINWQDVV 263
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 394-548 9.52e-26

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: 108.17  E-value: 9.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 394 AEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAV---DNlYSAPEVGGISELTEAC 465
Cdd:cd05598  108 AELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfRWTHDSKYYLAHSLvgtPN-YIAPEVLLRTGYTQLC 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 466 DWWSFGSLLYELLTGMA--LSQShpsgiQAHTQLQLPEW-----------LSRPAASLLTELLQFEPTRrlgMGEGGVSK 532
Cdd:cd05598  187 DWWSVGVILYEMLVGQPpfLAQT-----PAETQLKVINWrttlkipheanLSPEAKDLILRLCCDAEDR---LGRNGADE 258

                        170
                 ....*....|....*.
gi 332801047 533 LKSHPFFSTIQWSKLV 548
Cdd:cd05598  259 IKAHPFFAGIDWEKLR 274
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
 385-547 1.01e-25

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: 107.86  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAvDnlYSAPEVGGI 458
Cdd:cd05587   95 KEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEgifggkTTRTFCGTP-D--YIAPEIIAY 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMA---------LSQShpsgIQAHTqLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGG 529
Cdd:cd05587  172 QPYGKSVDWWAYGVLLYEMLAGQPpfdgededeLFQS----IMEHN-VSYPKSLSKEAVSICKGLLTKHPAKRLGCGPTG 246

                        170
                 ....*....|....*...
gi 332801047 530 VSKLKSHPFFSTIQWSKL 547
Cdd:cd05587  247 ERDIKEHPFFRRIDWEKL 264
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 385-547 1.08e-25

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: 107.71  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYF----------------GQWSEVEPQCCGEAVDN 448
Cdd:cd05574  101 PEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvrksLRKGSRRSSVKSIEKET 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 449 L----------------YSAPEVGGISELTEACDWWSFGSLLYELLTG----------MALSQshpsgIQaHTQLQLPE- 501
Cdd:cd05574  181 FvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGttpfkgsnrdETFSN-----IL-KKELTFPEs 254

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332801047 502 -WLSRPAASLLTELLQFEPTRRLGmGEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05574  255 pPVSSEAKDLIRKLLVKDPSKRLG-SKRGASEIKRHPFFRGVNWALI 300
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
 386-539 1.47e-25

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: 105.80  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-----CGEAVdnlYSAPEVGGISE 460
Cdd:cd05578   99 EETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTlatstSGTKP---YMAPEVFMRAG 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGM----ALSQSHPSGIQA----HTQLQLPEWlSRPAASLLTELLQFEPTRRLgmgeGGVSK 532
Cdd:cd05578  176 YSFAVDWWSLGVTAYEMLRGKrpyeIHSRTSIEEIRAkfetASVLYPAGW-SEEAIDLINKLLERDPQKRL----GDLSD 250


                 ....*..
gi 332801047 533 LKSHPFF 539
Cdd:cd05578  251 LKNHPYF 257
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 386-548 5.71e-25

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: 105.81  E-value: 5.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCGEAVdnlYSAPEVGGIS 459
Cdd:cd05604   96 EPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGlckegiSNSDTTTTFCGTPE---YLAPEVIRKQ 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMALSQSHPSGIQ----AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEgGVSKLKS 535
Cdd:cd05604  173 PYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMyeniLHKPLVLRPGISLTAWSILEELLEKDRQLRLGAKE-DFLEIKN 251

                        170
                 ....*....|...
gi 332801047 536 HPFFSTIQWSKLV 548
Cdd:cd05604  252 HPFFESINWTDLV 264
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
 392-547 5.73e-25

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: 105.78  E-value: 5.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEvepQCCGEAVDNL------YSAPEVGGISELTEAC 465
Cdd:cd05619  111 YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKE---NMLGDAKTSTfcgtpdYIAPEILLGQKYNTSV 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 466 DWWSFGSLLYELLTGmalsQSHPSGIQAHTQLQ--------LPEWLSRPAASLLTELLQFEPTRRLGMGeggvSKLKSHP 537
Cdd:cd05619  188 DWWSFGVLLYEMLIG----QSPFHGQDEEELFQsirmdnpfYPRWLEKEAKDILVKLFVREPERRLGVR----GDIRQHP 259

                        170
                 ....*....|
gi 332801047 538 FFSTIQWSKL 547
Cdd:cd05619  260 FFREINWEAL 269
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
46-120 9.12e-25

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 97.76  E-value: 9.12e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047    46 KRDYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNCHLQR 120
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
 392-547 1.48e-24

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: 104.26  E-value: 1.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAVdnlYSAPEVGGISELTEAC 465
Cdd:cd05620  101 YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKEnvfgdnRASTFCGTPD---YIAPEILQGLKYTFSV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 466 DWWSFGSLLYELLTGmalsQSHPSG---------IQAHTQlQLPEWLSRPAASLLTELLQFEPTRRLGMgeggVSKLKSH 536
Cdd:cd05620  178 DWWSFGVLLYEMLIG----QSPFHGddedelfesIRVDTP-HYPRWITKESKDILEKLFERDPTRRLGV----VGNIRGH 248

                        170
                 ....*....|.
gi 332801047 537 PFFSTIQWSKL 547
Cdd:cd05620  249 PFFKTINWTAL 259
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 384-547 2.64e-24

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: 104.29  E-value: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAVDNL--------- 449
Cdd:cd05573   98 FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGlctkmNKSGDRESYLNDSVNTLfqdnvlarr 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 ------------------YSAPEVGGISELTEACDWWSFGSLLYELLTGMA-LSQSHPSG----IQAHTQ-LQLP--EWL 503
Cdd:cd05573  178 rphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPpFYSDSLVEtyskIMNWKEsLVFPddPDV 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332801047 504 SRPAASLLTELLQfEPTRRLGMGEGgvskLKSHPFFSTIQWSKL 547
Cdd:cd05573  258 SPEAIDLIRRLLC-DPEDRLGSAEE----IKAHPFFKGIDWENL 296
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 386-546 2.66e-24

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: 102.30  E-value: 2.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-----CG--EavdnlYSAPEVGGI 458
Cdd:cd05572   92 EYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRktwtfCGtpE-----YVAPEIILN 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGM---ALSQSHPSGI-----QAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGV 530
Cdd:cd05572  167 KGYDFSVDYWSLGILLYELLTGRppfGGDDEDPMKIyniilKGIDKIEFPKYIDKNAKNLIKQLLRRNPEERLGYLKGGI 246

                        170
                 ....*....|....*.
gi 332801047 531 SKLKSHPFFSTIQWSK 546
Cdd:cd05572  247 RDIKKHKWFEGFDWEG 262
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
 392-547 4.44e-24

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: 102.41  E-value: 4.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEV-EPQCCGEAVDNL-YSAPEVGGISELTEACDWWS 469
Cdd:cd05630  107 YAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVpEGQTIKGRVGTVgYMAPEVVKNERYTFSPDWWA 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 470 FGSLLYELLTGMALSQSHPSGIQ--------AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFFST 541
Cdd:cd05630  187 LGCLLYEMIAGQSPFQQRKKKIKreeverlvKEVPEEYSEKFSPQARSLCSMLLCKDPAERLGCRGGGAREVKEHPLFKK 266


                 ....*.
gi 332801047 542 IQWSKL 547
Cdd:cd05630  267 LNFKRL 272
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
 386-547 4.90e-24

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: 102.88  E-value: 4.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGeaVDNlYSAPEVGGIS 459
Cdd:cd05588   95 EEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEglrpgdTTSTFCG--TPN-YIAPEILRGE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTG-----MALSQSHPSG--------IQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLG-M 525
Cdd:cd05588  172 DYGFSVDWWALGVLMFEMLAGrspfdIVGSSDNPDQntedylfqVILEKPIRIPRSLSVKAASVLKGFLNKNPAERLGcH 251

                        170       180
                 ....*....|....*....|..
gi 332801047 526 GEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05588  252 PQTGFADIQSHPFFRTIDWEQL 273
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
 385-547 1.08e-23

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: 102.00  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQ-----WSEVEPQC-CGEAVdnlYSAPEVGGI 458
Cdd:cd05616   99 KEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMckeniWDGVTTKTfCGTPD---YIAPEIIAY 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMA---------LSQShpsgIQAHtQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGG 529
Cdd:cd05616  176 QPYGKSVDWWAFGVLLYEMLAGQApfegededeLFQS----IMEH-NVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEG 250

                        170
                 ....*....|....*...
gi 332801047 530 VSKLKSHPFFSTIQWSKL 547
Cdd:cd05616  251 ERDIKEHAFFRYIDWEKL 268
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 386-547 2.23e-23

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: 101.14  E-value: 2.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAVdnlYSAPEVGGIS 459
Cdd:cd05590   95 EARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEgifngkTTSTFCGTPD---YIAPEILQEM 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMAlsqshpsGIQAHTQLQL-----------PEWLSRPAASLLTELLQFEPTRRLG-MGE 527
Cdd:cd05590  172 LYGPSVDWWAMGVLLYEMLCGHA-------PFEAENEDDLfeailndevvyPTWLSQDAVDILKAFMTKNPTMRLGsLTL 244

                        170       180
                 ....*....|....*....|
gi 332801047 528 GGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05590  245 GGEEAILRHPFFKELDWEKL 264
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 392-544 2.71e-23

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: 100.20  E-value: 2.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVdnlYSAPEVGGISELTEACDWW 468
Cdd:cd05612  106 YASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTwtlCGTPE---YLAPEVIQSKGHNKAVDWW 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 469 SFGSLLYELLTGM-ALSQSHPSGIQAHT---QLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFFSTIQW 544
Cdd:cd05612  183 ALGILIYEMLVGYpPFFDDNPFGIYEKIlagKLEFPRHLDLYAKDLIKKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDW 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 386-547 2.79e-23

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: 100.77  E-value: 2.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepQCCGEAVDNL---------YSAPEVG 456
Cdd:cd05599  100 EEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFG-------LCTGLKKSHLaystvgtpdYIAPEVF 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMA--LSQSHPSG----IQAHTQLQLPEWLS-RPAASLLTELLQFEPTRRLgmGEGG 529
Cdd:cd05599  173 LQKGYGKECDWWSLGVIMYEMLIGYPpfCSDDPQETcrkiMNWRETLVFPPEVPiSPEAKDLIERLLCDAEHRL--GANG 250

                        170
                 ....*....|....*...
gi 332801047 530 VSKLKSHPFFSTIQWSKL 547
Cdd:cd05599  251 VEEIKSHPFFKGVDWDHI 268
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
 385-547 3.39e-23

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: 100.43  E-value: 3.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE-VEPQ-----CCGEAVdnlYSAPEVGGI 458
Cdd:cd05603   94 LEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEettstFCGTPE---YLAPEVLRK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMA------LSQSHPSGIqaHTQLQLPEWLSRPAASLLTELLQFEPTRRLGmGEGGVSK 532
Cdd:cd05603  171 EPYDRTVDWWCLGAVLYEMLYGLPpfysrdVSQMYDNIL--HKPLHLPGGKTVAACDLLQGLLHKDQRRRLG-AKADFLE 247

                        170
                 ....*....|....*
gi 332801047 533 LKSHPFFSTIQWSKL 547
Cdd:cd05603  248 IKNHVFFSPINWDDL 262
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 386-547 4.51e-23

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: 99.40  E-value: 4.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVdnlYSAPEVGGISELT 462
Cdd:cd14209  100 EPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTwtlCGTPE---YLAPEIILSKGYN 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGmalsqSHPSGIQAHTQL---------QLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKL 533
Cdd:cd14209  177 KAVDWWALGVLIYEMAAG-----YPPFFADQPIQIyekivsgkvRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDI 251

                        170
                 ....*....|....
gi 332801047 534 KSHPFFSTIQWSKL 547
Cdd:cd14209  252 KNHKWFATTDWIAI 265
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
 386-544 7.91e-23

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: 98.63  E-value: 7.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEV----------------------EPQCCG 443
Cdd:cd05609   99 VDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFG-LSKIglmslttnlyeghiekdtreflDKQVCG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 444 EAVdnlYSAPEVGGISELTEACDWWSFGSLLYELLTG-MALSQSHPSGIQAHT---QLQLPE---WLSRPAASLLTELLQ 516
Cdd:cd05609  178 TPE---YIAPEVILRQGYGKPVDWWAMGIILYEFLVGcVPFFGDTPEELFGQVisdEIEWPEgddALPDDAQDLITRLLQ 254

                        170       180
                 ....*....|....*....|....*...
gi 332801047 517 FEPTRRLGMgeGGVSKLKSHPFFSTIQW 544
Cdd:cd05609  255 QNPLERLGT--GGAEEVKQHPFFQDLDW 280
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
 386-547 8.05e-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: 100.10  E-value: 8.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE-VEPqccGEAVDNL-----YSAPEVGGIS 459
Cdd:cd05617  115 EEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEgLGP---GDTTSTFcgtpnYIAPEILRGE 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMAL-----------SQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMG-E 527
Cdd:cd05617  192 EYGFSVDWWALGVLMFEMMAGRSPfdiitdnpdmnTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQpQ 271

                        170       180
                 ....*....|....*....|
gi 332801047 528 GGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05617  272 TGFSDIKSHTFFRSIDWDLL 291
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 386-547 1.25e-22

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: 98.72  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAvDnlYSAPEVGGIS 459
Cdd:cd05591   95 EPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilngkTTTTFCGTP-D--YIAPEILQEL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGM----ALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLG--MGEGGVSKL 533
Cdd:cd05591  172 EYGPSVDWWALGVLMYEMMAGQppfeADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLGcvASQGGEDAI 251

                        170
                 ....*....|....
gi 332801047 534 KSHPFFSTIQWSKL 547
Cdd:cd05591  252 RQHPFFREIDWEAL 265
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
 386-547 1.26e-22

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: 98.14  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVePQccGEAVDNL-----YSAPEVGGISE 460
Cdd:cd05631  101 EQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI-PE--GETVRGRvgtvgYMAPEVINNEK 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSQSHPSGIQ--------AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSK 532
Cdd:cd05631  178 YTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKreevdrrvKEDQEEYSEKFSEDAKSICRMLLTKNPKERLGCRGNGAAG 257

                        170
                 ....*....|....*
gi 332801047 533 LKSHPFFSTIQWSKL 547
Cdd:cd05631  258 VKQHPIFKNINFKRL 272
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
 385-547 2.47e-22

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: 98.15  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAVdnlYSAPEVGGI 458
Cdd:cd05615  109 KEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEhmvegvTTRTFCGTPD---YIAPEIIAY 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMA---------LSQShpsgIQAHtQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGG 529
Cdd:cd05615  186 QPYGRSVDWWAYGVLLYEMLAGQPpfdgededeLFQS----IMEH-NVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEG 260

                        170
                 ....*....|....*...
gi 332801047 530 VSKLKSHPFFSTIQWSKL 547
Cdd:cd05615  261 ERDIREHAFFRRIDWDKL 278
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 386-547 3.59e-22

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: 97.38  E-value: 3.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQccgEAVDNL-------YSAPEV--- 455
Cdd:cd05601  101 ESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSD---KTVTSKmpvgtpdYIAPEVlts 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 ---GGISELTEACDWWSFGSLLYELLTG---MALSQSHP--SGIQAHTQ-LQLPE--WLSRPAASLLTELLQfEPTRRLG 524
Cdd:cd05601  178 mngGSKGTYGVECDWWSLGIVAYEMLYGktpFTEDTVIKtySNIMNFKKfLKFPEdpKVSESAVDLIKGLLT-DAKERLG 256

                        170       180
                 ....*....|....*....|...
gi 332801047 525 mGEGgvskLKSHPFFSTIQWSKL 547
Cdd:cd05601  257 -YEG----LCCHPFFSGIDWNNL 274
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 386-539 3.65e-22

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: 96.52  E-value: 3.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--------QWSEVEPQC---------------C 442
Cdd:cd05581  100 EKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvlgpdSSPESTKGDadsqiaynqaraasfV 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 443 GEAvdnLYSAPEVGGISELTEACDWWSFGSLLYELLTGmalsqSHP--SGIQAHT-------QLQLPEWLSRPAASLLTE 513
Cdd:cd05581  180 GTA---EYVSPELLNEKPAGKSSDLWALGCIIYQMLTG-----KPPfrGSNEYLTfqkivklEYEFPENFPPDAKDLIQK 251

                        170       180
                 ....*....|....*....|....*..
gi 332801047 514 LLQFEPTRRLGMGE-GGVSKLKSHPFF 539
Cdd:cd05581  252 LLVLDPSKRLGVNEnGGYDELKAHPFF 278
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 380-545 3.68e-22

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: 98.53  E-value: 3.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 380 ATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVDNL-YSAPEV 455
Cdd:cd05621  144 SNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGmvhCDTAVGTPdYISPEV 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 ----GGISELTEACDWWSFGSLLYELLTG------MALSQSHPSGIQAHTQLQLPE--WLSRPAASLLTELLQfepTRRL 523
Cdd:cd05621  224 lksqGGDGYYGRECDWWSVGVFLFEMLVGdtpfyaDSLVGTYSKIMDHKNSLNFPDdvEISKHAKNLICAFLT---DREV 300

                        170       180
                 ....*....|....*....|..
gi 332801047 524 GMGEGGVSKLKSHPFFSTIQWS 545
Cdd:cd05621  301 RLGRNGVEEIKQHPFFRNDQWN 322
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 386-547 6.03e-22

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: 97.03  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQ----------WSEVepqccgeAV---DnlYSA 452
Cdd:cd05597  101 EEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSclklredgtvQSSV-------AVgtpD--YIS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 453 PEV-----GGISELTEACDWWSFGSLLYELLTGM------ALSQSHpSGIQAHTQ-LQLP---EWLSRPAASLLTELLQF 517
Cdd:cd05597  172 PEIlqameDGKGRYGPECDWWSLGVCMYEMLYGEtpfyaeSLVETY-GKIMNHKEhFSFPddeDDVSEEAKDLIRRLICS 250

                        170       180       190
                 ....*....|....*....|....*....|
gi 332801047 518 EPTRrlgMGEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05597  251 RERR---LGQNGIDDFKKHPFFEGIDWDNI 277
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 380-545 7.45e-22

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: 97.77  E-value: 7.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 380 ATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVDNL-YSAPEV 455
Cdd:cd05622  165 SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvrCDTAVGTPdYISPEV 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 ----GGISELTEACDWWSFGSLLYELLTG------MALSQSHPSGIQAHTQLQLPE--WLSRPAASLLTELLQfepTRRL 523
Cdd:cd05622  245 lksqGGDGYYGRECDWWSVGVFLYEMLVGdtpfyaDSLVGTYSKIMNHKNSLTFPDdnDISKEAKNLICAFLT---DREV 321

                        170       180
                 ....*....|....*....|..
gi 332801047 524 GMGEGGVSKLKSHPFFSTIQWS 545
Cdd:cd05622  322 RLGRNGVEEIKRHLFFKNDQWA 343
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
 386-547 1.32e-21

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: 95.81  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVePQccGEAVDNL-----YSAPEVGGISE 460
Cdd:cd05632  103 EERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKI-PE--GESIRGRvgtvgYMAPEVLNNQR 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSQSHPSGIQ--------AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSK 532
Cdd:cd05632  180 YTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKreevdrrvLETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQEEGAGE 259

                        170
                 ....*....|....*
gi 332801047 533 LKSHPFFSTIQWSKL 547
Cdd:cd05632  260 VKRHPFFRNMNFKRL 274
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 386-548 1.32e-21

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: 96.24  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE-VEPQC-----CGEAVdnlYSAPEVGGIS 459
Cdd:cd05602  107 EPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKEnIEPNGttstfCGTPE---YLAPEVLHKQ 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMALSQSHPSGIQ----AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEgGVSKLKS 535
Cdd:cd05602  184 PYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMydniLNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKD-DFTEIKN 262

                        170
                 ....*....|...
gi 332801047 536 HPFFSTIQWSKLV 548
Cdd:cd05602  263 HIFFSPINWDDLI 275
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 384-545 1.74e-21

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: 95.91  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAV---DnlYSAPEV-- 455
Cdd:cd05596  122 VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGlvrSDTAVgtpD--YISPEVlk 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 --GGISELTEACDWWSFGSLLYELLTGMA--LSQSHP---SGIQAH-TQLQLPE--WLSRPAASLLTELLQfepTRRLGM 525
Cdd:cd05596  200 sqGGDGVYGRECDWWSVGVFLYEMLVGDTpfYADSLVgtyGKIMNHkNSLQFPDdvEISKDAKSLICAFLT---DREVRL 276

                        170       180
                 ....*....|....*....|
gi 332801047 526 GEGGVSKLKSHPFFSTIQWS 545
Cdd:cd05596  277 GRNGIEEIKAHPFFKNDQWT 296
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
 386-547 3.91e-21

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: 94.29  E-value: 3.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCG--EavdnlYSAPEVGG 457
Cdd:cd05589  100 EPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgfgdRTSTFCGtpE-----FLAPEVLT 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGmalsQSHPSG---------IqAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEG 528
Cdd:cd05589  175 DTSYTRAVDWWGLGVLIYEMLVG----ESPFPGddeeevfdsI-VNDEVRYPRFLSTEAISIMRRLLRKNPERRLGASER 249

                        170
                 ....*....|....*....
gi 332801047 529 GVSKLKSHPFFSTIQWSKL 547
Cdd:cd05589  250 DAEDVKKQPFFRNIDWEAL 268
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
 386-544 5.18e-21

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: 94.71  E-value: 5.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALH-EQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAVdnlYSAPEVGGI 458
Cdd:cd05594  124 EDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgikdgaTMKTFCGTPE---YLAPEVLED 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMA--LSQSHPSGIQA--HTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLK 534
Cdd:cd05594  201 NDYGRAVDWWGLGVVMYEMMCGRLpfYNQDHEKLFELilMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIM 280

                        170
                 ....*....|
gi 332801047 535 SHPFFSTIQW 544
Cdd:cd05594  281 QHKFFAGIVW 290
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
 386-544 8.06e-21

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: 93.99  E-value: 8.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAVdnlYSAPEVGGIS 459
Cdd:cd05593  114 EDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgitdaaTMKTFCGTPE---YLAPEVLEDN 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMA--LSQSHPSGIQ--AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKS 535
Cdd:cd05593  191 DYGRAVDWWGLGVVMYEMMCGRLpfYNQDHEKLFEliLMEDIKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMR 270


                 ....*....
gi 332801047 536 HPFFSTIQW 544
Cdd:cd05593  271 HSFFTGVNW 279
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 386-538 1.03e-20

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: 91.77  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQC-----CGeAVDnlYSAPEVGGISE 460
Cdd:cd14007   99 EKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG-WSVHAPSNrrktfCG-TLD--YLPPEMVEGKE 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMA--LSQSHPSGIQ--AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvskLKSH 536
Cdd:cd14007  175 YDYKVDIWSLGVLCYELLVGKPpfESKSHQETYKriQNVDIKFPSSVSPEAKDLISKLLQKDPSKRLSLEQ-----VLNH 249


                 ..
gi 332801047 537 PF 538
Cdd:cd14007  250 PW 251
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
 386-544 2.98e-20

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: 92.40  E-value: 2.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE------VEPQCCGEAVdnlYSAPEVGGIS 459
Cdd:cd05618  120 EEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEglrpgdTTSTFCGTPN---YIAPEILRGE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTG-----MALSQSHPS--------GIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLG-M 525
Cdd:cd05618  197 DYGFSVDWWALGVLMFEMMAGrspfdIVGSSDNPDqntedylfQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGcH 276

                        170
                 ....*....|....*....
gi 332801047 526 GEGGVSKLKSHPFFSTIQW 544
Cdd:cd05618  277 PQTGFADIQGHPFFRNVDW 295
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 385-548 5.21e-20

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: 92.02  E-value: 5.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE-VEPQCCG------EAVDNL-------- 449
Cdd:cd05600  109 SEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGtLSPKKIEsmkirlEEVKNTafleltak 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 -------------------------YSAPEVGGISELTEACDWWSFGSLLYELLTGMA-LSQSHPSGIQAH-----TQLQ 498
Cdd:cd05600  189 errniyramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPpFSGSTPNETWANlyhwkKTLQ 268

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 499 LPEW--------LSRPAASLLTELLQfEPTRRLgmgeGGVSKLKSHPFFSTIQWSKLV 548
Cdd:cd05600  269 RPVYtdpdlefnLSDEAWDLITKLIT-DPQDRL----QSPEQIKNHPFFKNIDWDRLR 321
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 386-547 6.10e-20

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: 91.99  E-value: 6.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCGEAVDnlYSAPEV---- 455
Cdd:cd05624  172 EDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGsclkmnDDGTVQSSVAVGTPD--YISPEIlqam 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 -GGISELTEACDWWSFGSLLYELLTG------MALSQSHPSGIQAHTQLQLPEWL---SRPAASLLTELLqfePTRRLGM 525
Cdd:cd05624  250 eDGMGKYGPECDWWSLGVCMYEMLYGetpfyaESLVETYGKIMNHEERFQFPSHVtdvSEEAKDLIQRLI---CSRERRL 326

                        170       180
                 ....*....|....*....|..
gi 332801047 526 GEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05624  327 GQNGIEDFKKHAFFEGLNWENI 348
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
 386-544 2.61e-19

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: 89.35  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQccGEAVDNLYSAPEV-GGISEL 461
Cdd:cd05633  107 EKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGlacDFSKKKPH--ASVGTHGYMAPEVlQKGTAY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHPSG-------IQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLK 534
Cdd:cd05633  185 DSSADWFSLGCMLFKLLRGHSPFRQHKTKdkheidrMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRLGCHGRGAQEVK 264

                        170
                 ....*....|
gi 332801047 535 SHPFFSTIQW 544
Cdd:cd05633  265 EHSFFKGIDW 274
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
 392-547 2.89e-19

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: 88.40  E-value: 2.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDWW 468
Cdd:cd05608  110 YTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGlavELKDGQTKTKGYAGTPGFMAPELLLGEEYDYSVDYF 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 469 SFGSLLYELLTGMALSQSHPSGIQA--------HTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFFS 540
Cdd:cd05608  190 TLGVTLYEMIAARGPFRARGEKVENkelkqrilNDSVTYSEKFSPASKSICEALLAKDPEKRLGFRDGNCDGLRTHPFFR 269


                 ....*..
gi 332801047 541 TIQWSKL 547
Cdd:cd05608  270 DINWRKL 276
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
 386-544 3.17e-19

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: 88.95  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQccGEAVDNLYSAPEV--GGISE 460
Cdd:cd14223  102 EAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGlacDFSKKKPH--ASVGTHGYMAPEVlqKGVAY 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEAcDWWSFGSLLYELLTGMALSQSHPSG-------IQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKL 533
Cdd:cd14223  180 DSSA-DWFSLGCMLFKLLRGHSPFRQHKTKdkheidrMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCMGRGAQEV 258

                        170
                 ....*....|.
gi 332801047 534 KSHPFFSTIQW 544
Cdd:cd14223  259 KEEPFFRGLDW 269
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 385-538 4.68e-19

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: 86.80  E-value: 4.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-----CGEAVdnlYSAPEV-GGI 458
Cdd:cd14003   97 SEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSllktfCGTPA---YAAPEVlLGR 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGmAL-----SQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvskL 533
Cdd:cd14003  174 KYDGPKADVWSLGVILYAMLTG-YLpfdddNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRITIEE-----I 247


                 ....*
gi 332801047 534 KSHPF 538
Cdd:cd14003  248 LNHPW 252
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 386-537 5.10e-19

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: 85.79  E-value: 5.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQW-----SEVEPQCCGEAVDNLYSAPEVGGISE 460
Cdd:cd00180   91 EEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAkdldsDDSLLKTTGGTTPPYYAPPELLGGRY 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332801047 461 LTEACDWWSFGSLLYELltgmalsqshpsgiqahtqlqlpewlsRPAASLLTELLQFEPTRRLGMGEggvskLKSHP 537
Cdd:cd00180  171 YGPKVDIWSLGVILYEL---------------------------EELKDLIRRMLQYDPKKRPSAKE-----LLEHL 215
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
 386-547 1.74e-18

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: 87.76  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCGEAVDnlYSAPEV---- 455
Cdd:cd05623  172 EDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGsclklmEDGTVQSSVAVGTPD--YISPEIlqam 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 -GGISELTEACDWWSFGSLLYELLTG------MALSQSHPSGIQAHTQLQLPEWL---SRPAASLLTELLqfePTRRLGM 525
Cdd:cd05623  250 eDGKGKYGPECDWWSLGVCMYEMLYGetpfyaESLVETYGKIMNHKERFQFPTQVtdvSENAKDLIRRLI---CSREHRL 326

                        170       180
                 ....*....|....*....|..
gi 332801047 526 GEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05623  327 GQNGIEDFKNHPFFVGIDWDNI 348
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 386-537 2.33e-18

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: 84.74  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSevEPQ---------CCGEAVdnlYSAPE-V 455
Cdd:cd14078  100 EDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCA--KPKggmdhhletCCGSPA---YAAPElI 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 GGISELTEACDWWSFGSLLYELLTG---------MALSQSHPSGiqahtQLQLPEWLSRPAASLLTELLQFEPTRRLGMG 526
Cdd:cd14078  175 QGKPYIGSEADVWSMGVLLYALLCGflpfdddnvMALYRKIQSG-----KYEEPEWLSPSSKLLLDQMLQVDPKKRITVK 249

                        170
                 ....*....|.
gi 332801047 527 EggvskLKSHP 537
Cdd:cd14078  250 E-----LLNHP 255
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
 386-545 2.57e-18

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: 87.02  E-value: 2.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----------------------------QWSE 436
Cdd:cd05625  100 EDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdhlrqdsmdfsnEWGD 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 437 VEPQCCGEAVDNL---------------------YSAPEVGGISELTEACDWWSFGSLLYELLTGMA--LSQS----HPS 489
Cdd:cd05625  180 PENCRCGDRLKPLerraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPpfLAQTpletQMK 259

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 490 GIQAHTQLQLPEW--LSRPAASLLTELLQfEPTRRLgmGEGGVSKLKSHPFFSTIQWS 545
Cdd:cd05625  260 VINWQTSLHIPPQakLSPEASDLIIKLCR-GPEDRL--GKNGADEIKAHPFFKTIDFS 314
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
 386-545 5.90e-18

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: 85.83  E-value: 5.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQ-----------------------------WSE 436
Cdd:cd05626  100 EVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthnskyyqkgshirqdsmepsdlWDD 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 437 VEPQCCGEAVDNL---------------------YSAPEVGGISELTEACDWWSFGSLLYELLTGM------ALSQSHPS 489
Cdd:cd05626  180 VSNCRCGDRLKTLeqratkqhqrclahslvgtpnYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQppflapTPTETQLK 259

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 490 GIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRrlgMGEGGVSKLKSHPFFSTIQWS 545
Cdd:cd05626  260 VINWENTLHIPPQvkLSPEAVDLITKLCCSAEER---LGRNGADDIKAHPFFSEVDFS 314
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
 383-547 2.11e-17

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: 83.95  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNL------------- 449
Cdd:cd05627   98 TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLthnppsdfsfqnm 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 -------------------------YSAPEVGGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLS 504
Cdd:cd05627  178 nskrkaetwkknrrqlaystvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLV 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 332801047 505 RPAASLLTE-----LLQFEPTRRLGMGEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05627  258 FPPEVPISEkakdlILRFCTDAENRIGSNGVEEIKSHPFFEGVDWEHI 305
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
 392-548 3.17e-17

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 83.11  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVdnlYSAPEVGGISELTEACDWW 468
Cdd:PTZ00426 136 YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTytlCGTPE---YIAPEILLNVGHGKAADWW 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 469 SFGSLLYELLTG---------MALSQSHPSGIqahtqLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFF 539
Cdd:PTZ00426 213 TLGIFIYEILVGcppfyanepLLIYQKILEGI-----IYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWF 287


                 ....*....
gi 332801047 540 STIQWSKLV 548
Cdd:PTZ00426 288 GNIDWVSLL 296
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 50-115 4.80e-17

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 75.27  E-value: 4.80e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047   50 LVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFN 115
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 386-539 7.01e-17

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: 80.32  E-value: 7.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPEVGGISE 460
Cdd:cd05122   97 EQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSD---GKTRNTFvgtpyWMAPEVIQGKP 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMA-LSQSHPS------GIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRlgmgeGGVSKL 533
Cdd:cd05122  174 YGFKADIWSLGITAIEMAEGKPpYSELPPMkalfliATNGPPGLRNPKKWSKEFKDFLKKCLQKDPEKR-----PTAEQL 248


                 ....*.
gi 332801047 534 KSHPFF 539
Cdd:cd05122  249 LKHPFI 254
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
 386-539 8.47e-17

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: 80.26  E-value: 8.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNL-----YSAPEVGGISE 460
Cdd:cd06606   98 EPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTKSLrgtpyWMAPEVIRGEG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTG----------MAL------SQSHPsgiqahtqlQLPEWLSRPAASLLTELLQFEPTRRlg 524
Cdd:cd06606  178 YGRAADIWSLGCTVIEMATGkppwselgnpVAAlfkigsSGEPP---------PIPEHLSEEAKDFLRKCLQRDPKKR-- 246

                        170
                 ....*....|....*
gi 332801047 525 mgeGGVSKLKSHPFF 539
Cdd:cd06606  247 ---PTADELLQHPFL 258
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
 386-547 1.23e-16

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: 81.08  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwseVEPQCCGEAVDNL------YSAPEVgGIS 459
Cdd:cd05586   95 EDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGL---SKADLTDNKTTNTfcgtteYLAPEV-LLD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 E--LTEACDWWSFGSLLYELLTGMalSQSHPSGIQ------AHTQLQLP-EWLSRPAASLLTELLQFEPTRRLGMGEGGV 530
Cdd:cd05586  171 EkgYTKMVDFWSLGVLVFEMCCGW--SPFYAEDTQqmyrniAFGKVRFPkDVLSDEGRSFVKGLLNRNPKHRLGAHDDAV 248

                        170
                 ....*....|....*..
gi 332801047 531 sKLKSHPFFSTIQWSKL 547
Cdd:cd05586  249 -ELKEHPFFADIDWDLL 264
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 386-538 1.30e-16

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: 80.03  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEP--------QCCGEAVDN--------- 448
Cdd:cd14010   93 ESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFG-LARREGeilkelfgQFSDEGNVNkvskkqakr 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 449 ---LYSAPEVGGISELTEACDWWSFGSLLYELLTGmalsqsHPSgIQAHTQLQL-------------PEWLSRPAA---S 509
Cdd:cd14010  172 gtpYYMAPELFQGGVHSFASDLWALGCVLYEMFTG------KPP-FVAESFTELvekilnedpppppPKVSSKPSPdfkS 244

                        170       180
                 ....*....|....*....|....*....
gi 332801047 510 LLTELLQFEPTRRLGMGEggvskLKSHPF 538
Cdd:cd14010  245 LLKGLLEKDPAKRLSWDE-----LVKHPF 268
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 384-539 2.78e-16

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: 78.43  E-value: 2.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQA-GHIRLTYFGQWSEVEPQCCGEAVDNL-YSAPEV-GGISE 460
Cdd:cd05118   98 LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFTSPPYTPYVATRwYRAPEVlLGAKP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSqshpSGIQAHTQLQLPEWL--SRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPF 538
Cdd:cd05118  178 YGSSIDIWSLGCILAELLTGRPLF----PGDSEVDQLAKIVRLlgTPEALDLLSKMLKYDPAKRI-----TASQALAHPY 248


                 .
gi 332801047 539 F 539
Cdd:cd05118  249 F 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 386-539 3.16e-16

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: 78.42  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQcCGEAVDNLY-SAPEVGGISEL 461
Cdd:cd06627   98 ESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGvatKLNEVEKD-ENSVVGTPYwMAPEVIEMSGV 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTG---------MA-----LSQSHPSgiqahtqlqLPEWLSRPAASLLTELLQFEPTRRlgmge 527
Cdd:cd06627  177 TTASDIWSVGCTVIELLTGnppyydlqpMAalfriVQDDHPP---------LPENISPELRDFLLQCFQKDPTLR----- 242

                        170
                 ....*....|....
gi 332801047 528 ggVS--KLKSHPFF 539
Cdd:cd06627  243 --PSakELLKHPWL 254
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
 386-547 4.81e-16

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: 79.89  E-value: 4.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------------------QWSEVEPQCCGE--- 444
Cdd:cd05629  100 EDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGlstgfhkqhdsayyqkllQGKSNKNRIDNRnsv 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 445 AVDNL-----------------------------YSAPEVGGISELTEACDWWSFGSLLYELLTG---MALSQSHPSG-- 490
Cdd:cd05629  180 AVDSInltmsskdqiatwkknrrlmaystvgtpdYIAPEIFLQQGYGQECDWWSLGAIMFECLIGwppFCSENSHETYrk 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 491 -IQAHTQLQLPE--WLSRPAASLLTELLQfEPTRRLgmGEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05629  260 iINWRETLYFPDdiHLSVEAEDLIRRLIT-NAENRL--GRGGAHEIKSHPFFRGVDWDTI 316
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 386-538 2.54e-15

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: 75.98  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFG---QWSEVEP--QCCGEAvdnLYSAPEVGG 457
Cdd:cd05117   98 EREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGlakIFEEGEKlkTVCGTP---YYVAPEVLK 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGmalsqSHPsgIQAHTQLQL-------------PEW--LSRPAASLLTELLQFEPTRR 522
Cdd:cd05117  175 GKGYGKKCDIWSLGVILYILLCG-----YPP--FYGETEQELfekilkgkysfdsPEWknVSEEAKDLIKRLLVVDPKKR 247

                        170
                 ....*....|....*.
gi 332801047 523 LgmgegGVSKLKSHPF 538
Cdd:cd05117  248 L-----TAAEALNHPW 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 386-522 7.02e-15

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: 74.55  E-value: 7.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqccGEAVDNL---------YSAPEVG 456
Cdd:cd14014   99 PREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL-----GDSGLTQtgsvlgtpaYMAPEQA 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMAL--SQSHPSGIQAHTQLQLPEW------LSRPAASLLTELLQFEPTRR 522
Cdd:cd14014  174 RGGPVDPRSDIYSLGVVLYELLTGRPPfdGDSPAAVLAKHLQEAPPPPsplnpdVPPALDAIILRALAKDPEER 247
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 383-539 7.83e-15

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: 74.53  E-value: 7.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQC-----CGEAVdnlYSAPE 454
Cdd:cd14080   98 ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarLCPDDDGDVlsktfCGSAA---YAAPE 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 V-GGISELTEACDWWSFGSLLYELLTG-MALSQSHPSG-IQAHTQ--LQLP---EWLSRPAASLLTELLQFEPTRRLGMG 526
Cdd:cd14080  175 IlQGIPYDPKKYDIWSLGVILYIMLCGsMPFDDSNIKKmLKDQQNrkVRFPssvKKLSPECKDLIDQLLEPDPTKRATIE 254

                        170
                 ....*....|...
gi 332801047 527 EggvskLKSHPFF 539
Cdd:cd14080  255 E-----ILNHPWL 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
386-522 1.21e-14

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 76.20  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNL-YSAPEVGGISEL 461
Cdd:COG0515  106 PAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGiarALGGATLTQTGTVVGTPgYMAPEQARGEPV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332801047 462 TEACDWWSFGSLLYELLTGMAL--SQSHPSGIQAHTQ----------LQLPEWLSRpaasLLTELLQFEPTRR 522
Cdd:COG0515  186 DPRSDVYSLGVTLYELLTGRPPfdGDSPAELLRAHLRepppppselrPDLPPALDA----IVLRALAKDPEER 254
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
 386-547 3.24e-14

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: 74.15  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--------------------------QWSEVEP 439
Cdd:cd05610  103 EEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGlskvtlnrelnmmdilttpsmakpknDYSRTPG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 440 QCC-----------------------GEAVDNL-------YSAPEVGGISELTEACDWWSFGSLLYELLTGM-ALSQSHP 488
Cdd:cd05610  183 QVLslisslgfntptpyrtpksvrrgAARVEGErilgtpdYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIpPFNDETP 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047 489 SGI-QAHTQLQLP-----EWLSRPAASLLTELLQFEPTRRLGMGEggvskLKSHPFFSTIQWSKL 547
Cdd:cd05610  263 QQVfQNILNRDIPwpegeEELSVNAQNAIEILLTMDPTKRAGLKE-----LKQHPLFHGVDWENL 322
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
 383-547 7.92e-14

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: 73.15  E-value: 7.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNL------------- 449
Cdd:cd05628   97 TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLnhslpsdftfqnm 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 -------------------------YSAPEVGGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLS 504
Cdd:cd05628  177 nskrkaetwkrnrrqlafstvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLI 256

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 332801047 505 RPAASLLTE-----LLQFEPTRRLGMGEGGVSKLKSHPFFSTIQWSKL 547
Cdd:cd05628  257 FPPEVPISEkakdlILRFCCEWEHRIGAPGVEEIKTNPFFEGVDWEHI 304
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
 386-539 1.10e-13

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: 71.05  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQ------CCGeaVDNlYSAPEV--GG 457
Cdd:cd14099  100 EPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDgerkktLCG--TPN-YIAPEVleKK 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEAcDWWSFGSLLYELLTGMALSQSHP-----SGIQaHTQLQLPE--WLSRPAASLLTELLQFEPTRRLGMGEggv 530
Cdd:cd14099  177 KGHSFEV-DIWSLGVILYTLLVGKPPFETSDvketyKRIK-KNEYSFPShlSISDEAKDLIRSMLQPDPTKRPSLDE--- 251


                 ....*....
gi 332801047 531 skLKSHPFF 539
Cdd:cd14099  252 --ILSHPFF 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 386-539 3.60e-13

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: 69.89  E-value: 3.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwSEVEPQCCGEAVDN----LYSAPEV--GGIS 459
Cdd:cd14008  107 EETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV-SEMFEDGNDTLQKTagtpAFLAPELcdGDSK 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 EL-TEACDWWSFGSLLYELLTG---------MALSQShpsgIQAHTQ-LQLPEWLSRPAASLLTELLQFEPTRRLGMGEg 528
Cdd:cd14008  186 TYsGKAADIWALGVTLYCLVFGrlpfngdniLELYEA----IQNQNDeFPIPPELSPELKDLLRRMLEKDPEKRITLKE- 260

                        170
                 ....*....|.
gi 332801047 529 gvskLKSHPFF 539
Cdd:cd14008  261 ----IKEHPWV 267
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 385-538 2.54e-12

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: 67.04  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP--------QCCGEAVdnlYSAPEVg 456
Cdd:cd14663   98 KEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQfrqdgllhTTCGTPN---YVAPEV- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 457 giseLTE------ACDWWSFGSLLYELLTG---------MALSQSHPSGiqahtQLQLPEWLSRPAASLLTELLQFEPTR 521
Cdd:cd14663  174 ----LARrgydgaKADIWSCGVILFVLLAGylpfddenlMALYRKIMKG-----EFEYPRWFSPGAKSLIKRILDPNPST 244

                        170
                 ....*....|....*..
gi 332801047 522 RLGMgeggvSKLKSHPF 538
Cdd:cd14663  245 RITV-----EQIMASPW 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 385-523 6.28e-12

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: 66.26  E-value: 6.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFGQWSEVEPQC-----CGEAvdnLYSAPEV- 455
Cdd:cd14084  109 KEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSKILGETSlmktlCGTP---TYLAPEVl 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332801047 456 --GGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQ------LPEW---LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14084  186 rsFGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILsgkytfIPKAwknVSEEAKDLVKKMLVVDPSRRP 264
Pkinase pfam00069
Protein kinase domain;
450-539 6.64e-12

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.96  E-value: 6.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047  450 YSAPEVGGISELTEACDWWSFGSLLYELLTG-MALSQSHPSGIQAHTQLQ------LPEWLSRPAASLLTELLQFEPTRR 522
Cdd:pfam00069 126 YMAPEVLGGNPYGPKVDVWSLGCILYELLTGkPPFPGINGNEIYELIIDQpyafpeLPSNLSEEAKDLLKKLLKKDPSKR 205

                          90
                  ....*....|....*..
gi 332801047  523 LGMGEggvskLKSHPFF 539
Cdd:pfam00069 206 LTATQ-----ALQHPWF 217
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 387-522 8.62e-12

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: 65.25  E-value: 8.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCGEAvdnLYSAPEVGGISE 460
Cdd:cd13999   91 SLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGlsriknSTTEKMTGVVGTP---RWMAPEVLRGEP 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 461 LTEACDWWSFGSLLYELLTG------MALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd13999  168 YTEKADVYSFGIVLWELLTGevpfkeLSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEKR 235
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 383-538 1.20e-11

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: 65.16  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-----CGE---AVDNL----- 449
Cdd:cd14077  109 KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNLYDPRRllrtfCGSlyfAAPELlqaqp 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 YSAPEVggiselteacDWWSFGSLLYELLTG-MALSQSHPSGIQAHTQ---LQLPEWLSRPAASLLTELLQFEPTRRLGM 525
Cdd:cd14077  189 YTGPEV----------DVWSFGVVLYVLVCGkVPFDDENMPALHAKIKkgkVEYPSYLSSECKSLISRMLVVDPKKRATL 258

                        170
                 ....*....|...
gi 332801047 526 GEggvskLKSHPF 538
Cdd:cd14077  259 EQ-----VLNHPW 266
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
 395-539 1.30e-11

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: 65.07  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-QWSEVEPQCCGEAVDN------LYSAPEVggISEL---TEA 464
Cdd:cd06610  110 EVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGvSASLATGGDRTRKVRKtfvgtpCWMAPEV--MEQVrgyDFK 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTG-------------MALSQSHPSGIQAHTQLQLpewLSRPAASLLTELLQFEPTRRlgmgeGGVS 531
Cdd:cd06610  188 ADIWSFGITAIELATGaapyskyppmkvlMLTLQNDPPSLETGADYKK---YSKSFRKMISLCLQKDPSKR-----PTAE 259


                 ....*...
gi 332801047 532 KLKSHPFF 539
Cdd:cd06610  260 ELLKHKFF 267
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 383-538 1.56e-11

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: 64.69  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGQWSEVEPQCCGEAVDNLYS----APEV 455
Cdd:cd14012  100 SVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMCSRGSLDEFKQtywlPPEL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 GGIS-ELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEwlsrPAASLLTELLQFEPTRRLGMGEggvskLK 534
Cdd:cd14012  180 AQGSkSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLDLSA----SLQDFLSKCLSLDPKKRPTALE-----LL 250


                 ....
gi 332801047 535 SHPF 538
Cdd:cd14012  251 PHEF 254
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 383-539 1.65e-11

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: 64.99  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPEVGG 457
Cdd:cd14181  112 TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEP---GEKLRELcgtpgYLAPEILK 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 IS--ELTEA----CDWWSFGSLLYELLTGmalsqSHPSG-----------IQAHTQLQLPEWLSRP--AASLLTELLQFE 518
Cdd:cd14181  189 CSmdETHPGygkeVDLWACGVILFTLLAG-----SPPFWhrrqmlmlrmiMEGRYQFSSPEWDDRSstVKDLISRLLVVD 263

                        170       180
                 ....*....|....*....|.
gi 332801047 519 PTRRLgmgegGVSKLKSHPFF 539
Cdd:cd14181  264 PEIRL-----TAEQALQHPFF 279
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 386-538 1.82e-11

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: 64.63  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQ----CCGEaVDNL-----YSAPEV- 455
Cdd:cd06626   98 EAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNtttmAPGE-VNSLvgtpaYMAPEVi 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 --GGISELTEACDWWSFGSLLYELLTGmalsqSHP-------------SGIQAHTQLQLPEWLSRPAASLLTELLQFEPT 520
Cdd:cd06626  177 tgNKGEGHGRAADIWSLGCVVLEMATG-----KRPwseldnewaimyhVGMGHKPPIPDSLQLSPEGKDFLSRCLESDPK 251

                        170
                 ....*....|....*...
gi 332801047 521 RRLgmgegGVSKLKSHPF 538
Cdd:cd06626  252 KRP-----TASELLDHPF 264
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
 395-539 3.23e-11

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: 63.81  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWS-EVEPQC----CGEAvdnLYSAPEV-GGISELTEACDWW 468
Cdd:cd14081  109 QIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASlQPEGSLletsCGSP---HYACPEViKGEKYDGRKADIW 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 469 SFGSLLYELLTGmAL---SQSHPSGIQA--HTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvskLKSHPFF 539
Cdd:cd14081  186 SCGVILYALLVG-ALpfdDDNLRQLLEKvkRGVFHIPHFISPDAQDLLRRMLEVNPEKRITIEE-----IKKHPWF 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 386-538 3.87e-11

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: 63.42  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEpqcCGEAVDN------LYSAPEVggIS 459
Cdd:cd14002   98 EEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS---CNTLVLTsikgtpLYMAPEL--VQ 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 E--LTEACDWWSFGSLLYELLTGMA--LSQSHPSGIQ--AHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvskL 533
Cdd:cd14002  173 EqpYDHTADLWSLGCILYELFVGQPpfYTNSIYQLVQmiVKDPVKWPSNMSPEFKSFLQGLLNKDPSKRLSWPD-----L 247


                 ....*
gi 332801047 534 KSHPF 538
Cdd:cd14002  248 LEHPF 252
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 379-538 4.01e-11

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: 63.86  E-value: 4.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFGQWSEVEPQCCGEA--VDNLYSAP 453
Cdd:cd14172   95 RGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNALQTpcYTPYYVAP 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 454 EVGGISELTEACDWWSFGSLLYELL---------TGMALSQSHPSGIQ-AHTQLQLPEW--LSRPAASLLTELLQFEPTR 521
Cdd:cd14172  175 EVLGPEKYDKSCDMWSLGVIMYILLcgfppfysnTGQAISPGMKRRIRmGQYGFPNPEWaeVSEEAKQLIRHLLKTDPTE 254

                        170
                 ....*....|....*..
gi 332801047 522 RLgmgegGVSKLKSHPF 538
Cdd:cd14172  255 RM-----TITQFMNHPW 266
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 399-539 4.30e-11

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: 64.24  E-value: 4.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAG---HIRLTYFGqWSEVEPQC------CGeavdNL-YSAPEV----GGISELTEA 464
Cdd:cd14092  111 AVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFG-FARLKPENqplktpCF----TLpYAAPEVlkqaLSTQGYDES 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQL----------PEW--LSRPAASLLTELLQFEPTRRLGMgeggvSK 532
Cdd:cd14092  186 CDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRiksgdfsfdgEEWknVSSEAKSLIQGLLTVDPSKRLTM-----SE 260


                 ....*..
gi 332801047 533 LKSHPFF 539
Cdd:cd14092  261 LRNHPWL 267
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 377-539 5.07e-11

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: 63.02  E-value: 5.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 377 CGRAT----WSVR----EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP------QCC 442
Cdd:cd14189   83 CSRKSlahiWKARhtllEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPpeqrkkTIC 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 443 GEAVdnlYSAPEVGGISELTEACDWWSFGSLLYELLTG------MALSQSHPSGIQAHtqLQLPEWLSRPAASLLTELLQ 516
Cdd:cd14189  163 GTPN---YLAPEVLLRQGHGPESDVWSLGCVMYTLLCGnppfetLDLKETYRCIKQVK--YTLPASLSLPARHLLAGILK 237

                        170       180
                 ....*....|....*....|...
gi 332801047 517 FEPTRRLGMGEggvskLKSHPFF 539
Cdd:cd14189  238 RNPGDRLTLDQ-----ILEHEFF 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 386-523 9.68e-11

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: 62.28  E-value: 9.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQC-----CGeAVDnlYSAPEVGGISE 460
Cdd:cd14116  104 EQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG-WSVHAPSSrrttlCG-TLD--YLPPEMIEGRM 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332801047 461 LTEACDWWSFGSLLYELLTGMA--LSQSHPSGIQA--HTQLQLPEWLSRPAASLLTELLQFEPTRRL 523
Cdd:cd14116  180 HDEKVDLWSLGVLCYEFLVGKPpfEANTYQETYKRisRVEFTFPDFVTEGARDLISRLLKHNPSQRP 246
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 383-539 9.83e-11

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: 62.63  E-value: 9.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP-----QCCGEAVdnlYSAPEVGG 457
Cdd:cd14182  106 TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPgeklrEVCGTPG---YLAPEIIE 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTE------ACDWWSFGSLLYELLTG---------MALSQSHPSGiqaHTQLQLPEWLSRP--AASLLTELLQFEPT 520
Cdd:cd14182  183 CSMDDNhpgygkEVDMWSTGVIMYTLLAGsppfwhrkqMLMLRMIMSG---NYQFGSPEWDDRSdtVKDLISRFLVVQPQ 259

                        170
                 ....*....|....*....
gi 332801047 521 RRLGMGEGGVsklksHPFF 539
Cdd:cd14182  260 KRYTAEEALA-----HPFF 273
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
 386-539 1.12e-10

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: 62.77  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVDNLYSAPEV-GGISEL 461
Cdd:cd07845  107 ESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAkpmTPKVVTLWYRAPELlLGCTTY 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGMAL----SQSH-----------P--------SGIQAHTQLQLPE-----------WLSRPA 507
Cdd:cd07845  187 TTAIDMWAVGCILAELLAHKPLlpgkSEIEqldliiqllgtPnesiwpgfSDLPLVGKFTLPKqpynnlkhkfpWLSEAG 266

                        170       180       190
                 ....*....|....*....|....*....|..
gi 332801047 508 ASLLTELLQFEPTRRLGMGEGgvskLKsHPFF 539
Cdd:cd07845  267 LRLLNFLLMYDPKKRATAEEA----LE-SSYF 293
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 390-538 1.23e-10

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: 61.85  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 390 KQWAAemlvALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFG------QWSEVEpQCCGEAvdnLYSAPEVGGISE 460
Cdd:cd14009   99 QQLAS----GLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGfarslqPASMAE-TLCGSP---LYMAPEILQFQK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMAlsqshPSGIQAHTQL-------------QLPEWLSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd14009  171 YDAKADLWSVGAILFEMLVGKP-----PFRGSNHVQLlrniersdavipfPIAAQLSPDCKDLLRRLLRRDPAERISFEE 245

                        170
                 ....*....|.
gi 332801047 528 ggvskLKSHPF 538
Cdd:cd14009  246 -----FFAHPF 251
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
 386-538 1.28e-10

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: 62.19  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQC-----CGeAVDnlYSAPEVGGISE 460
Cdd:cd14117  105 EQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG-WSVHAPSLrrrtmCG-TLD--YLPPEMIEGRT 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSQShPSGIQAHTQ-----LQLPEWLSRPAASLLTELLQFEPTRRLGMgeGGVSKlks 535
Cdd:cd14117  181 HDEKVDLWCIGVLCYELLVGMPPFES-ASHTETYRRivkvdLKFPPFLSDGSRDLISKLLRYHPSERLPL--KGVME--- 254


                 ...
gi 332801047 536 HPF 538
Cdd:cd14117  255 HPW 257
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 395-525 1.38e-10

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: 62.75  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFGqWSEVEPQccgeavDNL----------YSAPEVGGISEL 461
Cdd:cd14179  110 KLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFG-FARLKPP------DNQplktpcftlhYAAPELLNYNGY 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPE-------------W--LSRPAASLLTELLQFEPTRRLGM 525
Cdd:cd14179  183 DESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMKkikqgdfsfegeaWknVSQEAKDLIQGLLTVDPNKRIKM 261
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
 386-543 1.58e-10

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: 62.66  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEV-GGISELTEA 464
Cdd:cd07880  117 EDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVVTRWYRAPEViLNWMHYTQT 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSH---------------PSgiQAHTQ-LQ----------LPEWLSRPAASLLT------ 512
Cdd:cd07880  197 VDIWSVGCIMAEMLTGKPLFKGHdhldqlmeimkvtgtPS--KEFVQkLQsedaknyvkkLPRFRKKDFRSLLPnanpla 274

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 332801047 513 -----ELLQFEPTRRLGMGEGgvsklKSHPFFSTIQ 543
Cdd:cd07880  275 vnvleKMLVLDAESRITAAEA-----LAHPYFEEFH 305
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 386-539 2.33e-10

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: 61.60  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPEV----- 455
Cdd:cd14093  108 EKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDE---GEKLRELcgtpgYLAPEVlkcsm 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 -GGISELTEACDWWSFGSLLYELLTG----------MALSQShpsgIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRR 522
Cdd:cd14093  185 yDNAPGYGKEVDMWACGVIMYTLLAGcppfwhrkqmVMLRNI----MEGKYEFGSPEWddISDTAKDLISKLLVVDPKKR 260

                        170
                 ....*....|....*..
gi 332801047 523 LGMGEGgvskLKsHPFF 539
Cdd:cd14093  261 LTAEEA----LE-HPFF 272
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
 384-539 2.35e-10

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: 61.19  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWS--------EVEPQCCGEAVdnlYSAPEV 455
Cdd:cd14069   97 MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATvfrykgkeRLLNKMCGTLP---YVAPEL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 -GGISELTEACDWWSFGSLLYELLTG-------MALSQSHPSGIQAHTQLQLPeW--LSRPAASLLTELLQFEPTRRLgm 525
Cdd:cd14069  174 lAKKKYRAEPVDVWSCGIVLFAMLAGelpwdqpSDSCQEYSDWKENKKTYLTP-WkkIDTAALSLLRKILTENPNKRI-- 250

                        170
                 ....*....|....
gi 332801047 526 gegGVSKLKSHPFF 539
Cdd:cd14069  251 ---TIEDIKKHPWY 261
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
 395-539 2.47e-10

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: 61.13  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAvdNlYSAPEVggISELTEA---CD 466
Cdd:cd14079  110 QIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGlsnimRDGEFLKTSCGSP--N-YAAPEV--ISGKLYAgpeVD 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 467 WWSFGSLLYELLTGM---------ALSQSHPSGIQAhtqlqLPEWLSRPAASLLTELLQFEPTRRLGMGEggvskLKSHP 537
Cdd:cd14079  185 VWSCGVILYALLCGSlpfddehipNLFKKIKSGIYT-----IPSHLSPGARDLIKRMLVVDPLKRITIPE-----IRQHP 254


                 ..
gi 332801047 538 FF 539
Cdd:cd14079  255 WF 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 386-539 2.93e-10

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: 61.34  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQCCGEAVDNL-YSAPEV-GGISEL 461
Cdd:cd07829   97 PNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGlaRAFGIPLRTYTHEVVTLwYRAPEIlLGSKHY 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGMAL--SQSH-------------PS-----GIQA--HTQLQLPEWLSRP-----------AA 508
Cdd:cd07829  177 STAVDIWSVGCIFAELITGKPLfpGDSEidqlfkifqilgtPTeeswpGVTKlpDYKPTFPKWPKNDlekvlprldpeGI 256

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332801047 509 SLLTELLQFEPTRRLGMGEGgvskLKsHPFF 539
Cdd:cd07829  257 DLLSKMLQYNPAKRISAKEA----LK-HPYF 282
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
 387-547 2.94e-10

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: 61.46  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVE--PQCCGEAVDNLYSAPEVGGISELTEA 464
Cdd:cd05607  104 ERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKegKPITQRAGTNGYMAPEILKEESYSYP 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSHPSG----------IQAHTQLQLPEWlSRPAASLLTELLQFEPTRRLGMGEGGVSKLK 534
Cdd:cd05607  184 VDWFAMGCSIYEMVAGRTPFRDHKEKvskeelkrrtLEDEVKFEHQNF-TEEAKDICRLFLAKKPENRLGSRTNDDDPRK 262

                        170
                 ....*....|...
gi 332801047 535 sHPFFSTIQWSKL 547
Cdd:cd05607  263 -HEFFKSINFPRL 274
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 385-525 3.84e-10

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: 60.48  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwSEVEPQCCGEAVDN--LYSAPEVGGISELT 462
Cdd:cd08530  101 PEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGI-SKVLKKNLAKTQIGtpLYAAPEVWKGRPYD 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 463 EACDWWSFGSLLYELLTG--------MA-LSQShpsgIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGM 525
Cdd:cd08530  180 YKSDIWSLGCLLYEMATFrppfeartMQeLRYK----VCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSC 247
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
 384-538 5.71e-10

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: 60.12  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL-DQAGHIRLTYFGQWSEVEPqccGEAVDN-----LYSAPEVG- 456
Cdd:cd14074  100 LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQP---GEKLETscgslAYSAPEILl 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMA-LSQSHPSGIQAHT---QLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvsk 532
Cdd:cd14074  177 GDEYDAPAVDIWSLGVILYMLVCGQPpFQEANDSETLTMImdcKYTVPAHVSPECKDLIRRMLIRDPKKRASLEE----- 251


                 ....*.
gi 332801047 533 LKSHPF 538
Cdd:cd14074  252 IENHPW 257
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 394-539 5.71e-10

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: 59.96  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 394 AEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwseVEPQCCGEAVDNL---------YSAPEV--GGISELT 462
Cdd:cd14119  104 VQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFG----VAEALDLFAEDDTcttsqgspaFQPPEIanGQDSFSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTG---------MALSQSHPSGiqahtQLQLPEWLSRPAASLLTELLQFEPTRRLgmgegGVSKL 533
Cdd:cd14119  180 FKVDIWSAGVTLYNMTTGkypfegdniYKLFENIGKG-----EYTIPDDVDPDLQDLLRGMLEKDPEKRF-----TIEQI 249


                 ....*.
gi 332801047 534 KSHPFF 539
Cdd:cd14119  250 RQHPWF 255
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 383-538 6.32e-10

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: 60.11  E-value: 6.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDN--LYSAPEV--GGI 458
Cdd:cd06632   98 AFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFKGspYWMAPEVimQKN 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGmALSQSHPSGIQAHTQL-------QLPEWLSRPAASLLTELLQFEPTRRlgmgeGGVS 531
Cdd:cd06632  178 SGYGLAVDIWSLGCTVLEMATG-KPPWSQYEGVAAIFKIgnsgelpPIPDHLSPDAKDFIRLCLQRDPEDR-----PTAS 251


                 ....*..
gi 332801047 532 KLKSHPF 538
Cdd:cd06632  252 QLLEHPF 258
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
 386-527 6.35e-10

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: 59.83  E-value: 6.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWS---------EVEPQCCGEAvdnlYSAPEVG 456
Cdd:cd14070  102 EREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcagilgysdPFSTQCGSPA----YAAPELL 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQA-HTQL------QLPEWLSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd14070  178 ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRAlHQKMvdkemnPLPTDLSPGAISFLRSLLEPDPLKRPNIKQ 255
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 377-498 7.58e-10

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: 59.98  E-value: 7.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 377 CGratwsVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLdQAGHIRLTY----FGQWSEVEP-QCCGEAVDNL-Y 450
Cdd:cd14038   96 CG-----LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGEQRLIHkiidLGYAKELDQgSLCTSFVGTLqY 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 332801047 451 SAPEVGGISELTEACDWWSFGSLLYELLTGMA--LSQSHPsgIQAHTQLQ 498
Cdd:cd14038  170 LAPELLEQQKYTVTVDYWSFGTLAFECITGFRpfLPNWQP--VQWHGKVR 217
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
 386-483 9.04e-10

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: 60.30  E-value: 9.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEV-GGISELTEA 464
Cdd:cd07879  116 EDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEViLNWMHYNQT 195

                         90
                 ....*....|....*....
gi 332801047 465 CDWWSFGSLLYELLTGMAL 483
Cdd:cd07879  196 VDIWSVGCIMAEMLTGKTL 214
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 386-522 9.25e-10

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: 59.40  E-value: 9.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQ---CCGEAvdnLYSAPEVggis 459
Cdd:cd08215  102 EEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGiskVLESTTDLaktVVGTP---YYLSPEL---- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 elteaC---------DWWSFGSLLYELLTGmalsqSHPsgIQAHTQLQL------------PEWLSRPAASLLTELLQFE 518
Cdd:cd08215  175 -----CenkpynyksDIWALGCVLYELCTL-----KHP--FEANNLPALvykivkgqyppiPSQYSSELRDLVNSMLQKD 242


                 ....
gi 332801047 519 PTRR 522
Cdd:cd08215  243 PEKR 246
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 386-537 9.31e-10

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: 59.68  E-value: 9.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqccgEAVDNLYS---------APEV- 455
Cdd:cd14118  114 EETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEF------EGDDALLSstagtpafmAPEAl 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 --GGISELTEACDWWSFGSLLYELLTG-MALSQSHPSGIQ---AHTQLQLPE--WLSRPAASLLTELLQFEPTRRLgmge 527
Cdd:cd14118  188 seSRKKFSGKALDIWAMGVTLYCFVFGrCPFEDDHILGLHekiKTDPVVFPDdpVVSEQLKDLILRMLDKNPSERI---- 263

                        170
                 ....*....|
gi 332801047 528 gGVSKLKSHP 537
Cdd:cd14118  264 -TLPEIKEHP 272
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
 386-483 1.04e-09

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: 59.65  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQ----WSEVEPQCCGEAVDNLYSAPEV-GGISE 460
Cdd:cd07832   99 EAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLarlfSEEDPRLYSHQVATRWYRAPELlYGSRK 178

                         90       100
                 ....*....|....*....|...
gi 332801047 461 LTEACDWWSFGSLLYELLTGMAL 483
Cdd:cd07832  179 YDEGVDLWAVGCIFAELLNGSPL 201
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
 386-485 1.09e-09

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: 59.50  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNL-YSAPEV-GGISE 460
Cdd:cd07840  103 ESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGlarPYTKENNADYTNRVITLwYRPPELlLGATR 182

                         90       100
                 ....*....|....*....|....*
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSQ 485
Cdd:cd07840  183 YGPEVDMWSVGCILAELFTGKPIFQ 207
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 359-522 1.47e-09

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: 58.93  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 359 CGRGMDQSCLSADGAGRgcgratwSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVE 438
Cdd:cd13997   82 CENGSLQDALEELSPIS-------KLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 439 PQCCGEAVDNLYSAPEV-GGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHT-QLQLPEWLSRPA--ASLLTEL 514
Cdd:cd13997  155 TSGDVEEGDSRYLAPELlNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQgKLPLPPGLVLSQelTRLLKVM 234


                 ....*...
gi 332801047 515 LQFEPTRR 522
Cdd:cd13997  235 LDPDPTRR 242
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 383-538 1.52e-09

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: 59.08  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDN---------LYSAP 453
Cdd:cd06628  102 AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNNGarpslqgsvFWMAP 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 454 EVGGISELTEACDWWSFGSLLYELLTGmalsqSHPsgIQAHTQLQ------------LPEWLSRPAASLLTELLQFEPTR 521
Cdd:cd06628  182 EVVKQTSYTRKADIWSLGCLVVEMLTG-----THP--FPDCTQMQaifkigenasptIPSNISSEARDFLEKTFEIDHNK 254

                        170
                 ....*....|....*..
gi 332801047 522 RlgmgeGGVSKLKSHPF 538
Cdd:cd06628  255 R-----PTADELLKHPF 266
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
 396-542 1.60e-09

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: 59.46  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 396 MLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQccgEAVDNL--------YSAPEV-GGISELTEACD 466
Cdd:cd07834  112 ILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPD---EDKGFLteyvvtrwYRAPELlLSSKKYTKAID 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 467 WWSFGSLLYELLTGMAL--SQSH---------------PSGIQAHTQLQLPEWLSR-------------PAAS-----LL 511
Cdd:cd07834  189 IWSVGCIFAELLTRKPLfpGRDYidqlnlivevlgtpsEEDLKFISSEKARNYLKSlpkkpkkplsevfPGASpeaidLL 268

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332801047 512 TELLQFEPTRRLgmgegGVSKLKSHPFFSTI 542
Cdd:cd07834  269 EKMLVFNPKKRI-----TADEALAHPYLAQL 294
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
 377-542 1.63e-09

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: 59.25  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 377 CGRatwSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAP 453
Cdd:cd07873   93 CGN---SINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGlarAKSIPTKTYSNEVVTLWYRPP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 454 EV-GGISELTEACDWWSFGSLLYELLTGMAL-------SQSH--------PS-----GIQAHTQLQ---LPEW------- 502
Cdd:cd07873  170 DIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLfpgstveEQLHfifrilgtPTeetwpGILSNEEFKsynYPKYradalhn 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332801047 503 ----LSRPAASLLTELLQFEPTRRLGMGEGgvsklKSHPFFSTI 542
Cdd:cd07873  250 haprLDSDGADLLSKLLQFEGRKRISAEEA-----MKHPYFHSL 288
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
 399-538 2.12e-09

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: 58.53  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAG---------HIRLTYFG-----QWSEVEPQCCGEAvdnLYSAPEVGGISELTEA 464
Cdd:cd14120  104 AMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGfarflQDGMMAATLCGSP---MYMAPEVIMSLQYDAK 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQ-SHPSGIQA----HTQLQ--LPEWLSRPAASLLTELLQFEPTRRLGMGEGGvsklkSHP 537
Cdd:cd14120  181 ADLWSIGTIVYQCLTGKAPFQaQTPQELKAfyekNANLRpnIPSGTSPALKDLLLGLLKRNPKDRIDFEDFF-----SHP 255


                 .
gi 332801047 538 F 538
Cdd:cd14120  256 F 256
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
 383-539 2.48e-09

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: 58.48  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG---------HIRLTYFG-----QWSEVEPQCCGEAvdn 448
Cdd:cd14202   97 TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGfarylQNNMMAATLCGSP--- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 449 LYSAPEVGGISELTEACDWWSFGSLLYELLTGMALSQ-SHPSGIQAHTQLQ------LPEWLSRPAASLLTELLQFEPTR 521
Cdd:cd14202  174 MYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQaSSPQDLRLFYEKNkslspnIPRETSSHLRQLLLGLLQRNQKD 253

                        170
                 ....*....|....*...
gi 332801047 522 RLGMGEggvskLKSHPFF 539
Cdd:cd14202  254 RMDFDE-----FFHHPFL 266
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
 388-541 2.56e-09

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: 58.74  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-------QWSEVEPQccgeAVDNLYSAPEV-GGIS 459
Cdd:cd07841  103 DIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGlarsfgsPNRKMTHQ----VVTRWYRAPELlFGAR 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGM-----------------ALSQSHPSGIQAHTQLQLP-EWLSRP---------AAS--- 509
Cdd:cd07841  179 HYGVGVDMWSVGCIFAELLLRVpflpgdsdidqlgkifeALGTPTEENWPGVTSLPDYvEFKPFPptplkqifpAASdda 258

                        170       180       190
                 ....*....|....*....|....*....|....
gi 332801047 510 --LLTELLQFEPTRRLGMGEGgvskLKsHPFFST 541
Cdd:cd07841  259 ldLLQRLLTLNPNKRITARQA----LE-HPYFSN 287
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 399-539 5.17e-09

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: 57.01  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP----QCCGeAVDnlYSAPEV-GGISELTEACDWWSFGSL 473
Cdd:cd14004  121 AVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIKSgpfdTFVG-TID--YAAPEVlRGNPYGGKEQDIWALGVL 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 474 LYELLTGMALSQSHPSGIQAhtQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvskLKSHPFF 539
Cdd:cd14004  198 LYTLVFKENPFYNIEEILEA--DLRIPYAVSEDLIDLISRMLNRDVGDRPTIEE-----LLTDPWL 256
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 383-541 5.20e-09

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: 57.25  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQccGEAVDNL-----YSAPEVGG 457
Cdd:cd14187  103 ALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD--GERKKTLcgtpnYIAPEVLS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGM------ALSQSHPSgIQAHtQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvs 531
Cdd:cd14187  181 KKGHSFEVDIWSIGCIMYTLLVGKppfetsCLKETYLR-IKKN-EYSIPKHINPVAASLIQKMLQTDPTARPTINE---- 254

                        170
                 ....*....|
gi 332801047 532 kLKSHPFFST 541
Cdd:cd14187  255 -LLNDEFFTS 263
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 389-539 5.44e-09

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: 57.28  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQ--AGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVggISEL--TEA 464
Cdd:cd14133  104 IRKIAQQILEALVFLHSLGLIHCDLKPENILLASysRCQIKIIDFGSSCFLTQRLYSYIQSRYYRAPEV--ILGLpyDEK 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLpewLSRPAASLLTE--------------LLQFEPTRRLGMGEggv 530
Cdd:cd14133  182 IDMWSLGCILAELYTGEPLFPGASEVDQLARIIGT---IGIPPAHMLDQgkaddelfvdflkkLLEIDPKERPTASQ--- 255


                 ....*....
gi 332801047 531 skLKSHPFF 539
Cdd:cd14133  256 --ALSHPWL 262
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
 400-523 6.26e-09

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: 57.34  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLL-LDQAGH---IRLTYFGQWSEVEPQCcGEAVDNLYSA----PEVGGISELTEACDWWSFG 471
Cdd:cd14175  108 VEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAEN-GLLMTPCYTAnfvaPEVLKRQGYDEGCDIWSLG 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332801047 472 SLLYELLTGMALSQSHPSGI---------QAHTQLQLPEW--LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14175  187 ILLYTMLAGYTPFANGPSDTpeeiltrigSGKFTLSGGNWntVSDAAKDLVSKMLHVDPHQRL 249
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 386-539 6.85e-09

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: 57.43  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV---DNLYSAPEVGGISELT 462
Cdd:cd06655  114 EAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTmvgTPYWMAPEVVTRKAYG 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRlgmgeGGVSKLKS 535
Cdd:cd06655  194 PKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKR-----GSAKELLQ 268


                 ....
gi 332801047 536 HPFF 539
Cdd:cd06655  269 HPFL 272
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
 388-539 8.03e-09

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: 57.13  E-value: 8.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwsevePQCCG--------EAVDNLYSAPEV-GGI 458
Cdd:cd07860  101 LIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGL-----ARAFGvpvrtythEVVTLWYRAPEIlLGC 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMAL--------------------SQSHPSGIqahTQL-----QLPEW----------- 502
Cdd:cd07860  176 KYYSTAVDIWSLGCIFAEMVTRRALfpgdseidqlfrifrtlgtpDEVVWPGV---TSMpdykpSFPKWarqdfskvvpp 252

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 332801047 503 LSRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPFF 539
Cdd:cd07860  253 LDEDGRDLLSQMLHYDPNKRI-----SAKAALAHPFF 284
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
 386-539 8.21e-09

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: 57.04  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV---DNLYSAPEVGGISELT 462
Cdd:cd06656  114 EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTmvgTPYWMAPEVVTRKAYG 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRlgmgeGGVSKLKS 535
Cdd:cd06656  194 PKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRR-----GSAKELLQ 268


                 ....
gi 332801047 536 HPFF 539
Cdd:cd06656  269 HPFL 272
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 386-522 9.70e-09

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: 56.57  E-value: 9.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLL---LDQAGHIRLTYFGqWSEVE------PQCCGEAVdnlYSAPEVG 456
Cdd:cd14167  100 ERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFG-LSKIEgsgsvmSTACGTPG---YVAPEVL 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMAL------SQSHPSGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRR 522
Cdd:cd14167  176 AQKPYSKAVDCWSIGVIAYILLCGYPPfydendAKLFEQILKAEYEFDSPYWddISDSAKDFIQHLMEKDPEKR 249
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 378-539 9.79e-09

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: 56.25  E-value: 9.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 378 GRATWSVREEQVKQwaaeMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEP--QCCGEAVdnlYSA 452
Cdd:cd14071   94 GRMSEKEARKKFWQ----ILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGfsnFFKPGELlkTWCGSPP---YAA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 453 PEV-GGISELTEACDWWSFGSLLYELLTGM---------ALSQSHPSGiqahtQLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14071  167 PEVfEGKEYEGPQLDIWSLGVVLYVLVCGAlpfdgstlqTLRDRVLSG-----RFRIPFFMSTDCEHLIRRMLVLDPSKR 241

                        170
                 ....*....|....*..
gi 332801047 523 LGMgeggvSKLKSHPFF 539
Cdd:cd14071  242 LTI-----EQIKKHKWM 253
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 386-538 9.80e-09

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: 56.41  E-value: 9.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVE-PQ-----CCGEAVdnlYSAPEVGGIS 459
Cdd:cd14186  101 EDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKmPHekhftMCGTPN---YISPEIATRS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGM------ALSQSHPSGIQAhtQLQLPEWLSRPAASLLTELLQFEPTRRLGMgeggvSKL 533
Cdd:cd14186  178 AHGLESDVWSLGCMFYTLLVGRppfdtdTVKNTLNKVVLA--DYEMPAFLSREAQDLIHQLLRKNPADRLSL-----SSV 250


                 ....*
gi 332801047 534 KSHPF 538
Cdd:cd14186  251 LDHPF 255
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
 379-539 1.13e-08

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: 56.56  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG---------HIRLTYFG-----QWSEVEPQCCGE 444
Cdd:cd14201   97 QAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGfarylQSNMMAATLCGS 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 445 AvdnLYSAPEVGGISELTEACDWWSFGSLLYELLTGMALSQSH-PSGIQ------AHTQLQLPEWLSRPAASLLTELLQF 517
Cdd:cd14201  177 P---MYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANsPQDLRmfyeknKNLQPSIPRETSPYLADLLLGLLQR 253

                        170       180
                 ....*....|....*....|..
gi 332801047 518 EPTRRLGMgeggvSKLKSHPFF 539
Cdd:cd14201  254 NQKDRMDF-----EAFFSHPFL 270
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 399-540 1.26e-08

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: 56.58  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQA---GHIRLTYFGQWSEVEPQ--CCGEAVDNLYSAPEVGGISELTEACDWWSFGSL 473
Cdd:cd14170  113 AIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSHnsLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVI 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332801047 474 LYELLT---------GMALSQSHPSGIQ-AHTQLQLPEW--LSRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPFFS 540
Cdd:cd14170  193 MYILLCgyppfysnhGLAISPGMKTRIRmGQYEFPNPEWseVSEEVKMLIRNLLKTEPTQRM-----TITEFMNHPWIM 266
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 50-113 1.28e-08

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 51.93  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047  50 LVDAATQ-IRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEI 113
Cdd:cd02656    2 LLQQAKElIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFL 66
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 386-539 1.42e-08

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: 55.79  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP------QCCGEAVdnlYSAPEVggIS 459
Cdd:cd14188  100 EPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPlehrrrTICGTPN---YLSPEV--LN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEAC--DWWSFGSLLYELLTG------MALSQSHPSGIQAhtQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEggvs 531
Cdd:cd14188  175 KQGHGCesDIWALGCVMYTMLLGrppfetTNLKETYRCIREA--RYSLPSSLLAPAKHLIASMLSKNPEDRPSLDE---- 248


                 ....*...
gi 332801047 532 kLKSHPFF 539
Cdd:cd14188  249 -IIRHDFF 255
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 395-538 1.45e-08

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: 56.15  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFGqWSEVEPQ-----CCGEAVdnlYSAPEVGGISELTEACD 466
Cdd:cd14166  108 QVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFG-LSKMEQNgimstACGTPG---YVAPEVLAQKPYSKAVD 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 467 WWSFGSLLYELLTGM------ALSQSHPSGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPF 538
Cdd:cd14166  184 CWSIGVITYILLCGYppfyeeTESRLFEKIKEGYYEFESPFWddISESAKDFIRHLLEKNPSKRY-----TCEKALSHPW 258
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
 400-523 1.59e-08

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: 56.57  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLL-LDQAGH---IRLTYFGQWSEVEPQCcGEAVDNLYSA----PEVGGISELTEACDWWSFG 471
Cdd:cd14176  126 VEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN-GLLMTPCYTAnfvaPEVLERQGYDAACDIWSLG 204

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332801047 472 SLLYELLTGMAL----SQSHPSGIQAHT-----QLQLPEW--LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14176  205 VLLYTMLTGYTPfangPDDTPEEILARIgsgkfSLSGGYWnsVSDTAKDLVSKMLHVDPHQRL 267
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
 386-540 1.73e-08

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: 55.68  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqccGEAVDNLYS--------APEVGG 457
Cdd:cd06614   96 ESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL-----TKEKSKRNSvvgtpywmAPEVIK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTG----------MALSQSHPSGIqahTQLQLPEWLSRPAASLLTELLQFEPTRRlgmge 527
Cdd:cd06614  171 RKDYGPKVDIWSLGIMCIEMAEGeppyleepplRALFLITTKGI---PPLKNPEKWSPEFKDFLNKCLVKDPEKR----- 242

                        170
                 ....*....|...
gi 332801047 528 GGVSKLKSHPFFS 540
Cdd:cd06614  243 PSAEELLQHPFLK 255
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 48-113 1.86e-08

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 51.50  E-value: 1.86e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047  48 DYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEI 113
Cdd:cd02678    1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKL 66
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
 383-480 1.91e-08

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: 55.35  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLD--QAGHIRLTYFGQWSEVEPqccGEAVDNLYS-----APEV 455
Cdd:cd14006   85 SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNP---GEELKEIFGtpefvAPEI 161

                         90       100
                 ....*....|....*....|....*
gi 332801047 456 GGISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14006  162 VNGEPVSLATDMWSIGVLTYVLLSG 186
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 385-524 2.17e-08

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: 55.53  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGQWSEVEPQC-CGEAVDNL-YSAPEVGGIS 459
Cdd:cd13989  100 KESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKELDQGSlCTSFVGTLqYLAPELFESK 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTG--------------MALSQSHPSGIQA----------HTQLQLPEWLSRPAA----SLL 511
Cdd:cd13989  180 KYTCTVDYWSFGTLAFECITGyrpflpnwqpvqwhGKVKQKKPEHICAyedltgevkfSSELPSPNHLSSILKeyleSWL 259

                        170
                 ....*....|...
gi 332801047 512 TELLQFEPTRRLG 524
Cdd:cd13989  260 QLMLRWDPRQRGG 272
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
 400-523 2.46e-08

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: 55.41  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLL-LDQAGH---IRLTYFGQWSEVEPQCcGEAVDNLYSA----PEVGGISELTEACDWWSFG 471
Cdd:cd14178  110 VEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAEN-GLLMTPCYTAnfvaPEVLKRQGYDAACDIWSLG 188

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 472 SLLYELLTGMALSQSHP------------SGIQAhtqLQLPEW--LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14178  189 ILLYTMLAGFTPFANGPddtpeeilarigSGKYA---LSGGNWdsISDAAKDIVSKMLHVDPHQRL 251
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
 389-483 2.63e-08

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: 55.91  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH--IRLTYFGQwSEVEPQCCGEAVDN-LYSAPEVGGISELTEAC 465
Cdd:cd14224  170 VRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGS-SCYEHQRIYTYIQSrFYRAPEVILGARYGMPI 248

                         90
                 ....*....|....*...
gi 332801047 466 DWWSFGSLLYELLTGMAL 483
Cdd:cd14224  249 DMWSFGCILAELLTGYPL 266
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
 386-540 2.73e-08

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: 55.34  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEV---GGIS 459
Cdd:cd14200  123 EDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGvsnQFEGNDALLSSTAGTPAFMAPETlsdSGQS 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTG---------MALSQSHPSGIqahtqLQLPE--WLSRPAASLLTELLQFEPTRRLgmgeg 528
Cdd:cd14200  203 FSGKALDVWAMGVTLYCFVYGkcpfidefiLALHNKIKNKP-----VEFPEepEISEELKDLILKMLDKNPETRI----- 272

                        170
                 ....*....|..
gi 332801047 529 GVSKLKSHPFFS 540
Cdd:cd14200  273 TVPEIKVHPWVT 284
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
 388-539 2.81e-08

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: 55.18  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG----------QWSEvepqccgEAVDNLYSAPEV-G 456
Cdd:cd07836  101 TVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGlarafgipvnTFSN-------EVVTLWYRAPDVlL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMALSqshpSGIQAHTQL-------------------QLPEW--------------- 502
Cdd:cd07836  174 GSRTYSTSIDIWSVGCIMAEMITGRPLF----PGTNNEDQLlkifrimgtptestwpgisQLPEYkptfpryppqdlqql 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 332801047 503 ---LSRPAASLLTELLQFEPTRRLGMGEGgvsklKSHPFF 539
Cdd:cd07836  250 fphADPLGIDLLHRLLQLNPELRISAHDA-----LQHPWF 284
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
 386-541 3.34e-08

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: 55.45  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqcCGEAVDN-----------LYSAPE 454
Cdd:cd07855  108 LEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGL----CTSPEEHkyfmteyvatrWYRAPE 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 VG-GISELTEACDWWSFGSLLYELLTGMAL----SQSH-----------PSG--------------IQAHTQLQLPEW-- 502
Cdd:cd07855  184 LMlSLPEYTQAIDMWSVGCIFAEMLGRRQLfpgkNYVHqlqliltvlgtPSQavinaigadrvrryIQNLPNKQPVPWet 263

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 332801047 503 ----LSRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPFFST 541
Cdd:cd07855  264 lypkADQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAK 301
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
 389-539 3.51e-08

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: 55.02  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQC-CGEAVDNLYSAPEV-GGISELTEA 464
Cdd:cd07871  105 VKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGlaRAKSVPTKTySNEVVTLWYRPPDVlLGSTEYSTP 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMAL---------------------SQSHPsGIQAHTQLQ---LPEWLSRP-----------AAS 509
Cdd:cd07871  185 IDMWGVGCILYEMATGRPMfpgstvkeelhlifrllgtptEETWP-GVTSNEEFRsylFPQYRAQPlinhaprldtdGID 263

                        170       180       190
                 ....*....|....*....|....*....|
gi 332801047 510 LLTELLQFEPTRRLGmGEGGVsklkSHPFF 539
Cdd:cd07871  264 LLSSLLLYETKSRIS-AEAAL----RHSYF 288
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 389-539 3.70e-08

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: 55.08  E-value: 3.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQC-CGEAVDNLYSAPEV-GGISELTEA 464
Cdd:cd07844  100 VRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGlaRAKSVPSKTySNEVVTLWYRPPDVlLGSTEYSTS 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALsqsHPSGIQAHTQLQL---------------------------PEWLSRP----------- 506
Cdd:cd07844  180 LDMWGVGCIFYEMATGRPL---FPGSTDVEDQLHKifrvlgtpteetwpgvssnpefkpysfPFYPPRPlinhaprldri 256

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 332801047 507 --AASLLTELLQFEPTRRLGMGEGgvsklKSHPFF 539
Cdd:cd07844  257 phGEELALKFLQYEPKKRISAAEA-----MKHPYF 286
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
 386-483 3.87e-08

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: 55.44  E-value: 3.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVG-GISELTEA 464
Cdd:cd07878  117 DEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVATRWYRAPEIMlNWMHYNQT 196

                         90
                 ....*....|....*....
gi 332801047 465 CDWWSFGSLLYELLTGMAL 483
Cdd:cd07878  197 VDIWSVGCIMAELLKGKAL 215
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 399-539 4.35e-08

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: 54.40  E-value: 4.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVE----------PQCCGEAVdnlYSAPEV-GGISELTEACDW 467
Cdd:cd14165  114 AIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLrdengrivlsKTFCGSAA---YAAPEVlQGIPYDPRIYDI 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 468 WSFGSLLYELLTG-MALSQSHPSG---IQAHTQLQLPEW--LSRPAASLLTELLQFEPTRRLGMgeggvSKLKSHPFF 539
Cdd:cd14165  191 WSLGVILYIMVCGsMPYDDSNVKKmlkIQKEHRVRFPRSknLTSECKDLIYRLLQPDVSQRLCI-----DEVLSHPWL 263
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 386-522 6.18e-08

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: 53.82  E-value: 6.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQ---WSEVEPQCCGEAVDNLYSAPEVGGISELT 462
Cdd:cd08219   99 EDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSarlLTSPGAYACTYVGTPYYVPPEIWENMPYN 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 463 EACDWWSFGSLLYELLTgmaLSQSHPSGIQAHTQLQ--------LPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd08219  179 NKSDIWSLGCILYELCT---LKHPFQANSWKNLILKvcqgsykpLPSHYSYELRSLIKQMFKRNPRSR 243
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 386-539 6.32e-08

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: 54.16  E-value: 6.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEA--VDNLY-SAPEVGGISELT 462
Cdd:cd06647  102 EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGTPYwMAPEVVTRKAYG 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRlgmgeGGVSKLKS 535
Cdd:cd06647  182 PKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR-----GSAKELLQ 256


                 ....
gi 332801047 536 HPFF 539
Cdd:cd06647  257 HPFL 260
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
 392-522 6.81e-08

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: 53.89  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGV---LCRDLHPGN-LLLDQAGH-------IRLTYFG---QWSEVEPQccGEAVDNLYSAPEVGG 457
Cdd:cd14146  107 WAVQIARGMLYLHEEAVvpiLHRDLKSSNiLLLEKIEHddicnktLKITDFGlarEWHRTTKM--SAAGTYAWMAPEVIK 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTqLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14146  185 SSLFSKGSDIWSYGVLLWELLTGEvpyrgidGLAVAYGVAVNKLT-LPIPSTCPEPFAKLMKECWEQDPHIR 255
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
 397-540 8.41e-08

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: 54.10  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 397 LVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNL--------YSAPEV-GGISELTEACDW 467
Cdd:cd07852  117 LKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDENPVLtdyvatrwYRAPEIlLGSTRYTKGVDM 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 468 WSFGSLLYELLTGMAL--------------------SQSHPSGIQ---AHTQL-QLPEWLSRP-----------AASLLT 512
Cdd:cd07852  197 WSVGCILGEMLLGKPLfpgtstlnqlekiievigrpSAEDIESIQspfAATMLeSLPPSRPKSldelfpkaspdALDLLK 276

                        170       180
                 ....*....|....*....|....*...
gi 332801047 513 ELLQFEPTRRLGMGEGgvskLKsHPFFS 540
Cdd:cd07852  277 KLLVFNPNKRLTAEEA----LR-HPYVA 299
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
 383-537 8.51e-08

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: 53.47  E-value: 8.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV--DNLYSAPEV-GGIs 459
Cdd:cd14050   96 SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQegDPRYMAPELlQGS- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 eLTEACDWWSFGSLLYELLTGMALsqshPSGIQAHTQL---QLPE----WLSRPAASLLTELLQFEPTRRlgmgeGGVSK 532
Cdd:cd14050  175 -FTKAADIFSLGITILELACNLEL----PSGGDGWHQLrqgYLPEeftaGLSPELRSIIKLMMDPDPERR-----PTAED 244


                 ....*
gi 332801047 533 LKSHP 537
Cdd:cd14050  245 LLALP 249
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
 386-527 9.67e-08

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: 53.70  E-value: 9.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGIS 459
Cdd:cd14094  108 EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGvaiQLGESGLVAGGRVGTPHFMAPEVVKRE 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047 460 ELTEACDWWSFGSLLYELLTGM-----ALSQSHPSGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd14094  188 PYGKPVDVWGCGVILFILLSGClpfygTKERLFEGIIKGKYKMNPRQWshISESAKDLVRRMLMLDPAERITVYE 262
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
 399-523 9.72e-08

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: 53.45  E-value: 9.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGQWSEVE-------PQCCgeavdNLYSAPEVGGISELTEACDWW 468
Cdd:cd14089  112 AVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTtkkslqtPCYT-----PYYVAPEVLGPEKYDKSCDMW 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332801047 469 SFGSLLYELL---------TGMALSQSHPSGI-QAHTQLQLPEW--LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14089  187 SLGVIMYILLcgyppfysnHGLAISPGMKKRIrNGQYEFPNPEWsnVSEEAKDLIRGLLKTDPSERL 253
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
 387-499 1.01e-07

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: 54.36  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQC--CGEAVDNLYSAPEV-GGISEL 461
Cdd:cd07853  103 DHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGlaRVEEPDESKhmTQEVVTQYYRAPEIlMGSRHY 182

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHpSGIQahtQLQL 499
Cdd:cd07853  183 TSAVDIWSVGCIFAELLGRRILFQAQ-SPIQ---QLDL 216
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 383-539 1.09e-07

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: 53.51  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPE 454
Cdd:cd14106  104 CLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVIGE---GEEIREIlgtpdYVAPE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 VGGISELTEACDWWSFGSLLYELLTGMAlsqshPSGIQ---------AHTQLQLPEWL----SRPAASLLTELLQFEPTR 521
Cdd:cd14106  181 ILSYEPISLATDMWSIGVLTYVLLTGHS-----PFGGDdkqetflniSQCNLDFPEELfkdvSPLAIDFIKRLLVKDPEK 255

                        170
                 ....*....|....*...
gi 332801047 522 RLGMGEggvskLKSHPFF 539
Cdd:cd14106  256 RLTAKE-----CLEHPWL 268
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 395-488 1.22e-07

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: 53.40  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL-----------YSAPEVGGISELTE 463
Cdd:cd06609  106 EVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG--------VSGQLTSTMskrntfvgtpfWMAPEVIKQSGYDE 177

                         90       100
                 ....*....|....*....|....*.
gi 332801047 464 ACDWWSFGSLLYELLTGMA-LSQSHP 488
Cdd:cd06609  178 KADIWSLGITAIELAKGEPpLSDLHP 203
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 386-539 1.35e-07

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: 53.20  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG-HIRLTYFGQWSEVEPQC--CGEAVDNL-----YSAPEVGG 457
Cdd:cd06630  102 ENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGtgAGEFQGQLlgtiaFMAPEVLR 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGmalsqSHP---SGIQAHTQL-----------QLPEWLSRPAASLLTELLQFEPTRRL 523
Cdd:cd06630  182 GEQYGRSCDVWSVGCVIIEMATA-----KPPwnaEKISNHLALifkiasattppPIPEHLSPGLRDVTLRCLELQPEDRP 256

                        170
                 ....*....|....*.
gi 332801047 524 GMGEggvskLKSHPFF 539
Cdd:cd06630  257 PARE-----LLKHPVF 267
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 383-527 1.46e-07

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: 52.86  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG--HIRLTYFG-----QWSEVEPQCCGEAVdnlYSAPEV 455
Cdd:cd14098   97 AIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGlakviHTGTFLVTFCGTMA---YLAPEI 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 ---------GGISELTeacDWWSFGSLLYELLTGmAL---SQSHPSGIQAHTQLQLPEW------LSRPAASLLTELLQF 517
Cdd:cd14098  174 lmskeqnlqGGYSNLV---DMWSVGCLVYVMLTG-ALpfdGSSQLPVEKRIRKGRYTQPplvdfnISEEAIDFILRLLDV 249

                        170
                 ....*....|
gi 332801047 518 EPTRRLGMGE 527
Cdd:cd14098  250 DPEKRMTAAQ 259
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
 394-538 1.48e-07

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: 52.87  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 394 AEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP-------QCCGEAVdnlYSAPEVGGISELTEA-- 464
Cdd:cd14076  113 AQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHfngdlmsTSCGSPC---YAAPELVVSDSMYAGrk 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSHPSGIQA-----------HTQLQLPEWLSRPAASLLTELLQFEPTRRLGMgeggvSKL 533
Cdd:cd14076  190 ADIWSCGVILYAMLAGYLPFDDDPHNPNGdnvprlyryicNTPLIFPEYVTPKARDLLRRILVPNPRKRIRL-----SAI 264


                 ....*
gi 332801047 534 KSHPF 538
Cdd:cd14076  265 MRHAW 269
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
 384-522 1.58e-07

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: 52.52  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-----CGEAVdnlYSAPEV-GG 457
Cdd:cd14072   96 MKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNkldtfCGSPP---YAAPELfQG 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGmalsqSHPSGIQAHTQL---------QLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14072  173 KKYDGPEVDVWSLGVILYTLVSG-----SLPFDGQNLKELrervlrgkyRIPFYMSTDCENLLKKFLVLNPSKR 241
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 379-480 1.64e-07

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: 52.69  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-------QWSEVEPQCCG----EAvd 447
Cdd:cd13994   90 EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaevfgmPAEKESPMSAGlcgsEP-- 167

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332801047 448 nlYSAPEV-GGISELTEACDWWSFGSLLYELLTG 480
Cdd:cd13994  168 --YMAPEVfTSGSYDGRAVDVWSCGIVLFALFTG 199
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 386-539 1.71e-07

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: 53.19  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV---DNLYSAPEVGGISELT 462
Cdd:cd06654  115 EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTmvgTPYWMAPEVVTRKAYG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRlgmgeGGVSKLKS 535
Cdd:cd06654  195 PKVDIWSLGIMAIEMIEGEppylnenPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR-----GSAKELLQ 269


                 ....
gi 332801047 536 HPFF 539
Cdd:cd06654  270 HQFL 273
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 386-480 1.74e-07

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: 52.68  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----------QWSEVEPQCCGEAvdnlYSAPE 454
Cdd:cd14162   99 EPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGfargvmktkdgKPKLSETYCGSYA----YASPE 174

                         90       100
                 ....*....|....*....|....*..
gi 332801047 455 V-GGISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14162  175 IlRGIPYDPFLSDIWSMGVVLYTMVYG 201
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
 388-527 1.80e-07

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: 52.55  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG-HIRLTYFG------QWSEVEPQCCGEAVdnlYSAPEV-GGIS 459
Cdd:cd14164  101 LARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGfarfveDYPELSTTFCGSRA---YTPPEViLGTP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTG----------MALSQS----HPSGIQahtqlqlpewLSRPAASLLTELLQFEPTRRLGM 525
Cdd:cd14164  178 YDPKKYDVWSLGVVLYVMVTGtmpfdetnvrRLRLQQrgvlYPSGVA----------LEEPCRALIRTLLQFNPSTRPSI 247


                 ..
gi 332801047 526 GE 527
Cdd:cd14164  248 QQ 249
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
 384-539 1.97e-07

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: 52.76  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCcGEAVDNL----YSAPE-VGGI 458
Cdd:cd07847   97 VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPG-DDYTDYVatrwYRAPElLVGD 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMAL-------SQSH----------PSGIQAHTQ------LQLPE------------WL 503
Cdd:cd07847  176 TQYGPPVDVWAIGCVFAELLTGQPLwpgksdvDQLYlirktlgdliPRHQQIFSTnqffkgLSIPEpetrepleskfpNI 255

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 332801047 504 SRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPFF 539
Cdd:cd07847  256 SSPALSFLKGCLQMDPTERL-----SCEELLEHPYF 286
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
 385-539 2.07e-07

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: 52.51  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLdQAGHIRLTYFGQWSEVEPqccGEAVDNLYS-----APEVGGIS 459
Cdd:cd14109   97 TERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLR---GKLTTLIYGspefvSPEIVNSY 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMA--LSQSHPSGI----QAHTQLQLPEW--LSRPAASLLTELLQFEPTRRLGMGEGgvs 531
Cdd:cd14109  173 PVTLATDMWSVGVLTYVLLGGISpfLGDNDRETLtnvrSGKWSFDSSPLgnISDDARDFIKKLLVYIPESRLTVDEA--- 249


                 ....*...
gi 332801047 532 kLKsHPFF 539
Cdd:cd14109  250 -LN-HPWF 255
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
 386-539 2.14e-07

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: 52.35  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQ-GVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL---------YSAPEV 455
Cdd:cd06605   98 ERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFG--------VSGQLVDSLaktfvgtrsYMAPER 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 GGISELTEACDWWSFGSLLYELLTG---MALSQSHPSG--IQAHTQL------QLP-EWLSRPAASLLTELLQFEPTRRl 523
Cdd:cd06605  170 ISGGKYTVKSDIWSLGLSLVELATGrfpYPPPNAKPSMmiFELLSYIvdepppLLPsGKFSPDFQDFVSQCLQKDPTER- 248

                        170
                 ....*....|....*.
gi 332801047 524 gmgeGGVSKLKSHPFF 539
Cdd:cd06605  249 ----PSYKELMEHPFI 260
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
 386-539 2.59e-07

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: 52.28  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQCCGEAVDNLYSAPEVGGISELTE 463
Cdd:cd07838  106 PETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGlaRIYSFEMALTSVVVTLWYRAPEVLLQSSYAT 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 464 ACDWWSFGSLLYEL---------------------LTGM----------ALSQSH-PSGIQAHTQLQLPEwLSRPAASLL 511
Cdd:cd07838  186 PVDMWSVGCIFAELfnrrplfrgsseadqlgkifdVIGLpseeewprnsALPRSSfPSYTPRPFKSFVPE-IDEEGLDLL 264

                        170       180
                 ....*....|....*....|....*...
gi 332801047 512 TELLQFEPTRRLgmgegGVSKLKSHPFF 539
Cdd:cd07838  265 KKMLTFNPHKRI-----SAFEALQHPYF 287
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
 389-539 2.72e-07

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: 52.50  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQA-GHIRLTYFGQWSEVEPqccGEA-----VDNLYSAPE-VGGISEL 461
Cdd:cd14137  108 VKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFGSAKRLVP---GEPnvsyiCSRYYRAPElIFGATDY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHPSGIQA---------------------HTQLQLPEWLSRP------------AA 508
Cdd:cd14137  185 TTAIDIWSAGCVLAELLLGQPLFPGESSVDQLveiikvlgtptreqikamnpnYTEFKFPQIKPHPwekvfpkrtppdAI 264

                        170       180       190
                 ....*....|....*....|....*....|..
gi 332801047 509 SLLTELLQFEPTRRL-GMgeggvsKLKSHPFF 539
Cdd:cd14137  265 DLLSKILVYNPSKRLtAL------EALAHPFF 290
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
 388-483 2.92e-07

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: 52.23  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEV-GGISELTE 463
Cdd:cd07843  107 EVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGlarEYGSPLKPYTQLVVTLWYRAPELlLGAKEYST 186

                         90       100
                 ....*....|....*....|
gi 332801047 464 ACDWWSFGSLLYELLTGMAL 483
Cdd:cd07843  187 AIDMWSVGCIFAELLTKKPL 206
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 395-522 2.94e-07

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: 51.99  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQ--------CCGEAVDN-------LYSAP 453
Cdd:cd14046  112 QILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlatsnkLNVELATQdinkstsaALGSSGDLtgnvgtaLYVAP 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 454 EV--GGISELTEACDWWSFGSLLYELL----TGMalsqshpSGIQAHTQLQLPEWLSRPA---------ASLLTELLQFE 518
Cdd:cd14046  192 EVqsGTKSTYNEKVDMYSLGIIFFEMCypfsTGM-------ERVQILTALRSVSIEFPPDfddnkhskqAKLIRWLLNHD 264


                 ....
gi 332801047 519 PTRR 522
Cdd:cd14046  265 PAKR 268
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 395-479 3.20e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 53.10  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSE-----VEPQCCGEAvdnLYSAPEVGGISELTEACD 466
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGfskQYSDsvsldVASSFCGTP---YYLAPELWERKRYSKKAD 253

                         90
                 ....*....|...
gi 332801047 467 WWSFGSLLYELLT 479
Cdd:PTZ00267 254 MWSLGVILYELLT 266
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
 384-538 3.55e-07

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: 51.52  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG--HIRLTYFGQWSEVEPQCCGEAVDN--LYSAPEVGGIS 459
Cdd:cd14121   92 LPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKPNDEAHSLRGspLYMAPEMILKK 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMALSQSHP-----SGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRRLGMGEggvsk 532
Cdd:cd14121  172 KYDARVDLWSVGVILYECLFGRAPFASRSfeeleEKIRSSKPIEIPTRpeLSADCRDLLLRLLQRDPDRRISFEE----- 246


                 ....*.
gi 332801047 533 LKSHPF 538
Cdd:cd14121  247 FFAHPF 252
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 386-479 4.57e-07

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: 51.35  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALH-EQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISEL 461
Cdd:cd08528  112 EDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGlakQKGPESSKMTSVVGTILYSCPEIVQNEPY 191

                         90
                 ....*....|....*...
gi 332801047 462 TEACDWWSFGSLLYELLT 479
Cdd:cd08528  192 GEKADIWALGCILYQMCT 209
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
 386-538 4.62e-07

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: 51.50  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqccgEAVDNLYS---------APEVg 456
Cdd:cd14199  125 EDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEF------EGSDALLTntvgtpafmAPET- 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 457 gISELT-----EACDWWSFGSLLYELLTG---------MALSQShpsgIQAHTqLQLPEW--LSRPAASLLTELLQFEPT 520
Cdd:cd14199  198 -LSETRkifsgKALDVWAMGVTLYCFVFGqcpfmderiLSLHSK----IKTQP-LEFPDQpdISDDLKDLLFRMLDKNPE 271

                        170
                 ....*....|....*...
gi 332801047 521 RRLgmgegGVSKLKSHPF 538
Cdd:cd14199  272 SRI-----SVPEIKLHPW 284
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
 386-539 4.68e-07

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: 51.55  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSE-VEPQCCGEAVDNLYSAPEV-GGISE 460
Cdd:cd07833   99 PDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGfarALTArPASPLTDYVATRWYRAPELlVGDTN 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMAL----------------------------------------SQSHPSGIqahtQLQLP 500
Cdd:cd07833  179 YGKPVDVWAIGCIMAELLDGEPLfpgdsdidqlyliqkclgplppshqelfssnprfagvafpEPSQPESL----ERRYP 254

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332801047 501 EWLSRPAASLLTELLQFEPTRRLGMGEggvskLKSHPFF 539
Cdd:cd07833  255 GKVSSPALDFLKACLRMDPKERLTCDE-----LLQHPYF 288
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
 386-514 5.21e-07

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: 51.96  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVG-GISELTEA 464
Cdd:cd07877  119 DDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMlNWMHYNQT 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332801047 465 CDWWSFGSLLYELLTGMALSqshpSGIQAHTQLQLPEWLS-RPAASLLTEL 514
Cdd:cd07877  199 VDIWSVGCIMAELLTGRTLF----PGTDHIDQLKLILRLVgTPGAELLKKI 245
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 383-482 5.34e-07

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: 51.06  E-value: 5.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG--HIRLTYFGQWSEV---EPQCCGEAVDNlYSAPEVGG 457
Cdd:cd14108   93 TVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELtpnEPQYCKYGTPE-FVAPEIVN 171

                         90       100
                 ....*....|....*....|....*
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGMA 482
Cdd:cd14108  172 QSPVSKVTDIWPVGVIAYLCLTGIS 196
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 386-522 5.49e-07

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: 51.11  E-value: 5.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAvdnLYSAPE-VGGIS 459
Cdd:cd14161  101 ELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGlsnlyNQDKFLQTYCGSP---LYASPEiVNGRP 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332801047 460 ELTEACDWWSFGSLLYELLTG-MALS-QSHPSGIQAHTQLQLPEwLSRP--AASLLTELLQFEPTRR 522
Cdd:cd14161  178 YIGPEVDSWSLGVLLYILVHGtMPFDgHDYKILVKQISSGAYRE-PTKPsdACGLIRWLLMVNPERR 243
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
 386-539 5.53e-07

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: 51.29  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVggISEL- 461
Cdd:cd06648  102 EEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGfcaQVSKEVPRRKSLVGTPYWMAPEV--ISRLp 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 --TEAcDWWSFGSLLYELLTGMALSQSHPSgIQAHTQLQ--LPEWLSRPA------ASLLTELLQFEPTRRLGMGEggvs 531
Cdd:cd06648  180 ygTEV-DIWSLGIMVIEMVDGEPPYFNEPP-LQAMKRIRdnEPPKLKNLHkvsprlRSFLDRMLVRDPAQRATAAE---- 253


                 ....*...
gi 332801047 532 kLKSHPFF 539
Cdd:cd06648  254 -LLNHPFL 260
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 392-522 6.27e-07

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: 51.18  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQG---VLCRDLHPGNLLLDQAGH--------IRLTYFG---QWSEVEPQccGEAVDNLYSAPEVGG 457
Cdd:cd14147  106 WAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIEnddmehktLKITDFGlarEWHKTTQM--SAAGTYAWMAPEVIK 183

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGMA-------LSQSHPSGIQAHTqLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14147  184 ASTFSKGSDVWSFGVLLWELLTGEVpyrgidcLAVAYGVAVNKLT-LPIPSTCPEPFAQLMADCWAQDPHRR 254
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 386-540 6.44e-07

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: 51.42  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQW-AAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVggisELT-- 462
Cdd:cd07856  106 EKQFIQYfLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEI----MLTwq 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 ---EACDWWSFGSLLYELLTGMAL--SQSHPSGIQAHTQL----------------------QLPEWLSRP--------- 506
Cdd:cd07856  182 kydVEVDIWSAGCIFAEMLEGKPLfpGKDHVNQFSIITELlgtppddvinticsentlrfvqSLPKRERVPfsekfknad 261

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 332801047 507 --AASLLTELLQFEPTRRLGMGEGgvsklKSHPFFS 540
Cdd:cd07856  262 pdAIDLLEKMLVFDPKKRISAAEA-----LAHPYLA 292
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
 395-540 7.83e-07

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: 51.25  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-------QWSEVEPQCCGEAVDNLYSAPEVG-GISELTEACD 466
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGlargfseNPGENAGFMTEYVATRWYRAPEIMlSFQSYTKAID 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 467 WWSFGSLLYELLTGMAL-----------------------SQSHPSGIQAHTQL-QLPEWLSRP-----------AASLL 511
Cdd:cd07857  193 VWSVGCILAELLGRKPVfkgkdyvdqlnqilqvlgtpdeeTLSRIGSPKAQNYIrSLPNIPKKPfesifpnanplALDLL 272

                        170       180
                 ....*....|....*....|....*....
gi 332801047 512 TELLQFEPTRRLgmgegGVSKLKSHPFFS 540
Cdd:cd07857  273 EKLLAFDPTKRI-----SVEEALEHPYLA 296
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 395-534 8.35e-07

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: 50.55  E-value: 8.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEA--VDNLY-SAPEV--GGISELTEAcDWWS 469
Cdd:cd06917  109 EVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRStfVGTPYwMAPEVitEGKYYDTKA-DIWS 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 470 FGSLLYELLTGmalsqSHP-SGIQAHTQLQL------PEWLSRPAASLLTEL----LQFEPTRRLGMGEggVSKLK 534
Cdd:cd06917  188 LGITTYEMATG-----NPPySDVDALRAVMLipkskpPRLEGNGYSPLLKEFvaacLDEEPKDRLSADE--LLKSK 256
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 399-527 8.51e-07

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: 50.40  E-value: 8.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLL--DQAG--HIRLTYFGQWSEVEPQ---CCGEAVdnlYSAPEVggISELTEAC--DWWS 469
Cdd:cd14095  110 ALKYLHSLSIVHRDIKPENLLVveHEDGskSLKLADFGLATEVKEPlftVCGTPT---YVAPEI--LAETGYGLkvDIWA 184

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332801047 470 FGSLLYELLTGMALSQShPSG--------IQA-HTQLQLPEW--LSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd14095  185 AGVITYILLCGFPPFRS-PDRdqeelfdlILAgEFEFLSPYWdnISDSAKDLISRMLVVDPEKRYSAGQ 252
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
 386-522 8.67e-07

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: 50.40  E-value: 8.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG--HIRLTYFGqwsevEPQCCGEAVDNL-----YSAPEVGGI 458
Cdd:cd13987   90 EERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFG-----LTRRVGSTVKRVsgtipYTAPEVCEA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SE-----LTEACDWWSFGSLLYELLTGM---ALSQSHPSGIQAHTQLQ------LP-EW--LSRPAASLLTELLQFEPTR 521
Cdd:cd13987  165 KKnegfvVDPSIDVWAFGVLLFCCLTGNfpwEKADSDDQFYEEFVRWQkrkntaVPsQWrrFTPKALRMFKKLLAPEPER 244


                 .
gi 332801047 522 R 522
Cdd:cd13987  245 R 245
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 386-527 9.03e-07

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: 51.03  E-value: 9.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGqWSEVEPQCCGEAVDNL----YSAPEVGGI 458
Cdd:cd14180  100 ESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFG-FARLRPQGSRPLQTPCftlqYAAPELFSN 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLTGMALSQSHpSGIQAHTQ--------------LQLPEW--LSRPAASLLTELLQFEPTRR 522
Cdd:cd14180  179 QGYDESCDLWSLGVILYTMLSGQVPFQSK-RGKMFHNHaadimhkikegdfsLEGEAWkgVSEEAKDLVRGLLTVDPAKR 257


                 ....*
gi 332801047 523 LGMGE 527
Cdd:cd14180  258 LKLSE 262
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 386-522 1.01e-06

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: 50.34  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHI-RLTYFG------QWSEVEPQCCGEAvdnLYSAPEVGGI 458
Cdd:cd08225  100 EDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGiarqlnDSMELAYTCVGTP---YYLSPEICQN 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 459 SELTEACDWWSFGSLLYELLT------GMALSQSHPSGIQAHTQLQLPEWlSRPAASLLTELLQFEPTRR 522
Cdd:cd08225  177 RPYNNKTDIWSLGCVLYELCTlkhpfeGNNLHQLVLKICQGYFAPISPNF-SRDLRSLISQLFKVSPRDR 245
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
 400-522 1.02e-06

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: 50.78  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLL-LDQAGH---IRLTYFGQWSEVEPQCcGEAVDNLYSA----PEVGGISELTEACDWWSFG 471
Cdd:cd14177  111 VDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGEN-GLLLTPCYTAnfvaPEVLMRQGYDAACDIWSLG 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 472 SLLYELLTGMALSQSHPSGIQAHTQLQLPE---------W--LSRPAASLLTELLQFEPTRR 522
Cdd:cd14177  190 VLLYTMLAGYTPFANGPNDTPEEILLRIGSgkfslsggnWdtVSDAAKDLLSHMLHVDPHQR 251
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 386-479 1.06e-06

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: 50.19  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWSEVEPQCCGEAvdnLYSAPEVGGIS 459
Cdd:cd08218  100 EDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGiarvlnSTVELARTCIGTP---YYLSPEICENK 176

                         90       100
                 ....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLT 479
Cdd:cd08218  177 PYNNKSDIWALGCVLYEMCT 196
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
 386-483 1.11e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 50.91  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------------QWSEVEPQC-----CGEAVDN 448
Cdd:PTZ00024 118 ESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGlarrygyppysdTLSKDETMQrreemTSKVVTL 197

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 332801047 449 LYSAPE-VGGISELTEACDWWSFGSLLYELLTGMAL 483
Cdd:PTZ00024 198 WYRAPElLMGAEKYHFAVDMWSVGCIFAELLTGKPL 233
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
 386-538 1.14e-06

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: 50.28  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQ-GVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP--QCCGEAVDNL-YSAPEVGGISEL 461
Cdd:cd06623   98 EPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENtlDQCNTFVGTVtYMSPERIQGESY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGM-----ALSQSHPSGIQAHTQLQLPEWLSRPA----ASLLTELLQFEPTRRLGMGEggvsk 532
Cdd:cd06623  178 SYAADIWSLGLTLLECALGKfpflpPGQPSFFELMQAICDGPPPSLPAEEFspefRDFISACLQKDPKKRPSAAE----- 252


                 ....*.
gi 332801047 533 LKSHPF 538
Cdd:cd06623  253 LLQHPF 258
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
 386-522 1.16e-06

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: 50.57  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQ---WSEVEPQCCGEAVDNL-YSAPE-VGGISE 460
Cdd:cd07864  115 EDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLarlYNSEESRPYTNKVITLwYRPPElLLGEER 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHT---------------QLQLPEW-------------------LSRP 506
Cdd:cd07864  195 YGPAIDVWSCGCILGELFTKKPIFQANQELAQLELisrlcgspcpavwpdVIKLPYFntmkpkkqyrrrlreefsfIPTP 274

                        170
                 ....*....|....*.
gi 332801047 507 AASLLTELLQFEPTRR 522
Cdd:cd07864  275 ALDLLDHMLTLDPSKR 290
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
 392-522 1.18e-06

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: 49.99  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQG---VLCRDLHPGNLLLDQAGH--------IRLTYFG---QWSEVEPQccGEAVDNLYSAPEVGG 457
Cdd:cd14148   97 WAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPIEnddlsgktLKITDFGlarEWHKTTKM--SAAGTYAWMAPEVIR 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTqLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14148  175 LSLFSKSSDVWSFGVLLWELLTGEvpyreidALAVAYGVAMNKLT-LPIPSTCPEPFARLLEECWDPDPHGR 245
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 395-538 1.19e-06

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: 50.50  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFGQWSEVE---PQCCGEAVDNLYSAPEVGGISELTEACDWW 468
Cdd:cd14086  108 QILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQgdqQAWFGFAGTPGYLSPEVLRKDPYGKPVDIW 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 469 SFGSLLYELLTG----------------MALSQSHPSgiqahtqlqlPEW--LSRPAASLLTELLQFEPTRRLGMGEGgv 530
Cdd:cd14086  188 ACGVILYILLVGyppfwdedqhrlyaqiKAGAYDYPS----------PEWdtVTPEAKDLINQMLTVNPAKRITAAEA-- 255


                 ....*...
gi 332801047 531 skLKsHPF 538
Cdd:cd14086  256 --LK-HPW 260
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
 389-543 1.42e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 50.80  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH-IRLTYFGQWSEV--EPQCCGEAVDNLYSAPEVG-GISELTEA 464
Cdd:PTZ00036 172 VKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLlaGQRSVSYICSRFYRAPELMlGATNYTTH 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSHPS-----------GIQAHTQLQ----------------------LPEWLSRPAASLL 511
Cdd:PTZ00036 252 IDLWSLGCIIAEMILGYPIFSGQSSvdqlvriiqvlGTPTEDQLKemnpnyadikfpdvkpkdlkkvFPKGTPDDAINFI 331

                        170       180       190
                 ....*....|....*....|....*....|..
gi 332801047 512 TELLQFEPTRRLGMGEGgvsklKSHPFFSTIQ 543
Cdd:PTZ00036 332 SQFLKYEPLKRLNPIEA-----LADPFFDDLR 358
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
 387-539 1.45e-06

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: 49.96  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwseVEPQCCGEAVDNL-----YSAPEVGGISEL 461
Cdd:cd07863  108 ETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGL---ARIYSCQMALTPVvvtlwYRAPEVLLQSTY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELL-------------------------------TGMALSQSH--PSGIQAHTQLqLPEwLSRPAA 508
Cdd:cd07863  185 ATPVDMWSVGCIFAEMFrrkplfcgnseadqlgkifdliglppeddwpRDVTLPRGAfsPRGPRPVQSV-VPE-IEESGA 262

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332801047 509 SLLTELLQFEPTRRLgmgegGVSKLKSHPFF 539
Cdd:cd07863  263 QLLLEMLTFNPHKRI-----SAFRALQHPFF 288
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 60-116 1.48e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239147  Cd Length: 75  Bit Score: 45.96  E-value: 1.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332801047  60 ALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNC 116
Cdd:cd02684   13 AVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKAL 69
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 383-523 1.51e-06

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: 49.89  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLD---QAGHIRLTYFGqWSEVEPQ-----CCGEAVdnlYSAPE 454
Cdd:cd14169   97 SYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFG-LSKIEAQgmlstACGTPG---YVAPE 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332801047 455 VGGISELTEACDWWSFGSLLYELLTGMAL------SQSHPSGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14169  173 LLEQKPYGKAVDVWAIGVISYILLCGYPPfydendSELFNQILKAEYEFDSPYWddISESAKDFIRHLLERDPEKRF 249
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
 389-522 1.55e-06

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: 49.66  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQaGHIRLTYFGQWSEVEPQCCGEAVDNL--------YSAPEV----- 455
Cdd:cd14063   99 TVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSLSGLLQPGRREDTLvipngwlcYLAPEIirals 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 -----GGISELTEACDWWSFGSLLYELLTG-MALSQSHPSGI---------QAHTQLQLPewlsRPAASLLTELLQFEPT 520
Cdd:cd14063  178 pdldfEESLPFTKASDVYAFGTVWYELLAGrWPFKEQPAESIiwqvgcgkkQSLSQLDIG----REVKDILMQCWAYDPE 253


                 ..
gi 332801047 521 RR 522
Cdd:cd14063  254 KR 255
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
 379-523 1.84e-06

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: 49.35  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYfgqwSEVEPQCCGEAVDN---------L 449
Cdd:cd13976   76 RSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRL----ESLEDAVILEGEDDslsdkhgcpA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 YSAPEV--GGISELTEACDWWSFGSLLYELLTG-MALSQSHPSGIQA---HTQLQLPEWLSRPAASLLTELLQFEPTRRL 523
Cdd:cd13976  152 YVSPEIlnSGATYSGKAADVWSLGVILYTMLVGrYPFHDSEPASLFAkirRGQFAIPETLSPRARCLIRSLLRREPSERL 231
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 404-522 1.95e-06

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: 49.31  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 404 HEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAvdnLYSAPE-VGGISELTEACDWWSFGSLLYEL 477
Cdd:cd14073  118 HKNGVVHRDLKLENILLDQNGNAKIADFGlsnlySKDKLLQTFCGSP---LYASPEiVNGTPYQGPEVDCWSLGVLLYTL 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 332801047 478 LTGmalsqSHPSGIQAHTQL--QL-------PEWLSRpAASLLTELLQFEPTRR 522
Cdd:cd14073  195 VYG-----TMPFDGSDFKRLvkQIssgdyrePTQPSD-ASGLIRWMLTVNPKRR 242
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
 389-542 2.03e-06

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: 49.61  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEV-GGISELTEA 464
Cdd:cd07872  106 VKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGlarAKSVPTKTYSNEVVTLWYRPPDVlLGSSEYSTQ 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 465 CDWWSFGSLLYELLTGMAL--------------------SQSHPSGIQAHTQLQ---LPEWLSRP-----------AASL 510
Cdd:cd07872  186 IDMWGVGCIFFEMASGRPLfpgstvedelhlifrllgtpTEETWPGISSNDEFKnynFPKYKPQPlinhaprldteGIEL 265

                        170       180       190
                 ....*....|....*....|....*....|..
gi 332801047 511 LTELLQFEPTRRLGMGEGgvsklKSHPFFSTI 542
Cdd:cd07872  266 LTKFLQYESKKRISAEEA-----MKHAYFRSL 292
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 384-480 2.05e-06

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: 49.54  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQA---GHIRLTYFGQWSEVEPQCcgEAVDNL----YSAPEVG 456
Cdd:cd14198  107 VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHAC--ELREIMgtpeYLAPEIL 184

                         90       100
                 ....*....|....*....|....
gi 332801047 457 GISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14198  185 NYDPITTATDMWNIGVIAYMLLTH 208
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
 371-539 2.42e-06

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: 49.45  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 371 DGAGRGCGRatwSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQA-GHIRLTYFG---QWSEVEPQCCGEAV 446
Cdd:cd07837   96 DSYGRGPHN---PLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGlgrAFTIPIKSYTHEIV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 447 DNLYSAPEV-GGISELTEACDWWSFGSLLYEL---------------------LTGMALSQSHPSGIQAHTQLQLPEW-- 502
Cdd:cd07837  173 TLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMsrkqplfpgdselqqllhifrLLGTPNEEVWPGVSKLRDWHEYPQWkp 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 332801047 503 ---------LSRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPFF 539
Cdd:cd07837  253 qdlsravpdLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
 387-539 2.61e-06

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: 49.49  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLT-YFGQWSEVEPQCC-------GEAVDN---------- 448
Cdd:cd14134  115 EHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYnPKKKRQIRVPKSTdiklidfGSATFDdeyhssivst 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 449 -LYSAPEVggISEL--TEACDWWSFGSLLYELLTGMALSQSH----------------PS------------GIQAHTQL 497
Cdd:cd14134  195 rHYRAPEV--ILGLgwSYPCDVWSIGCILVELYTGELLFQTHdnlehlammerilgplPKrmirrakkgakyFYFYHGRL 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 498 QLPEwLSRPAAS------------------------LLTELLQFEPTRRLGMGEGgvskLKsHPFF 539
Cdd:cd14134  273 DWPE-GSSSGRSikrvckplkrlmllvdpehrllfdLIRKMLEYDPSKRITAKEA----LK-HPFF 332
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
 382-522 2.78e-06

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: 49.20  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 382 W-SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGQWSEVEP-----QCCGEAVdnlYSA 452
Cdd:cd14113   97 WgNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNTtyyihQLLGSPE---FAA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 453 PEV--GGISELTEacDWWSFGSLLYELLTGMA--LSQSHPSGIQAHTQLQLP------EWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14113  174 PEIilGNPVSLTS--DLWSIGVLTYVLLSGVSpfLDESVEETCLNICRLDFSfpddyfKGVSQKAKDFVCFLLQMDPAKR 251
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
 386-539 2.92e-06

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: 49.24  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEA-----------VDNLYS 451
Cdd:cd07866  114 ESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGlarPYDGPPPNPKGGGgggtrkytnlvVTRWYR 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 452 APE-VGGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAH---------TQLQLPEWLSRPA-------------- 507
Cdd:cd07866  194 PPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHlifklcgtpTEETWPGWRSLPGcegvhsftnyprtl 273

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 332801047 508 -----------ASLLTELLQFEPTRRLGMGEGgvsklKSHPFF 539
Cdd:cd07866  274 eerfgklgpegLDLLSKLLSLDPYKRLTASDA-----LEHPYF 311
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 395-522 2.97e-06

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: 49.28  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYFG-----QWSEVEPQCCGEAVdnlYSAPEVGGISELTEACD 466
Cdd:cd14168  116 QVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGlskmeGKGDVMSTACGTPG---YVAPEVLAQKPYSKAVD 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332801047 467 WWSFGSLLYELLTGMAL------SQSHPSGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRR 522
Cdd:cd14168  193 CWSIGVIAYILLCGYPPfydendSKLFEQILKADYEFDSPYWddISDSAKDFIRNLMEKDPNKR 256
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 395-480 4.43e-06

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: 48.52  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLL---LDQAGHIRLTYFGqWSEVEPQ-----CCGEAVdnlYSAPEVGGISELTEACD 466
Cdd:cd14083  109 QVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFG-LSKMEDSgvmstACGTPG---YVAPEVLAQKPYGKAVD 184

                         90
                 ....*....|....
gi 332801047 467 WWSFGSLLYELLTG 480
Cdd:cd14083  185 CWSIGVISYILLCG 198
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
 386-483 4.58e-06

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: 48.83  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVggI---SELT 462
Cdd:cd07851  117 DDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEI--MlnwMHYN 194

                         90       100
                 ....*....|....*....|.
gi 332801047 463 EACDWWSFGSLLYELLTGMAL 483
Cdd:cd07851  195 QTVDIWSVGCIMAELLTGKTL 215
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
 399-487 5.41e-06

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: 48.38  E-value: 5.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLL-----DQAGHIRLTYFGqwseVEPQCCGEAVDNL-----YSAPEVG-GISELTEACDW 467
Cdd:cd14000  124 GLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYG----ISRQCCRMGAKGSegtpgFRAPEIArGNVIYNEKVDV 199

                         90       100
                 ....*....|....*....|
gi 332801047 468 WSFGSLLYELLTGMALSQSH 487
Cdd:cd14000  200 FSFGMLLYEILSGGAPMVGH 219
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
 385-538 5.74e-06

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: 48.15  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqcCGEAVDNLYS------------- 451
Cdd:cd06629  106 EEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFG---------ISKKSDDIYGnngatsmqgsvfw 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 452 -APEVggISELTEA----CDWWSFGSLLYELLTG----------------MALSQSHPsgiqahtqlqLPE--WLSRPAA 508
Cdd:cd06629  177 mAPEV--IHSQGQGysakVDIWSLGCVVLEMLAGrrpwsddeaiaamfklGNKRSAPP----------VPEdvNLSPEAL 244

                        170       180       190
                 ....*....|....*....|....*....|
gi 332801047 509 SLLTELLQFEPTRRLGMGEggvskLKSHPF 538
Cdd:cd06629  245 DFLNACFAIDPRDRPTAAE-----LLSHPF 269
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
 384-539 5.79e-06

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: 48.11  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVggISE 460
Cdd:cd06658  115 MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGfcaQVSKEVPKRKSLVGTPYWMAPEV--ISR 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 L---TEAcDWWSFGSLLYELLTGMALSQSHPSgIQAHTQLQ--LPEWL--SRPAASLLTELLQF----EPTRRLGMGEgg 529
Cdd:cd06658  193 LpygTEV-DIWSLGIMVIEMIDGEPPYFNEPP-LQAMRRIRdnLPPRVkdSHKVSSVLRGFLDLmlvrEPSQRATAQE-- 268

                        170
                 ....*....|
gi 332801047 530 vskLKSHPFF 539
Cdd:cd06658  269 ---LLQHPFL 275
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 393-538 6.44e-06

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: 48.19  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 393 AAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL---------YSAPE--VGGISEL 461
Cdd:cd06621  111 AESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFG--------VSGELVNSLagtftgtsyYMAPEriQGGPYSI 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TeaCDWWSFGsllyelLTGMALSQSH----PSGIQAHTQLQL---------PE----------WlSRPAASLLTELLQFE 518
Cdd:cd06621  183 T--SDVWSLG------LTLLEVAQNRfpfpPEGEPPLGPIELlsyivnmpnPElkdepengikW-SESFKDFIEKCLEKD 253

                        170       180
                 ....*....|....*....|
gi 332801047 519 PTRRlgmgeGGVSKLKSHPF 538
Cdd:cd06621  254 GTRR-----PGPWQMLAHPW 268
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
 386-542 6.66e-06

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: 47.82  E-value: 6.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-------------------QWSEVEPQCCGEAV 446
Cdd:cd06611  102 EPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGvsaknkstlqkrdtfigtpYWMAPEVVACETFK 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 447 DNLYSApevggiselteACDWWSFGSLLYELLTGMAL-SQSHPSGIQAHTQLQLPEWLSRPA------ASLLTELLQFEP 519
Cdd:cd06611  182 DNPYDY-----------KADIWSLGITLIELAQMEPPhHELNPMRVLLKILKSEPPTLDQPSkwsssfNDFLKSCLVKDP 250

                        170       180
                 ....*....|....*....|...
gi 332801047 520 TRRLGMGEggvskLKSHPFFSTI 542
Cdd:cd06611  251 DDRPTAAE-----LLKHPFVSDQ 268
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
 392-480 6.72e-06

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: 47.49  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCcGEAVDNLYSAPEVGGISELTEACDWW 468
Cdd:cd14059   86 WSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGtskELSEKSTKM-SFAGTVAWMAPEVIRNEPCSEKVDIW 164

                         90
                 ....*....|..
gi 332801047 469 SFGSLLYELLTG 480
Cdd:cd14059  165 SFGVVLWELLTG 176
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
 391-489 6.81e-06

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: 48.09  E-value: 6.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 391 QWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQC--------CGEAVDNLYsAPEVGGISELT 462
Cdd:cd14205  112 QYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFG-LTKVLPQDkeyykvkePGESPIFWY-APESLTESKFS 189

                         90       100
                 ....*....|....*....|....*..
gi 332801047 463 EACDWWSFGSLLYELLTGMALSQSHPS 489
Cdd:cd14205  190 VASDVWSFGVVLYELFTYIEKSKSPPA 216
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
 379-483 7.24e-06

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: 48.14  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEV 455
Cdd:cd07858  100 RSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGlarTTSEKGDFMTEYVVTRWYRAPEL 179

                         90       100
                 ....*....|....*....|....*....
gi 332801047 456 -GGISELTEACDWWSFGSLLYELLTGMAL 483
Cdd:cd07858  180 lLNCSEYTTAIDVWSVGCIFAELLGRKPL 208
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
 386-539 9.05e-06

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: 47.67  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG----------QWSEvepqccgEAVDNLYSAPEV 455
Cdd:cd07835   98 PPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGlarafgvpvrTYTH-------EVVTLWYRAPEI 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 --GGISELTeACDWWSFGSLLYELLTGMAL---------------------SQSHPsGIqahTQLQ-----LPEW----- 502
Cdd:cd07835  171 llGSKHYST-PVDIWSVGCIFAEMVTRRPLfpgdseidqlfrifrtlgtpdEDVWP-GV---TSLPdykptFPKWarqdl 245

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 332801047 503 ------LSRPAASLLTELLQFEPTRRLgmgegGVSKLKSHPFF 539
Cdd:cd07835  246 skvvpsLDEDGLDLLSQMLVYDPAKRI-----SAKAALQHPYF 283
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
 395-480 9.27e-06

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: 47.65  E-value: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVDNLYSAPEV-GGISELTEACDWWSF 470
Cdd:cd07870  106 QLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSqtySSEVVTLWYRPPDVlLGATDYSSALDIWGA 185

                         90
                 ....*....|
gi 332801047 471 GSLLYELLTG 480
Cdd:cd07870  186 GCIFIEMLQG 195
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 385-527 1.01e-05

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: 47.33  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqccGEAVDNL-----YSAPE----- 454
Cdd:cd14075   99 SESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR---GETLNTFcgsppYAAPElfkde 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 455 --VGgiseltEACDWWSFGSLLYELLTGMAlsqshPsgIQAHT-----------QLQLPEWLSRPAASLLTELLQFEPTR 521
Cdd:cd14075  176 hyIG------IYVDIWALGVLLYFMVTGVM-----P--FRAETvaklkkcilegTYTIPSYVSEPCQELIRGILQPVPSD 242


                 ....*.
gi 332801047 522 RLGMGE 527
Cdd:cd14075  243 RYSIDE 248
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
 383-480 1.02e-05

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: 47.26  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGN-LLLDQAG---HIRLTYFGQWSEVEPqccGEAVDNLYS-----AP 453
Cdd:cd14196  104 SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIED---GVEFKNIFGtpefvAP 180

                         90       100
                 ....*....|....*....|....*..
gi 332801047 454 EVGGISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14196  181 EIVNYEPLGLEADMWSIGVITYILLSG 207
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 395-538 1.04e-05

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: 47.21  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQaGHIRLTYFGQWSEVEP--------QCCG-------EAVDNLYSAPEVGGIS 459
Cdd:cd14131  111 QMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAIQNdttsivrdSQVGtlnymspEAIKDTSASGEGKPKS 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMALSQSHPSGIQ-------AHTQLQLPEWLSRPAASLLTELLQFEPTRRLgmgegGVSK 532
Cdd:cd14131  190 KIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAklqaiidPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRP-----SIPE 264


                 ....*.
gi 332801047 533 LKSHPF 538
Cdd:cd14131  265 LLNHPF 270
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
 387-482 1.07e-05

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: 47.38  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEV-GGISELT 462
Cdd:cd07869  103 ENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGlarAKSVPSHTYSNEVVTLWYRPPDVlLGSTEYS 182

                         90       100
                 ....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGMA 482
Cdd:cd07869  183 TCLDMWGVGCIFVEMIQGVA 202
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
 393-522 1.19e-05

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: 46.86  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 393 AAEMLV----ALEALHEQGVLCRDLHPGNLLL----DQAGHIRLTYFGQWSEV-EP--QCCGEAVdnlYSAPEVGGISEL 461
Cdd:cd14185  100 AALMIIdlceALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVtGPifTVCGTPT---YVAPEILSEKGY 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHPSG-------IQ-AHTQLQLPEW--LSRPAASLLTELLQFEPTRR 522
Cdd:cd14185  177 GLEVDMWAAGVILYILLCGFPPFRSPERDqeelfqiIQlGHYEFLPPYWdnISEAAKDLISRLLVVDPEKR 247
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
 379-527 1.28e-05

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: 46.80  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwseVEPQCCGEAVDN---------L 449
Cdd:cd14024   76 RRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVN----LEDSCPLNGDDDsltdkhgcpA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 YSAPEV--GGISELTEACDWWSFGSLLYELLTGMALSQ-SHPSGIQAHTQ---LQLPEWLSRPAASLLTELLQFEPTRRL 523
Cdd:cd14024  152 YVGPEIlsSRRSYSGKAADVWSLGVCLYTMLLGRYPFQdTEPAALFAKIRrgaFSLPAWLSPGARCLVSCMLRRSPAERL 231


                 ....
gi 332801047 524 GMGE 527
Cdd:cd14024  232 KASE 235
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
 384-478 1.41e-05

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: 46.95  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQCCGEAVDNLYSAPEVGGISEL 461
Cdd:cd07862  107 VPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGlaRIYSFQMALTSVVVTLWYRAPEVLLQSSY 186

                         90
                 ....*....|....*..
gi 332801047 462 TEACDWWSFGSLLYELL 478
Cdd:cd07862  187 ATPVDLWSVGCIFAEMF 203
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 385-482 1.54e-05

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: 46.85  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQA---GHIRLTYFG-----QWSEVEPQCCGEAVdnlYSAPEVG 456
Cdd:cd14197  109 KEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGlsrilKNSEELREIMGTPE---YVAPEIL 185

                         90       100
                 ....*....|....*....|....*.
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGMA 482
Cdd:cd14197  186 SYEPISTATDMWSIGVLAYVMLTGIS 211
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 392-480 1.87e-05

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: 46.57  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQG---VLCRDLHPGNLLLDQAGH--------IRLTYFG---QWSEVEPQCCGEAVdnLYSAPEVGG 457
Cdd:cd14145  109 WAVQIARGMNYLHCEAivpVIHRDLKSSNILILEKVEngdlsnkiLKITDFGlarEWHRTTKMSAAGTY--AWMAPEVIR 186

                         90       100
                 ....*....|....*....|...
gi 332801047 458 ISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14145  187 SSMFSKGSDVWSYGVLLWELLTG 209
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
 387-522 1.92e-05

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: 46.10  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQG---VLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNL-YSAPEVGGISELT 462
Cdd:cd14060   84 DQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVGTFpWMAPEVIQSLPVS 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 463 EACDWWSFGSLLYELLT------GMALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14060  164 ETCDTYSYGVVLWEMLTrevpfkGLEGLQVAWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKER 229
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
 392-522 1.99e-05

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: 46.23  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQG---VLCRDLHPGNLLLDQAGH--------IRLTYFGQWSEV-EPQCCGEAVDNLYSAPEVGGIS 459
Cdd:cd14061   97 WAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIEnedlenktLKITDFGLAREWhKTTRMSAAGTYAWMAPEVIKSS 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGM-------ALSQSHPSGIQAHTqLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14061  177 TFSKASDVWSYGVLLWELLTGEvpykgidGLAVAYGVAVNKLT-LPIPSTCPEPFAQLMKDCWQPDPHDR 245
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 399-480 2.13e-05

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: 46.22  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEV-EPQCCGEAVDNL-----YSAPEVGGISELTEACDWWSFGS 472
Cdd:cd13979  115 ALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLgEGNEVGTPRSHIggtytYRAPELLKGERVTPKADIYSFGI 194


                 ....*...
gi 332801047 473 LLYELLTG 480
Cdd:cd13979  195 TLWQMLTR 202
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
 379-522 2.30e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 47.17  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWS-----EVEPQCCGEAvdnLY 450
Cdd:PTZ00283 135 KTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGfskMYAatvsdDVGRTFCGTP---YY 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 451 SAPEVGGISELTEACDWWSFGSLLYELLTgmalsQSHP-SGIQAHTQLQ---------LPEWLSRPAASLLTELLQFEPT 520
Cdd:PTZ00283 212 VAPEIWRRKPYSKKADMFSLGVLLYELLT-----LKRPfDGENMEEVMHktlagrydpLPPSISPEMQEIVTALLSSDPK 286


                 ..
gi 332801047 521 RR 522
Cdd:PTZ00283 287 RR 288
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 53-113 2.30e-05

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239146  Cd Length: 77  Bit Score: 42.80  E-value: 2.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332801047  53 AATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEI 113
Cdd:cd02683    6 AKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAI 66
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
 379-539 2.34e-05

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: 46.18  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLtyfgQWSEVEPQCCGEAVDN---------L 449
Cdd:cd14022   76 RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRV----KLESLEDAYILRGHDDslsdkhgcpA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 YSAPEV----GGISelTEACDWWSFGSLLYELLTG-MALSQSHPSGIQAHT---QLQLPEWLSRPAASLLTELLQFEPTR 521
Cdd:cd14022  152 YVSPEIlntsGSYS--GKAADVWSLGVMLYTMLVGrYPFHDIEPSSLFSKIrrgQFNIPETLSPKAKCLIRSILRREPSE 229

                        170
                 ....*....|....*...
gi 332801047 522 RLGMGEggvskLKSHPFF 539
Cdd:cd14022  230 RLTSQE-----ILDHPWF 242
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
 384-542 2.39e-05

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: 46.18  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL-----------YSA 452
Cdd:cd06644  107 LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFG--------VSAKNVKTLqrrdsfigtpyWMA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 453 PEVGGISELTEA-----CDWWSFGSLLYEL---------LTGM----ALSQSHPSGiqahtqLQLPEWLSRPAASLLTEL 514
Cdd:cd06644  179 PEVVMCETMKDTpydykADIWSLGITLIEMaqiepphheLNPMrvllKIAKSEPPT------LSQPSKWSMEFRDFLKTA 252

                        170       180
                 ....*....|....*....|....*...
gi 332801047 515 LQFEPTRRlgmgeGGVSKLKSHPFFSTI 542
Cdd:cd06644  253 LDKHPETR-----PSAAQLLEHPFVSSV 275
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 387-479 2.73e-05

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: 46.26  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQwsevePQCCG--------EAVDNLYSAPEV-GG 457
Cdd:cd07861  101 ELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGL-----ARAFGipvrvythEVVTLWYRAPEVlLG 175

                         90       100
                 ....*....|....*....|..
gi 332801047 458 ISELTEACDWWSFGSLLYELLT 479
Cdd:cd07861  176 SPRYSTPVDIWSIGTIFAEMAT 197
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 386-480 2.85e-05

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: 46.18  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYF--GQWSEVEPQC-----------CGEAVdnl 449
Cdd:cd14174   99 EREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFdlGSGVKLNSACtpittpelttpCGSAE--- 175

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 332801047 450 YSAPEVggISELTEA-------CDWWSFGSLLYELLTG 480
Cdd:cd14174  176 YMAPEV--VEVFTDEatfydkrCDLWSLGVILYIMLSG 211
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
 400-522 3.11e-05

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: 45.83  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQCCGEAVDN-------LYSAPEVGGISELTEACDWWSFGS 472
Cdd:cd05038  122 MEYLGSQRYIHRDLAARNILVESEDLVKISDFG-LAKVLPEDKEYYYVKepgespiFWYAPECLRESRFSSASDVWSFGV 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 473 LLYELLTGMALSQS----------HPSGIQAHTQ----LQLPEWLSRPAA------SLLTELLQFEPTRR 522
Cdd:cd05038  201 TLYELFTYGDPSQSppalflrmigIAQGQMIVTRllelLKSGERLPRPPScpdevyDLMKECWEYEPQDR 270
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
 375-538 3.28e-05

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: 45.76  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 375 RGCGRatwSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQ------CCGEAvdn 448
Cdd:cd06608  104 RKKGK---RLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDSTlgrrntFIGTP--- 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 449 LYSAPEVGGISELTEA-----CDWWSFGSLLYELLTGMA-LSQSHPsgIQAHTQ--------LQLPEWLSRPAASLLTEL 514
Cdd:cd06608  178 YWMAPEVIACDQQPDAsydarCDVWSLGITAIELADGKPpLCDMHP--MRALFKiprnppptLKSPEKWSKEFNDFISEC 255

                        170       180
                 ....*....|....*....|....
gi 332801047 515 LQFEPTRRLGMGEggvskLKSHPF 538
Cdd:cd06608  256 LIKNYEQRPFTEE-----LLEHPF 274
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 386-480 3.33e-05

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: 45.58  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC---CGEAVDNL-YSAPEVGGISEL 461
Cdd:cd14111   98 EDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSlrqLGRRTGTLeYMAPEMVKGEPV 177

                         90
                 ....*....|....*....
gi 332801047 462 TEACDWWSFGSLLYELLTG 480
Cdd:cd14111  178 GPPADIWSIGVLTYIMLSG 196
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 396-480 3.50e-05

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: 45.83  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 396 MLVA-LEALH----EQGVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDN----------LYSAPEVGGISE 460
Cdd:cd06618  119 MTVSiVKALHylkeKHGVIHRDVKPSNILLDESGNVKLCDFG--------ISGRLVDSkaktrsagcaAYMAPERIDPPD 190

                         90       100
                 ....*....|....*....|...
gi 332801047 461 LTE---ACDWWSFGSLLYELLTG 480
Cdd:cd06618  191 NPKydiRADVWSLGISLVELATG 213
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
 386-483 3.68e-05

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: 45.88  E-value: 3.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQccGEAVDNL-----YSAPE-VGGIS 459
Cdd:cd07846   99 ESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP--GEVYTDYvatrwYRAPElLVGDT 176

                         90       100
                 ....*....|....*....|....
gi 332801047 460 ELTEACDWWSFGSLLYELLTGMAL 483
Cdd:cd07846  177 KYGKAVDVWAVGCLVTEMLTGEPL 200
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 399-480 4.14e-05

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: 45.43  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQ-GVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL----------YSAPEVGGISELTEA--- 464
Cdd:cd06616  121 ALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFG--------ISGQLVDSIaktrdagcrpYMAPERIDPSASRDGydv 192

                         90
                 ....*....|....*..
gi 332801047 465 -CDWWSFGSLLYELLTG 480
Cdd:cd06616  193 rSDVWSLGITLYEVATG 209
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
 386-539 4.31e-05

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: 45.75  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISELT 462
Cdd:cd06659  116 EEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGfcaQISKDVPKRKSLVGTPYWMAPEVISRCPYG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 463 EACDWWSFGSLLYELLTGMALSQSHpSGIQAHTQLQ---LPEWLSRPAAS-----LLTELLQFEPTRRlgmgeGGVSKLK 534
Cdd:cd06659  196 TEVDIWSLGIMVIEMVDGEPPYFSD-SPVQAMKRLRdspPPKLKNSHKASpvlrdFLERMLVRDPQER-----ATAQELL 269


                 ....*
gi 332801047 535 SHPFF 539
Cdd:cd06659  270 DHPFL 274
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
 384-480 4.38e-05

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: 45.40  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISE 460
Cdd:cd06657  113 MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaQVSKEVPRRKSLVGTPYWMAPELISRLP 192

                         90       100
                 ....*....|....*....|
gi 332801047 461 LTEACDWWSFGSLLYELLTG 480
Cdd:cd06657  193 YGPEVDIWSLGIMVIEMVDG 212
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
 386-522 4.58e-05

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: 45.09  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQccgeavDNL---------YSAPEVG 456
Cdd:cd08529  100 EDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDT------TNFaqtivgtpyYLSPELC 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 457 GISELTEACDWWSFGSLLYELLTGmalsqSHPSGIQAHTQLQL----------PEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd08529  174 EDKPYNEKSDVWALGCVLYELCTG-----KHPFEAQNQGALILkivrgkyppiSASYSQDLSQLIDSCLTKDYRQR 244
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 386-539 5.28e-05

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: 44.92  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLD-QAGHIRLTYFGQWSEVEPQC----CGEAVdnlYSAPEvggise 460
Cdd:cd14005  106 ENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALLKDSVytdfDGTRV---YSPPE------ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 461 lteacdW-------------WSFGSLLYELLTGmALSQSHPSGIqAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd14005  177 ------WirhgryhgrpatvWSLGILLYDMLCG-DIPFENDEQI-LRGNVLFRPRLSKECCDLISRCLQFDPSKRPSLEQ 248

                        170
                 ....*....|..
gi 332801047 528 ggvskLKSHPFF 539
Cdd:cd14005  249 -----ILSHPWF 255
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 386-527 5.48e-05

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: 45.11  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQaGHIRLTYFGQwSEVEPQCCGEAV----DNLYSAPEVGGISEL 461
Cdd:cd08222  105 ENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGI-SRILMGTSDLATtftgTPYYMSPEVLKHEGY 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 462 TEACDWWSFGSLLYELLT------GMALSQSHPSGIQAHTQlQLPEWLSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd08222  183 NSKSDIWSLGCILYEMCClkhafdGQNLLSVMYKIVEGETP-SLPDKYSKELNAIYSRMLNKDPALRPSAAE 253
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
 386-540 6.40e-05

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: 45.16  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHI-RLTYFGQWSEVEPQCCGEA------VDNLYSAPE-VGG 457
Cdd:cd07854  113 EEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARIVDPHYSHKGylseglVTKWYRSPRlLLS 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTG-MALSQSH---------------------------PSGI-----QAHTQLQ--LPEw 502
Cdd:cd07854  193 PNNYTKAIDMWAAGCIFAEMLTGkPLFAGAHeleqmqlilesvpvvreedrnellnviPSFVrndggEPRRPLRdlLPG- 271

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332801047 503 LSRPAASLLTELLQFEPTRRLGMGEGgvsklKSHPFFS 540
Cdd:cd07854  272 VNPEALDFLEQILTFNPMDRLTAEEA-----LMHPYMS 304
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
 375-539 6.56e-05

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: 44.65  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 375 RGCGRatwsVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL--DQAGHIRLTyfgqwSEVEPQCCGEAVDNL--- 449
Cdd:cd14023   76 RSCKR----LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsdEERTQLRLE-----SLEDTHIMKGEDDALsdk 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 -----YSAPEV----GGISelTEACDWWSFGSLLYELLTG-MALSQSHPSGIQAHT---QLQLPEWLSRPAASLLTELLQ 516
Cdd:cd14023  147 hgcpaYVSPEIlnttGTYS--GKSADVWSLGVMLYTLLVGrYPFHDSDPSALFSKIrrgQFCIPDHVSPKARCLIRSLLR 224

                        170       180
                 ....*....|....*....|...
gi 332801047 517 FEPTRRLGMGEggvskLKSHPFF 539
Cdd:cd14023  225 REPSERLTAPE-----ILLHPWF 242
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
 399-481 6.71e-05

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: 44.85  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLL--DQAGHIRLTYFGQWSEVEPqccGEAVDNLYS-----APEVGGISELTEACDWWSFG 471
Cdd:cd14104  109 ALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQLKP---GDKFRLQYTsaefyAPEVHQHESVSTATDMWSLG 185

                         90
                 ....*....|
gi 332801047 472 SLLYELLTGM 481
Cdd:cd14104  186 CLVYVLLSGI 195
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 377-524 7.80e-05

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: 44.91  E-value: 7.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 377 CGratwsVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLL-DQAGHI--RLTYFGQWSEVEP-QCCGEAVDNL-YS 451
Cdd:cd14039   94 CG-----LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDLDQgSLCTSFVGTLqYL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 452 APEVGGISELTEACDWWSFGSLLYELLTGM--------------ALSQSHPSGIQAH----------TQLQLPEWLSR-- 505
Cdd:cd14039  169 APELFENKSYTVTVDYWSFGTMVFECIAGFrpflhnlqpftwheKIKKKDPKHIFAVeemngevrfsTHLPQPNNLCSli 248

                        170       180
                 ....*....|....*....|.
gi 332801047 506 --PAASLLTELLQFEPTRRLG 524
Cdd:cd14039  249 vePMEGWLQLMLNWDPVQRGG 269
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 378-522 9.60e-05

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: 44.48  E-value: 9.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 378 GRATWSVREEQV-KQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---------------QWSEVEPQC 441
Cdd:cd14048  108 RRCTMESRELFVcLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGlvtamdqgepeqtvlTPMPAYAKH 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 442 CGEAVDNLYSAPEVGGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLSR--PAASLLT-ELLQFE 518
Cdd:cd14048  188 TGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFSTQMERIRTLTDVRKLKFPALFTNkyPEERDMVqQMLSPS 267


                 ....
gi 332801047 519 PTRR 522
Cdd:cd14048  268 PSER 271
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
 383-480 1.06e-04

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: 44.22  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGN-LLLDQAG---HIRLTYFGQWSEVEpqcCGEAVDNLYS-----AP 453
Cdd:cd14195  104 SLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIE---AGNEFKNIFGtpefvAP 180

                         90       100
                 ....*....|....*....|....*..
gi 332801047 454 EVGGISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14195  181 EIVNYEPLGLEADMWSIGVITYILLSG 207
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
 386-479 1.12e-04

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: 44.18  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQaGHIRLTYFGqwsevepQCCGEAVDNLYS---------APEVg 456
Cdd:cd07831   99 EKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFG-------SCRGIYSKPPYTeyistrwyrAPEC- 169

                         90       100
                 ....*....|....*....|....*...
gi 332801047 457 gisELTE-----ACDWWSFGSLLYELLT 479
Cdd:cd07831  170 ---LLTDgyygpKMDIWAVGCVFFEILS 194
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 399-480 1.33e-04

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: 43.86  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLL---DQAGHIRLTYF--GQWSEVEPQC-----------CGEAVdnlYSAPEVggISELT 462
Cdd:cd14173  112 ALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFdlGSGIKLNSDCspistpelltpCGSAE---YMAPEV--VEAFN 186

                         90       100
                 ....*....|....*....|....*
gi 332801047 463 EA-------CDWWSFGSLLYELLTG 480
Cdd:cd14173  187 EEasiydkrCDLWSLGVILYIMLSG 211
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
 387-479 1.43e-04

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: 43.58  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALH---EQGVLCRDLHPGNLLL-DQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVGGISELT 462
Cdd:cd14058   89 AHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPNLLLtNGGTVLKICDFGTACDISTHMTNNKGSAAWMAPEVFEGSKYS 168

                         90
                 ....*....|....*..
gi 332801047 463 EACDWWSFGSLLYELLT 479
Cdd:cd14058  169 EKCDVFSWGIILWEVIT 185
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
387-480 1.44e-04

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----------QWSEV---------EpQCCGEAV 446
Cdd:NF033483 107 EEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaralssttmtQTNSVlgtvhylspE-QARGGTV 185

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332801047 447 DN---LYSApevgGIselteacdwwsfgsLLYELLTG 480
Cdd:NF033483 186 DArsdIYSL----GI--------------VLYEMLTG 204
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
 386-488 1.44e-04

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: 43.91  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISELT 462
Cdd:cd06641  100 ETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGvagQLTDTQIKRN*FVGTPFWMAPEVIKQSAYD 179

                         90       100
                 ....*....|....*....|....*..
gi 332801047 463 EACDWWSFGSLLYELLTGM-ALSQSHP 488
Cdd:cd06641  180 SKADIWSLGITAIELARGEpPHSELHP 206
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
 388-505 1.70e-04

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: 43.73  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEV----EPQCCGEAVDN--LYSAPEVGGISEL 461
Cdd:cd05080  108 QLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVpeghEYYRVREDGDSpvFWYAPECLKEYKF 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332801047 462 TEACDWWSFGSLLYELLTGMALSQSHPS------GIQAH--TQLQLPEWLSR 505
Cdd:cd05080  188 YYASDVWSFGVTLYELLTHCDSSQSPPTkflemiGIAQGqmTVVRLIELLER 239
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
 397-527 1.88e-04

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: 43.87  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 397 LVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqcCGEAVDNLY-SAPEVggISELTEA-----CDWWSF 470
Cdd:cd06633  131 LQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP--ANSFVGTPYwMAPEV--ILAMDEGqydgkVDIWSL 206

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332801047 471 GSLLYEL------LTGM-ALSQSHPSGIQAHTQLQLPEWlSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd06633  207 GITCIELaerkppLFNMnAMSALYHIAQNDSPTLQSNEW-TDSFRGFVDYCLQKIPQERPSSAE 269
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
 399-480 1.93e-04

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: 43.57  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQ-GVLCRDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL----------YSAPEvgGISELTEA--- 464
Cdd:cd06617  115 ALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFG--------ISGYLVDSVaktidagckpYMAPE--RINPELNQkgy 184

                         90
                 ....*....|....*....
gi 332801047 465 ---CDWWSFGSLLYELLTG 480
Cdd:cd06617  185 dvkSDVWSLGITMIELATG 203
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 386-479 2.47e-04

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: 42.80  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQccGEAVDNL-----YSAPEVGGISE 460
Cdd:cd08221  100 EEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSE--SSMAESIvgtpyYMSPELVQGVK 177

                         90
                 ....*....|....*....
gi 332801047 461 LTEACDWWSFGSLLYELLT 479
Cdd:cd08221  178 YNFKSDIWAVGCVLYELLT 196
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 386-477 2.48e-04

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: 42.80  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHI-RLTYFGQWSEVEPQCCGEAV--DNLYSAPEVGGISELT 462
Cdd:cd08220  100 EEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKSKAYTVvgTPCYISPELCEGKPYN 179

                         90
                 ....*....|....*
gi 332801047 463 EACDWWSFGSLLYEL 477
Cdd:cd08220  180 QKSDIWALGCVLYEL 194
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
 386-539 2.61e-04

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: 43.06  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLdQAGHIRLTYFG-------QWSEVEPQCCGEAVdnlYSAPEV-GG 457
Cdd:cd14163  100 EHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGfakqlpkGGRELSQTFCGSTA---YAAPEVlQG 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 458 ISELTEACDWWSFGSLLYELLTG-MALSQSHPSGIQAHTQ--LQLPEWL--SRPAASLLTELLqfEPTRRLgmgEGGVSK 532
Cdd:cd14163  176 VPHDSRKGDIWSMGVVLYVMLCAqLPFDDTDIPKMLCQQQkgVSLPGHLgvSRTCQDLLKRLL--EPDMVL---RPSIEE 250


                 ....*..
gi 332801047 533 LKSHPFF 539
Cdd:cd14163  251 VSWHPWL 257
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
 396-480 2.65e-04

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: 42.91  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 396 MLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGQWSEVE--PQC-----CGEAVdnlYSAPEVGGISELTEAC 465
Cdd:cd14087  106 VLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKkgPNClmkttCGTPE---YIAPEILLRKPYTQSV 182

                         90
                 ....*....|....*
gi 332801047 466 DWWSFGSLLYELLTG 480
Cdd:cd14087  183 DMWAVGVIAYILLSG 197
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 381-494 2.84e-04

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: 42.72  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 381 TWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV---DNLYSAPEVGG 457
Cdd:cd06645  102 TGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSfigTPYWMAPEVAA 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 332801047 458 ISE---LTEACDWWSFGsllyelLTGMALSQSHPSGIQAH 494
Cdd:cd06645  182 VERkggYNQLCDIWAVG------ITAIELAELQPPMFDLH 215
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
 399-480 2.87e-04

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: 42.79  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLL---LDQAGHIRLTYFGQWSEVE-----------PQC---CGEAVdnlYSAPEV-----G 456
Cdd:cd14090  112 ALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKlsstsmtpvttPELltpVGSAE---YMAPEVvdafvG 188

                         90       100
                 ....*....|....*....|....
gi 332801047 457 GISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14090  189 EALSYDKRCDLWSLGVILYIMLCG 212
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 386-479 3.77e-04

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: 42.42  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCcgEAVDNL-----YSAPEVGGISE 460
Cdd:cd08223  101 ERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSS--DMATTLigtpyYMSPELFSNKP 178

                         90
                 ....*....|....*....
gi 332801047 461 LTEACDWWSFGSLLYELLT 479
Cdd:cd08223  179 YNHKSDVWALGCCVYEMAT 197
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
 396-478 3.81e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.91  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 396 MLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVE-----PQCCGEAVDNLYSAPEVGGISELTEACDWWSF 470
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDahpdtPQCYGWSGTLETNSPELLALDPYCAKTDIWSA 273


                 ....*...
gi 332801047 471 GSLLYELL 478
Cdd:PHA03207 274 GLVLFEMS 281
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
 395-488 3.85e-04

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: 42.29  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwseVEPQccgeaVDNLYS------------APEVGGI---S 459
Cdd:cd06613  105 ETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFG----VSAQ-----LTATIAkrksfigtpywmAPEVAAVerkG 175

                         90       100       110
                 ....*....|....*....|....*....|
gi 332801047 460 ELTEACDWWSFGSLLYELLTGM-ALSQSHP 488
Cdd:cd06613  176 GYDGKCDIWALGITAIELAELQpPMFDLHP 205
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
 383-482 4.39e-04

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: 42.47  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAG----HIRLTYFGQWSEVEPqccGEAVDNL-----YSAP 453
Cdd:cd14105  104 SLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAHKIED---GNEFKNIfgtpeFVAP 180

                         90       100
                 ....*....|....*....|....*....
gi 332801047 454 EVGGISELTEACDWWSFGSLLYELLTGMA 482
Cdd:cd14105  181 EIVNYEPLGLEADMWSIGVITYILLSGAS 209
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
 386-514 4.63e-04

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: 42.35  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISELT 462
Cdd:cd06640  100 EFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGvagQLTDTQIKRNTFVGTPFWMAPEVIQQSAYD 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332801047 463 EACDWWSFGsllyelLTGMALSQSHPSGIQAHTQLQLPEWLSRPAASLLTEL 514
Cdd:cd06640  180 SKADIWSLG------ITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDF 225
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 399-538 4.77e-04

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: 41.94  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLL----DQAGHIRLTYFGQWSEVEP---QCCGEAVdnlYSAPEVGGISELTEACDWWSFG 471
Cdd:cd14184  111 ALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGplyTVCGTPT---YVAPEIIAETGYGLKVDIWAAG 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332801047 472 SLLYELLTGMALSQSHpSGIQ---------AHTQLQLPEW--LSRPAASLLTELLQFEPTRRLGMGEggvskLKSHPF 538
Cdd:cd14184  188 VITYILLCGFPPFRSE-NNLQedlfdqillGKLEFPSPYWdnITDSAKELISHMLQVNVEARYTAEQ-----ILSHPW 259
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 386-538 5.13e-04

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: 42.06  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFG-----QWSEVEPQccgeaVDNLYSAPEV-- 455
Cdd:cd14171  108 EKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGfakvdQGDLMTPQ-----FTPYYVAPQVle 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 456 ----------GGISELT-----EACDWWSFGSLLYELLTGMALSQS-HPSG---------IQAHTqLQLPE--W--LSRP 506
Cdd:cd14171  183 aqrrhrkersGIPTSPTpytydKSCDMWSLGVIIYIMLCGYPPFYSeHPSRtitkdmkrkIMTGS-YEFPEeeWsqISEM 261

                        170       180       190
                 ....*....|....*....|....*....|..
gi 332801047 507 AASLLTELLQFEPTRRLGMGEggvskLKSHPF 538
Cdd:cd14171  262 AKDIVRKLLCVDPEERMTIEE-----VLHHPW 288
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
 375-522 5.23e-04

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: 41.78  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 375 RGCGRATwsVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQccgeAVDNL----- 449
Cdd:cd05083   90 RSRGRAL--VPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG-LAKVGSM----GVDNSrlpvk 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 450 YSAPEVGGISELTEACDWWSFGSLLYELLT-------GMALSQSHPSgIQAHTQLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd05083  163 WTAPEALKNKKFSSKSDVWSYGVLLWEVFSygrapypKMSVKEVKEA-VEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKR 241
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 389-483 5.23e-04

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: 42.38  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH--IRLTYFGQwSEVEPQCCGEAVDN-LYSAPEV-GGISELTeA 464
Cdd:cd14225  148 IRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGS-SCYEHQRVYTYIQSrFYRSPEViLGLPYSM-A 225

                         90
                 ....*....|....*....
gi 332801047 465 CDWWSFGSLLYELLTGMAL 483
Cdd:cd14225  226 IDMWSLGCILAELYTGYPL 244
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
 395-480 5.44e-04

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: 42.10  E-value: 5.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIR-----LTYFGQWS-----------EVEPQCCGEAVDNLYSAPE-VGG 457
Cdd:cd14027   98 EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKiadlgLASFKMWSkltkeehneqrEVDGTAKKNAGTLYYMAPEhLND 177

                         90       100
                 ....*....|....*....|....
gi 332801047 458 I-SELTEACDWWSFGSLLYELLTG 480
Cdd:cd14027  178 VnAKPTEKSDVYSFAIVLWAIFAN 201
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
 359-491 5.79e-04

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: 42.04  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 359 CGRGMDqsCLSADGAGRgcgRATWsVREEQVKQWAAEMLVALEALHEQ-GVLCRDLHPGNLLLDQAGHIRLTYFGqwsev 437
Cdd:cd06620   82 CMEYMD--CGSLDKILK---KKGP-FPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFG----- 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332801047 438 epqCCGEAVDNL---------YSAPEVGGISELTEACDWWSFGSLLYELLTG---------MALSQSHPSGI 491
Cdd:cd06620  151 ---VSGELINSIadtfvgtstYMSPERIQGGKYSVKSDVWSLGLSIIELALGefpfagsndDDDGYNGPMGI 219
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 395-523 5.85e-04

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: 42.12  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGH---IRLTYFGQWSEVEPQCCGEAVDNL--YSAPEVGGISELTEACDWWS 469
Cdd:cd14085  106 QILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQVTMKTVCGTpgYCAPEILRGCAYGPEVDMWS 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332801047 470 FGSLLYELLTGM-------ALSQSHPSGIQAHTQLQLPEW--LSRPAASLLTELLQFEPTRRL 523
Cdd:cd14085  186 VGVITYILLCGFepfyderGDQYMFKRILNCDYDFVSPWWddVSLNAKDLVKKLIVLDPKKRL 248
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
 395-483 5.96e-04

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: 42.34  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDWWSFGS 472
Cdd:cd07875  134 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGlaRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC 213

                         90
                 ....*....|.
gi 332801047 473 LLYELLTGMAL 483
Cdd:cd07875  214 IMGEMIKGGVL 224
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
 380-480 6.26e-04

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 41.55  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 380 ATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqwseVEPqccgeavdnlysapevggis 459
Cdd:cd13973   93 ESGPLDPEAAARAVAELAEALAAAHRAGLALGIDHPDRVRISSDGRVVLAFPA----VLA-------------------- 148

                         90       100
                 ....*....|....*....|.
gi 332801047 460 ELTEACDWWSFGSLLYELLTG 480
Cdd:cd13973  149 ALSPATDVRALGALLYALLTG 169
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
 395-516 6.62e-04

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: 41.94  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDWWSFGS 472
Cdd:cd07876  131 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGlaRTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 332801047 473 LLYELLTGMALSQSHPSGIQAHtqlQLPEWLSRPAASLLTELLQ 516
Cdd:cd07876  211 IMGELVKGSVIFQGTDHIDQWN---KVIEQLGTPSAEFMNRLQP 251
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
 389-477 6.71e-04

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: 41.65  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSE--VEPQC-CGEAVDNLYSAPEV-GGISELTEA 464
Cdd:cd07839  101 VKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAfgIPVRCySAEVVTLWYRPPDVlFGAKLYSTS 180

                         90
                 ....*....|...
gi 332801047 465 CDWWSFGSLLYEL 477
Cdd:cd07839  181 IDMWSAGCIFAEL 193
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
 395-488 7.25e-04

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: 41.54  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGI-----SELTEACD 466
Cdd:cd06638  132 EALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGvsaQLTSTRLRRNTSVGTPFWMAPEVIACeqqldSTYDARCD 211

                         90       100
                 ....*....|....*....|...
gi 332801047 467 WWSFGSLLYELLTG-MALSQSHP 488
Cdd:cd06638  212 VWSLGITAIELGDGdPPLADLHP 234
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 386-479 7.60e-04

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: 41.55  E-value: 7.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQG--VLCRDLHPGNLLLDQAGHIRLTYFG----QWSEVEPQC-CGEAVDNL-------YS 451
Cdd:cd13985  102 EEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattEHYPLERAEeVNIIEEEIqknttpmYR 181

                         90       100       110
                 ....*....|....*....|....*....|.
gi 332801047 452 APE---VGGISELTEACDWWSFGSLLYELLT 479
Cdd:cd13985  182 APEmidLYSKKPIGEKADIWALGCLLYKLCF 212
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
 383-522 7.76e-04

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 41.66  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALH--EQGVLCRDLHPGNLLLDQAGHIRLtyfgqwSEVEP-------QCCGEAVDNL-YSA 452
Cdd:cd14034  114 TMNEKAWKRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKI------GSVAPdtinnhvKTCREEQKNLhFFA 187

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047 453 PEVGGISELTEACDWWSFGSLLYEL----LTGMALSQSHPS-GIQAHTQLqLPEWLSRpaaSLLTELLQFEPTRR 522
Cdd:cd14034  188 PEYGEVANVTTAVDIYSFGMCALEMavleIQGNGESSYVPQeAINSAIQL-LEDPLQR---EFIQKCLEVDPSKR 258
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
 393-523 8.68e-04

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: 41.49  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 393 AAEMLVALEALHEQGVLCRDLHPGNLL---LDQAGHI--RLTYFGqwseVEPQCCGEAVDNL-----YSAPEVGGISELT 462
Cdd:cd14067  120 AYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHIniKLSDYG----ISRQSFHEGALGVegtpgYQAPEIRPRIVYD 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 463 EACDWWSFGSLLYELLTGmalsqSHPSgiQAHTQLQLPEWLS---RPA------------ASLLTELLQFEPTRRL 523
Cdd:cd14067  196 EKVDMFSYGMVLYELLSG-----QRPS--LGHHQLQIAKKLSkgiRPVlgqpeevqffrlQALMMECWDTKPEKRP 264
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 386-480 1.03e-03

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: 41.13  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQ---GVLCRDLHPGNLLLDQAGHIRLTYFGQWS----EVEPQCCGEAVDNL--------Y 450
Cdd:cd13986  105 EDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSMNpariEIEGRREALALQDWaaehctmpY 184

                         90       100       110
                 ....*....|....*....|....*....|...
gi 332801047 451 SAPE---VGGISELTEACDWWSFGSLLYELLTG 480
Cdd:cd13986  185 RAPElfdVKSHCTIDEKTDIWSLGCTLYALMYG 217
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 399-527 1.05e-03

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: 40.99  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAG-------HIRLTYFGQwsEVEPQCCGEAV------DNLYSAPEVGGISELTEAC 465
Cdd:cd14097  112 AVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGL--SVQKYGLGEDMlqetcgTPIYMAPEVISAHGYSQQC 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 466 DWWSFGSLLYELLTGMA--LSQSHPSGIQAHTQLQL----PEW--LSRPAASLLTELLQFEPTRRLGMGE 527
Cdd:cd14097  190 DIWSIGVIMYMLLCGEPpfVAKSEEKLFEEIRKGDLtftqSVWqsVSDAAKNVLQQLLKVDPAHRMTASE 259
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 399-479 1.08e-03

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: 40.94  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047  399 ALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG----QWSEVEPQCCGEAVDNL-YSAPEVggISE--LTEACDWWSFG 471
Cdd:pfam07714 114 GMEYLESKNFVHRDLAARNCLVSENLVVKISDFGlsrdIYDDDYYRKRGGGKLPIkWMAPES--LKDgkFTSKSDVWSFG 191


                  ....*...
gi 332801047  472 SLLYELLT 479
Cdd:pfam07714 192 VLLWEIFT 199
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
 411-543 1.14e-03

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: 40.89  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 411 RDLHPGNLLLDQAGHIRLTYFGQwSEVEPQCCGEAVDNL------YSAPEVGGISELTEACDWWSFGSLLYELLTGMALS 484
Cdd:cd05041  118 RDLAARNCLVGENNVLKISDFGM-SREEEDGEYTVSDGLkqipikWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATP 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332801047 485 QSHPSGIQAHTQLQ----------LPEWLSRpaasLLTELLQFEPTRRlgmgeggvsklkshPFFSTIQ 543
Cdd:cd05041  197 YPGMSNQQTREQIEsgyrmpapelCPEAVYR----LMLQCWAYDPENR--------------PSFSEIY 247
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 47-96 1.20e-03

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 38.03  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 332801047  47 RDYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERR 96
Cdd:cd02679    2 RGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVPSAGV 51
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
 379-479 1.30e-03

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: 40.84  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 379 RATWSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC-CGEAVDNL-----YSA 452
Cdd:cd06651  103 KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICmSGTGIRSVtgtpyWMS 182

                         90       100
                 ....*....|....*....|....*..
gi 332801047 453 PEVGGISELTEACDWWSFGSLLYELLT 479
Cdd:cd06651  183 PEVISGEGYGRKADVWSLGCTVVEMLT 209
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
 383-479 1.37e-03

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 40.90  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEP---QCCGeavDNLYS-----APE 454
Cdd:cd05043  112 ALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPmdyHCLG---DNENRpikwmSLE 188

                         90       100
                 ....*....|....*....|....*
gi 332801047 455 VGGISELTEACDWWSFGSLLYELLT 479
Cdd:cd05043  189 SLVNKEYSSASDVWSFGVLLWELMT 213
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
 399-479 1.50e-03

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: 40.62  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEV----EPQCCGEAVDNLYSAPEVGGISELTEACDWWSFGSLL 474
Cdd:cd05114  112 GMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVlddqYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLM 191


                 ....*
gi 332801047 475 YELLT 479
Cdd:cd05114  192 WEVFT 196
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 383-539 1.73e-03

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: 40.26  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH--IRLTYFGQWSEVEPqccgeaVDNLYS--------A 452
Cdd:cd14107   94 VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEITP------SEHQFSkygspefvA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 453 PEVGGISELTEACDWWSFGSLLYelltgMALSQSHPSGIQAH--TQLQLPE----W-------LSRPAASLLTELLQFEP 519
Cdd:cd14107  168 PEIVHQEPVSAATDIWALGVIAY-----LSLTCHSPFAGENDraTLLNVAEgvvsWdtpeithLSEDAKDFIKRVLQPDP 242

                        170       180
                 ....*....|....*....|
gi 332801047 520 TRRlgmgeGGVSKLKSHPFF 539
Cdd:cd14107  243 EKR-----PSASECLSHEWF 257
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
 400-480 1.85e-03

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: 40.32  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLLL-----DQAGHIRLTYFGqwseVEPQCCGEAVDNL-----YSAPEVG-GISELTEACDWW 468
Cdd:cd14068   99 LRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYG----IAQYCCRMGIKTSegtpgFRAPEVArGNVIYNQQADVY 174

                         90
                 ....*....|..
gi 332801047 469 SFGSLLYELLTG 480
Cdd:cd14068  175 SFGLLLYDILTC 186
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
 452-522 1.93e-03

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 40.28  E-value: 1.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332801047 452 APE-VGGISELTEACDWWSFGSLLYELLTG--MALSQSHPSGIQA--HTQLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd05076  187 APEcVPGGNSLSTAADKWGFGATLLEICFNgeAPLQSRTPSEKERfyQRQHRLPEPSCPELATLISQCLTYEPTQR 262
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
 400-522 2.08e-03

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: 40.21  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHE--QGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqcCGEAVDNL--------YSAPEV-GGISELTEACDWW 468
Cdd:cd14064  106 MEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFL----QSLDEDNMtkqpgnlrWMAPEVfTQCTRYSIKADVF 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 469 SFGSLLYELLTG-MALSQSHPSGIQA-----HTQLQLPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14064  182 SYALCLWELLTGeIPFAHLKPAAAAAdmayhHIRPPIGYSIPKPISSLLMRGWNAEPESR 241
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
 395-539 2.13e-03

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: 39.90  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLD-QAGHIRLTYFG--QWSEVEPQ----CCGEAVdnlYSAPEVggiseL------ 461
Cdd:cd14019  109 NLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGlaQREEDRPEqrapRAGTRG---FRAPEV-----Lfkcphq 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 462 TEACDWWSFGSLLYELLTGmalsqSHPSGIQAHTQLQLPEWLS----RPAASLLTELLQFEPTRRLGMGEggvsKLKsHP 537
Cdd:cd14019  181 TTAIDIWSAGVILLSILSG-----RFPFFFSSDDIDALAEIATifgsDEAYDLLDKLLELDPSKRITAEE----ALK-HP 250


                 ..
gi 332801047 538 FF 539
Cdd:cd14019  251 FF 252
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
 382-482 2.25e-03

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: 39.99  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 382 WSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLL-LDQAG-HIRLTYFGQWSEVEPQCCGEAVDNL--YSAPEVGG 457
Cdd:cd14191   95 FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRLENAGSLKVLFGTpeFVAPEVIN 174

                         90       100
                 ....*....|....*....|....*
gi 332801047 458 ISELTEACDWWSFGSLLYELLTGMA 482
Cdd:cd14191  175 YEPIGYATDMWSIGVICYILVSGLS 199
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
 386-432 2.31e-03

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: 40.01  E-value: 2.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG 432
Cdd:cd06643  102 EPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFG 148
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
 392-489 2.45e-03

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: 39.88  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGqWSEVEPQCCGEAVDN-------LYSAPEVGGISELTEA 464
Cdd:cd05081  113 YSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFG-LAKLLPLDKDYYVVRepgqspiFWYAPESLSDNIFSRQ 191

                         90       100
                 ....*....|....*....|....*
gi 332801047 465 CDWWSFGSLLYELLTGMALSQSHPS 489
Cdd:cd05081  192 SDVWSFGVVLYELFTYCDKSCSPSA 216
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
 387-483 2.69e-03

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: 39.98  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAV-DNLYSAPEVGGISELT 462
Cdd:cd07848  100 EKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGfarNLSEGSNANYTEYVaTRWYRSPELLLGAPYG 179

                         90       100
                 ....*....|....*....|.
gi 332801047 463 EACDWWSFGSLLYELLTGMAL 483
Cdd:cd07848  180 KAVDMWSVGCILGELSDGQPL 200
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
 399-480 3.18e-03

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: 39.52  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLL-LDQAGH-IRLTYFGQWSEVEPQ-----CCG--EAVdnlysAPEVGGISELTEACDWWS 469
Cdd:cd14103  103 GVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDkklkvLFGtpEFV-----APEVVNYEPISYATDMWS 177

                         90
                 ....*....|.
gi 332801047 470 FGSLLYELLTG 480
Cdd:cd14103  178 VGVICYVLLSG 188
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
 387-479 3.27e-03

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: 39.53  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV-DNLYS-----APEVGGISE 460
Cdd:cd05079  109 KQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVkDDLDSpvfwyAPECLIQSK 188

                         90
                 ....*....|....*....
gi 332801047 461 LTEACDWWSFGSLLYELLT 479
Cdd:cd05079  189 FYIASDVWSFGVTLYELLT 207
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
 385-477 3.60e-03

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: 39.36  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 385 REEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPqcCGEAVDNLY-SAPEVggISELTE 463
Cdd:cd06607   99 QEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCP--ANSFVGTPYwMAPEV--ILAMDE 174

                         90
                 ....*....|....*....
gi 332801047 464 A-----CDWWSFGSLLYEL 477
Cdd:cd06607  175 GqydgkVDVWSLGITCIEL 193
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
 389-480 3.89e-03

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: 39.51  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 389 VKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGH-IRLTYFGQWSEVEPqccGEA----VDNLYSAPEVggISELT- 462
Cdd:cd14135  107 VRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSASDIGE---NEItpylVSRFYRAPEI--ILGLPy 181

                         90
                 ....*....|....*....
gi 332801047 463 -EACDWWSFGSLLYELLTG 480
Cdd:cd14135  182 dYPIDMWSVGCTLYELYTG 200
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 384-486 4.07e-03

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: 39.24  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 384 VREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRL--TYFGQWSEVEPQCCGEAVDN-LYSAPEVGGISE 460
Cdd:cd08228  103 IPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLgdLGLGRFFSSKTTAAHSLVGTpYYMSPERIHENG 182

                         90       100
                 ....*....|....*....|....*.
gi 332801047 461 LTEACDWWSFGSLLYElltgMALSQS 486
Cdd:cd08228  183 YNFKSDIWSLGCLLYE----MAALQS 204
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
 392-479 4.87e-03

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: 39.28  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 392 WAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAVDNLYSAPEVGGISELTEACD 466
Cdd:cd05110  114 WCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGlarllEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSD 193

                         90
                 ....*....|...
gi 332801047 467 WWSFGSLLYELLT 479
Cdd:cd05110  194 VWSYGVTIWELMT 206
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 382-481 5.52e-03

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: 39.09  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 382 WSVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAV-DNLYSAPEVGGISE 460
Cdd:cd06619   90 RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVgTNAYMAPERISGEQ 169

                         90       100
                 ....*....|....*....|.
gi 332801047 461 LTEACDWWSFGSLLYELLTGM 481
Cdd:cd06619  170 YGIHSDVWSLGISFMELALGR 190
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
 400-480 5.78e-03

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: 38.53  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 400 LEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG------QWS--EVEPQCCGEAvdnLYSAPEV---GGISELTEACDWW 468
Cdd:cd14062  102 MDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGlatvktRWSgsQQFEQPTGSI---LWMAPEVirmQDENPYSFQSDVY 178

                         90
                 ....*....|..
gi 332801047 469 SFGSLLYELLTG 480
Cdd:cd14062  179 AFGIVLYELLTG 190
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 399-480 6.34e-03

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: 38.58  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 399 ALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVepqccgeaVDNLY------------SAPEVGGISELTEACD 466
Cdd:cd05059  112 AMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYV--------LDDEYtssvgtkfpvkwSPPEVFMYSKFSSKSD 183

                         90
                 ....*....|....
gi 332801047 467 WWSFGSLLYELLTG 480
Cdd:cd05059  184 VWSFGVLMWEVFSE 197
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
 382-523 6.51e-03

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: 38.59  E-value: 6.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 382 WSVReeqvKQWAAEMLVALEALH--EQGVLCRDLHPGNLLLDQAGHIRLTYFG-----QWSEVEPQCCGEAVDN---LYS 451
Cdd:cd13978   92 WSLR----FRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGlsklgMKSISANRRRGTENLGgtpIYM 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332801047 452 APEV--GGISELTEACDWWSFGSLLYELLTGmalSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRL 523
Cdd:cd13978  168 APEAfdDFNKKPTSKSDVYSFAIVIWAVLTR---KEPFENAINPLLIMQIVSKGDRPSLDDIGRLKQIENVQEL 238
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
 395-488 6.91e-03

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: 38.50  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 395 EMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG---QWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDWWSFG 471
Cdd:cd06642  109 EILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGvagQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLG 188

                         90
                 ....*....|....*...
gi 332801047 472 SLLYELLTGM-ALSQSHP 488
Cdd:cd06642  189 ITAIELAKGEpPNSDLHP 206
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 411-481 6.92e-03

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: 38.57  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 411 RDLHPGNLLLDQAGHIRLTYFGqwsevepqCCGEAVDNL---------YSAPEVGGISELTEACDWWSFGSLLYELLTGM 481
Cdd:cd06615  124 RDVKPSNILVNSRGEIKLCDFG--------VSGQLIDSMansfvgtrsYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGR 195
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
 383-488 7.29e-03

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: 38.55  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 383 SVREEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEpQCCGEAVDNL----YSAPEVGGI 458
Cdd:cd06637  107 TLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD-RTVGRRNTFIgtpyWMAPEVIAC 185

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 332801047 459 SELTEAC-----DWWSFGSLLYELLTGM-ALSQSHP 488
Cdd:cd06637  186 DENPDATydfksDLWSLGITAIEMAEGApPLCDMHP 221
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
 388-476 7.32e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 39.11  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 388 QVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG-------QWSEVEPQCCGEAVDNlySAPEVGGISE 460
Cdd:PHA03211 261 QVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGaacfargSWSTPFHYGIAGTVDT--NAPEVLAGDP 338

                         90
                 ....*....|....*.
gi 332801047 461 LTEACDWWSFGSLLYE 476
Cdd:PHA03211 339 YTPSVDIWSAGLVIFE 354
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
 387-478 7.70e-03

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: 38.92  E-value: 7.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 387 EQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFG--QWSEVEPQCCGEAVDNLYSAPEVGGISELTEA 464
Cdd:cd07874  119 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGlaRTAGTSFMMTPYVVTRYYRAPEVILGMGYKEN 198

                         90
                 ....*....|....
gi 332801047 465 CDWWSFGSLLYELL 478
Cdd:cd07874  199 VDIWSVGCIMGEMV 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
 386-522 8.14e-03

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: 38.28  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 386 EEQVKQWAAEMLVALEALHEQGVLCRDLHPGNLLLD--QAGHIRLTYFGQWSEVEPQCCGEAVDNL-YSAPEV-GGISEL 461
Cdd:cd14112   98 EEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKVSKLGKVPVDGDTdWASPEFhNPETPI 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332801047 462 TEACDWWSFGSLLYELLTGMalsqsHP--SGIQAHTQLQ------------LPEWLSRPAASLLTELLQFEPTRR 522
Cdd:cd14112  178 TVQSDIWGLGVLTFCLLSGF-----HPftSEYDDEEETKenvifvkcrpnlIFVEATQEALRFATWALKKSPTRR 247
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
 391-480 8.94e-03

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. 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 STK_BAK1-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: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 38.25  E-value: 8.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801047 391 QWAAEMLVALEA------LHEQG---VLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQC--CGEAVDNLYS--APEVGG 457
Cdd:cd14664   92 DWETRQRIALGSarglayLHHDCsplIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDshVMSSVAGSYGyiAPEYAY 171

                         90       100
                 ....*....|....*....|...
gi 332801047 458 ISELTEACDWWSFGSLLYELLTG 480
Cdd:cd14664  172 TGKVSEKSDVYSYGVVLLELITG 194
 
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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