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Conserved domains on  [gi|5031975|ref|NP_005875|]
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serine/threonine-protein kinase PAK 4 isoform 1 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase PAK( domain architecture ID 10099575)

serine/threonine-protein kinase PAK (p21-activated kinase) 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_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
300-591 0e+00

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: 576.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  300 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 379
Cdd:cd06657   1 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 459
Cdd:cd06657  81 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  460 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 539
Cdd:cd06657 161 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLH 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 591
Cdd:cd06657 241 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVPLMRQNRMR 292
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
10-55 3.21e-17

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


:

Pssm-ID: 238526  Cd Length: 46  Bit Score: 75.38  E-value: 3.21e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 5031975   10 EISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESArRPKPLVD 55
Cdd:cd01093   2 EISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSG-ITKEEQK 46
 
Name Accession Description Interval E-value
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
300-591 0e+00

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: 576.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  300 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 379
Cdd:cd06657   1 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 459
Cdd:cd06657  81 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  460 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 539
Cdd:cd06657 161 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLH 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 591
Cdd:cd06657 241 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVPLMRQNRMR 292
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
326-572 6.77e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.28  E-value: 6.77e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQ-QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:smart00220   6 KLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPRRKSLVGTPYWMA 483
Cdd:smart00220  86 DlLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG-EKLTTFVGTPEYMA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     484 PELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRAT 562
Cdd:smart00220 165 PEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGdDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLT 244
                          250
                   ....*....|
gi 5031975     563 AAELLKHPFL 572
Cdd:smart00220 245 AEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
326-572 6.88e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 200.93  E-value: 6.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQ--QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    404 TD-IVTHTRMNEEQIAAVCLAVLQALsvlhaqgvihrdiksdsillthDGRVKLSDFgfcaqvskevprrkslVGTPYWM 482
Cdd:pfam00069  86 FDlLSEKGAFSEREAKFIMKQILEGL----------------------ESGSSLTTF----------------VGTPWYM 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRAT 562
Cdd:pfam00069 128 APEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLT 207
                         250
                  ....*....|
gi 5031975    563 AAELLKHPFL 572
Cdd:pfam00069 208 ATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
326-568 4.11e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 188.68  E-value: 4.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:COG0515  14 LLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGES 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF-CAQVSKEVPRRKSLVGTPY 480
Cdd:COG0515  94 LADLLrRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIaRALGGATLTQTGTVVGTPG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH-KVSPSLKGFLDRLLVRDPAQ 559
Cdd:COG0515 174 YMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRpDLPPALDAIVLRALAKDPEE 253
                       250
                ....*....|
gi 5031975  560 R-ATAAELLK 568
Cdd:COG0515 254 RyQSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
327-575 2.91e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 141.11  E-value: 2.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKclkKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   404 -TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcaqvSKEVPRRK-SLVGTPYW 481
Cdd:PTZ00263 106 fTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF----AKKVPDRTfTLCGTPEY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:PTZ00263 182 LAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKI---LAGRLKFPNWFDGRARDLVKGLLQTDHTKRL 258
                        250
                 ....*....|....*....
gi 5031975   562 TA-----AELLKHPFLAKA 575
Cdd:PTZ00263 259 GTlkggvADVKNHPYFHGA 277
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
375-567 5.42e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 106.03  E-value: 5.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   375 HENVVEMYNsylVGDE---LWVVMEFLEGGALTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH 450
Cdd:NF033483  66 HPNIVSVYD---VGEDggiPYIVMEYVDGRTLKDYIrEHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   451 DGRVKLSDFGFC--------AQVSkevprrkSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK 522
Cdd:NF033483 143 DGRVKVTDFGIAralssttmTQTN-------SVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPVS 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5031975   523 -AMKMIRDNLP-PRLKNlHKVSPSlkgfLDRL----LVRDPAQR-ATAAELL 567
Cdd:NF033483 216 vAYKHVQEDPPpPSELN-PGIPQS----LDAVvlkaTAKDPDDRyQSAAEMR 262
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
10-55 3.21e-17

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 75.38  E-value: 3.21e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 5031975   10 EISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESArRPKPLVD 55
Cdd:cd01093   2 EISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSG-ITKEEQK 46
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
10-63 6.06e-16

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 72.34  E-value: 6.06e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975     10 EISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESA-RRPKPLVDPACITSIQ 63
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGiTEDEQKENPKAVLDVL 55
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
11-43 1.52e-11

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 59.14  E-value: 1.52e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 5031975      11 ISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLI 43
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFTGLPTEWKSLL 33
 
Name Accession Description Interval E-value
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
300-591 0e+00

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: 576.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  300 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 379
Cdd:cd06657   1 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 459
Cdd:cd06657  81 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  460 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 539
Cdd:cd06657 161 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLH 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 591
Cdd:cd06657 241 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVPLMRQNRMR 292
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
313-573 0e+00

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: 563.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  313 DPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELW 392
Cdd:cd06648   1 SPGDPRSDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR 472
Cdd:cd06648  81 VVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRL 552
Cdd:cd06648 161 KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRM 240
                       250       260
                ....*....|....*....|.
gi 5031975  553 LVRDPAQRATAAELLKHPFLA 573
Cdd:cd06648 241 LVRDPAQRATAAELLNHPFLA 261
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
299-591 0e+00

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: 528.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  299 VSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENV 378
Cdd:cd06659   1 VTHEQFKAALRMVVDQGDPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  379 VEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSD 458
Cdd:cd06659  81 VEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  459 FGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNL 538
Cdd:cd06659 161 FGFCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  539 HKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 591
Cdd:cd06659 241 HKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVPLIQQYRKR 293
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
298-589 0e+00

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: 520.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  298 RVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHEN 377
Cdd:cd06658   1 RVSHEQFRAALQLVVSPGDPREYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  378 VVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLS 457
Cdd:cd06658  81 VVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  458 DFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKN 537
Cdd:cd06658 161 DFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKD 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  538 LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNR 589
Cdd:cd06658 241 SHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLKLAGPPSCIVPLMRQYR 292
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
320-573 1.94e-161

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: 460.91  E-value: 1.94e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQqRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd06614   1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQ-NKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHT--RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG 477
Cdd:cd06614  80 GGSLTDIITQNpvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSVVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDP 557
Cdd:cd06614 160 TPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFLNKCLVKDP 239
                       250
                ....*....|....*.
gi 5031975  558 AQRATAAELLKHPFLA 573
Cdd:cd06614 240 EKRPSAEELLQHPFLK 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
320-572 1.35e-131

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: 385.02  E-value: 1.35e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHT--RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRrKSLVG 477
Cdd:cd05122  81 GGSLKDLLKNTnkTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTR-NTFVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDP 557
Cdd:cd05122 160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFKDFLKKCLQKDP 239
                       250
                ....*....|....*
gi 5031975  558 AQRATAAELLKHPFL 572
Cdd:cd05122 240 EKRPTAEQLLKHPFI 254
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
315-572 2.35e-119

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: 353.85  E-value: 2.35e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  315 GDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd06647   3 GDPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06647  83 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLV 554
Cdd:cd06647 163 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLE 242
                       250
                ....*....|....*...
gi 5031975  555 RDPAQRATAAELLKHPFL 572
Cdd:cd06647 243 MDVEKRGSAKELLQHPFL 260
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
300-585 1.20e-108

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: 327.84  E-value: 1.20e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  300 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 379
Cdd:cd06654   1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 459
Cdd:cd06654  81 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  460 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 539
Cdd:cd06654 161 GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLM 585
Cdd:cd06654 241 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLI 286
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
302-585 1.23e-108

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: 327.83  E-value: 1.23e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  302 EQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEM 381
Cdd:cd06656   2 EEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  382 YNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF 461
Cdd:cd06656  82 LDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  462 CAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKV 541
Cdd:cd06656 162 CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERL 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031975  542 SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLM 585
Cdd:cd06656 242 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLI 285
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
302-589 1.66e-108

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: 327.45  E-value: 1.66e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  302 EQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEM 381
Cdd:cd06655   2 EEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  382 YNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF 461
Cdd:cd06655  82 LDSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  462 CAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKV 541
Cdd:cd06655 162 CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKL 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  542 SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPL-------MRQNR 589
Cdd:cd06655 242 SPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLilaakeaMKSNR 296
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
326-572 6.77e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.28  E-value: 6.77e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQ-QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:smart00220   6 KLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPRRKSLVGTPYWMA 483
Cdd:smart00220  86 DlLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG-EKLTTFVGTPEYMA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     484 PELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRAT 562
Cdd:smart00220 165 PEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGdDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLT 244
                          250
                   ....*....|
gi 5031975     563 AAELLKHPFL 572
Cdd:smart00220 245 AEEALQHPFF 254
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
326-572 3.18e-92

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 284.16  E-value: 3.18e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM----DLrkqqrrELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd06612  10 KLGEGSYGSVYKAIHKETGQVVAIKVVpveeDL------QEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd06612  84 SVSDIMkiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVIGTP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd06612 164 FWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKDPEE 243
                       250
                ....*....|...
gi 5031975  560 RATAAELLKHPFL 572
Cdd:cd06612 244 RPSAIQLLQHPFI 256
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
326-571 8.05e-91

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: 280.73  E-value: 8.05e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd06613   7 RIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGSLQD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAP 484
Cdd:cd06613  87 IYQVTGpLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFIGTPYWMAP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  485 ELIS---RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--RDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd06613 167 EVAAverKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIpkSNFDPPKLKDKEKWSPDFHDFIKKCLTKNPKK 246
                       250
                ....*....|..
gi 5031975  560 RATAAELLKHPF 571
Cdd:cd06613 247 RPTATKLLQHPF 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
326-587 1.50e-86

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: 269.88  E-value: 1.50e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd06609   8 RIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEiEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGSVL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAP 484
Cdd:cd06609  88 DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTFVGTPFWMAP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  485 ELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKnLHKVSPSLKGFLDRLLVRDPAQRATAA 564
Cdd:cd06609 168 EVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLE-GNKFSKPFKDFVELCLNKDPKERPSAK 246
                       250       260
                ....*....|....*....|...
gi 5031975  565 ELLKHPFLAKAGPPASIVPLMRQ 587
Cdd:cd06609 247 ELLKHKFIKKAKKTSYLTLLIER 269
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
327-572 2.20e-79

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: 250.90  E-value: 2.20e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd06606   8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELeaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR--RKSLVGTPYW 481
Cdd:cd06606  88 SLLkKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGegTKSLRGTPYW 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMI--RDNLPPRLKNLhkvSPSLKGFLDRLLVRDPA 558
Cdd:cd06606 168 MAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIgsSGEPPPIPEHL---SEEAKDFLRKCLQRDPK 244
                       250
                ....*....|....
gi 5031975  559 QRATAAELLKHPFL 572
Cdd:cd06606 245 KRPTADELLQHPFL 258
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
327-572 7.03e-78

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: 247.60  E-value: 7.03e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFnEVVIMRDY-QHENVVEMYNSYL------VGDELWVVMEFLE 399
Cdd:cd06608  14 IGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKL-EINILRKFsNHPNIATFYGAFIkkdppgGDDQLWLVMEYCG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHT-----RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06608  93 GGSVTDLVKGLrkkgkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDSTLGRRNT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFL 549
Cdd:cd06608 173 FIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSPEKWSKEFNDFI 252
                       250       260
                ....*....|....*....|...
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06608 253 SECLIKNYEQRPFTEELLEHPFI 275
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
326-571 6.75e-77

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: 244.96  E-value: 6.75e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd06610   8 VIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSmDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTH---TRMNEEQIAAVCL-AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR----RKSLV 476
Cdd:cd06610  88 DIMKSsypRGGLDEAIIATVLkEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRtrkvRKTFV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRL---KNLHKVSPSLKGFLDRL 552
Cdd:cd06610 168 GTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLetgADYKKYSKSFRKMISLC 247
                       250
                ....*....|....*....
gi 5031975  553 LVRDPAQRATAAELLKHPF 571
Cdd:cd06610 248 LQKDPSKRPTAEELLKHKF 266
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
326-572 6.25e-75

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: 239.05  E-value: 6.25e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd06627   7 LIGRGAFGSVYKGLNLNTGEFVAIKQISLEKipKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWM 482
Cdd:cd06627  87 ASIIkKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGTPYWM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNLPPRLKNlhkVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd06627 167 APEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALfRIVQDDHPPLPEN---ISPELRDFLLQCFQKDPTLRP 243
                       250
                ....*....|.
gi 5031975  562 TAAELLKHPFL 572
Cdd:cd06627 244 SAKELLKHPWL 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
316-576 6.31e-73

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: 235.02  E-value: 6.31e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd06611   2 NPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK 473
Cdd:cd06611  82 EFCDGGALDSIMLELErgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELI-----SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGF 548
Cdd:cd06611 162 TFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSKWSSSFNDF 241
                       250       260
                ....*....|....*....|....*...
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLAKAG 576
Cdd:cd06611 242 LKSCLVKDPDDRPTAAELLKHPFVSDQS 269
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
326-571 2.56e-70

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: 227.36  E-value: 2.56e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05117   7 VLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlkSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFcAQVSKEVPRRKSLVGTP 479
Cdd:cd05117  87 FDrIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGL-AKIFEEGEKLKTVCGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPPrlKNLHKVSPSLKGFLDRLLVRD 556
Cdd:cd05117 166 YYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKgkySFDS--PEWKNVSEEAKDLIKRLLVVD 243
                       250
                ....*....|....*
gi 5031975  557 PAQRATAAELLKHPF 571
Cdd:cd05117 244 PKKRLTAAEALNHPW 258
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
327-582 4.31e-66

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: 216.96  E-value: 4.31e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIV----CIATvrssGKLVAVKKMDLRKQ-------QRRELLFNEvviMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd06917   9 VGRGSYGAVyrgyHVKT----GRVVALKVLNLDTDdddvsdiQKEVALLSQ---LKLGQPKNIIKYYGSYLKGPSLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL 475
Cdd:cd06917  82 DYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLkNLHKVSPSLKGFLDRLLV 554
Cdd:cd06917 162 VGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRL-EGNGYSPLLKEFVAACLD 240
                       250       260
                ....*....|....*....|....*....
gi 5031975  555 RDPAQRATAAELLKHPFL-AKAGPPASIV 582
Cdd:cd06917 241 EEPKDRLSADELLKSKWIkQHSKTPTSVL 269
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
327-572 1.86e-63

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: 209.23  E-value: 1.86e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAl 403
Cdd:cd06607   9 IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwqdIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCLGSA- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIV-THTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvprrKSLVGTPYW 481
Cdd:cd06607  88 SDIVeVHKKpLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPA----NSFVGTPYW 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRL---PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHkVSPSLKGFLDRLLVRDPA 558
Cdd:cd06607 164 MAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLSSGE-WSDDFRNFVDSCLQKIPQ 242
                       250
                ....*....|....
gi 5031975  559 QRATAAELLKHPFL 572
Cdd:cd06607 243 DRPSAEDLLKHPFV 256
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
326-567 2.09e-63

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: 209.36  E-value: 2.09e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14014   7 LLGRGGMGEVYRARDTLLGRPVAIKVLrpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR-KSLVGTPY 480
Cdd:cd14014  87 LADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQtGSVLGTPA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHK-VSPSLKGFLDRLLVRDPAQ 559
Cdd:cd14014 167 YMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPdVPPALDAIILRALAKDPEE 246

                ....*....
gi 5031975  560 R-ATAAELL 567
Cdd:cd14014 247 RpQSAAELL 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
326-572 4.93e-62

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: 205.39  E-value: 4.93e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd08215   7 VIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmsEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMN-----EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT 478
Cdd:cd08215  87 AQKIKKQKKKgqpfpEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLAKTVVGT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPLkAMKMIRDNLPPrLKNlhKVSPSLKGFLDRLLVRD 556
Cdd:cd08215 167 PYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFeaNNLPAL-VYKIVKGQYPP-IPS--QYSSELRDLVNSMLQKD 242
                       250
                ....*....|....*.
gi 5031975  557 PAQRATAAELLKHPFL 572
Cdd:cd08215 243 PEKRPSANEILSSPFI 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
316-574 5.07e-61

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: 204.11  E-value: 5.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd06644   9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK 473
Cdd:cd06644  89 EFCPGGAVDAIMLELDrgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELI-----SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGF 548
Cdd:cd06644 169 SFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPSKWSMEFRDF 248
                       250       260
                ....*....|....*....|....*.
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd06644 249 LKTALDKHPETRPSAAQLLEHPFVSS 274
Pkinase pfam00069
Protein kinase domain;
326-572 6.88e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 200.93  E-value: 6.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQ--QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    404 TD-IVTHTRMNEEQIAAVCLAVLQALsvlhaqgvihrdiksdsillthDGRVKLSDFgfcaqvskevprrkslVGTPYWM 482
Cdd:pfam00069  86 FDlLSEKGAFSEREAKFIMKQILEGL----------------------ESGSSLTTF----------------VGTPWYM 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRAT 562
Cdd:pfam00069 128 APEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLT 207
                         250
                  ....*....|
gi 5031975    563 AAELLKHPFL 572
Cdd:pfam00069 208 ATQALQHPWF 217
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
316-574 8.87e-61

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: 202.97  E-value: 8.87e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd06645   8 NPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06645  88 EFCGGGSLQDIYHVTgPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELIS---RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNL-PPRLKNLHKVSPSLKGFL 549
Cdd:cd06645 168 FIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALfLMTKSNFqPPKLKDKMKWSNSFHHFV 247
                       250       260
                ....*....|....*....|....*
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd06645 248 KMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
326-571 1.76e-60

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: 201.21  E-value: 1.76e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14003   7 TLGEGSFGKVKLARHKLTGEKVAIKIIDKSKlkEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TD-IVTHTRMNEE-------QIaavclavLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPRRKSL 475
Cdd:cd14003  87 FDyIVNNGRLSEDearrffqQL-------ISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG-SLLKTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYF--NEPPLKAMKMIRDNLPPRlknlhKVSPSLKGFLDRL 552
Cdd:cd14003 159 CGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDddNDSKLFRKILKGKYPIPS-----HLSPDARDLIRRM 233
                       250
                ....*....|....*....
gi 5031975  553 LVRDPAQRATAAELLKHPF 571
Cdd:cd14003 234 LVVDPSKRITIEEILNHPW 252
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
327-570 2.74e-60

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: 199.42  E-value: 2.74e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR-RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKlLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG--TPYW 481
Cdd:cd00180  81 LLKENKgpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttPPYY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMvdgeppyfnepplkamkmirdnlpprlknlhkvsPSLKGFLDRLLVRDPAQRA 561
Cdd:cd00180 161 APPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRRMLQYDPKKRP 206

                ....*....
gi 5031975  562 TAAELLKHP 570
Cdd:cd00180 207 SAKELLEHL 215
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
316-573 3.01e-60

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: 201.79  E-value: 3.01e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd06643   2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK 473
Cdd:cd06643  82 EFCAGGAVDAVMLELErpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELI-----SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGF 548
Cdd:cd06643 162 SFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSPEFKDF 241
                       250       260
                ....*....|....*....|....*
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd06643 242 LRKCLEKNVDARWTTSQLLQHPFVS 266
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
327-571 7.04e-60

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: 199.67  E-value: 7.04e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkeIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 -TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWM 482
Cdd:cd05123  81 fSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEYL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPRLKnlHKVSPSLKGFLDRLLVRDPAQR-- 560
Cdd:cd05123 161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKIL-KSPLKFP--EYVSPEAKSLISGLLQKDPTKRlg 237
                       250
                ....*....|..
gi 5031975  561 -ATAAELLKHPF 571
Cdd:cd05123 238 sGGAEEIKAHPF 249
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
316-589 1.57e-59

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: 201.03  E-value: 1.57e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELW 392
Cdd:cd06633  18 DPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwqdIIKEVKFLQQLKHPNTIEYKGCYLKDHTAW 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpr 471
Cdd:cd06633  98 LVMEYCLGSASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPA--- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 rKSLVGTPYWMAPELISRL---PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlHKVSPSLKGF 548
Cdd:cd06633 175 -NSFVGTPYWMAPEVILAMdegQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQS-NEWTDSFRGF 252
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNR 589
Cdd:cd06633 253 VDYCLQKIPQERPSSAELLRHDFVRRERPPRVLIDLIQRTK 293
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
316-572 1.97e-59

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 199.46  E-value: 1.97e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFnEVVIMRDY-QHENVVEMYNSYLV------G 388
Cdd:cd06636  13 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKL-EINMLKKYsHHRNIATYYGAFIKksppghD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  389 DELWVVMEFLEGGALTDIVTHTRMN---EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 465
Cdd:cd06636  92 DQLWLVMEFCGAGSVTDLVKNTKGNalkEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlHK 540
Cdd:cd06636 172 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLKS-KK 250
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031975  541 VSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06636 251 WSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
326-572 3.17e-59

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: 198.08  E-value: 3.17e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14007   7 PLGKGKFGNVYLAREKKSGFIVALKVIsksQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 L-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpRRKSLVGTPYW 481
Cdd:cd14007  87 LyKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSN--RRKTFCGTLDY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPRLKNlhKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd14007 165 LPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQ-NVDIKFPS--SVSPEAKDLISKLLQKDPSKRL 241
                       250
                ....*....|.
gi 5031975  562 TAAELLKHPFL 572
Cdd:cd14007 242 SLEQVLNHPWI 252
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
326-572 4.36e-59

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 198.33  E-value: 4.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd06646  16 RVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAP 484
Cdd:cd06646  96 IYHVTgPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKSFIGTPYWMAP 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  485 ELIS---RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNL-PPRLKNLHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd06646 176 EVAAvekNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALfLMSKSNFqPPKLKDKTKWSSTFHNFVKISLTKNPKK 255
                       250
                ....*....|...
gi 5031975  560 RATAAELLKHPFL 572
Cdd:cd06646 256 RPTAERLLTHLFV 268
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
319-575 4.77e-59

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: 197.81  E-value: 4.77e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  319 SYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKK--MDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLL-RELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06623  80 YMDGGSLADLLkKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR---DNLPPRLKNlHKVSPSLKGFLDR 551
Cdd:cd06623 160 FVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQaicDGPPPSLPA-EEFSPEFRDFISA 238
                       250       260
                ....*....|....*....|....
gi 5031975  552 LLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06623 239 CLQKDPKKRPSAAELLQHPFIKKA 262
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
327-572 3.34e-58

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: 195.31  E-value: 3.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK--KMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKevSLVDDDKKSRESvkqLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVT-HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPY 480
Cdd:cd06632  88 SIHKLLQrYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGM-AKHVEAFSFAKSFKGSPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISR--LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--RDNLPPRLKNLhkvSPSLKGFLDRLLVRD 556
Cdd:cd06632 167 WMAPEVIMQknSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIgnSGELPPIPDHL---SPDAKDFIRLCLQRD 243
                       250
                ....*....|....*.
gi 5031975  557 PAQRATAAELLKHPFL 572
Cdd:cd06632 244 PEDRPTASQLLEHPFV 259
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
316-574 5.89e-57

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: 192.96  E-value: 5.89e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd06640   1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06640  81 MEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlhKVSPSLKGFLDRLLV 554
Cdd:cd06640 161 FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVG--DFSKPFKEFIDACLN 238
                       250       260
                ....*....|....*....|
gi 5031975  555 RDPAQRATAAELLKHPFLAK 574
Cdd:cd06640 239 KDPSFRPTAKELLKHKFIVK 258
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
316-580 9.00e-57

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: 192.21  E-value: 9.00e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd06641   1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06641  81 MEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN* 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlhKVSPSLKGFLDRLLV 554
Cdd:cd06641 161 FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEG--NYSKPLKEFVEACLN 238
                       250       260
                ....*....|....*....|....*.
gi 5031975  555 RDPAQRATAAELLKHPFLAKAGPPAS 580
Cdd:cd06641 239 KEPSFRPTAKELLKHKFILRNAKKTS 264
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
316-572 4.07e-56

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: 191.47  E-value: 4.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDY-QHENVVEMYNSYL------VG 388
Cdd:cd06637   3 DPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIK-QEINMLKKYsHHRNIATYYGAFIkknppgMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  389 DELWVVMEFLEGGALTDIVTHTRMN---EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 465
Cdd:cd06637  82 DQLWLVMEFCGAGSVTDLIKNTKGNtlkEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlHK 540
Cdd:cd06637 162 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKS-KK 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031975  541 VSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06637 241 WSKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
327-572 6.96e-56

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


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 189.00  E-value: 6.96e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGgALT 404
Cdd:cd14002   9 IGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELrnLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG-ELF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMA 483
Cdd:cd14002  88 QILEDDGtLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTSIKGTPLYMA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  484 PELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLP-PrlKNLhkvSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd14002 168 PELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIvKDPVKwP--SNM---SPEFKSFLQGLLNKDPSKRL 242
                       250
                ....*....|.
gi 5031975  562 TAAELLKHPFL 572
Cdd:cd14002 243 SWPDLLEHPFV 253
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
316-589 1.07e-55

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: 189.50  E-value: 1.07e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd06642   1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06642  81 MEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHkvSPSLKGFLDRLLV 554
Cdd:cd06642 161 FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQH--SKPFKEFVEACLN 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031975  555 RDPAQRATAAELLKHPFLAKAGPPAS-IVPLMRQNR 589
Cdd:cd06642 239 KDPRFRPTAKELLKHKFITRYTKKTSfLTELIDRYK 274
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
315-572 4.00e-55

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 188.28  E-value: 4.00e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  315 GDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSY-----LVGD 389
Cdd:cd06639  18 ADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFykadqYVGG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  390 ELWVVMEFLEGGALTDIVTH-----TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ 464
Cdd:cd06639  98 QLWLVLELCNGGSVTELVKGllkcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  465 VSKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 539
Cdd:cd06639 178 LTSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLLNPE 257
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06639 258 KWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
327-568 4.12e-55

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: 186.59  E-value: 4.12e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKM---DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLkveDDNDELLKEFR-REVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVT--HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd13999  78 YDLLHkkKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPRW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd13999 158 MAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQK-GLRPPIPPDCPPELSKLIKRCWNEDPEKRP 236

                ....*..
gi 5031975  562 TAAELLK 568
Cdd:cd13999 237 SFSEIVK 243
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
326-572 2.56e-54

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: 185.20  E-value: 2.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR--ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd06626   7 KIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtiKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRM-NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfCAQVSK------EVPRRKSLV 476
Cdd:cd06626  87 EELLRHGRIlDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKLKnntttmAPGEVNSLV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLP---YGPEVDIWSLGIMVIEMVDGEPP-YFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRL 552
Cdd:cd06626 166 GTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPwSELDNEWAIMYHVGMGHKPPIPDSLQLSPEGKDFLSRC 245
                       250       260
                ....*....|....*....|
gi 5031975  553 LVRDPAQRATAAELLKHPFL 572
Cdd:cd06626 246 LESDPKKRPTASELLDHPFI 265
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
326-572 3.79e-54

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


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 185.05  E-value: 3.79e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLEGG 401
Cdd:cd08217   7 TIGKGSFGTVRKVRRKSDGKILVWKEIDYGKmsEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVMEYCEGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIV-----THTRMNEEQIAAVCLAVLQALSVLHA-----QGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 471
Cdd:cd08217  87 DLAQLIkkckkENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSSF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMKM-IRDNLPPRLKnlHKVSPSLKGFLD 550
Cdd:cd08217 167 AKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPP-FQAANQLELAKkIKEGKFPRIP--SRYSSELNEVIK 243
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd08217 244 SMLNVDPDKRPSVEELLQLPLI 265
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
326-568 4.11e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 188.68  E-value: 4.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:COG0515  14 LLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGES 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF-CAQVSKEVPRRKSLVGTPY 480
Cdd:COG0515  94 LADLLrRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIaRALGGATLTQTGTVVGTPG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH-KVSPSLKGFLDRLLVRDPAQ 559
Cdd:COG0515 174 YMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRpDLPPALDAIVLRALAKDPEE 253
                       250
                ....*....|
gi 5031975  560 R-ATAAELLK 568
Cdd:COG0515 254 RyQSAAELAA 263
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
327-572 3.03e-52

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: 180.06  E-value: 3.03e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRE-----------LLFNEVVIMRDYQHENVVEMYN--SYLVGDE 390
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKifnKSRLRKRREGKndrgkiknaldDVRREIAIMKKLDHPNIVRLYEviDDPESDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSK 467
Cdd:cd14008  81 LYLVLEYCEGGPVMELDSGDRvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG----VSE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EVPRRKSLV----GTPYWMAPEL--ISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPRLKNlh 539
Cdd:cd14008 157 MFEDGNDTLqktaGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIqNQNDEFPIPP-- 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14008 235 ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
313-572 1.83e-51

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: 178.67  E-value: 1.83e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  313 DPGDPRSYLDNfikIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYL-----V 387
Cdd:cd06638  15 DPSDTWEIIET---IGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYkkdvkN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  388 GDELWVVMEFLEGGALTDIVTH-----TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC 462
Cdd:cd06638  92 GDQLWLVLELCNGGSVTDLVKGflkrgERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVS 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  463 AQVSKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKN 537
Cdd:cd06638 172 AQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTLHQ 251
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031975  538 LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06638 252 PELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
327-573 2.45e-51

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: 177.79  E-value: 2.45e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDLYAIKVIkkrDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF---------------CAQVSK 467
Cdd:cd05579  81 YSLLENVGALDEDVARIYIAeIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLskvglvrrqiklsiqKKSNGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--RDNLPPRLKNlhkVSPSL 545
Cdd:cd05579 161 PEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNIlnGKIEWPEDPE---VSDEA 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031975  546 KGFLDRLLVRDPAQRA---TAAELLKHPFLA 573
Cdd:cd05579 238 KDLISKLLTPDPEKRLgakGIEEIKNHPFFK 268
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
321-575 8.06e-51

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: 176.00  E-value: 8.06e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFIKIGEGSTGIVCIATVRSSGKLVAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd06605   3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIrlEIDEALQKQIL-RELDVLHKCNSPYIVGFYGAFYSEGDISICMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKSLV 476
Cdd:cd06605  82 DGGSLDKILKEVgRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLA--KTFV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP------PLKAMKMIRDNLPPRLKNlHKVSPSLKGFLD 550
Cdd:cd06605 160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNakpsmmIFELLSYIVDEPPPLLPS-GKFSPDFQDFVS 238
                       250       260
                ....*....|....*....|....*
gi 5031975  551 RLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06605 239 QCLQKDPTERPSYKELMEHPFIKRY 263
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
316-589 8.48e-51

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 177.55  E-value: 8.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELW 392
Cdd:cd06635  22 DPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqdIIKEVKFLQRIKHPNSIEYKGCYLREHTAW 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpr 471
Cdd:cd06635 102 LVMEYCLGSASDLLEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPA--- 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 rKSLVGTPYWMAPELISRL---PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlHKVSPSLKGF 548
Cdd:cd06635 179 -NSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQS-NEWSDYFRNF 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNR 589
Cdd:cd06635 257 VDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTK 297
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
316-589 2.05e-50

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 176.37  E-value: 2.05e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELW 392
Cdd:cd06634  12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwqdIIKEVKFLQKLRHPNTIEYRGCYLREHTAW 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpr 471
Cdd:cd06634  92 LVMEYCLGSASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPA--- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 rKSLVGTPYWMAPELISRL---PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHkVSPSLKGF 548
Cdd:cd06634 169 -NSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGH-WSEYFRNF 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNR 589
Cdd:cd06634 247 VDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLIQRTK 287
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
327-572 4.85e-50

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 174.16  E-value: 4.85e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVrSSGKLVAVKKMDL------RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd06631   9 LGKGAYGTVYCGLT-STGQLIAVKQVELdtsdkeKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTRMNEEQIaaVCL---AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----FCAQVSKEVPRR- 472
Cdd:cd06631  88 GSIASILARFGALEEPV--FCRytkQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLSSGSQSQl 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 -KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--RDNLPPRLKNlhKVSPSLKGFL 549
Cdd:cd06631 166 lKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsGRKPVPRLPD--KFSPEARDFV 243
                       250       260
                ....*....|....*....|...
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06631 244 HACLTRDQDERPSAEQLLKHPFI 266
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
327-572 1.16e-49

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: 173.10  E-value: 1.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL---------RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVELpsvsaenkdRKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVT-HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV------SKEVP 470
Cdd:cd06628  88 VPGGSVATLLNnYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLeanslsTKNNG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlhKVSPSLKGFLD 550
Cdd:cd06628 168 ARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPS--NISSEARDFLE 245
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06628 246 KTFEIDHNKRPTADELLKHPFL 267
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
327-572 9.88e-49

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: 170.04  E-value: 9.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14099   9 LGKGGFAKCYEVTDMSTGKVYAGKvvpKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGSL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWM 482
Cdd:cd14099  89 MELLkRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTPNYI 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLP-YGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAM-KMIRDN---LPPRLknlhKVSPSLKGFLDRLLVRDP 557
Cdd:cd14099 169 APEVLEKKKgHSFEVDIWSLGVILYTLLVGKPP-FETSDVKETyKRIKKNeysFPSHL----SISDEAKDLIRSMLQPDP 243
                       250
                ....*....|....*
gi 5031975  558 AQRATAAELLKHPFL 572
Cdd:cd14099 244 TKRPSLDEILSHPFF 258
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
323-571 9.96e-49

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: 170.55  E-value: 9.96e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFI---KIGEGSTGIVCIATVRSSGKLVAVKKMDlrKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14010   1 NYVlydEIGRGKHSVVYKGRRKGTIEFVAIKCVD--KSKRPEVL-NEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG-----------FCAQVSK 467
Cdd:cd14010  78 GGDLETLLRQdGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGlarregeilkeLFGQFSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 E-----VPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--RDNLPPRLKNLHK 540
Cdd:cd14010 158 EgnvnkVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKIlnEDPPPPPPKVSSK 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031975  541 VSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14010 238 PSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
327-571 1.87e-48

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: 169.33  E-value: 1.87e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKklQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEE-------QIAAvclavlqALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFcAQVSKEVPRRK 473
Cdd:cd14009  81 QyIRKRGRLPEAvarhfmqQLAS-------GLKFLRSKNIIHRDLKPQNLLLStsgDDPVLKIADFGF-ARSLQPASMAE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPRLKNLHKVSPSLKGFLDRL 552
Cdd:cd14009 153 TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIeRSDAVIPFPIAAQLSPDCKDLLRRL 232
                       250
                ....*....|....*....
gi 5031975  553 LVRDPAQRATAAELLKHPF 571
Cdd:cd14009 233 LRRDPAERISFEEFFAHPF 251
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
401-580 2.19e-48

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 166.42  E-value: 2.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     401 GALTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGvihrdiKSDSILLTHDGRVKLsdFGFCAQVSKEVPRrkslvGT 478
Cdd:smart00750   1 VSLADILEVRGrpLNEEEIWAVCLQCLGALRELHRQA------KSGNILLTWDGLLKL--DGSVAFKTPEQSR-----PD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRL-----KNLHKVS--PSLKGFLDR 551
Cdd:smart00750  68 PYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADdprdrSNLEGVSaaRSFEDFMRL 147
                          170       180
                   ....*....|....*....|....*....
gi 5031975     552 LLVRDPAQRATAAELLKHPFLAKAGPPAS 580
Cdd:smart00750 148 CASRLPQRREAANHYLAHCRALFAETLEL 176
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
327-571 1.78e-47

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 166.76  E-value: 1.78e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL---RKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd06625   8 LGQGAFGQVYLCYDADTGRELAVKQVEIdpiNTEASKEVkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEV------PRRKS 474
Cdd:cd06625  88 SVKDeIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFG----ASKRLqticssTGMKS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNLPPRLKNlhKVSPSLKGFLDRLL 553
Cdd:cd06625 164 VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIfKIATQPTNPQLPP--HVSEDARDFLSLIF 241
                       250
                ....*....|....*...
gi 5031975  554 VRDPAQRATAAELLKHPF 571
Cdd:cd06625 242 VRNKKQRPSAEELLSHSF 259
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
323-573 1.90e-46

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: 165.06  E-value: 1.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIK-IGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05580   4 EFLKtLGTGSFGRVRLVKHKDSGKYYALKILkkaKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGaltDIVTHTRMN---EEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCaqvsKEVPRR-K 473
Cdd:cd05580  84 PGG---ELFSLLRRSgrfPNDVAKFYAAeVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFA----KRVKDRtY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlppRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd05580 157 TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEG---KIRFPSFFDPDAKDLIKRLL 233
                       250       260
                ....*....|....*....|....*
gi 5031975  554 VRDPAQR-----ATAAELLKHPFLA 573
Cdd:cd05580 234 VVDLTKRlgnlkNGVEDIKNHPWFA 258
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
325-572 7.81e-46

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 162.58  E-value: 7.81e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd06624  14 VVLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHT----RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL-THDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd06624  94 ALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLAGINPCTETFTGTL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLP--YGPEVDIWSLGIMVIEMVDGEPPYFNE-PPLKAM-KM----IRDNLPPRLknlhkvSPSLKGFLDR 551
Cdd:cd06624 174 QYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMfKVgmfkIHPEIPESL------SEEAKSFILR 247
                       250       260
                ....*....|....*....|.
gi 5031975  552 LLVRDPAQRATAAELLKHPFL 572
Cdd:cd06624 248 CFEPDPDKRATASDLLQDPFL 268
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
324-571 1.05e-45

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: 162.77  E-value: 1.05e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  324 FIK-IGEGSTGIVCIATVRSSGKLVAVKKMDLR---KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd05581   5 FGKpLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiiKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----FCA----------- 463
Cdd:cd05581  85 NGDLLEYIRKyGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvLGPdsspestkgda 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 --QVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPL--KAMKM---IRDNLPPR 534
Cdd:cd05581 165 dsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFrgSNEYLTfqKIVKLeyeFPENFPPD 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031975  535 LKNLhkvspslkgfLDRLLVRDPAQRATAA------ELLKHPF 571
Cdd:cd05581 245 AKDL----------IQKLLVLDPSKRLGVNenggydELKAHPF 277
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
326-572 1.37e-44

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: 159.90  E-value: 1.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM------DLRKQQRRELLFNevvimRDYQHENVVEMYNSYLvgDE----LWVVM 395
Cdd:cd06621   8 SLGEGAGGSVTKCRLRNTKTIFALKTIttdpnpDVQKQILRELEIN-----KSCASPYIVKYYGAFL--DEqdssIGIAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHT-----RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVP 470
Cdd:cd06621  81 EYCEGGSLDSIYKKVkkkggRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFG----VSGELV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RR--KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP-----PLKAMKMIRDNLPPRLK----NLH 539
Cdd:cd06621 157 NSlaGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGepplgPIELLSYIVNMPNPELKdepeNGI 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  540 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06621 237 KWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWI 269
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
326-586 2.12e-44

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 160.15  E-value: 2.12e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVR--SSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd08216   5 EIGKCFKGGGVVHLAKhkPTNTLVAVKKINLESDSKEDLkfLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTD-IVTH--TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT 478
Cdd:cd08216  85 SCRDlLKTHfpEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVVHDF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 P-------YWMAPELI--SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPlkaMKM----IRDNLPPRL---------- 535
Cdd:cd08216 165 PksseknlPWLSPEVLqqNLLGYNEKSDIYSVGITACELANGVVPFSDMPA---TQMllekVRGTTPQLLdcstypleed 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031975  536 --------KNLHKV-------------SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK-AGPPASIVPLMR 586
Cdd:cd08216 242 smsqsedsSTEHPNnrdtrdipyqrtfSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQcRRSNTSLLDLLK 314
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
326-572 4.51e-44

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: 158.63  E-value: 4.51e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlrKQQR-----RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd07833   8 VVGEGAYGVVLKCRNKATGEIVAIKKF---KESEddedvKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRRKSLVGT 478
Cdd:cd07833  85 TLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTaRPASPLTDYVAT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPPR-----LKNLH---------- 539
Cdd:cd07833 165 RWYRAPElLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKclgPLPPShqelfSSNPRfagvafpeps 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031975  540 -----------KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07833 245 qpeslerrypgKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
322-572 6.99e-44

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: 157.19  E-value: 6.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd08529   3 EILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRkmREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 476
Cdd:cd08529  83 NGDLHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPLkAMKMIRDNLPPRLKnlhKVSPSLKGFLDRLLV 554
Cdd:cd08529 163 GTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFeaQNQGAL-ILKIVRGKYPPISA---SYSQDLSQLIDSCLT 238
                       250
                ....*....|....*...
gi 5031975  555 RDPAQRATAAELLKHPFL 572
Cdd:cd08529 239 KDYRQRPDTTELLRNPSL 256
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
326-570 8.17e-44

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: 156.78  E-value: 8.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLR--KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd08530   7 KLGKGSYGSVYKVKRLSDNQVYALKEVNLGslSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMN-----EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRR--KSLV 476
Cdd:cd08530  87 SKLISKRKKKrrlfpEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLG----ISKVLKKNlaKTQI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLK--AMKMIRDNLPPrlknLHKV-SPSLKGFLDRLL 553
Cdd:cd08530 163 GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPP-FEARTMQelRYKVCRGKFPP----IPPVySQDLQQIIRSLL 237
                       250
                ....*....|....*..
gi 5031975  554 VRDPAQRATAAELLKHP 570
Cdd:cd08530 238 QVNPKKRPSCDKLLQSP 254
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
326-572 1.00e-43

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: 157.26  E-value: 1.00e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ--------RrellfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd07829   6 KLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipstalR------EISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEggalTDI-----VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR 472
Cdd:cd07829  80 CD----QDLkkyldKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELI--SRLpYGPEVDIWSLGIMVIEMVDGEPPY------------F------NE---PPLKAMKMIRD 529
Cdd:cd07829 156 THEVVTLWYRAPEILlgSKH-YSTAVDIWSVGCIFAELITGKPLFpgdseidqlfkiFqilgtpTEeswPGVTKLPDYKP 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 5031975  530 NLPPRLKN-LHKVSPSLKG----FLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07829 235 TFPKWPKNdLEKVLPRLDPegidLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
327-570 1.96e-43

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: 155.50  E-value: 1.96e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 405
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVL-REISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH--DGRVKLSDFGFCAQVSKEVPRrKSLVGTPYWMA 483
Cdd:cd14006  80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARKLNPGEEL-KEIFGTPEFVA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  484 PELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPRLKNLHK--VSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd14006 159 PEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANIS-ACRVDFSEEYFssVSQEAKDFIRKLLVKEPRKRP 237

                ....*....
gi 5031975  562 TAAELLKHP 570
Cdd:cd14006 238 TAQEALQHP 246
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
326-582 2.45e-43

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: 156.81  E-value: 2.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14086   8 ELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHqkLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 -TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL---THDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd14086  88 fEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGFAGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR----DNLPPRLKNlhkVSPSLKGFLDRLLVR 555
Cdd:cd14086 168 GYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKagayDYPSPEWDT---VTPEAKDLINQMLTV 244
                       250       260
                ....*....|....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFLAKAGPPASIV 582
Cdd:cd14086 245 NPAKRITAAEALKHPWICQRDRVASMV 271
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
326-570 2.83e-43

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: 155.56  E-value: 2.83e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14095   7 VIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGGDLF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGfcaqVSKEVPRRKSLV-GT 478
Cdd:cd14095  87 DaITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFG----LATEVKEPLFTVcGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF----NEPPL--KAMKMIRDNLPPRLKNlhkVSPSLKGFLDRL 552
Cdd:cd14095 163 PTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspdrDQEELfdLILAGEFEFLSPYWDN---ISDSAKDLISRM 239
                       250
                ....*....|....*...
gi 5031975  553 LVRDPAQRATAAELLKHP 570
Cdd:cd14095 240 LVVDPEKRYSAGQVLDHP 257
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
327-572 6.81e-43

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: 154.85  E-value: 6.81e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL------RKQQRRELLFN----EVVIMRDYQHENVVemynSYL----VGDELW 392
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKQVELpktssdRADSRQKTVVDalksEIDTLKDLDHPNIV----QYLgfeeTEDYFS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGALTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVP- 470
Cdd:cd06629  85 IFLEYVPGGSIGSCLrKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFG----ISKKSDd 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 -----RRKSLVGTPYWMAPELI--SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--RDNLPPRLKNLHkV 541
Cdd:cd06629 161 iygnnGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnKRSAPPVPEDVN-L 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031975  542 SPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06629 240 SPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
326-572 7.45e-43

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 153.93  E-value: 7.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFnEVVIMR----DYQHENVVEMYNSYL--VGDELWVVMEFLe 399
Cdd:cd05118   6 KIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALR-EIKLLKhlndVEGHPNIVKLLDVFEhrGGNHLCLVFELM- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTH--TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR-VKLSDFGFCAQVSkeVPRRKSLV 476
Cdd:cd05118  84 GMNLYELIKDypRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARSFT--SPPYTPYV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRL-PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLknlhkvspsLKGFLDRLLVR 555
Cdd:cd05118 162 ATRWYRAPEVLLGAkPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTPE---------ALDLLSKMLKY 232
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd05118 233 DPAKRITASQALAHPYF 249
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
327-571 8.55e-43

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: 154.56  E-value: 8.55e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRK----QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14098   8 LGSGTFAEVKKAVEVETGKMRAIKQIVKRKvagnDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFcAQVSKEVPRRKSLVGTP 479
Cdd:cd14098  88 LMDfIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGL-AKVIHTGTFLVTFCGTM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELI----SRLP--YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDN---LPPRLKNlhKVSPSLKGFLD 550
Cdd:cd14098 167 AYLAPEILmskeQNLQggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGrytQPPLVDF--NISEEAIDFIL 244
                       250       260
                ....*....|....*....|.
gi 5031975  551 RLLVRDPAQRATAAELLKHPF 571
Cdd:cd14098 245 RLLDVDPEKRMTAAQALDHPW 265
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
325-572 1.50e-42

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: 153.49  E-value: 1.50e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSG--KLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14080   6 KTIGEGSYSKVKLAEYTKSGlkEKVACKIIDKKKAPKDFLekfLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcaqvSKEVPRRKSLV-- 476
Cdd:cd14080  86 HGDLLEyIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGF----ARLCPDDDGDVls 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 ----GTPYWMAPELISRLPYGPEV-DIWSLGIMVIEMVDGEPPyFNEPPLKamKMIRDNLPPRL---KNLHKVSPSLKGF 548
Cdd:cd14080 162 ktfcGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMP-FDDSNIK--KMLKDQQNRKVrfpSSVKKLSPECKDL 238
                       250       260
                ....*....|....*....|....
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14080 239 IDQLLEPDPTKRATIEEILNHPWL 262
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
326-573 5.65e-42

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 152.79  E-value: 5.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIV--CIAtvRSSGKLVAVKKMDLRKQQRREllfnEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14091   7 EIGKGSYSVCkrCIH--KATGKEYAVKIIDKSKRDPSE----EIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLRGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR----VKLSDFGFCAQVSKEvprrKSLVG 477
Cdd:cd14091  81 LLDrILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQLRAE----NGLLM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TP-Y---WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMIRD-NLPPRLKNLHKVSPSLKGFL 549
Cdd:cd14091 157 TPcYtanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPndtPEVILARIGSgKIDLSGGNWDHVSDSAKDLV 236
                       250       260
                ....*....|....*....|....
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd14091 237 RKMLHVDPSQRPTAAQVLQHPWIR 260
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
326-572 1.64e-41

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: 151.01  E-value: 1.64e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK---QQRREL-----LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14084  13 TLGSGACGEVKLAYDKSTCKKVAIKIINKRKftiGSRREInkprnIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLEL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHTRMNEEQIA-----AVCLAVLqalsVLHAQGVIHRDIKSDSILL-THDGR--VKLSDFGFcAQVSKEV 469
Cdd:cd14084  93 MEGGELFDRVVSNKRLKEAICklyfyQMLLAVK----YLHSNGIIHRDLKPENVLLsSQEEEclIKITDFGL-SKILGET 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRRKSLVGTPYWMAPELI---SRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEpPLKAMKMIRDNLPPRLKNLHK----VS 542
Cdd:cd14084 168 SLMKTLCGTPTYLAPEVLrsfGTEGYTRAVDCWSLGVILFICLSGYPP-FSE-EYTQMSLKEQILSGKYTFIPKawknVS 245
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  543 PSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14084 246 EEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
327-572 2.53e-41

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 150.17  E-value: 2.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14069   9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR--KSLVGTPYW 481
Cdd:cd14069  89 DkIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERllNKMCGTLPY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYfnEPPLKAMKMIRDNLPPRLKNLH---KVSPSLKGFLDRLLVRDP 557
Cdd:cd14069 169 VAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPW--DQPSDSCQEYSDWKENKKTYLTpwkKIDTAALSLLRKILTENP 246
                       250
                ....*....|....*
gi 5031975  558 AQRATAAELLKHPFL 572
Cdd:cd14069 247 NKRITIEDIKKHPWY 261
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
323-571 4.39e-41

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: 152.05  E-value: 4.39e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIK-IGEGSTGIVCIATVRSSGKLVAVKKMdlRK----QQRRELLFN-EVVIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd05573   4 EVIKvIGRGAFGEVWLVRDKDTGQVYAMKIL--RKsdmlKREQIAHVRaERDILADADSPWIVRLHYAFQDEDHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGAL-TDIVTHTRMNEEQ----IAAVCLAVLQalsvLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV--SKEV 469
Cdd:cd05573  82 YMPGGDLmNLLIKYDVFPEETarfyIAELVLALDS----LHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnkSGDR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 P---------------------------RRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK 522
Cdd:cd05573 158 EsylndsvntlfqdnvlarrrphkqrrvRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  523 -AMKMI--RDNL--PPRlknlHKVSPSLKGFLDRLLvRDPAQR-ATAAELLKHPF 571
Cdd:cd05573 238 tYSKIMnwKESLvfPDD----PDVSPEAIDLIRRLL-CDPEDRlGSAEEIKAHPF 287
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
326-569 6.55e-41

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: 148.80  E-value: 6.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    326 KIGEGSTGIVCIATVRSSGK----LVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKGEGEntkiKVAVKtlKEGADEEEREDFL-EEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    400 GGALTD-IVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG 477
Cdd:pfam07714  85 GGDLLDfLRKHKRkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRGGG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    478 -TPY-WMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPYFNEPPLKAMKMIRDNlpPRLKNLHKVSPSLKGFLDRLLV 554
Cdd:pfam07714 165 kLPIkWMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDG--YRLPQPENCPDELYDLMKQCWA 242
                         250
                  ....*....|....*
gi 5031975    555 RDPAQRATAAELLKH 569
Cdd:pfam07714 243 YDPEDRPTFSELVED 257
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
325-572 1.65e-40

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 147.76  E-value: 1.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM--EFLEG 400
Cdd:cd13983   7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKlpKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELMTS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQG--VIHRDIKSDSILLT-HDGRVKLSDFGFCAQvsKEVPRRKSLV 476
Cdd:cd13983  87 GTLkQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATL--LRQSFAKSVI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRlPYGPEVDIWSLGIMVIEMVDGEPPYfNE--PPLKAMKMIRDNLPPrlKNLHKV-SPSLKGFLDRLL 553
Cdd:cd13983 165 GTPEFMAPEMYEE-HYDEKVDIYAFGMCLLEMATGEYPY-SEctNAAQIYKKVTSGIKP--ESLSKVkDPELKDFIEKCL 240
                       250
                ....*....|....*....
gi 5031975  554 vRDPAQRATAAELLKHPFL 572
Cdd:cd13983 241 -KPPDERPSARELLEHPFF 258
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
327-572 2.56e-40

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: 147.53  E-value: 2.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14078  11 IGSGGFAKVKLATHILTGEKVAIKIMD-KKALGDDLprVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR-KSLVGTPYWM 482
Cdd:cd14078  90 DyIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHHlETCCGSPAYA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd14078 170 APELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDD---NVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRI 246
                       250
                ....*....|.
gi 5031975  562 TAAELLKHPFL 572
Cdd:cd14078 247 TVKELLNHPWV 257
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
327-571 2.67e-40

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: 149.29  E-value: 2.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKqqrrellfnEVVIMRDY---------------QHENVVEMYNSYLVGDEL 391
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKV--LKK---------EVIIEDDDvectmtekrvlalanRHPFLTGLHACFQTEDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALT-DIVTHTRMNEEQ----IAAVCLAvlqaLSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS 466
Cdd:cd05570  72 YFVMEYVNGGDLMfHIQRARRFTEERarfyAAEICLA----LQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLk 546
Cdd:cd05570 148 WGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSI- 226
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  547 gfLDRLLVRDPAQR-----ATAAELLKHPF 571
Cdd:cd05570 227 --LKGLLTKDPARRlgcgpKGEADIKAHPF 254
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
326-568 4.53e-40

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 146.52  E-value: 4.53e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     326 KIGEGSTGIVCIATVRSSGK----LVAVKKMDLRK--QQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:smart00219   6 KLGEGAFGEVYKGKLKGKGGkkkvEVAVKTLKEDAseQQIEEFL-REARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     400 GGALTDIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKSLVG 477
Cdd:smart00219  85 GGDLLSYLrkNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG----LSRDLYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     478 T----PY-WMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLKGFLDR 551
Cdd:smart00219 161 RggklPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKNGY--RLPQPPNCPPELYDLMLQ 238
                          250
                   ....*....|....*..
gi 5031975     552 LLVRDPAQRATAAELLK 568
Cdd:smart00219 239 CWAEDPEDRPTFSELVE 255
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
326-572 1.21e-39

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: 145.47  E-value: 1.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFN---EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14081   8 TLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKverEIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14081  88 LFDyLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGM-ASLQPEGSLLETSCGSPHY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAM----KMIRDNLPprlknlHKVSPSLKGFLDRLLVRD 556
Cdd:cd14081 167 ACPEVIKGEKYdGRKADIWSCGVILYALLVGALP-FDDDNLRQLlekvKRGVFHIP------HFISPDAQDLLRRMLEVN 239
                       250
                ....*....|....*.
gi 5031975  557 PAQRATAAELLKHPFL 572
Cdd:cd14081 240 PEKRITIEEIKKHPWF 255
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
326-575 1.41e-39

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: 146.05  E-value: 1.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK------KMDLRKQQRRELlfnevVIMRDYQHENVVEMYNSYLV-GDELWVVMEFL 398
Cdd:cd06620  12 DLGAGNGGSVSKVLHIPTGTIMAKKvihidaKSSVRKQILREL-----QILHECHSPYIVSFYGAFLNeNNNIIICMEYM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVT-HTRMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRR--KS 474
Cdd:cd06620  87 DCGSLDKILKkKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFG----VSGELINSiaDT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPP------------LKAMKMIRDNLPPRLKNLHKVS 542
Cdd:cd06620 163 FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFP-FAGSNddddgyngpmgiLDLLQRIVNEPPPRLPKDRIFP 241
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  543 PSLKGFLDRLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06620 242 KDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQA 274
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
327-571 2.82e-39

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: 144.43  E-value: 2.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKL-VAVK---KMDLRKQQrrELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKPDLpVAIKcitKKNLSKSQ--NLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG---------RVKLSDFGFCAQVSKEVpRR 472
Cdd:cd14120  79 LADYLQAKGtLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFLQDGM-MA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPP-YFNEPP-LKAMKMIRDNLPPRLKNlhKVSPSLKGFLD 550
Cdd:cd14120 158 ATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPfQAQTPQeLKAFYEKNANLRPNIPS--GTSPALKDLLL 235
                       250       260
                ....*....|....*....|.
gi 5031975  551 RLLVRDPAQRATAAELLKHPF 571
Cdd:cd14120 236 GLLKRNPKDRIDFEDFFSHPF 256
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
326-568 3.07e-39

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 144.23  E-value: 3.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     326 KIGEGSTGIVCIATVRSSGK----LVAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:smart00221   6 KLGEGAFGEVYKGTLKGKGDgkevEVAVKTLkeDASEQQIEEFL-REARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     400 GGALTDIV---THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKSLV 476
Cdd:smart00221  85 GGDLLDYLrknRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG----LSRDLYDDDYYK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975     477 GT----PY-WMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLKGFLD 550
Cdd:smart00221 161 VKggklPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKKGY--RLPKPPNCPPELYKLML 238
                          250
                   ....*....|....*...
gi 5031975     551 RLLVRDPAQRATAAELLK 568
Cdd:smart00221 239 QCWAEDPEDRPTFSELVE 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
326-571 5.16e-39

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: 143.58  E-value: 5.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGK-LVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14121   2 KLGSGTYATVYKAYRKSGAReVVAVKCVSKSSLNKasTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDGRV--KLSDFGFcAQVSKEVPRRKSLVGTP 479
Cdd:cd14121  82 LSRFIRSRRTLPESTVRRFLQQLaSALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGF-AQHLKPNDEAHSLRGSP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY----FNEPPLKamkmIRDNLPPRLKNLHKVSPSLKGFLDRLLVR 555
Cdd:cd14121 161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFasrsFEELEEK----IRSSKPIEIPTRPELSADCRDLLLRLLQR 236
                       250
                ....*....|....*.
gi 5031975  556 DPAQRATAAELLKHPF 571
Cdd:cd14121 237 DPDRRISFEEFFAHPF 252
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
327-570 5.92e-39

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: 143.67  E-value: 5.92e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14083  11 LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEdSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGELFD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 -IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL---LTHDGRVKLSDFGFCAQVSKEVprRKSLVGTPYW 481
Cdd:cd14083  91 rIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKMEDSGV--MSTACGTPGY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR-----------DNlpprlknlhkVSPSLKGFLD 550
Cdd:cd14083 169 VAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILkaeyefdspywDD----------ISDSAKDFIR 238
                       250       260
                ....*....|....*....|
gi 5031975  551 RLLVRDPAQRATAAELLKHP 570
Cdd:cd14083 239 HLMEKDPNKRYTCEQALEHP 258
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
327-572 7.15e-39

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: 143.55  E-value: 7.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE---LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGal 403
Cdd:cd05578   8 IGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDsvrNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGG-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 tDIVTH----TRMNEEQIA--AVCLAVlqALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVpRRKSLVG 477
Cdd:cd05578  86 -DLRYHlqqkVKFSEETVKfyICEIVL--ALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGT-LATSTSG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYfnepPLKAMKMIRDNLPPRLKNLHKVSPS----LKGFLDRLL 553
Cdd:cd05578 162 TKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPY----EIHSRTSIEEIRAKFETASVLYPAGwseeAIDLINKLL 237
                       250       260
                ....*....|....*....|
gi 5031975  554 VRDPAQR-ATAAELLKHPFL 572
Cdd:cd05578 238 ERDPQKRlGDLSDLKNHPYF 257
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
327-572 7.53e-39

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: 143.65  E-value: 7.53e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIV--CIAtvRSSGKLVAVKKMDLRKQQR--------RELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVM 395
Cdd:cd14093  11 LGRGVSSTVrrCIE--KETGQEFAVKIIDITGEKSseneaeelREATRREIEILRQVSgHPNIIELHDVFESPTFIFLVF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVsKEVPRRKS 474
Cdd:cd14093  89 ELCRKGELFDYLTEVvTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL-DEGEKLRE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELIS-----RLP-YGPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDNLPPRLK----NLHKVSPS 544
Cdd:cd14093 168 LCGTPGYLAPEVLKcsmydNAPgYGKEVDMWACGVIMYTLLAGCPPFWHR---KQMVMLRNIMEGKYEfgspEWDDISDT 244
                       250       260
                ....*....|....*....|....*...
gi 5031975  545 LKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14093 245 AKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
326-572 1.21e-38

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 143.44  E-value: 1.21e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlrKQ---------QRRELLFnevvIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd07830   6 QLGDGTFGSVYLARNKETGELVAIKKM---KKkfysweecmNLREVKS----LRKLNEHPNIVKLKEVFRENDELYFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfCAQVSKEVPRRKS 474
Cdd:cd07830  79 YMEGNLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFG-LAREIRSRPPYTD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEP--PYFNE------------PPLK-----AMKMIRD---NL 531
Cdd:cd07830 158 YVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPlfPGSSEidqlykicsvlgTPTKqdwpeGYKLASKlgfRF 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  532 PPRL-KNLHKV----SPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07830 238 PQFApTSLHQLipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
326-571 1.35e-38

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: 143.67  E-value: 1.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM-----DLrkqQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd07847   8 KIGEGSYGVVFKCRNRETGQIVAIKKFvesedDP---VIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd07847  85 TVLNELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYVATR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL------------------------PPR 534
Cdd:cd07847 165 WYRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLgdliprhqqifstnqffkglsipePET 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  535 LKNLH----KVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07847 245 REPLEskfpNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
327-572 1.79e-38

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: 142.45  E-value: 1.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRS--SGKLVAVKKmdLRK-------QQRRELLFNEVVIMRDYQHENVVEMYnSYLV--GDELWVVM 395
Cdd:cd13994   1 IGKGATSVVRIVTKKNprSGVLYAVKE--YRRrddeskrKDYVKRLTSEYIISSKLHHPNIVKVL-DLCQdlHGKWCLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----FCAQVSKEVP 470
Cdd:cd13994  78 EYCPGGDLfTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaevFGMPAEKESP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPYGPE-VDIWSLGIMVIEMVDGEPPY----FNEPP-LKAMKMIRDNLPPRLKNLHKVSPS 544
Cdd:cd13994 158 MSAGLCGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPWrsakKSDSAyKAYEKSGDFTNGPYEPIENLLPSE 237
                       250       260
                ....*....|....*....|....*...
gi 5031975  545 LKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd13994 238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
326-573 3.98e-38

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: 141.95  E-value: 3.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14169  10 KLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEaMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGfcaqVSK--EVPRRKSLVGT 478
Cdd:cd14169  90 DrIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFG----LSKieAQGMLSTACGT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnlpprLKNLHK--------VSPSLKGFLD 550
Cdd:cd14169 166 PGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQI-------LKAEYEfdspywddISESAKDFIR 238
                       250       260
                ....*....|....*....|...
gi 5031975  551 RLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd14169 239 HLLERDPEKRFTCEQALQHPWIS 261
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
346-572 4.58e-38

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: 141.03  E-value: 4.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  346 LVAVKKMDLRK---QQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD-IVTHTR--MNEEQIAA 419
Cdd:cd08221  27 LVVWKEVNLSRlseKERRDAL-NEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDkIAQQKNqlFPEEVVLW 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  420 VCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIW 499
Cdd:cd08221 106 YLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIW 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031975  500 SLGIMVIEMVDGEPPYFNEPPLK-AMKMIRDNlppRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd08221 186 AVGCVLYELLTLKRTFDATNPLRlAVKIVQGE---YEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
327-573 4.70e-38

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: 141.46  E-value: 4.70e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDL-RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05611   4 ISKGAFGSVYLAKKRSTGDYFAIKvlkKSDMiAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05611  84 CASLIKTLGGLPEDWAKQYIAeVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL-SRNGLEKRHNKKFVGTPDY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI---RDNLPPRLKNLhkVSPSLKGFLDRLLVRDPA 558
Cdd:cd05611 163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNIlsrRINWPEEVKEF--CSPEAVDLINRLLCMDPA 240
                       250
                ....*....|....*...
gi 5031975  559 QRATA---AELLKHPFLA 573
Cdd:cd05611 241 KRLGAngyQEIKSHPFFK 258
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
326-571 5.47e-38

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: 141.93  E-value: 5.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlRKQQRRELL----FNEVVIMRDYQHENVV---EMYNSYLVGD---ELWVVM 395
Cdd:cd07840   6 QIGEGTYGQVYKARNKKTGELVALKKI--RMENEKEGFpitaIREIKLLQKLDHPNVVrlkEIVTSKGSAKykgSIYMVF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGaLTDIVTHT--RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR- 472
Cdd:cd07840  84 EYMDHD-LTGLLDNPevKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNADy 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELI---SRlpYGPEVDIWSLGIMVIEMVDGEP--------------------------PYFNEPPLKA 523
Cdd:cd07840 163 TNRVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPifqgkteleqlekifelcgspteenwPGVSDLPWFE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  524 MKMIRDNLPPRLKNL--HKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07840 241 NLKPKKPYKRRLREVfkNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
324-572 8.29e-38

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: 140.66  E-value: 8.29e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  324 FIK-IGEGSTGIVCIATVRSSGKLVAVK------------------KMDLRKQQRrelLFNEVVIMRDYQHENVVEMYNS 384
Cdd:cd14077   5 FVKtIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglkkerekrlEKEISRDIR---TIREAALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  385 YLVGDELWVVMEFLEGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA 463
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDyIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 QVSKEvPRRKSLVGTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNE--PPLKAmkMIRDNlppRLKNLHK 540
Cdd:cd14077 162 LYDPR-RLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDEnmPALHA--KIKKG---KVEYPSY 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031975  541 VSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14077 236 LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
327-572 1.08e-37

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: 140.36  E-value: 1.08e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 405
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIE-TKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELFDr 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH---DGRVKLSDFGFCAQVSK-EVPRRKSLVGTPYW 481
Cdd:cd14087  88 IIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpgpDSKIMITDFGLASTRKKgPNCLMKTTCGTPEY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQR 560
Cdd:cd14087 168 IAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQIlRAKYSYSGEPWPSVSNLAKDFIDRLLTVNPGER 247
                       250
                ....*....|..
gi 5031975  561 ATAAELLKHPFL 572
Cdd:cd14087 248 LSATQALKHPWI 259
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
327-573 1.21e-37

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: 141.98  E-value: 1.21e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKQqrrELLFNEVV--------IMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05599   9 IGRGAFGEVRLVRKKDTGHVYAMKK--LRKS---EMLEKEQVahvraerdILAEADNPWVVKLYYSFQDEENLYLIMEFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALT------DIVThtrmnEEQ----IAAVCLAVlqalSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE 468
Cdd:cd05599  84 PGGDMMtllmkkDTLT-----EEEtrfyIAETVLAI----ESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 vPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI---RDNL--PPRLknlhKVSP 543
Cdd:cd05599 155 -HLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKImnwRETLvfPPEV----PISP 229
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  544 SLKGFLDRLLVrDPAQRATA---AELLKHPFLA 573
Cdd:cd05599 230 EAKDLIERLLC-DAEHRLGAngvEEIKSHPFFK 261
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
326-569 1.63e-37

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 139.60  E-value: 1.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGK---LVAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd00192   2 KLGEGAFGEVYKGKLKGGDGktvDVAVKTLkeDASESERKDFL-KEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GAL----------TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd00192  81 GDLldflrksrpvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSlVGTP---YWMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLK 546
Cdd:cd00192 161 YRKK-TGGKlpiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEVLEYLRKGY--RLPKPENCPDELY 237
                       250       260
                ....*....|....*....|...
gi 5031975  547 GFLDRLLVRDPAQRATAAELLKH 569
Cdd:cd00192 238 ELMLSCWQLDPEDRPTFSELVER 260
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
326-572 1.65e-37

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: 139.56  E-value: 1.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd08218   7 KIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPkeREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd08218  87 YKRINAQRgvlFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIGTPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLK--AMKMIRDNLPPRLKnlhKVSPSLKGFLDRLLVRDPA 558
Cdd:cd08218 167 YLSPEICENKPYNNKSDIWALGCVLYEMCTLKHA-FEAGNMKnlVLKIIRGSYPPVPS---RYSYDLRSLVSQLFKRNPR 242
                       250
                ....*....|....
gi 5031975  559 QRATAAELLKHPFL 572
Cdd:cd08218 243 DRPSINSILEKPFI 256
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
327-571 1.66e-37

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: 140.58  E-value: 1.66e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM----DLRKQQRreLLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEflegga 402
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGTIMAVKRIrstvDEKEQKR--LLMDLDVVMRSSDCPYIVKFYGALFREGDCWICME------ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDI-----------VTHTRMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd06616  86 LMDIsldkfykyvyeVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSIA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYwMAPELI----SRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNePPLKAMKMIRDNLPPRLKNLHK--VS 542
Cdd:cd06616 166 KTRDAGCRPY-MAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYpkWN-SVFDQLTQVVKGDPPILSNSEEreFS 243
                       250       260
                ....*....|....*....|....*....
gi 5031975  543 PSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd06616 244 PSFVNFVNLCLIKDESKRPKYKELLKHPF 272
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
327-570 1.97e-37

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: 139.80  E-value: 1.97e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQ---QRR-----------------ELLFNEVVIMRDYQHENVVEMyN 383
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKilsKKKLLKQagfFRRppprrkpgalgkpldplDRVYREIAILKKLDHPNVVKL-V 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  384 SYL---VGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG 460
Cdd:cd14118  81 EVLddpNEDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  461 FCAQVSKEVPRRKSLVGTPYWMAPELI--SRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPRLKN 537
Cdd:cd14118 161 VSNEFEGDDALLSSTAGTPAFMAPEALseSRKKFsGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIK-TDPVVFPD 239
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  538 LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14118 240 DPVVSEQLKDLILRMLDKNPSERITLPEIKEHP 272
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
327-573 2.17e-37

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: 139.39  E-value: 2.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL-LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETsIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 -IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL---LTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14167  91 rIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL-SKIEGSGSVMSTACGTPGY 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnlpprLKNLHK--------VSPSLKGFLDRLL 553
Cdd:cd14167 170 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQI-------LKAEYEfdspywddISDSAKDFIQHLM 242
                       250       260
                ....*....|....*....|
gi 5031975  554 VRDPAQRATAAELLKHPFLA 573
Cdd:cd14167 243 EKDPEKRFTCEQALQHPWIA 262
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
326-572 2.48e-37

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 139.32  E-value: 2.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQ--QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd08225   7 KIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMpvKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRV-KLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd08225  87 MKRINRQRgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAYTCVGTP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY-FNEPPLKAMKMIRDNLPPrlknlhkVSPS----LKGFLDRLLV 554
Cdd:cd08225 167 YYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFeGNNLHQLVLKICQGYFAP-------ISPNfsrdLRSLISQLFK 239
                       250
                ....*....|....*...
gi 5031975  555 RDPAQRATAAELLKHPFL 572
Cdd:cd08225 240 VSPRDRPSITSILKRPFL 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
326-568 2.69e-37

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 139.33  E-value: 2.69e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKK------MDlrKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd08224   7 KIGKGQFSVVYRARCLLDGRLVALKKvqifemMD--AKARQDCL-KEIDLLQQLNHPNIIKYLASFIENNELNIVLELAD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd08224  84 AGDLSRLIKHFKkqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAAHS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEpplkamKMirdNL------------PPrLKNLHkVS 542
Cdd:cd08224 164 LVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGE------KM---NLyslckkiekceyPP-LPADL-YS 232
                       250       260
                ....*....|....*....|....*.
gi 5031975  543 PSLKGFLDRLLVRDPAQRATAAELLK 568
Cdd:cd08224 233 QELRDLVAACIQPDPEKRPDISYVLD 258
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
327-575 2.91e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 141.11  E-value: 2.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKclkKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   404 -TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcaqvSKEVPRRK-SLVGTPYW 481
Cdd:PTZ00263 106 fTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF----AKKVPDRTfTLCGTPEY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:PTZ00263 182 LAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKI---LAGRLKFPNWFDGRARDLVKGLLQTDHTKRL 258
                        250
                 ....*....|....*....
gi 5031975   562 TA-----AELLKHPFLAKA 575
Cdd:PTZ00263 259 GTlkggvADVKNHPYFHGA 277
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
327-571 5.17e-37

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: 138.51  E-value: 5.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM------DLRKQqrrELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVkkrhivQTRQQ---EHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDI-VTHTRMNEEQiAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGT 478
Cdd:cd05572  78 GELWTIlRDRGLFDEYT-ARFYTAcVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGF-AKKLGSGRKTWTFCGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEP---PLKAMKMIRDNLpPRLKNLHKVSPSLKGFLDRLLVR 555
Cdd:cd05572 156 PEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPP-FGGDdedPMKIYNIILKGI-DKIEFPKYIDKNAKNLIKQLLRR 233
                       250       260
                ....*....|....*....|.
gi 5031975  556 DPAQR-----ATAAELLKHPF 571
Cdd:cd05572 234 NPEERlgylkGGIRDIKKHKW 254
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
327-571 5.95e-37

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: 138.16  E-value: 5.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14185   8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEdMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEVprrKSLVGTPY 480
Cdd:cd14185  88 AIIESVKFTEHDAALMIIDLcEALVYIHSKHIVHRDLKPENLLVQHNPdkstTLKLADFGLAKYVTGPI---FTVCGTPT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMKMIR-------DNLPPRLKNlhkVSPSLKGFLDRLL 553
Cdd:cd14185 165 YVAPEILSEKGYGLEVDMWAAGVILYILLCGFPP-FRSPERDQEELFQiiqlghyEFLPPYWDN---ISEAAKDLISRLL 240
                       250
                ....*....|....*...
gi 5031975  554 VRDPAQRATAAELLKHPF 571
Cdd:cd14185 241 VVDPEKRYTAKQVLQHPW 258
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
327-567 6.31e-37

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: 138.62  E-value: 6.31e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGD----ELWVVMEFLeGG 401
Cdd:cd13985   8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSegrkEVLLLMEYC-PG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTH---TRMNEEQIAAVCLAVLQALSVLHAQG--VIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 476
Cdd:cd13985  87 SLVDILEKsppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLERAEEVN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 ---------GTPYWMAPELI---SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMkmirdNLPPRLKNLHKVSPS 544
Cdd:cd13985 167 iieeeiqknTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIV-----AGKYSIPEQPRYSPE 241
                       250       260
                ....*....|....*....|...
gi 5031975  545 LKGFLDRLLVRDPAQRATAAELL 567
Cdd:cd13985 242 LHDLIRHMLTPDPAERPDIFQVI 264
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
326-570 1.40e-36

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: 136.74  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM--DLRKQQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd13997   7 QIGSGSFSEVFKVRSKVDGCLYAVKKSkkPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELCENGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDI----VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKslvGT 478
Cdd:cd13997  87 LQDAleelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEE---GD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLknlhKVSPSLKGFLDRLLVRDP 557
Cdd:cd13997 164 SRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQGKLPLPPGL----VLSQELTRLLKVMLDPDP 239
                       250
                ....*....|...
gi 5031975  558 AQRATAAELLKHP 570
Cdd:cd13997 240 TRRPTADQLLAHD 252
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
327-573 2.04e-36

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: 137.43  E-value: 2.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 405
Cdd:cd14166  11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDr 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL-LTHD--GRVKLSDFGFCAQVSKEVprRKSLVGTPYWM 482
Cdd:cd14166  91 ILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDenSKIMITDFGLSKMEQNGI--MSTACGTPGYV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL----PPRLKNlhkVSPSLKGFLDRLLVRDPA 558
Cdd:cd14166 169 APEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYyefeSPFWDD---ISESAKDFIRHLLEKNPS 245
                       250
                ....*....|....*
gi 5031975  559 QRATAAELLKHPFLA 573
Cdd:cd14166 246 KRYTCEKALSHPWII 260
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
327-574 2.56e-36

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: 138.43  E-value: 2.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM----DLRKQQRRELlfNEVVIMRDYQHENVVEMYN-----SYLVGDELWVVMEF 397
Cdd:cd07834   8 IGSGAYGVVCSAYDKRTGRKVAIKKIsnvfDDLIDAKRIL--REIKILRHLKHENIIGLLDilrppSPEEFNDVYIVTEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEggalTD----IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRK 473
Cdd:cd07834  86 ME----TDlhkvIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGL-ARGVDPDEDKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SL---VGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEP--P---YFNE----------PPLKAMKMIRD----- 529
Cdd:cd07834 161 FLteyVVTRWYRAPELLlSSKKYTKAIDIWSVGCIFAELLTRKPlfPgrdYIDQlnlivevlgtPSEEDLKFISSekarn 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  530 ---NLPPR-LKNLHKV----SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd07834 241 ylkSLPKKpKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
327-568 4.33e-36

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: 135.73  E-value: 4.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14072   8 IGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLqkLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkevPRRK--SLVGTPYW 481
Cdd:cd14072  88 DyLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFT---PGNKldTFCGSPPY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEpplkAMKMIRDNLpprLKNLHKV----SPSLKGFLDRLLVRD 556
Cdd:cd14072 165 AAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQ----NLKELRERV---LRGKYRIpfymSTDCENLLKKFLVLN 237
                       250
                ....*....|..
gi 5031975  557 PAQRATAAELLK 568
Cdd:cd14072 238 PSKRGTLEQIMK 249
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
327-572 5.80e-36

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: 135.47  E-value: 5.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK--------KMDLRKQQRRELLfnevvIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd14079  10 LGVGSFGKVKLAEHELTGHKVAVKilnrqkikSLDMEEKIRREIQ-----ILKLFRHPHIIRLYEVIETPTDIFMVMEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVG 477
Cdd:cd14079  85 SGGELFDyIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL-SNIMRDGEFLKTSCG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELIS-RLPYGPEVDIWSLGIMVIEMVDGEPPYFNE--PPLkaMKMIRD---NLPprlknlHKVSPSLKGFLDR 551
Cdd:cd14079 164 SPNYAAPEVISgKLYAGPEVDVWSCGVILYALLCGSLPFDDEhiPNL--FKKIKSgiyTIP------SHLSPGARDLIKR 235
                       250       260
                ....*....|....*....|.
gi 5031975  552 LLVRDPAQRATAAELLKHPFL 572
Cdd:cd14079 236 MLVVDPLKRITIPEIRQHPWF 256
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
327-560 6.36e-36

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: 135.71  E-value: 6.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGivCIATVR---SSGKLVAVKKMDL-----------RKQQRRELLfNEVVIMRD-YQHENVVEMYNSYLVGDEL 391
Cdd:cd08528   8 LGSGAFG--CVYKVRkksNGQTLLALKEINMtnpafgrteqeRDKSVGDII-SEVNIIKEqLRHPNIVRYYKTFLENDRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALTDIVT-----HTRMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 465
Cdd:cd08528  85 YIVMELIEGAPLGEHFSslkekNEHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLGEDDKVTITDFGLAKQK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK-AMKMIRDNLPPRLKNLHkvSPS 544
Cdd:cd08528 165 GPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTlATKIVEAEYEPLPEGMY--SDD 242
                       250
                ....*....|....*.
gi 5031975  545 LKGFLDRLLVRDPAQR 560
Cdd:cd08528 243 ITFVIRSCLTPDPEAR 258
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
326-572 7.22e-36

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: 135.92  E-value: 7.22e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGa 402
Cdd:cd07832   7 RIGEGAHGIVFKAKDRETGETVALKKVALRKLEGgiPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLSS- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS-LVGTP 479
Cdd:cd07832  86 LSEVLRDEErpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYShQVATR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELI--SRlPYGPEVDIWSLGIMVIEMVDGEP--------------------------PYFNEPPLKAMKMIRDNL 531
Cdd:cd07832 166 WYRAPELLygSR-KYDEGVDLWAVGCIFAELLNGSPlfpgendieqlaivlrtlgtpnektwPELTSLPDYNKITFPESK 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 5031975  532 PPRLKNLH-KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07832 245 GIRLEEIFpDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
327-572 7.53e-36

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: 135.87  E-value: 7.53e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD-----LRKQQRREL---LFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14181  18 IGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerLSPEQLEEVrssTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVFDL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKsLV 476
Cdd:cd14181  98 MRRGELFDYLTEkVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRE-LC 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELI------SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL----PPRLKNLhkvSPSLK 546
Cdd:cd14181 177 GTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRyqfsSPEWDDR---SSTVK 253
                       250       260
                ....*....|....*....|....*.
gi 5031975  547 GFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14181 254 DLISRLLVVDPEIRLTAEQALQHPFF 279
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
322-575 1.03e-35

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: 135.63  E-value: 1.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKI---GEGSTGIVCIATVRSSGKLVAVKKM--DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd06617   1 DDLEVIeelGRGAYGVVDKMRHVPTGTIMAVKRIraTVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGgALTDIVTHT-----RMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd06617  81 VMDT-SLDKFYKKVydkglTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYwMAPELI----SRLPYGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPRLKNlHKVSPSL 545
Cdd:cd06617 160 KTIDAGCKPY-MAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDSwKTPFQQLKQVVEEPSPQLPA-EKFSPEF 237
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  546 KGFLDRLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06617 238 QDFVNKCLKKNYKERPNYPELLQHPFFELH 267
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
327-571 2.29e-35

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: 134.55  E-value: 2.29e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR-RELLfnevvIMRDYQHENVVEMYNSYLVGDE------LWVVMEFLE 399
Cdd:cd14137  12 IGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKnRELQ-----IMRRLKHPNIVKLKYFFYSSGEkkdevyLNLVMEYMP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GgALTDIVTHTRMNEEQIAAVCLAV-----LQALSVLHAQGVIHRDIKSDSILLTHD-GRVKLSDFGfCAQVSKEVPRRK 473
Cdd:cd14137  87 E-TLYRVIRHYSKNKQTIPIIYVKLysyqlFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFG-SAKRLVPGEPNV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEP--P----------------YFNEPPLKAMK-MIRDNLPP 533
Cdd:cd14137 165 SYICSRYYRAPELIFGATdYTTAIDIWSAGCVLAELLLGQPlfPgessvdqlveiikvlgTPTREQIKAMNpNYTEFKFP 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031975  534 RLK--NLHKV-----SPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14137 245 QIKphPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
318-572 2.63e-35

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: 133.75  E-value: 2.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  318 RSYLDNfIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSYLVGD-ELWV 393
Cdd:cd14165   1 RGYILG-INLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDdfvEKFLPRELEILARLNHKSIIKTYEIFETSDgKVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR 472
Cdd:cd14165  80 VMELGVQGDLLEFIKLRGALPEDVARKMFHQLsSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 ----KSLVGTPYWMAPELISRLPYGPEV-DIWSLGIMVIEMVDGEPPYFN---EPPLKAMKMIRDNLPPRlKNLhkvSPS 544
Cdd:cd14165 160 ivlsKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDsnvKKMLKIQKEHRVRFPRS-KNL---TSE 235
                       250       260
                ....*....|....*....|....*...
gi 5031975  545 LKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14165 236 CKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
326-572 2.77e-35

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: 133.28  E-value: 2.77e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14073   8 TLGKGTYGKVKLAIERATGREVAIKsikKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14073  88 LYDyISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGL-SNLYSKDKLLQTFCGSPLY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL---PPRLKNLHkvspslkGFLDRLLVRDP 557
Cdd:cd14073 167 ASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDyrePTQPSDAS-------GLIRWMLTVNP 239
                       250
                ....*....|....*
gi 5031975  558 AQRATAAELLKHPFL 572
Cdd:cd14073 240 KRRATIEDIANHWWV 254
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
322-571 2.97e-35

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: 134.09  E-value: 2.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd07846   4 ENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKmvKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT 478
Cdd:cd07846  84 HTVLDDLEKYPNgLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVAT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEpPYF----NEPPLKAMKMIRDNLPPRLKNLH-------------- 539
Cdd:cd07846 164 RWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGE-PLFpgdsDIDQLYHIIKCLGNLIPRHQELFqknplfagvrlpev 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031975  540 -----------KVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07846 243 keveplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
321-572 4.58e-35

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: 134.04  E-value: 4.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFIKIGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVViMRDYQHENVVEMYNSYLVGDELWVVMEf 397
Cdd:cd06618  17 LENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMrrsGNKEENKRILMDLDVV-LKSHDCPYIVKCYGYFITDSDVFICME- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHTR--MNEEQIAAVCLAVLQALSVL-HAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd06618  95 LMSTCLDKLLKRIQgpIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRS 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 lVGTPYWMAPELISRLP---YGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLD 550
Cdd:cd06618 175 -AGCAAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRNcKTEFEVLTKILNEEPPSLPPNEGFSPDFCSFVD 253
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd06618 254 LCLTKDHRYRPKYRELLQHPFI 275
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
327-572 5.22e-35

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: 133.12  E-value: 5.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL---------RKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVME 396
Cdd:cd14182  11 LGRGVSSVVRRCIHKPTRQEYAVKIIDItgggsfspeEVQELREATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkEVPRRKSL 475
Cdd:cd14182  91 LMKKGELFDYLTEkVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLD-PGEKLREV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELI------SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlpprlkNLHKVSP------ 543
Cdd:cd14182 170 CGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSG------NYQFGSPewddrs 243
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  544 -SLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14182 244 dTVKDLISRFLVVQPQKRYTAEEALAHPFF 273
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
327-572 6.12e-35

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: 132.83  E-value: 6.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKL-VAVK---KMDLRKQQrrELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14202  10 IGHGAFAVVFKGRHKEKHDLeVAVKcinKKNLAKSQ--TLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG---------RVKLSDFGFcAQVSKEVPRR 472
Cdd:cd14202  88 LADYLHTMRtLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF-ARYLQNNMMA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPP--LKAMKMIRDNLPPRLKnlHKVSPSLKGFLD 550
Cdd:cd14202 167 ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPqdLRLFYEKNKSLSPNIP--RETSSHLRQLLL 244
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14202 245 GLLQRNQKDRMDFDEFFHHPFL 266
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
327-572 6.54e-35

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: 134.26  E-value: 6.54e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK--KMDLRKQQRR-ELLFNEVVIMR-DYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKvlKKDVILQDDDvECTMTEKRILSlARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05590  83 LMFHIQKSRRFDEARARFYAAeITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTPDY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPplkamkmiRDNLPPRLKNLHKVSPSL-----KGFLDRLLVRD 556
Cdd:cd05590 163 IAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAEN--------EDDLFEAILNDEVVYPTWlsqdaVDILKAFMTKN 234
                       250       260
                ....*....|....*....|..
gi 5031975  557 PAQRATAAEL------LKHPFL 572
Cdd:cd05590 235 PTMRLGSLTLggeeaiLRHPFF 256
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
327-573 2.28e-34

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: 132.09  E-value: 2.28e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL-LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14168  18 LGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 -IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL---THDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14168  98 rIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGL-SKMEGKGDVMSTACGTPGY 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQR 560
Cdd:cd14168 177 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIlKADYEFDSPYWDDISDSAKDFIRNLMEKDPNKR 256
                       250
                ....*....|...
gi 5031975  561 ATAAELLKHPFLA 573
Cdd:cd14168 257 YTCEQALRHPWIA 269
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
321-560 4.45e-34

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: 131.02  E-value: 4.45e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLR---KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPeviRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVskeVPRRKSLV 476
Cdd:cd05612  83 VPGGELFSYLRNSGRFSNSTGLFYASeIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL---RDRTWTLC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRD 556
Cdd:cd05612 160 GTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKI---LAGKLEFPRHLDLYAKDLIKKLLVVD 236

                ....
gi 5031975  557 PAQR 560
Cdd:cd05612 237 RTRR 240
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
327-572 6.31e-34

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


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 129.47  E-value: 6.31e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKK--MDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd08220   8 VGRGAYGTVYLCRRKDDNKLVIIKQipVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT-HDGRVKLSDFGfcaqVSKEVPRRK---SLVG 477
Cdd:cd08220  88 EYIQQRKgslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNkKRTVVKIGDFG----ISKILSSKSkayTVVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKA--MKMIRDNLPPRLKnlhKVSPSLKGFLDRLLVR 555
Cdd:cd08220 164 TPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRA-FEAANLPAlvLKIMRGTFAPISD---RYSEELRHLILSMLHL 239
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd08220 240 DPNKRPTLSEIMAQPII 256
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
326-578 7.04e-34

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: 130.77  E-value: 7.04e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlRKQQRREL-------LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd07841   7 KLGEGTYAVVYKARDKETGRIVAIKKI--KLGERKEAkdginftALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGaLTDIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ-VSkevPRRK-- 473
Cdd:cd07841  85 ETD-LEKVIkdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSfGS---PNRKmt 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELI--SRLpYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--------RDNLPP--RLKNLHKV 541
Cdd:cd07841 161 HQVVTRWYRAPELLfgARH-YGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIfealgtptEENWPGvtSLPDYVEF 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  542 SP----SLKG-----------FLDRLLVRDPAQRATAAELLKHPFLAKAGPP 578
Cdd:cd07841 240 KPfpptPLKQifpaasddaldLLQRLLTLNPNKRITARQALEHPYFSNDPAP 291
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
327-572 7.18e-34

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: 129.78  E-value: 7.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQ---QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14106  16 LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRgqdCRNEILHEIAVLELCKDCPRVVNLHEVYETRSELILILELAAGGEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMNEEQIAAVCL-AVLQALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSKEVPRRKsLVGTP 479
Cdd:cd14106  96 QTLLDEEECLTEADVRRLMrQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRVIGEGEEIRE-ILGTP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF----NEPPLKAMKMIRDnLPPRLknLHKVSPSLKGFLDRLLVR 555
Cdd:cd14106 175 DYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGgddkQETFLNISQCNLD-FPEEL--FKDVSPLAIDFIKRLLVK 251
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd14106 252 DPEKRLTAKECLEHPWL 268
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
322-560 8.26e-34

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: 130.22  E-value: 8.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKI---GEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd14209   1 DDFDRIktlGTGSFGRVMLVRHKETGNYYAMKildKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKevpRRKS 474
Cdd:cd14209  81 EYVPGGEMFSHLRRIgRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG---RTWT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLV 554
Cdd:cd14209 158 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI---VSGKVRFPSHFSSDLKDLLRNLLQ 234

                ....*.
gi 5031975  555 RDPAQR 560
Cdd:cd14209 235 VDLTKR 240
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
369-578 1.28e-33

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: 130.60  E-value: 1.28e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  369 IMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSIL 447
Cdd:cd05584  53 ILEAVKHPFIVDLHYAFQTGGKLYLILEYLSGGELFMHLEREGIFMEDTACFYLAeITLALGHLHSLGIIYRDLKPENIL 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  448 LTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI 527
Cdd:cd05584 133 LDAQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKI 212
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031975  528 ---RDNLPPRLknlhkvSPSLKGFLDRLLVRDPAQR-----ATAAELLKHPF---------LAKAGPP 578
Cdd:cd05584 213 lkgKLNLPPYL------TNEARDLLKKLLKRNVSSRlgsgpGDAEEIKAHPFfrhinwddlLAKKVEP 274
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
327-571 1.35e-33

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: 129.00  E-value: 1.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14184   9 IGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH--DG--RVKLSDFGFCAQVSKEVprrKSLVGTPY 480
Cdd:cd14184  89 AITSsTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypDGtkSLKLGDFGLATVVEGPL---YTVCGTPT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK-----AMKMIRDNLP-PRLKNlhkVSPSLKGFLDRLLV 554
Cdd:cd14184 166 YVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQedlfdQILLGKLEFPsPYWDN---ITDSAKELISHMLQ 242
                       250
                ....*....|....*..
gi 5031975  555 RDPAQRATAAELLKHPF 571
Cdd:cd14184 243 VNVEARYTAEQILSHPW 259
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
327-571 1.41e-33

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: 130.51  E-value: 1.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKLYAVKvlqkKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05575  83 LFFHLQRERHFPEPRARFYAAeIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTPEY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKMIRDNL---PPRLKnlHKVSPSLKGFLDRLLVRDPA 558
Cdd:cd05575 163 LAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYS----RDTAEMYDNIlhkPLRLR--TNVSPSARDLLEGLLQKDRT 236
                       250
                ....*....|....*..
gi 5031975  559 QRATAA----ELLKHPF 571
Cdd:cd05575 237 KRLGSGndflEIKNHSF 253
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
327-565 1.59e-33

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 128.93  E-value: 1.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSsGKLVAVKKMDLRKQQRRELLFN-EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14066   1 IGSGGFGTVYKGVLEN-GTVVAVKRLNEMNCAASKKEFLtELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNE----EQIAAVCLAVLQALSVLHAQG---VIHRDIKSDSILLTHDGRVKLSDFGFC-AQVSKEVPRRKSLV- 476
Cdd:cd14066  80 RLHCHKGSPplpwPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLArLIPPSESVSKTSAVk 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLpprlknLHKVSPSLKGFLDRLLVRD 556
Cdd:cd14066 160 GTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWV------ESKGKEELEDILDKRLVDD 233

                ....*....
gi 5031975  557 PAQRATAAE 565
Cdd:cd14066 234 DGVEEEEVE 242
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
326-578 1.80e-33

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 129.20  E-value: 1.80e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRellFNEVVIMRDYQHENV----VEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd06622   8 ELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESK---FNQIIMELDILHKAVspyiVDFYGAFFIEGAVYMCMEYMDAG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDI----VTHTRMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKSLV 476
Cdd:cd06622  85 SLDKLyaggVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLA--KTNI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELIS------RLPYGPEVDIWSLGIMVIEMVDGEPPYfnePP------LKAMKMIRDNLPPRLKNlhKVSPS 544
Cdd:cd06622 163 GCQSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGRYPY---PPetyaniFAQLSAIVDGDPPTLPS--GYSDD 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031975  545 LKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPP 578
Cdd:cd06622 238 AQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNA 271
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
327-572 1.80e-33

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: 128.11  E-value: 1.80e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAVCL--AVLQALSVLHAQGVIHRDIKSDSIL-LTHDG-RVKLSDFGFcAQvsKEVPRR--KSLVGTPY 480
Cdd:cd14103  81 VVDDDFELTERDCILFmrQICEGVQYMHKQGILHLDLKPENILcVSRTGnQIKIIDFGL-AR--KYDPDKklKVLFGTPE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplkamkmirDNLPPRLKNLHK------------VSPSLKGF 548
Cdd:cd14103 158 FVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMG-----------DNDAETLANVTRakwdfddeafddISDEAKDF 226
                       250       260
                ....*....|....*....|....
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14103 227 ISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
327-572 1.91e-33

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: 128.30  E-value: 1.91e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14074  11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKldDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHD-GRVKLSDFGFCaqvSKEVPRRK--SLVGTP 479
Cdd:cd14074  91 DyIMKHENGLNEDLARKYFRqIVSAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFS---NKFQPGEKleTSCGSL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPPRlknlhkVSPSLKGFLDRLLVR 555
Cdd:cd14074 168 AYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDckyTVPAH------VSPECKDLIRRMLIR 241
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd14074 242 DPKKRASLEEIENHPWL 258
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
326-572 1.96e-33

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: 128.44  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14097   8 KLGQGSFGVVIEATHKETQTKWAIKKINREKagSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRM---NEEQIAAVCLAvlQALSVLHAQGVIHRDIKSDSILLTHDG-------RVKLSDFGFCAQ-VSKEVPRR 472
Cdd:cd14097  88 KELLLRKGFfseNETRHIIQSLA--SAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQkYGLGEDML 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDnlpprlKNLH-------KVSPSL 545
Cdd:cd14097 166 QETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRK------GDLTftqsvwqSVSDAA 239
                       250       260
                ....*....|....*....|....*..
gi 5031975  546 KGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14097 240 KNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
323-572 2.09e-33

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: 128.32  E-value: 2.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIK-IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE--LLFNEVVIMRDYQHENVVEMYNSYLVGD-ELWVVMEFL 398
Cdd:cd08223   3 QFLRvIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRErkAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGFC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGaltDIVTHTRMN------EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR 472
Cdd:cd08223  83 EGG---DLYTRLKEQkgvlleERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAM--KMIRDNLPPRLKnlhKVSPSLKGFLD 550
Cdd:cd08223 160 TTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHA-FNAKDMNSLvyKILEGKLPPMPK---QYSPELGELIK 235
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd08223 236 AMLHQDPEKRPSVKRILRQPYI 257
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
326-572 2.45e-33

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: 129.17  E-value: 2.45e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14085  10 ELGRGATSVVYRCRQKGTQKPYAVKKL--KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCL-AVLQALSVLHAQGVIHRDIKSDSILLTH---DGRVKLSDFGFCAQVSKEVpRRKSLVGTPYW 481
Cdd:cd14085  88 RIVEKGYYSERDAADAVkQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKIVDQQV-TMKTVCGTPGY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM--KMIR---DNLPPRLKNlhkVSPSLKGFLDRLLVRD 556
Cdd:cd14085 167 CAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMfkRILNcdyDFVSPWWDD---VSLNAKDLVKKLIVLD 243
                       250
                ....*....|....*.
gi 5031975  557 PAQRATAAELLKHPFL 572
Cdd:cd14085 244 PKKRLTTQQALQHPWV 259
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
347-572 3.32e-33

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: 128.20  E-value: 3.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  347 VAVKKMDLRKQQRRELLF-NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV-THTRMNEEQIAAVCLAV 424
Cdd:cd14201  35 VAIKSINKKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLqAKGTLSEDTIRVFLQQI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  425 LQALSVLHAQGVIHRDIKSDSILLTHDGR---------VKLSDFGFCAQVSKEVpRRKSLVGTPYWMAPELISRLPYGPE 495
Cdd:cd14201 115 AAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIADFGFARYLQSNM-MAATLCGSPMYMAPEVIMSQHYDAK 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031975  496 VDIWSLGIMVIEMVDGEPPYFNEPP--LKAMKMIRDNLPPRLKNlhKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14201 194 ADLWSIGTVIYQCLVGKPPFQANSPqdLRMFYEKNKNLQPSIPR--ETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
327-572 3.53e-33

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 127.43  E-value: 3.53e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRrellfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA-LTD 405
Cdd:cd13995  12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKP-----SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSvLEK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVkLSDFGFCAQVSKEVPRRKSLVGTPYWMAPE 485
Cdd:cd13995  87 LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEIYMSPE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  486 LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA----MKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd13995 166 VILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRS 245
                       250
                ....*....|.
gi 5031975  562 TAAELLKHPFL 572
Cdd:cd13995 246 SAAELLKHEAL 256
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
327-572 5.25e-33

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: 127.69  E-value: 5.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKviPLDITVELQKQIM-SELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSLD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 divTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKSLVGTPYWMAP 484
Cdd:cd06619  88 ---VYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIA--KTYVGTNAYMAP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  485 ELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF----NEP---PLKAMKMIRDNLPPRLKnLHKVSPSLKGFLDRLLVRDP 557
Cdd:cd06619 163 ERISGEQYGIHSDVWSLGISFMELALGRFPYPqiqkNQGslmPLQLLQCIVDEDPPVLP-VGQFSEKFVHFITQCMRKQP 241
                       250
                ....*....|....*
gi 5031975  558 AQRATAAELLKHPFL 572
Cdd:cd06619 242 KERPAPENLMDHPFI 256
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
325-573 7.15e-33

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: 128.97  E-value: 7.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IK-IGEGSTGIVCIATVRSSGKLVAVK---KMD-LRKQQ------RREllfnevvIMRDYQHENVVEMYNSYLVGDELWV 393
Cdd:cd05598   6 IKtIGVGAFGEVSLVRKKDTNALYAMKtlrKKDvLKRNQvahvkaERD-------ILAEADNEWVVKLYYSFQDKENLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-----SK 467
Cdd:cd05598  79 VMDYIPGGDLMSLLIKKGIFEEDLARFYIAELvCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EVPRRkSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIrdNLPPRLKNLHKVSPSLK 546
Cdd:cd05598 159 YYLAH-SLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETqLKVI--NWRTTLKIPHEANLSPE 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031975  547 GF-LDRLLVRDPAQR---ATAAELLKHPFLA 573
Cdd:cd05598 236 AKdLILRLCCDAEDRlgrNGADEIKAHPFFA 266
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
327-573 8.07e-33

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: 128.54  E-value: 8.07e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKvlqkKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05604  84 LFFHLQRERSFPEPRARFYAAeIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGTPEY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKMIRDNLpprlknLHK-------VSPSLKGFLDRLLV 554
Cdd:cd05604 164 LAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYC----RDTAEMYENI------LHKplvlrpgISLTAWSILEELLE 233
                       250       260
                ....*....|....*....|...
gi 5031975  555 RDPAQRATAA----ELLKHPFLA 573
Cdd:cd05604 234 KDRQLRLGAKedflEIKNHPFFE 256
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
318-572 9.50e-33

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: 126.20  E-value: 9.50e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  318 RSYLDNFIkIGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd14189   1 RSYCKGRL-LGKGGFARCYEMTDLATNKTYAVKVIPhsrVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDI--VTHTrMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR 472
Cdd:cd14189  80 LELCSRKSLAHIwkARHT-LLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLK----AMKMIRDNLPPRLknlhkvSPSLKGF 548
Cdd:cd14189 159 KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPP-FETLDLKetyrCIKQVKYTLPASL------SLPARHL 231
                       250       260
                ....*....|....*....|....
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14189 232 LAGILKRNPGDRLTLDQILEHEFF 255
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
327-574 9.72e-33

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: 127.45  E-value: 9.72e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREllfnEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14175   9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSE----EIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGELLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 -IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEvprrKSLVGTPY 480
Cdd:cd14175  85 kILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQLRAE----NGLLMTPC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 W----MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMI-RDNLPPRLKNLHKVSPSLKGFLDRL 552
Cdd:cd14175 161 YtanfVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPsdtPEEILTRIgSGKFTLSGGNWNTVSDAAKDLVSKM 240
                       250       260
                ....*....|....*....|..
gi 5031975  553 LVRDPAQRATAAELLKHPFLAK 574
Cdd:cd14175 241 LHVDPHQRLTAKQVLQHPWITQ 262
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
327-571 1.38e-32

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: 125.98  E-value: 1.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR---ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14663   8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqVSKEVPRRKSL---VGTP 479
Cdd:cd14663  88 FSkIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSA-LSEQFRQDGLLhttCGTP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAM--KMIRDNLP-PRLknlhkVSPSLKGFLDRLLVR 555
Cdd:cd14663 167 NYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLP-FDDENLMALyrKIMKGEFEyPRW-----FSPGAKSLIKRILDP 240
                       250
                ....*....|....*.
gi 5031975  556 DPAQRATAAELLKHPF 571
Cdd:cd14663 241 NPSTRITVEQIMASPW 256
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
327-574 1.46e-32

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: 127.61  E-value: 1.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKkmdlrkqqrreLLFNEVVIMRD---------------YQHENVVEMYNSYLVGDEL 391
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIK-----------VLKKDVILQDDdvdctmtekrilalaAKHPFLTALHSCFQTKDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd05591  72 FFVMEYVNGGDLMFQIQRARKFDEPRARFYAAeVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF--NEPPLKAMKMIRDNLPPRLKNLHKVSpSLKGF 548
Cdd:cd05591 152 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEadNEDDLFESILHDDVLYPVWLSKEAVS-ILKAF 230
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  549 ldrlLVRDPAQR-------ATAAELLKHPFLAK 574
Cdd:cd05591 231 ----MTKNPAKRlgcvasqGGEDAIRQHPFFRE 259
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
327-571 2.16e-32

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 125.52  E-value: 2.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL---RKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLE 399
Cdd:cd06653  10 LGRGAFGEVYLCYDADTGRELAVKQVPFdpdSQETSKEVnaLECEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS---KEVPRRKSL 475
Cdd:cd06653  90 GGSVKDqLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQticMSGTGIKSV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNLPPRLKNlhKVSPSLKGFLDRLLV 554
Cdd:cd06653 170 TGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIfKIATQPTKPQLPD--GVSDACRDFLRQIFV 247
                       250
                ....*....|....*..
gi 5031975  555 RDpAQRATAAELLKHPF 571
Cdd:cd06653 248 EE-KRRPTAEFLLRHPF 263
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
320-572 2.97e-32

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 125.00  E-value: 2.97e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14114   3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVT--HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT--HDGRVKLSDFGFCAQVS-KEVPrrKS 474
Cdd:cd14114  83 GGELFERIAaeHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDpKESV--KV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14114 161 TTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKScDWNFDDSAFSGISEEAKDFIRKLL 240
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14114 241 LADPNKRMTIHQALEHPWL 259
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
327-572 3.48e-32

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: 126.66  E-value: 3.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKQ---QRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKI--LRKEviiAKDEVahTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd05595  81 ELFFHLSRERVFTEDRARFYGAeIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDPAQR 560
Cdd:cd05595 161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELI---LMEEIRFPRTLSPEAKSLLAGLLKKDPKQR 237
                       250
                ....*....|....*..
gi 5031975  561 -----ATAAELLKHPFL 572
Cdd:cd05595 238 lgggpSDAKEVMEHRFF 254
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
317-574 3.59e-32

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: 126.99  E-value: 3.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDnFIKIGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRELL----FNEVVIMRDYQHENVVEMYNSYLVGDEL- 391
Cdd:cd07880  14 PDRYRD-LKQVGSGAYGTVCSALDRRTGAKVAIKK--LYRPFQSELFakraYRELRLLKHMKHENVIGLLDVFTPDLSLd 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 -----WVVMEFLeGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS 466
Cdd:cd07880  91 rfhdfYLVMPFM-GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVprrKSLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD--NLP----------- 532
Cdd:cd07880 170 SEM---TGYVVTRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKvtGTPskefvqklqse 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  533 ---------PRLKN------LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd07880 247 daknyvkklPRFRKkdfrslLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEE 303
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
320-567 3.89e-32

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 125.10  E-value: 3.89e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFI---KIGEGSTGIVCIATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd13996   4 YLNDFEeieLLGSGGFGSVYKVRNKVDGVTYAIKKIRLTeKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIV----THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT-HDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd13996  84 ELCEGGTLRDWIdrrnSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIGNQKR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSL--------------VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVdgeppyfnEPPLKAMKMIRdnlppRLK 536
Cdd:cd13996 164 ELNNLnnnnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML--------HPFKTAMERST-----ILT 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5031975  537 NLHK--VSPSLKG-------FLDRLLVRDPAQRATAAELL 567
Cdd:cd13996 231 DLRNgiLPESFKAkhpkeadLIQSLLSKNPEERPSAEQLL 270
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
327-572 4.66e-32

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: 124.43  E-value: 4.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14071   8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQldEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 D-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrRKSLVGTPYWMA 483
Cdd:cd14071  88 DyLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGEL-LKTWCGSPPYAA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  484 PELISRLPY-GPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMkmiRDN-LPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd14071 167 PEVFEGKEYeGPQLDIWSLGVVLYVLVCGALP-FDGSTLQTL---RDRvLSGRFRIPFFMSTDCEHLIRRMLVLDPSKRL 242
                       250
                ....*....|.
gi 5031975  562 TAAELLKHPFL 572
Cdd:cd14071 243 TIEQIKKHKWM 253
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
347-572 4.88e-32

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: 124.37  E-value: 4.88e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  347 VAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIAAVCLA 423
Cdd:cd14075  30 VAIKILDKTKldQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGELyTKISTEGKLSESEAKPLFAQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  424 VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYWMAPELISRLPY-GPEVDIWSLG 502
Cdd:cd14075 110 IVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGF-STHAKRGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALG 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031975  503 IMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPPRlknlhkVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14075 189 VLLYFMVTGVMPFRAETVAKLKKCILEgtyTIPSY------VSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
326-572 5.23e-32

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: 124.42  E-value: 5.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM-------DLRKQQRR-ELLFNEVVIM---RDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd14004   7 EMGEGAYGQVNLAIYKSKGKEVVIKFIfkerilvDTWVRDRKlGTVPLEIHILdtlNKRSHPNIVKLLDFFEDDEFYYLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 ME-FLEGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVsKEVPrR 472
Cdd:cd14004  87 MEkHGSGMDLFDfIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYI-KSGP-F 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNepplkamkmIRDNLPPRLKNLHKVSPSLKGFLDR 551
Cdd:cd14004 165 DTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYN---------IEEILEADLRIPYAVSEDLIDLISR 235
                       250       260
                ....*....|....*....|.
gi 5031975  552 LLVRDPAQRATAAELLKHPFL 572
Cdd:cd14004 236 MLNRDVGDRPTIEELLTDPWL 256
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
325-574 5.90e-32

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: 125.81  E-value: 5.90e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IK-IGEGSTGIVCIATVRSSGKLVAVKKMDL-----RKQQRRelLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05574   6 IKlLGKGDVGRVYLVRLKGTGKLFAMKVLDKeemikRNKVKR--VLTEREILATLDHPFLPTLYASFQTSTHLCFVMDYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTRMN--EEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF--GFCAQVSKEVPRRK 473
Cdd:cd05574  84 PGGELFRLLQKQPGKrlPEEVARFYAAeVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlSKQSSVTPPPVRKS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 ---------------------------SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKM 526
Cdd:cd05574 164 lrkgsrrssvksieketfvaepsarsnSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKG----SNRDE 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  527 IRDNL---PPRLKNLHKVSPSLKGFLDRLLVRDPAQR----ATAAELLKHPFLAK 574
Cdd:cd05574 240 TFSNIlkkELTFPESPPVSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFRG 294
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
353-571 6.82e-32

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: 124.01  E-value: 6.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  353 DLRKQ-QRRELLFNEVVIMRdyqHENVVEMYnSYLV----GDELWVV---MEFLEGGALTDIV-THTRMNEEQIAAVCLA 423
Cdd:cd14012  37 NGKKQiQLLEKELESLKKLR---HPNLVSYL-AFSIerrgRSDGWKVyllTEYAPGGSLSELLdSVGSVPLDTARRWTLQ 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  424 VLQALSVLHAQGVIHRDIKSDSILL---THDGRVKLSDFGFCAQVSKEVPRRKSLVGTP-YWMAPELI-SRLPYGPEVDI 498
Cdd:cd14012 113 LLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQtYWLPPELAqGSKSPTRKTDV 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031975  499 WSLGIMVIEMVDGEPPYfnepplkamkmIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14012 193 WDLGLLFLQMLFGLDVL-----------EKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
327-518 7.76e-32

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 124.06  E-value: 7.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD-LRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDkLRFPTKQEsQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDMLE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHT--RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG---RVKLSDFGFcAQVSKEVPRRKSLVGTP 479
Cdd:cd14082  91 MILSSEkgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGF-ARIIGEKSFRRSVVGTP 169
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNE 518
Cdd:cd14082 170 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFP-FNE 207
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
327-574 1.26e-31

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: 125.48  E-value: 1.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDEL------WVVMEF 397
Cdd:cd07851  23 VGSGAYGQVCSAFDTKTGRKVAIKKLS-RPFQSAIHakrTYRELRLLKHMKHENVIGLLDVFTPASSLedfqdvYLVTHL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LeGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVprrKSLVG 477
Cdd:cd07851 102 M-GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEM---TGYVA 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEP-----PYFNE----------PPLKAMKMIRD--------NLPP 533
Cdd:cd07851 178 TRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTlfpgsDHIDQlkrimnlvgtPDEELLKKISSesarnyiqSLPQ 257
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  534 R-LKNLHKV----SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd07851 258 MpKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAE 303
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
327-572 1.42e-31

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: 123.97  E-value: 1.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREllfnEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14178  11 IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSE----EIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMRGGELLD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEvprrKSLVGTPY 480
Cdd:cd14178  87 RILRQKcFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAE----NGLLMTPC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 W----MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPplkamkmirDNLPPRL-------------KNLHKVSP 543
Cdd:cd14178 163 YtanfVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGP---------DDTPEEIlarigsgkyalsgGNWDSISD 233
                       250       260
                ....*....|....*....|....*....
gi 5031975  544 SLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14178 234 AAKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
327-571 1.70e-31

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 123.23  E-value: 1.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL---RKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLE 399
Cdd:cd06652  10 LGQGAFGRVYLCYDADTGRELAVKQVQFdpeSPETSKEVnaLECEIQLLKNLLHERIVQYYGCLRDPQErtLSIFMEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK---EVPRRKSL 475
Cdd:cd06652  90 GGSIKDqLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTiclSGTGMKSV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-----RDNLPPRlknlhkVSPSLKGFLD 550
Cdd:cd06652 170 TGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIatqptNPQLPAH------VSDHCRDFLK 243
                       250       260
                ....*....|....*....|.
gi 5031975  551 RLLVrDPAQRATAAELLKHPF 571
Cdd:cd06652 244 RIFV-EAKLRPSADELLRHTF 263
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
326-570 2.06e-31

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: 122.42  E-value: 2.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM-------DLRKQQRRELLFNEVVimrdYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd14050   8 KLGEGSFGEVFKVRSREDGKLYAVKRSrsrfrgeKDRKRKLEEVERHEKL----GEHPNCVRFIKAWEEKGILYIQTELC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPRRKSLVGT 478
Cdd:cd14050  84 DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKE-DIHDAQEGD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELIsRLPYGPEVDIWSLGIMVIEMV-DGEPPYFNEpplkAMKMIRD-NLPPRLKNlhKVSPSLKGFLDRLLVRD 556
Cdd:cd14050 163 PRYMAPELL-QGSFTKAADIFSLGITILELAcNLELPSGGD----GWHQLRQgYLPEEFTA--GLSPELRSIIKLMMDPD 235
                       250
                ....*....|....
gi 5031975  557 PAQRATAAELLKHP 570
Cdd:cd14050 236 PERRPTAEDLLALP 249
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
327-573 2.16e-31

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: 125.19  E-value: 2.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD----LRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05593  23 LGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTL-TESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRM-NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05593 102 LFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd05593 182 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI---LMEDIKFPRTLSADAKSLLSGLLIKDPNKRL 258
                       250
                ....*....|....*..
gi 5031975  562 -----TAAELLKHPFLA 573
Cdd:cd05593 259 gggpdDAKEIMRHSFFT 275
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
326-572 2.21e-31

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: 123.09  E-value: 2.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIAtVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHE-NVVEMYNsYLVGDE---LWVVMEFLE 399
Cdd:cd14131   8 QLGKGGSSKVYKV-LNPKKKIYALKRVDLEGadEQTLQSYKNEIELLKKLKGSdRIIQLYD-YEVTDEddyLYMVMECGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 ggalTDIVT--HTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLThDGRVKLSDFGFCAQVSKEVPR-- 471
Cdd:cd14131  86 ----IDLATilKKKrpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV-KGRLKLIDFGIAKAIQNDTTSiv 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKSLVGTPYWMAPELI----------SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP-PLKAMKMIRDNLP----PRLK 536
Cdd:cd14131 161 RDSQVGTLNYMSPEAIkdtsasgegkPKSKIGRPSDVWSLGCILYQMVYGKTPFQHITnPIAKLQAIIDPNHeiefPDIP 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031975  537 NlhkvsPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14131 241 N-----PDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
322-575 2.40e-31

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: 123.70  E-value: 2.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKIGE---GSTGIVCIATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd06615   1 DDFEKLGElgaGNGGVVTKVLHRPSGLIMARKLIHLEiKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALtDIVTHT--RMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKS 474
Cdd:cd06615  81 MDGGSL-DQVLKKagRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA--NS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGE---PP--------YFNEPP-------------------LKAM 524
Cdd:cd06615 158 FVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRypiPPpdakeleaMFGRPVsegeakeshrpvsghppdsPRPM 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  525 KM------IRDNLPPRLKNLHkVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06615 238 AIfelldyIVNEPPPKLPSGA-FSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRA 293
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
318-569 2.71e-31

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 122.60  E-value: 2.71e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  318 RSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDL--RKQQRrellfnEVVIMRDYQHENVVEMYNSYLVGDE----- 390
Cdd:cd14047   5 RQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLnnEKAER------EVKALAKLDHPNIVRYNGCWDGFDYdpets 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 -----------LWVVMEFLEGGALTDIVThtRMNEEQ-----IAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRV 454
Cdd:cd14047  79 ssnssrsktkcLFIQMEFCEKGTLESWIE--KRNGEKldkvlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  455 KLSDFGFCAQVSKEVPRRKSLvGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPplKAMKMIRD-NLPP 533
Cdd:cd14047 157 KIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKS--KFWTDLRNgILPD 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031975  534 rlkNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKH 569
Cdd:cd14047 234 ---IFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
327-572 2.78e-31

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: 122.41  E-value: 2.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRK---QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14162   8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKapeDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL----VGT 478
Cdd:cd14162  88 LDYIrKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGKPKLsetyCGS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEV-DIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDnlPPRLKNLHKVSPSLKGFLDRLLVRDP 557
Cdd:cd14162 168 YAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR--RVVFPKNPTVSEECKDLILRMLSPVK 245
                       250
                ....*....|....*
gi 5031975  558 AqRATAAELLKHPFL 572
Cdd:cd14162 246 K-RITIEEIKRDPWF 259
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
327-570 3.93e-31

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: 122.15  E-value: 3.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL------LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTRMNEEQIA-AVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG-RVKLSDFGFCAQVSKEVPR----RKS 474
Cdd:cd06630  88 GSVASLLSKYGAFSENVIiNYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTGagefQGQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-----RDNLPPRLKNLhkvSPSLKGFL 549
Cdd:cd06630 168 LLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkiasATTPPPIPEHL---SPGLRDVT 244
                       250       260
                ....*....|....*....|.
gi 5031975  550 DRLLVRDPAQRATAAELLKHP 570
Cdd:cd06630 245 LRCLELQPEDRPPARELLKHP 265
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
327-572 4.22e-31

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: 123.52  E-value: 4.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKqqrrellfnEVVIMRDYQHENVVE---------------MYNSYLVGDEL 391
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKA--LKK---------DVVLIDDDVECTMVEkrvlalawenpflthLYCTFQTKEHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALT-DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd05620  72 FFVMEFLNGGDLMfHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLP--PRLknlhkVSPSLKGF 548
Cdd:cd05620 152 RASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPhyPRW-----ITKESKDI 226
                       250       260
                ....*....|....*....|....*
gi 5031975  549 LDRLLVRDPAQR-ATAAELLKHPFL 572
Cdd:cd05620 227 LEKLFERDPTRRlGVVGNIRGHPFF 251
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
321-572 5.20e-31

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: 121.60  E-value: 5.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNF---IKIGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd14116   4 LEDFeigRPLGKGKFGNVYLAREKQSKFILALKvlfKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcaQVSKEVPRRK 473
Cdd:cd14116  84 LEYAPLGTVyRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGW--SVHAPSSRRT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY---FNEPPLKAMKMIRDNLPPRlknlhkVSPSLKGFLD 550
Cdd:cd14116 162 TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFeanTYQETYKRISRVEFTFPDF------VTEGARDLIS 235
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14116 236 RLLKHNPSQRPMLREVLEHPWI 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
327-573 7.12e-31

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: 122.77  E-value: 7.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKvlqkKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05603  83 LFFHLQRERCFLEPRARFYAAeVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTPEY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKMIRDNL---PPRLKNLHKVSPSLkgFLDRLLVRDPA 558
Cdd:cd05603 163 LAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYS----RDVSQMYDNIlhkPLHLPGGKTVAACD--LLQGLLHKDQR 236
                       250
                ....*....|....*....
gi 5031975  559 QRATAA----ELLKHPFLA 573
Cdd:cd05603 237 RRLGAKadflEIKNHVFFS 255
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
326-578 7.23e-31

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: 122.48  E-value: 7.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRELL----FNEVVIMRDYQHENVVEMyNSYLVGDEL---WVVMEFL 398
Cdd:cd07845  14 RIGEGTYGIVYRARDTTSGEIVALKK--VRMDNERDGIpissLREITLLLNLRHPNIVEL-KEVVVGKHLdsiFLVMEYC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EG--GALTDIVThTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 476
Cdd:cd07845  91 EQdlASLLDNMP-TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMTPKV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEP--------------------------PYFNEPPLKAMKMIR- 528
Cdd:cd07845 170 VTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPllpgkseieqldliiqllgtpnesiwPGFSDLPLVGKFTLPk 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  529 ---DNLPPRLknlHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPP 578
Cdd:cd07845 250 qpyNNLKHKF---PWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEKPLP 299
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
327-571 8.41e-31

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 122.50  E-value: 8.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKkmdlrkqqrreLLFNEVVIMRDYQHENVVE---------------MYNSYLVGDEL 391
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIK-----------ILKKDVIIQDDDVECTMVEkrvlalsgkppfltqLHSCFQTMDRL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd05587  73 YFVMEYVNGGDLMYHIQQVGKFKEPVAVFYAAeIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSL-KGFl 549
Cdd:cd05587 153 TTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSIcKGL- 231
                       250       260
                ....*....|....*....|....*..
gi 5031975  550 drlLVRDPAQR----ATAAELLK-HPF 571
Cdd:cd05587 232 ---LTKHPAKRlgcgPTGERDIKeHPF 255
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
321-572 8.46e-31

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 122.72  E-value: 8.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFI---KIGEGSTGIVCIATVRSSGKLVAVKKmdLRKqqrrellfnEVVIMRD---------------YQHENVVEMY 382
Cdd:cd05619   4 IEDFVlhkMLGKGSFGKVFLAELKGTNQFFAIKA--LKK---------DVVLMDDdvectmvekrvlslaWEHPFLTHLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  383 NSYLVGDELWVVMEFLEGGALT-DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF 461
Cdd:cd05619  73 CTFQTKENLFFVMEYLNGGDLMfHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  462 CAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLP--PRLknlh 539
Cdd:cd05619 153 CKENMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPfyPRW---- 228
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031975  540 kVSPSLKGFLDRLLVRDPAQR-ATAAELLKHPFL 572
Cdd:cd05619 229 -LEKEAKDILVKLFVREPERRlGVRGDIRQHPFF 261
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
327-572 9.64e-31

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: 120.74  E-value: 9.64e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14186   9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMvqrVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14186  89 SRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCGTPNY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMIRDNLPPRLknlhkvSPSLKGFLDRLLVRDPA 558
Cdd:cd14186 169 ISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTvknTLNKVVLADYEMPAFL------SREAQDLIHQLLRKNPA 242
                       250
                ....*....|....
gi 5031975  559 QRATAAELLKHPFL 572
Cdd:cd14186 243 DRLSLSSVLDHPFM 256
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
326-574 9.94e-31

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: 122.67  E-value: 9.94e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM-D-LRKQ---QRrelLFNEVVIMRDY-QHENVVEMYNSYLV--GDELWVVMEF 397
Cdd:cd07852  14 KLGKGAYGIVWKAIDKKTGEVVALKKIfDaFRNAtdaQR---TFREIMFLQELnDHPNIIKLLNVIRAenDKDIYLVFEY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LE--------GGALTDIvtHTRMNEEQIaavclavLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV 469
Cdd:cd07852  91 MEtdlhavirANILEDI--HKQYIMYQL-------LKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRRKSLVGTPY----WM-APE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPY-----FNE---------PPLK------- 522
Cdd:cd07852 162 EDDENPVLTDYvatrWYrAPEiLLGSTRYTKGVDMWSVGCILGEMLLGKPLFpgtstLNQlekiievigRPSAediesiq 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031975  523 ---AMKMIRDNLPPRLKNLH----KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd07852 242 spfAATMLESLPPSRPKSLDelfpKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
327-574 1.41e-30

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: 121.28  E-value: 1.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE---LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTH---TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkEVPRRKSLVGTPY 480
Cdd:cd05630  88 KFHIYHmgqAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVP-EGQTIKGRVGTVG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKMIRDNLPPRLKNLH-----KVSPSLKGFLDRLLVR 555
Cdd:cd05630 167 YMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQ----RKKKIKREEVERLVKEVPeeyseKFSPQARSLCSMLLCK 242
                       250       260
                ....*....|....*....|....
gi 5031975  556 DPAQR-----ATAAELLKHPFLAK 574
Cdd:cd05630 243 DPAERlgcrgGGAREVKEHPLFKK 266
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
326-572 1.41e-30

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: 120.88  E-value: 1.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVA---VKKMDLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14195  12 ELGSGQFAIVRKCREKGTGKEYAakfIKKRRLSSSRRgvsREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL----THDGRVKLSDFGFCAQVsKEVPRRKS 474
Cdd:cd14195  92 GGELFDFLAEKEsLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKI-EAGNEFKN 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14195 171 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAvNYDFDEEYFSNTSELAKDFIRRLL 250
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14195 251 VKDPKKRMTIAQSLEHSWI 269
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
327-573 1.51e-30

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: 121.74  E-value: 1.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIA---TVRSSGKLVAVK-----KMDLRKQQRRELlfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05582   3 LGQGSFGKVFLVrkiTGPDAGTLYAMKvlkkaTLKVRDRVRTKM---ERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTRMNEEQIAAVCLAVLQ-ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG 477
Cdd:cd05582  80 RGGDLFTRLSKEVMFTEEDVKFYLAELAlALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDP 557
Cdd:cd05582 160 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMI---LKAKLGMPQFLSPEAQSLLRALFKRNP 236
                       250       260
                ....*....|....*....|.
gi 5031975  558 AQRATAA-----ELLKHPFLA 573
Cdd:cd05582 237 ANRLGAGpdgveEIKRHPFFA 257
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
326-572 1.80e-30

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: 120.28  E-value: 1.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVA---VKKMDLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14105  12 ELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRgvsREDIEREVSILRQVLHPNIITLHDVFENKTDVVLILELVA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFcAQVSKEVPRRKS 474
Cdd:cd14105  92 GGELFDFLAEKEsLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGL-AHKIEDGNEFKN 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14105 171 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItAVNYDFDDEYFSNTSELAKDFIRQLL 250
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14105 251 VKDPRKRMTIQESLRHPWI 269
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
327-572 1.84e-30

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: 122.05  E-value: 1.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREllfnEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14176  27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 -IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEvprrKSLVGTPY 480
Cdd:cd14176 103 kILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAE----NGLLMTPC 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 W----MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMI---RDNLPPRLKNlhKVSPSLKGFLD 550
Cdd:cd14176 179 YtanfVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIgsgKFSLSGGYWN--SVSDTAKDLVS 256
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14176 257 KMLHVDPHQRLTAALVLRHPWI 278
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
327-573 2.14e-30

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: 120.89  E-value: 2.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfneVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 405
Cdd:cd14177  12 IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEI---EILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDr 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEvprrKSLVGTPYW 481
Cdd:cd14177  89 ILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGE----NGLLLTPCY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 ----MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14177 165 tanfVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPndtPEEILLRIGSgKFSLSGGNWDTVSDAAKDLLSHML 244
                       250       260
                ....*....|....*....|
gi 5031975  554 VRDPAQRATAAELLKHPFLA 573
Cdd:cd14177 245 HVDPHQRYTAEQVLKHSWIA 264
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
327-573 2.22e-30

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: 121.31  E-value: 2.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKQ---QRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05571   3 LGKGTFGKVILCREKATGELYAIKI--LKKEviiAKDEVahTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd05571  81 ELFFHLSRERVFSEDRTRFYGAeIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP-----PLKAMKMIRdnLPPRLknlhkvSPSLKGFLDRLLVR 555
Cdd:cd05571 161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDhevlfELILMEEVR--FPSTL------SPEAKSLLAGLLKK 232
                       250       260
                ....*....|....*....|...
gi 5031975  556 DPAQR-----ATAAELLKHPFLA 573
Cdd:cd05571 233 DPKKRlgggpRDAKEIMEHPFFA 255
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
327-573 2.44e-30

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: 121.53  E-value: 2.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM-------DLRKQQRRELlfnevVIMRDYQHENVVEMYNSYLVGDE-LWVVMEFL 398
Cdd:cd07856  18 VGMGAFGLVCSARDQLTGQNVAVKKImkpfstpVLAKRTYREL-----KLLKHLRHENIISLSDIFISPLEdIYFVTELL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 eGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKevPRRKSLVGT 478
Cdd:cd07856  93 -GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGL-ARIQD--PQMTGYVST 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPY---------------FNEPPLKAMKMIR--------DNLPPR 534
Cdd:cd07856 169 RYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitelLGTPPDDVINTICsentlrfvQSLPKR 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031975  535 LK-----NLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd07856 249 ERvpfseKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLA 292
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
326-571 3.45e-30

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: 120.02  E-value: 3.45e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ--------RrellfnEVVIMRDYQHENVVEMyNSYLVG---DELWVV 394
Cdd:cd07843  12 RIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKegfpitslR------EINILLKLQHPNIVTV-KEVVVGsnlDKIYMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGgALTDIVTHtrMNEE----QIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkeVP 470
Cdd:cd07843  85 MEYVEH-DLKSLMET--MKQPflqsEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYG--SP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRK--SLVGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEP--------------------------PYFNEPPL 521
Cdd:cd07843 160 LKPytQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPlfpgkseidqlnkifkllgtptekiwPGFSELPG 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  522 -KAMKMIR---DNLPPRLKNLhkvSPSLKGF--LDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07843 240 aKKKTFTKypyNQLRKKFPAL---SLSDNGFdlLNRLLTYDPAKRISAEDALKHPY 292
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
327-570 3.90e-30

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: 118.90  E-value: 3.90e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIV-----CIATVRssgklVAVKKMDLRKQQR----RELLFNEVVIMRDYQHENVVEMYNsYLVGDE---LWVV 394
Cdd:cd14119   1 LGEGSYGKVkevldTETLCR-----RAVKILKKRKLRRipngEANVKREIQILRRLNHRNVIKLVD-VLYNEEkqkLYMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALT--DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP-- 470
Cdd:cd14119  75 MEYCVGGLQEmlDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAEdd 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPY--GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDN---LPPrlknlhKVSPSL 545
Cdd:cd14119 155 TCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGeytIPD------DVDPDL 228
                       250       260
                ....*....|....*....|....*
gi 5031975  546 KGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14119 229 QDLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
327-585 4.29e-30

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: 120.48  E-value: 4.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIV--CIAtvRSSGKLVAVKKMDLRKQQRREllfneVVIMRDYQ-HENVVEMYNSYlvGDEL--WVVMEFLEGG 401
Cdd:cd14092  14 LGDGSFSVCrkCVH--KKTGQEFAVKIVSRRLDTSRE-----VQLLRLCQgHPNIVKLHEVF--QDELhtYLVMELLRGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG---RVKLSDFGFcAQVSKEVPRRKSLVG 477
Cdd:cd14092  85 ELLErIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGF-ARLKPENQPLKTPCF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPE----VDIWSLGIMVIEMVDGEPPY----FNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGF 548
Cdd:cd14092 164 TLPYAAPEVLKQALSTQGydesCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSgDFSFDGEEWKNVSSEAKSL 243
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFLAKAGPPASiVPLM 585
Cdd:cd14092 244 IQGLLTVDPSKRLTMSELRNHPWLQGSSSPSS-TPLM 279
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
327-572 4.72e-30

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 119.33  E-value: 4.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE-LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14183  14 IGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT--HDGR--VKLSDFGFCAQVSKEVprrKSLVGTPY 480
Cdd:cd14183  94 AITSTnKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYehQDGSksLKLGDFGLATVVDGPL---YTVCGTPT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF-----NEPPLKAMKMIRDNLP-PRLKNlhkVSPSLKGFLDRLLV 554
Cdd:cd14183 171 YVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRgsgddQEVLFDQILMGQVDFPsPYWDN---VSDSAKELITMMLQ 247
                       250
                ....*....|....*...
gi 5031975  555 RDPAQRATAAELLKHPFL 572
Cdd:cd14183 248 VDVDQRYSALQVLEHPWV 265
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
321-572 4.89e-30

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 118.97  E-value: 4.89e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFIKIGE----GSTGIVCIATVRSSGKLVAVKKMDLRKQQR------RELLFNEVVIMRDYQHENVVEMYNSYLVGDE 390
Cdd:cd14194   3 VDDYYDTGEelgsGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsREDIEREVSILKEIQHPNVITLHEVYENKTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQV 465
Cdd:cd14194  83 VILILELVAGGELFDFLAEKEsLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SKEvPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPS 544
Cdd:cd14194 163 DFG-NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAvNYEFEDEYFSNTSAL 241
                       250       260
                ....*....|....*....|....*...
gi 5031975  545 LKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14194 242 AKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
326-574 6.52e-30

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: 120.55  E-value: 6.52e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM----DLRKQQRRELlfNEVVIMRDYQHENVVEMYN------SYLVGDELWVVM 395
Cdd:cd07855  12 TIGSGAYGVVCSAIDTKSGQKVAIKKIpnafDVVTTAKRTL--RELKILRHFKHDNIIAIRDilrpkvPYADFKDVYVVL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL 475
Cdd:cd07855  90 DLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHKYF 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 ----VGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVdGEPPYF----------------NEPPLKAMKMIR------ 528
Cdd:cd07855 170 mteyVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEML-GRRQLFpgknyvhqlqliltvlGTPSQAVINAIGadrvrr 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  529 --DNLPPR-LKNLHKVSPS----LKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd07855 249 yiQNLPNKqPVPWETLYPKadqqALDLLSQMLRFDPSERITVAEALQHPFLAK 301
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
327-574 6.61e-30

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: 119.17  E-value: 6.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDkkrIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMNEEQIAAVCLAVLQ---ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSlVGTPY 480
Cdd:cd05577  81 KYHIYNVGTRGFSEARAIFYAAEiicGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGR-VGTHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPRLKNLHKVSPSLKGFLDRLLVRDPA 558
Cdd:cd05577 160 YMAPEvLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELkRRTLEMAVEYPDSFSPEARSLCEGLLQKDPE 239
                       250       260
                ....*....|....*....|.
gi 5031975  559 QR-----ATAAELLKHPFLAK 574
Cdd:cd05577 240 RRlgcrgGSADEVKEHPFFRS 260
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
323-573 6.93e-30

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: 120.51  E-value: 6.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIK-IGEGSTGIVCIATVRSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd05602  10 HFLKvIGKGSFGKVLLARHKSDEKFYAVKvlqkKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 476
Cdd:cd05602  90 INGGELFYHLQRERCFLEPRARFYAAeIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTSTFC 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPRLKNlhKVSPSLKGFLDRLLVRD 556
Cdd:cd05602 170 GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNIL-NKPLQLKP--NITNSARHLLEGLLQKD 246
                       250       260
                ....*....|....*....|.
gi 5031975  557 PAQRATAA----ELLKHPFLA 573
Cdd:cd05602 247 RTKRLGAKddftEIKNHIFFS 267
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
326-570 7.69e-30

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: 118.11  E-value: 7.69e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRRELLFN-------EVVIMR---DYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd14005   7 LLGKGGFGTVYSGVRIRDGLPVAVKFVP-KSRVTEWAMINgpvpvplEIALLLkasKPGVPGVIRLLDWYERPDGFLLIM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGA-LTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD-GRVKLSDFGfCAQVSKEVPRR 472
Cdd:cd14005  86 ERPEPCQdLFDFITERgALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFG-CGALLKDSVYT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KsLVGTPYWMAPELIS-RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEpplkaMKMIRDNL--PPRLknlhkvSPSLKGFL 549
Cdd:cd14005 165 D-FDGTRVYSPPEWIRhGRYHGRPATVWSLGILLYDMLCGDIPFEND-----EQILRGNVlfRPRL------SKECCDLI 232
                       250       260
                ....*....|....*....|.
gi 5031975  550 DRLLVRDPAQRATAAELLKHP 570
Cdd:cd14005 233 SRCLQFDPSKRPSLEQILSHP 253
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
327-571 8.52e-30

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: 119.80  E-value: 8.52e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKqqrrellfnEVVIMRD---------------YQHENVVEMYNSYLVGDEL 391
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKA--LKK---------DVVLEDDdvectmierrvlalaSQHPFLTHLFCTFQTESHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALT-DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA-QVSKEV 469
Cdd:cd05592  72 FFVMEYLNGGDLMfHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKeNIYGEN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 pRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLP--PRLknlhkVSPSLKG 547
Cdd:cd05592 152 -KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPhyPRW-----LTKEAAS 225
                       250       260
                ....*....|....*....|....*....
gi 5031975  548 FLDRLLVRDPAQR-----ATAAELLKHPF 571
Cdd:cd05592 226 CLSLLLERNPEKRlgvpeCPAGDIRDHPF 254
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
327-571 9.68e-30

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 117.75  E-value: 9.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 405
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDy 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSKEVpRRKSLVGTPYWM 482
Cdd:cd14115  80 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHR-HVHHLLGNPEFA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRA 561
Cdd:cd14115 159 APEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETcINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRP 238
                       250
                ....*....|
gi 5031975  562 TAAELLKHPF 571
Cdd:cd14115 239 TAATCLQHPW 248
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
327-572 9.71e-30

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: 119.31  E-value: 9.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE---LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkEVPRRKSLVGTPY 480
Cdd:cd05632  90 KFHIYNMGnpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIP-EGESIRGRVGTVG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKMIRDNLPPRLKNLH-----KVSPSLKGFLDRLLVR 555
Cdd:cd05632 169 YMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRG----RKEKVKREEVDRRVLETEevysaKFSEEAKSICKMLLTK 244
                       250       260
                ....*....|....*....|..
gi 5031975  556 DPAQR-----ATAAELLKHPFL 572
Cdd:cd05632 245 DPKQRlgcqeEGAGEVKRHPFF 266
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
327-572 1.23e-29

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: 118.59  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIV--CIATVRSsgKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGA- 402
Cdd:cd14173  10 LGEGAYARVqtCINLITN--KEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSi 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDF---------GFCAQVSkeVP 470
Cdd:cd14173  88 LSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFdlgsgiklnSDCSPIS--TP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLP-----YGPEVDIWSLGIMVIEMVDGEPPYF-----------NEPPLKAMKMIRDNLP-- 532
Cdd:cd14173 166 ELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVgrcgsdcgwdrGEACPACQNMLFESIQeg 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5031975  533 ----PRlKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14173 246 kyefPE-KDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
327-574 1.26e-29

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: 119.34  E-value: 1.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05601   9 IGRGHFGEVQVVKEKATGDIYAMKVLkksETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVT-HTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS--KEVpRRKSLVGTP 479
Cdd:cd05601  89 LSLLSrYDDIFEESMARFYLAELvLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSsdKTV-TSKMPVGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRL------PYGPEVDIWSLGIMVIEMVDGEPPyFNEPplkAMKMIRDNLPPRLKNLH-----KVSPSLKGF 548
Cdd:cd05601 168 DYIAPEVLTSMnggskgTYGVECDWWSLGIVAYEMLYGKTP-FTED---TVIKTYSNIMNFKKFLKfpedpKVSESAVDL 243
                       250       260
                ....*....|....*....|....*.
gi 5031975  549 LDRLLVrDPAQRATAAELLKHPFLAK 574
Cdd:cd05601 244 IKGLLT-DAKERLGYEGLCCHPFFSG 268
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
327-571 1.35e-29

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: 118.28  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD-----LRKQqrRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05609   8 ISNGAYGAVYLVRHRETRQRFAMKKINkqnliLRNQ--IQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHTRMNEEQIAAVCLA--VLqALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC-------------AQVS 466
Cdd:cd05609  86 DCATLLKNIGPLPVDMARMYFAetVL-ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglmslttnlyeGHIE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVPR--RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDN---------LPPR 534
Cdd:cd05609 165 KDTREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFgQVISDEiewpegddaLPDD 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5031975  535 LKNLhkvspslkgfLDRLLVRDPAQR---ATAAELLKHPF 571
Cdd:cd05609 245 AQDL----------ITRLLQQNPLERlgtGGAEEVKQHPF 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
320-569 1.35e-29

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: 118.24  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKI---GEGSTGIVCIATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd14046   4 YLTDFEELqvlGKGAFGQVVKVRNKLDGRYYAIKKIKLRsESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTRMNE-EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG-----------FCA 463
Cdd:cd14046  84 EYCEKSTLRDLIDSGLFQDtDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlatsnklnvelATQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 QVSKEVPRRK-------SLVGTPYWMAPELISRLP--YGPEVDIWSLGIMVIEMVdgeppyfnEPP---------LKAMK 525
Cdd:cd14046 164 DINKSTSAALgssgdltGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC--------YPFstgmervqiLTALR 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031975  526 MIRDNLPPR-LKNLHKVSPSLkgfLDRLLVRDPAQRATAAELLKH 569
Cdd:cd14046 236 SVSIEFPPDfDDNKHSKQAKL---IRWLLNHDPAKRPSAQELLKS 277
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
327-567 1.85e-29

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 117.00  E-value: 1.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd08219   8 VGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAvEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTR---MNEEQI----AAVCLAVLQalsvLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT 478
Cdd:cd08219  88 KIKLQRgklFPEDTIlqwfVQMCLGVQH----IHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTYVGT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY----FNEPPLKAMKMIRDNLPPRLknlhkvSPSLKGFLDRLLV 554
Cdd:cd08219 164 PYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFqansWKNLILKVCQGSYKPLPSHY------SYELRSLIKQMFK 237
                       250
                ....*....|...
gi 5031975  555 RDPAQRATAAELL 567
Cdd:cd08219 238 RNPRSRPSATTIL 250
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
327-568 2.19e-29

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: 116.77  E-value: 2.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSsgKLVAVKKMDLrkQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDi 406
Cdd:cd14058   1 VGRGSFGVVCKARWRN--QIVAVKIIES--ESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAV-----CLAVLQALSVLHA---QGVIHRDIKSDSILLTHDGRV-KLSDFGFCAQVSKEVPRRKslvG 477
Cdd:cd14058  76 VLHGKEPKPIYTAAhamswALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDISTHMTNNK---G 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPLKAMKMI-RDNLPPRLKNLHKVspsLKGFLDRLLV 554
Cdd:cd14058 153 SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFdhIGGPAFRIMWAVhNGERPPLIKNCPKP---IESLMTRCWS 229
                       250
                ....*....|....
gi 5031975  555 RDPAQRATAAELLK 568
Cdd:cd14058 230 KDPEKRPSMKEIVK 243
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
326-572 2.23e-29

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: 117.34  E-value: 2.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14197  16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRkgQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFcAQVSKEVPRRKSLV 476
Cdd:cd14197  96 IFNQCVADReeaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGL-SRILKNSEELREIM 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLLVR 555
Cdd:cd14197 175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQmNVSYSEEEFEHLSESAIDFIKTLLIK 254
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd14197 255 KPENRATAEDCLKHPWL 271
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
326-572 2.45e-29

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: 116.75  E-value: 2.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSS---GKLVAVKKMDLRKQQRRELL--FNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd08222   7 KLGSGNFGTVYLVSDLKAtadEELKVLKEISVGELQPDETVdaNREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTRMN-----EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLtHDGRVKLSDFGFCAQVSKEVPRRKSL 475
Cdd:cd08222  87 GDLDDKISEYKKSgttidENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMGTSDLATTF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNlhKVSPSLKGFLDRLLVR 555
Cdd:cd08222 166 TGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSLPD--KYSKELNAIYSRMLNK 243
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd08222 244 DPALRPSAAEILKIPFI 260
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
327-572 2.52e-29

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 116.99  E-value: 2.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFDR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAVCLA--VLQALSVLHAQGVIHRDIKSDSIL-LTHDG-RVKLSDFGFcaqVSKEVPRRKSLV--GTPY 480
Cdd:cd14192  92 ITDESYQLTELDAILFTrqICEGVHYLHQHYILHLDLKPENILcVNSTGnQIKIIDFGL---ARRYKPREKLKVnfGTPE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd14192 169 FLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNcKWDFDAEAFENLSEEAKDFISRLLVKEKSC 248
                       250
                ....*....|...
gi 5031975  560 RATAAELLKHPFL 572
Cdd:cd14192 249 RMSATQCLKHEWL 261
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
317-579 2.53e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 119.16  E-value: 2.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKM------DLRKQQRREllfneVVIMRDYQHENVVEMYNSYLVGDE 390
Cdd:PLN00034  72 SLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygnhedTVRRQICRE-----IEILRDVNHPNVVKCHDMFDHNGE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   391 LWVVMEFLEGGALTDivthTRMNEE-QIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV 469
Cdd:PLN00034 147 IQVLLEFMDGGSLEG----THIADEqFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   470 PRRKSLVGTPYWMAPELISR-----LPYGPEVDIWSLGIMVIEMVDGEPPY----------------FNEPPlkamkmir 528
Cdd:PLN00034 223 DPCNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYLGRFPFgvgrqgdwaslmcaicMSQPP-------- 294
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 5031975   529 dnLPPRlknlhKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPA 579
Cdd:PLN00034 295 --EAPA-----TASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQ 338
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
327-573 3.17e-29

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: 118.98  E-value: 3.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVA---VKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05594  33 LGKGTFGKVILVKEKATGRYYAmkiLKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd05594 113 FFHLSRERVFSEDRARFYGAeIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEY 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDPAQR- 560
Cdd:cd05594 193 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI---LMEEIRFPRTLSPEAKSLLSGLLKKDPKQRl 269
                       250
                ....*....|....*..
gi 5031975  561 ----ATAAELLKHPFLA 573
Cdd:cd05594 270 gggpDDAKEIMQHKFFA 286
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
312-572 3.20e-29

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: 116.57  E-value: 3.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  312 VDPGDPRSYLDNFIkIGEGSTGIVCIATVRSSGKLVA---VKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVG 388
Cdd:cd14187   1 VDPRTRRRYVRGRF-LGKGGFAKCYEITDADTKEVFAgkiVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  389 DELWVVMEFLEGGALTDIvtHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 465
Cdd:cd14187  80 DFVYVVLELCRRRSLLEL--HKRrkaLTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMKM-IRDNLPPRLKNLHKVSPS 544
Cdd:cd14187 158 EYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPP-FETSCLKETYLrIKKNEYSIPKHINPVAAS 236
                       250       260
                ....*....|....*....|....*...
gi 5031975  545 LkgfLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14187 237 L---IQKMLQTDPTARPTINELLNDEFF 261
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
323-571 3.35e-29

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 116.24  E-value: 3.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIK-IGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14665   3 ELVKdIGSGNFGVARLMRDKQTKELVAVKYIE-RGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLthDG----RVKLSDFGFcAQVSKEVPRRKSLV 476
Cdd:cd14665  82 ELFErICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL--DGspapRLKICDFGY-SKSSVLHSQPKSTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPyFNEP--PLKAMKMIRDNLPPR--LKNLHKVSPSLKGFLDR 551
Cdd:cd14665 159 GTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYP-FEDPeePRNFRKTIQRILSVQysIPDYVHISPECRHLISR 237
                       250       260
                ....*....|....*....|
gi 5031975  552 LLVRDPAQRATAAELLKHPF 571
Cdd:cd14665 238 IFVADPATRITIPEIRNHEW 257
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
326-572 3.38e-29

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: 116.59  E-value: 3.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR------RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14196  12 ELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEVpRRKS 474
Cdd:cd14196  92 GGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV-EFKN 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14196 171 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvSYDFDEEFFSHTSELAKDFIRKLL 250
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14196 251 VKETRKRLTIQEALRHPWI 269
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
327-569 3.81e-29

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: 116.21  E-value: 3.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATvRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14161  11 LGKGTYGRVKKAR-DSSGRLVAIKsirKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYWM 482
Cdd:cd14161  90 YDYISERqRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL-SNLYNQDKFLQTYCGSPLYA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL---PPRLKNLHkvspslkGFLDRLLVRDPA 558
Cdd:cd14161 169 SPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAyrePTKPSDAC-------GLIRWLLMVNPE 241
                       250
                ....*....|.
gi 5031975  559 QRATAAELLKH 569
Cdd:cd14161 242 RRATLEDVASH 252
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
327-574 4.78e-29

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: 117.29  E-value: 4.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMdlRKQQ---RREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTI--RKAHivsRSEVthTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 AL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd05585  80 ELfHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQR 560
Cdd:cd05585 160 YLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDE---NTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKR 236
                       250
                ....*....|....*..
gi 5031975  561 ---ATAAELLKHPFLAK 574
Cdd:cd05585 237 lgyNGAQEIKNHPFFDQ 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
326-572 5.88e-29

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: 115.68  E-value: 5.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREL----LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14070   9 KLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYvtknLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF--CAQVSKEVPRRKSLVGT 478
Cdd:cd14070  89 NLMHrIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSDPFSTQCGS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP-PLKAM--KMIRDNLPPRLKNLhkvSPSLKGFLDRLLVR 555
Cdd:cd14070 169 PAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALhqKMVDKEMNPLPTDL---SPGAISFLRSLLEP 245
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd14070 246 DPLKRPNIKQALANRWL 262
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
327-571 9.72e-29

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 115.25  E-value: 9.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 405
Cdd:cd14662   8 IGSGNFGVARLMRNKETKELVAVKYIE-RGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELFEr 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLthDG----RVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14662  87 ICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL--DGspapRLKICDFGY-SKSSVLHSQPKSTVGTPAY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPyFNEPplKAMKMIRDNLpPRLKNLH-------KVSPSLKGFLDRLL 553
Cdd:cd14662 164 IAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYP-FEDP--DDPKNFRKTI-QRIMSVQykipdyvRVSQDCRHLLSRIF 239
                       250
                ....*....|....*...
gi 5031975  554 VRDPAQRATAAELLKHPF 571
Cdd:cd14662 240 VANPAKRITIPEIKNHPW 257
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
327-572 9.77e-29

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: 115.06  E-value: 9.77e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMR------DYQHENVVEMYNSYLVGDELWVVMEFLEg 400
Cdd:cd14133   7 LGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSL-DEIRLLEllnkkdKADKYHIVRLKDVFYFKNHLCIVFELLS- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 galTDIVTHTRMNEEQ------IAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSKevpRR 472
Cdd:cd14133  85 ---QNLYEFLKQNKFQylslprIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRcqIKIIDFGSSCFLTQ---RL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL---PPRLKNLHKVS-PSLKGF 548
Cdd:cd14133 159 YSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIgipPAHMLDQGKADdELFVDF 238
                       250       260
                ....*....|....*....|....
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14133 239 LKKLLEIDPKERPTASQALSHPWL 262
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
327-570 1.18e-28

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: 115.48  E-value: 1.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE---LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGal 403
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGG-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 tDIVTHTR------MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkEVPRRKSLVG 477
Cdd:cd05631  86 -DLKFHIYnmgnpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIP-EGETVRGRVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplKAMKMIRDNLPPRLKN-----LHKVSPSLKGFLDRL 552
Cdd:cd05631 164 TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRK----RKERVKREEVDRRVKEdqeeySEKFSEDAKSICRML 239
                       250       260
                ....*....|....*....|...
gi 5031975  553 LVRDPAQR-----ATAAELLKHP 570
Cdd:cd05631 240 LTKNPKERlgcrgNGAAGVKQHP 262
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
323-560 1.19e-28

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: 116.64  E-value: 1.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIKI-GEGSTGIVCIATVRSSGKLVAVKkmdlrkqqrreLLFNEVVIMRDYQHENVVE---------------MYNSYL 386
Cdd:cd05616   3 NFLMVlGKGSFGKVMLAERKGTDELYAVK-----------ILKKDVVIQDDDVECTMVEkrvlalsgkppfltqLHSCFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  387 VGDELWVVMEFLEGGALT-DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 465
Cdd:cd05616  72 TMDRLYFVMEYVNGGDLMyHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSL 545
Cdd:cd05616 152 IWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAI 231
                       250
                ....*....|....*.
gi 5031975  546 -KGfldrLLVRDPAQR 560
Cdd:cd05616 232 cKG----LMTKHPGKR 243
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
326-572 1.42e-28

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 115.45  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR--------------------------ELLFNEVVIMRDYQHENVV 379
Cdd:cd14199   9 EIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQagfprrppprgaraapegctqprgpiERVYQEIAILKKLDHPNVV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSY--LVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLS 457
Cdd:cd14199  89 KLVEVLddPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  458 DFGFCAQVSKEVPRRKSLVGTPYWMAPELIS---RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPR 534
Cdd:cd14199 169 DFGVSNEFEGSDALLTNTVGTPAFMAPETLSetrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIK-TQPLE 247
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  535 LKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14199 248 FPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
327-571 1.65e-28

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: 114.79  E-value: 1.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL-----RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLE 399
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGRELAAKQVQFdpespETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ---VSKEVPRRKSL 475
Cdd:cd06651  95 GGSVKDqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSGTGIRSV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNLPPRLKNlhKVSPSLKGFLDRLLV 554
Cdd:cd06651 175 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIfKIATQPTNPQLPS--HISEHARDFLGCIFV 252
                       250
                ....*....|....*..
gi 5031975  555 rDPAQRATAAELLKHPF 571
Cdd:cd06651 253 -EARHRPSAEELLRHPF 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
327-568 1.68e-28

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: 114.79  E-value: 1.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMDLRKQQR--RELLFNEVVIMRdYQHENVV--------EMYNSYLVgdelwVVME 396
Cdd:cd13979  11 LGSGGFGSVYKATYK--GETVAVKIVRRRRKNRasRQSFWAELNAAR-LRHENIVrvlaaetgTDFASLGL-----IIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRmnEEQIAAVCL----AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfCAQVSKEV--- 469
Cdd:cd13979  83 YCGNGTLQQLIYEGS--EPLPLAHRIlislDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG-CSVKLGEGnev 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 -PRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSP--SLK 546
Cdd:cd13979 160 gTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDSEFgqRLR 239
                       250       260
                ....*....|....*....|...
gi 5031975  547 GFLDRLLVRDPAQRATA-AELLK 568
Cdd:cd13979 240 SLISRCWSAQPAERPNAdESLLK 262
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
321-560 2.16e-28

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: 114.35  E-value: 2.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFI---KIGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd08228   1 LANFQiekKIGRGQFSEVYRATCLLDRKPVALKKVqifEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV 469
Cdd:cd08228  81 LELADAGDLSQMIKYFKkqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPP--LKAMKMIRDNLPPRLKNLHkVSPSLKG 547
Cdd:cd08228 161 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMnlFSLCQKIEQCDYPPLPTEH-YSEKLRE 239
                       250
                ....*....|...
gi 5031975  548 FLDRLLVRDPAQR 560
Cdd:cd08228 240 LVSMCIYPDPDQR 252
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
327-570 2.52e-28

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: 114.71  E-value: 2.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM--DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd07848   9 VGEGAYGVVLKCRHKETKEIVAIKKFkdSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV-PRRKSLVGTPYWM 482
Cdd:cd07848  89 LLEEMpNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSnANYTEYVATRWYR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---------------PLKAMKMIRDNlpPRLKNLHKVSPSLKG 547
Cdd:cd07848 169 SPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESeidqlftiqkvlgplPAEQMKLFYSN--PRFHGLRFPAVNHPQ 246
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 5031975  548 FLDR----------------LLVRDPAQRATAAELLKHP 570
Cdd:cd07848 247 SLERrylgilsgvlldlmknLLKLNPTDRYLTEQCLNHP 285
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
327-571 2.88e-28

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: 114.43  E-value: 2.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGA-LT 404
Cdd:cd14090  10 LGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRGGPlLS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFG------FCAQVSKEV--PRRK 473
Cdd:cd14090  90 HIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDlgsgikLSSTSMTPVttPELL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELI-----SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK-------AMKMIRDNLPPRL------ 535
Cdd:cd14090 170 TPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeACQDCQELLFHSIqegeye 249
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 5031975  536 ---KNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14090 250 fpeKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
323-518 2.95e-28

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: 115.94  E-value: 2.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIK-IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05596  29 DVIKvIGRGAFGEVQLVRHKSTKKVYAMKllsKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYM 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE-VPRRKSLVG 477
Cdd:cd05596 109 PGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDgLVRSDTAVG 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031975  478 TPYWMAPELISRLP----YGPEVDIWSLGIMVIEMVDGEPPYFNE 518
Cdd:cd05596 189 TPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYAD 233
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
327-562 3.42e-28

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: 114.47  E-value: 3.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLR---KQQRRELLFNEVVIMRDYQHENVVemyNSYLVGDELWVV--------- 394
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQElspSDKNRERWCLEVQIMKKLNHPNVV---SARDVPPELEKLspndlplla 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH-DGRV--KLSDFGFCAQVSK 467
Cdd:cd13989  78 MEYCSGGDLRKVLNQPEnccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgGGRViyKLIDLGYAKELDQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EvPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF-NEPPLKAMKMIRDNLP-------------- 532
Cdd:cd13989 158 G-SLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLpNWQPVQWHGKVKQKKPehicayedltgevk 236
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031975  533 --PRLKNLHKVSPSLKGFLDR----LLVRDPAQRAT 562
Cdd:cd13989 237 fsSELPSPNHLSSILKEYLESwlqlMLRWDPRQRGG 272
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
311-572 4.16e-28

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 117.81  E-value: 4.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   311 VVDPGDPRSYLDNFIKI-GEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLF-NEVVIMRDYQHENVVEMYNSYLVG 388
Cdd:PTZ00267  58 VPESNNPREHMYVLTTLvGRNPTTAAFVATRGSDPKEKVVAKFVMLNDERQAAYArSELHCLAACDHFGIVKHFDDFKSD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   389 DELWVVMEFLEGGALTDIVT-----HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA 463
Cdd:PTZ00267 138 DKLLLIMEYGSGGDLNKQIKqrlkeHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSK 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   464 QVSKEVPRR--KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI----RDNLPPrlkn 537
Cdd:PTZ00267 218 QYSDSVSLDvaSSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVlygkYDPFPC---- 293
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 5031975   538 lhKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:PTZ00267 294 --PVSSGMKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
314-572 6.95e-28

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 112.61  E-value: 6.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  314 PGDPRSYLDnfiKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWV 393
Cdd:cd14111   1 PQKPYTFLD---EKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVL-QEYEILKSLHHERIMALHEAYITPRYLVL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGA-LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----FCAQVSKE 468
Cdd:cd14111  77 IAEFCSGKElLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGsaqsFNPLSLRQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRkslVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGF 548
Cdd:cd14111 157 LGRR---TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKLYPNVSQSASLF 233
                       250       260
                ....*....|....*....|....
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14111 234 LKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
327-515 7.41e-28

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: 111.82  E-value: 7.41e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMdlrkqqrRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14059   1 LGSGAQGAVFLGKFR--GEEVAVKKV-------RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkEVPRRKSLVGTPYWMAPE 485
Cdd:cd14059  72 LRAGReITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELS-EKSTKMSFAGTVAWMAPE 150
                       170       180       190
                ....*....|....*....|....*....|
gi 5031975  486 LISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14059 151 VIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
324-573 7.48e-28

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: 115.49  E-value: 7.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  324 FIKI---GEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd05626   3 FVKIktlGIGAFGEVCLACKVDTHALYAMKtlrKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHTRMNEEQIAAVCLAVLQ-ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA------------- 463
Cdd:cd05626  83 IPGGDMMSLLIRMEVFPEVLARFYIAELTlAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyqk 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 -------------------------------QVSKEVPRR---KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV 509
Cdd:cd05626 163 gshirqdsmepsdlwddvsncrcgdrlktleQRATKQHQRclaHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEML 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975  510 DGEPPYFNEPPLKA-MKMIR----DNLPPRLknlhKVSPSLKGFLDRLL--VRDPAQRATAAELLKHPFLA 573
Cdd:cd05626 243 VGQPPFLAPTPTETqLKVINwentLHIPPQV----KLSPEAVDLITKLCcsAEERLGRNGADDIKAHPFFS 309
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
323-560 7.94e-28

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: 114.71  E-value: 7.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIKI-GEGSTGIVCIATVRSSGKLVAVKkmdlrkqqrreLLFNEVVIMRDYQHENVVE---------------MYNSYL 386
Cdd:cd05615  13 NFLMVlGKGSFGKVMLAERKGSDELYAIK-----------ILKKDVVIQDDDVECTMVEkrvlalqdkppfltqLHSCFQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  387 VGDELWVVMEFLEGGaltDIVTHT----RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC 462
Cdd:cd05615  82 TVDRLYFVMEYVNGG---DLMYHIqqvgKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  463 AQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVS 542
Cdd:cd05615 159 KEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEA 238
                       250
                ....*....|....*....
gi 5031975  543 PSL-KGfldrLLVRDPAQR 560
Cdd:cd05615 239 VSIcKG----LMTKHPAKR 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
327-572 8.90e-28

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: 113.14  E-value: 8.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMdlRKQQRRELL----FNEVVIMRD---YQHENVVEMYNSYLVGD-----ELWVV 394
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKV--RVPLSEEGIplstIREIALLKQlesFEHPNVVRLLDVCHGPRtdrelKLTLV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEggalTDIVTHTR------MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKE 468
Cdd:cd07838  85 FEHVD----QDLATYLDkcpkpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGL-ARIYSF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMvdgeppyFNEPPL-----------KAMKMI---------- 527
Cdd:cd07838 160 EMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAEL-------FNRRPLfrgsseadqlgKIFDVIglpseeewpr 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  528 -----RDNLPPRL-KNLHKVSPSL----KGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07838 233 nsalpRSSFPSYTpRPFKSFVPEIdeegLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
327-572 1.24e-27

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: 113.02  E-value: 1.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR-----ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14094  11 IGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALT-DIVTHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQVSKEVPRRK 473
Cdd:cd14094  91 DLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14094 171 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRML 250
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14094 251 MLDPAERITVYEALNHPWI 269
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
316-570 1.81e-27

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 116.12  E-value: 1.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   316 DPRSYLDNFIkiGEGSTGIVCIATVRSSGKLVAVKKMDL---------RKQQRRELLFN----------EVVIMRDYQHE 376
Cdd:PTZ00283  31 AKKYWISRVL--GSGATGTVLCAKRVSDGEPFAVKVVDMegmseadknRAQAEVCCLLNcdffsivkchEDFAKKDPRNP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   377 NVVEMynsylvgdeLWVVMEFLEGGAL-TDIVTHTRMN----EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD 451
Cdd:PTZ00283 109 ENVLM---------IALVLDYANAGDLrQEIKSRAKTNrtfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   452 GRVKLSDFGF----CAQVSKEVPRrkSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY----FNEPPLKA 523
Cdd:PTZ00283 180 GLVKLGDFGFskmyAATVSDDVGR--TFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFdgenMEEVMHKT 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 5031975   524 MKMIRDNLPPrlknlhKVSPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:PTZ00283 258 LAGRYDPLPP------SISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
326-572 1.82e-27

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: 112.35  E-value: 1.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQ---QRR--------------------ELLFNEVVIMRDYQHENVV 379
Cdd:cd14200   7 EIGKGSYGVVKLAYNESDDKYYAMKvlsKKKLLKQygfPRRppprgskaaqgeqakplaplERVYQEIAILKKLDHVNIV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSY--LVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLS 457
Cdd:cd14200  87 KLIEVLddPAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  458 DFGFCAQVSKEVPRRKSLVGTPYWMAPELIS---RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPR 534
Cdd:cd14200 167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLSdsgQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIK-NKPVE 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  535 LKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14200 246 FPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
326-572 2.13e-27

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 112.14  E-value: 2.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIAT-VRSSGKLVAVK---KMDL----RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14096   8 KIGEGAFSNVYKAVpLRNTGKPVAIKvvrKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL---------------LTHD---------- 451
Cdd:cd14096  88 ADGGEIFHqIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkADDDetkvdegefi 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  452 --------GRVKLSDFGFCAQVSKEvpRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP-PLK 522
Cdd:cd14096 168 pgvggggiGIVKLADFGLSKQVWDS--NTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDESiETL 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  523 AMKMIRDN---LPPRLKNlhkVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14096 246 TEKISRGDytfLSPWWDE---ISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
327-572 4.79e-27

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: 110.33  E-value: 4.79e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSY-LVGDELWVVMEFLEGGA 402
Cdd:cd14164   8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPdfvQKFLPRELSILRRVNHPNIVQMFECIeVANGRLYIVMEAAATDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR-VKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14164  88 LQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRkIKIADFGFARFVEDYPELSTTFCGSRAY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGP-EVDIWSLGIMVIEMVDGEPPYFNEpplkAMKMIRDNLPPRL--KNLhKVSPSLKGFLDRLLVRDPA 558
Cdd:cd14164 168 TPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDET----NVRRLRLQQRGVLypSGV-ALEEPCRALIRTLLQFNPS 242
                       250
                ....*....|....
gi 5031975  559 QRATAAELLKHPFL 572
Cdd:cd14164 243 TRPSIQQVAGNSWL 256
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
338-572 4.96e-27

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 110.50  E-value: 4.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  338 ATVRSSGKLVAVKKMdLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD-IVTHTRMNE 414
Cdd:cd14088  20 AKDKTTGKLYTCKKF-LKRDGRkvRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDwILDQGYYSE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  415 EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH---DGRVKLSDFGFcAQVskEVPRRKSLVGTPYWMAPELISRLP 491
Cdd:cd14088  99 RDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNrlkNSKIVISDFHL-AKL--ENGLIKEPCGTPEYLAPEVVGRQR 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  492 YGPEVDIWSLGIMVIEMVDGEPPYFNEpplkamkMIRDNLPPRLKNLHK----------------VSPSLKGFLDRLLVR 555
Cdd:cd14088 176 YGRPVDCWAIGVIMYILLSGNPPFYDE-------AEEDDYENHDKNLFRkilagdyefdspywddISQAAKDLVTRLMEV 248
                       250
                ....*....|....*..
gi 5031975  556 DPAQRATAAELLKHPFL 572
Cdd:cd14088 249 EQDQRITAEEAISHEWI 265
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
326-570 5.12e-27

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: 110.46  E-value: 5.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNevviMRDYQHENVV---EMY-NSYLVGDELWVVMEFLEGG 401
Cdd:cd14089   8 VLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELH----WRASGCPHIVriiDVYeNTYQGRKCLLVVMECMEGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIV---THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH---DGRVKLSDFGFcaqvSKEVPRRKSL 475
Cdd:cd14089  84 ELFSRIqerADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGF----AKETTTKKSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VG---TPYWMAPELISRLPYGPEVDIWSLG-IMVIeMVDGEPPYFNE------PPLKamKMIRD---NLP-PRLKNlhkV 541
Cdd:cd14089 160 QTpcyTPYYVAPEVLGPEKYDKSCDMWSLGvIMYI-LLCGYPPFYSNhglaisPGMK--KRIRNgqyEFPnPEWSN---V 233
                       250       260
                ....*....|....*....|....*....
gi 5031975  542 SPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14089 234 SEEAKDLIRGLLKTDPSERLTIEEVMNHP 262
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
324-572 5.27e-27

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: 113.22  E-value: 5.27e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  324 FIKI---GEGSTGIVCIATVRSSGKLVAVKKmdLRKQQrrELLFNEVV-------IMRDYQHENVVEMYNSYLVGDELWV 393
Cdd:cd05625   3 FVKIktlGIGAFGEVCLARKVDTKALYATKT--LRKKD--VLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQ-ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV------- 465
Cdd:cd05625  79 VMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdsk 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 ---SKEVPRR-------------------------------------KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMV 505
Cdd:cd05625 159 yyqSGDHLRQdsmdfsnewgdpencrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975  506 IEMVDGEPPYFNEPPLKA-MKMIRDNLPPRLKNLHKVSPSLKGFLDRlLVRDPAQRA---TAAELLKHPFL 572
Cdd:cd05625 239 FEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 308
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
326-571 5.53e-27

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: 110.67  E-value: 5.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKK--MDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG-- 401
Cdd:cd07860   7 KIGEGTYGVVYKARNKLTGEVVALKKirLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDlk 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd07860  87 KFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELI--SRLpYGPEVDIWSLGIMVIEMVD---------------------GEPPYFNEPPLKAMKMIRDNLPP-RLKN 537
Cdd:cd07860 167 RAPEILlgCKY-YSTAVDIWSLGCIFAEMVTrralfpgdseidqlfrifrtlGTPDEVVWPGVTSMPDYKPSFPKwARQD 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  538 LHKVSPSL----KGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07860 246 FSKVVPPLdedgRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
327-571 6.76e-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: 110.52  E-value: 6.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRE---LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGal 403
Cdd:cd05605   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGG-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 tDIVTHT-RMN----EEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVsKEVPRRKSLVG 477
Cdd:cd05605  86 -DLKFHIyNMGnpgfEEERAVFYAAeITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEI-PEGETIRGRVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYfnepPLKAMKMIRDNLPPRLKN-----LHKVSPSLKGFLDRL 552
Cdd:cd05605 164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPF----RARKEKVKREEVDRRVKEdqeeySEKFSEEAKSICSQL 239
                       250       260
                ....*....|....*....|....
gi 5031975  553 LVRDPAQR-----ATAAELLKHPF 571
Cdd:cd05605 240 LQKDPKTRlgcrgEGAEDVKSHPF 263
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
327-572 7.50e-27

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: 109.95  E-value: 7.50e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd14117  14 LGKGKFGNVYLAREKQSKFIVALKvlfKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 -TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcaQVSKEVPRRKSLVGTPYWM 482
Cdd:cd14117  94 yKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGW--SVHAPSLRRRTMCGTLDYL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRAT 562
Cdd:cd14117 172 PPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRI---VKVDLKFPPFLSDGSRDLISKLLRYHPSERLP 248
                       250
                ....*....|
gi 5031975  563 AAELLKHPFL 572
Cdd:cd14117 249 LKGVMEHPWV 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
326-572 7.72e-27

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: 110.63  E-value: 7.72e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNevviMRDYQHENVVEMYNSY-----LVGDE-----LWVVM 395
Cdd:cd14171  13 KLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLH----MMCSGHPNIVQIYDVYansvqFPGESsprarLLIVM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL---THDGRVKLSDFGFcAQVSK---E 468
Cdd:cd14171  89 ELMEGGELFDrISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGF-AKVDQgdlM 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRkslvgTPYWMAPELI---------------SRLPY--GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM--KMIRD 529
Cdd:cd14171 168 TPQF-----TPYYVAPQVLeaqrrhrkersgiptSPTPYtyDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTItkDMKRK 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031975  530 ------NLPPRlkNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14171 243 imtgsyEFPEE--EWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
327-573 9.12e-27

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 111.41  E-value: 9.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMY---------NSYLVG-----DELW 392
Cdd:cd07854  13 LGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVYevlgpsgsdLTEDVGsltelNSVY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGaLTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL-THDGRVKLSDFGFCAQVSKEVPR 471
Cdd:cd07854  93 IVQEYMETD-LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGLARIVDPHYSH 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKSL---VGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLP--------------- 532
Cdd:cd07854 172 KGYLsegLVTKWYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPvvreedrnellnvip 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031975  533 ---------PRlKNLHKVSPSLK----GFLDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd07854 252 sfvrndggePR-RPLRDLLPGVNpealDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
327-516 1.68e-26

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: 112.02  E-value: 1.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05622  81 IGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE-VPRRKSLVGTPYWM 482
Cdd:cd05622 161 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgMVRCDTAVGTPDYI 240
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5031975  483 APELISRLP----YGPEVDIWSLGIMVIEMVDGEPPYF 516
Cdd:cd05622 241 SPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY 278
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
326-572 1.88e-26

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 109.94  E-value: 1.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVI---MRD---YQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14210  20 VLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQAL-VEVKIlkhLNDndpDDKHNIVRYKDSFIFRGHLCIVFELLS 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 ggalTDIVTHTRMNE------EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSKEV-- 469
Cdd:cd14210  99 ----INLYELLKSNNfqglslSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSSCFEGEKVyt 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 ---PRrkslvgtpYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNEPPLKAM----------KMIR------ 528
Cdd:cd14210 175 yiqSR--------FYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPlfPGENEEEQLACimevlgvppkSLIDkasrrk 246
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  529 ----DNLPPRL-------------KNLHKV----SPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14210 247 kffdSNGKPRPttnskgkkrrpgsKSLAQVlkcdDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
326-572 2.05e-26

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: 108.92  E-value: 2.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRE----LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd07835   6 KIGEGTYGVVYKARDKLTGEIVALKK--IRLETEDEgvpsTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLDLD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 --ALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSkeVPRRKSL--VG 477
Cdd:cd07835  84 lkKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFG--VPVRTYTheVV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPE--LISRLpYGPEVDIWSLGIMVIEMVDGEPPY------------F------NE---PPLKAMKMIRDNLPP- 533
Cdd:cd07835 162 TLWYRAPEilLGSKH-YSTPVDIWSVGCIFAEMVTRRPLFpgdseidqlfriFrtlgtpDEdvwPGVTSLPDYKPTFPKw 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031975  534 RLKNLHKVSPSLK----GFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07835 241 ARQDLSKVVPSLDedglDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
327-572 2.21e-26

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: 111.24  E-value: 2.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05621  60 IGRGAFGEVQLVRHKASQKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDL 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE-VPRRKSLVGTPYWM 482
Cdd:cd05621 140 VNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETgMVHCDTAVGTPDYI 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLP----YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-----NLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd05621 220 SPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDhknslNFPDDVEISKHAKNLICAFLTDRE 299
                       250
                ....*....|....*....
gi 5031975  554 VRdpAQRATAAELLKHPFL 572
Cdd:cd05621 300 VR--LGRNGVEEIKQHPFF 316
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
327-572 2.27e-26

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 108.47  E-value: 2.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFER 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAVCLA--VLQALSVLHAQGVIHRDIKSDSILL--THDGRVKLSDFGFCAQVSkevPRRKSLV--GTPY 480
Cdd:cd14190  92 IVDEDYHLTEVDAMVFVrqICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYN---PREKLKVnfGTPE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd14190 169 FLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLnNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSA 248
                       250
                ....*....|...
gi 5031975  560 RATAAELLKHPFL 572
Cdd:cd14190 249 RMSATQCLKHPWL 261
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
327-574 2.87e-26

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: 108.93  E-value: 2.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRS---SGKLVAVKKMD----LRKQQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05613   8 LGTGAYGKVFLVRKVSghdAGKLYAMKVLKkatiVQKAKTAEHTRTERQVLEHIrQSPFLVTLHYAFQTDTKLHLILDYI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ-VSKEVPRRKSLV 476
Cdd:cd05613  88 NGGELfTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEfLLDENERAYSFC 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPE--VDIWSLGIMVIEMVDGEPPYF----NEPPLKAMKMIRDNLPPRLKNLhkvSPSLKGFLD 550
Cdd:cd05613 168 GTIEYMAPEIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEM---SALAKDIIQ 244
                       250       260
                ....*....|....*....|....*....
gi 5031975  551 RLLVRDPAQR-----ATAAELLKHPFLAK 574
Cdd:cd05613 245 RLLMKDPKKRlgcgpNGADEIKKHPFFQK 273
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
326-572 3.36e-26

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: 107.69  E-value: 3.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIAT-------VRSSGKLVAVKKMDLRKQQRRelLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14019   8 KIGEGTFSSVYKAEdklhdlyDRNKGRLVALKHIYPTSSPSR--ILNELECLERLGgSNNVSGLITAFRNEDQVVAVLPY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHtrMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT-HDGRVKLSDFGFCAQVSKEVPRRKSLV 476
Cdd:cd14019  86 IEHDDFRDFYRK--MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQREEDRPEQRAPRA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGE-PPYFNEPPLKAMKMIrdnlpprlknlhkvsPSLKG------F 548
Cdd:cd14019 164 GTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEI---------------ATIFGsdeaydL 228
                       250       260
                ....*....|....*....|....
gi 5031975  549 LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14019 229 LDKLLELDPSKRITAEEALKHPFF 252
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
326-560 3.71e-26

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 108.58  E-value: 3.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM---DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd08229  31 KIGRGQFSEVYRATCLLDGVPVALKKVqifDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG 477
Cdd:cd08229 111 LSRMIKHFKkqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVG 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPP--LKAMKMIRDNLPPRLKNLHkVSPSLKGFLDRLLVR 555
Cdd:cd08229 191 TPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMnlYSLCKKIEQCDYPPLPSDH-YSEELRQLVNMCINP 269

                ....*
gi 5031975  556 DPAQR 560
Cdd:cd08229 270 DPEKR 274
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
342-572 3.82e-26

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 107.79  E-value: 3.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  342 SSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV-THTRMNEEQI 417
Cdd:cd14188  24 TTNKVYAAKIIPhsrVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILkARKVLTEPEV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  418 AAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVD 497
Cdd:cd14188 104 RYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESD 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031975  498 IWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPPRLknlhkvSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14188 184 IWALGCVMYTMLLGRPPFETTNLKETYRCIREarySLPSSL------LAPAKHLIASMLSKNPEDRPSLDEIIRHDFF 255
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
326-571 4.15e-26

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 109.00  E-value: 4.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKK--MDLRKQQRRELLFNEVVIMRDYQHENVVE----------MYNSYlvGDELWV 393
Cdd:cd07865  19 KIGQGTFGEVFKARHRKTGQIVALKKvlMENEKEGFPITALREIKILQLLKHENVVNlieicrtkatPYNRY--KGSIYL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLE---GGALTDIvtHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----FCAQVS 466
Cdd:cd07865  97 VFEFCEhdlAGLLSNK--NVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGlaraFSLAKN 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEP-------------------------------- 513
Cdd:cd07865 175 SQPNRYTNRVVTLWYRPPElLLGERDYGPPIDMWGAGCIMAEMWTRSPimqgnteqhqltlisqlcgsitpevwpgvdkl 254
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  514 PYFNEPPLKA--MKMIRDNLPPRLKNLHKVSpslkgFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07865 255 ELFKKMELPQgqKRKVKERLKPYVKDPYALD-----LIDKLLVLDPAKRIDADTALNHDF 309
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
326-568 5.48e-26

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 107.44  E-value: 5.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKM------------DLRKQQRRELlfneVVIMRDYQHENVVEMYNSYLVGDELWV 393
Cdd:cd13993   7 PIGEGAYGVVYLAVDLRTGRKYAIKCLyksgpnskdgndFQKLPQLREI----DLHRRVSRHPNIITLHDVFETEVAIYI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTRM---NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD-GRVKLSDFGFcAQVSKEV 469
Cdd:cd13993  83 VLEYCPNGDLFEAITENRIyvgKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGL-ATTEKIS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRRKslVGTPYWMAPELI-----SRLPYGP-EVDIWSLGIMVIEMVDGEPPYfnEPPLKAMKMIRDNLPPRlKNLHKVSP 543
Cdd:cd13993 162 MDFG--VGSEFYMAPECFdevgrSLKGYPCaAGDIWSLGIILLNLTFGRNPW--KIASESDPIFYDYYLNS-PNLFDVIL 236
                       250       260
                ....*....|....*....|....*....
gi 5031975  544 SLKGFLDRLLVR----DPAQRATAAELLK 568
Cdd:cd13993 237 PMSDDFYNLLRQiftvNPNNRILLPELQL 265
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
327-573 6.22e-26

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: 109.20  E-value: 6.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRD----YQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05610  12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMV-HQVQAERDalalSKSPFIVHLYYSLQSANNVYLVMEYLIGGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF----------------CAQV 465
Cdd:cd05610  91 VKSLLHIYGYFDEEMAVKYISeVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLskvtlnrelnmmdiltTPSM 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 SK-----------------------EVPRR--KS------------LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEM 508
Cdd:cd05610 171 AKpkndysrtpgqvlslisslgfntPTPYRtpKSvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEF 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  509 VDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd05610 251 LTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFH 315
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
327-571 6.72e-26

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: 107.09  E-value: 6.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCI---ATVRSSGKLVAVKKMD----LRKQQRRELLFNE-VVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05583   2 LGTGAYGKVFLvrkVGGHDAGKLYAMKVLKkatiVQKAKTAEHTMTErQVLEAVRQSPFLVTLHYAFQTDAKLHLILDYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKE-VP----RR 472
Cdd:cd05583  82 NGGELfTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFG----LSKEfLPgendRA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPE--VDIWSLGIMVIEMVDGEPPYFNEPPLKAM----KMIRDNLPPRLKNLhkvSPSLK 546
Cdd:cd05583 158 YSFCGTIEYMAPEVVRGGSDGHDkaVDWWSLGVLTYELLTGASPFTVDGERNSQseisKRILKSHPPIPKTF---SAEAK 234
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  547 GFLDRLLVRDPAQR-----ATAAELLKHPF 571
Cdd:cd05583 235 DFILKLLEKDPKKRlgagpRGAHEIKEHPF 264
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
326-573 9.53e-26

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 108.55  E-value: 9.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ---RRELlfNEVVIMRDYQHENVVEMYN-----SYLVGDELWVVMEF 397
Cdd:cd07849  12 YIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQtycLRTL--REIKILLRFKHENIIGILDiqrppTFESFKDVYIVQEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEggalTDI--VTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKS 474
Cdd:cd07849  90 ME----TDLykLIKTqHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTGF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 L---VGTPYWMAPE--LISRLpYGPEVDIWSLGIMVIEMVDGEP--P---YFNEPPL-------------------KAMK 525
Cdd:cd07849 166 LteyVATRWYRAPEimLNSKG-YTKAIDIWSVGCILAEMLSNRPlfPgkdYLHQLNLilgilgtpsqedlnciislKARN 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  526 MIRdNLP-----PRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd07849 245 YIK-SLPfkpkvPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLE 296
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
323-583 9.55e-26

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: 107.27  E-value: 9.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIKIGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd05608   5 DFRVLGKGGFGEVSACQMRATGKLYACKKLNkkrLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGaltDIVTHTR--------MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 471
Cdd:cd05608  85 GG---DLRYHIYnvdeenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYfnepPLKAMKMIRDNLPPRLKN-----LHKVSPSLK 546
Cdd:cd05608 162 TKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPF----RARGEKVENKELKQRILNdsvtySEKFSPASK 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  547 GFLDRLLVRDPAQR-----ATAAELLKHPFLA-------KAGP-PASIVP 583
Cdd:cd05608 238 SICEALLAKDPEKRlgfrdGNCDGLRTHPFFRdinwrklEAGIlPPPFVP 287
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
327-572 9.70e-26

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 106.54  E-value: 9.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFDR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAVCL--AVLQALSVLHAQGVIHRDIKSDSILLTH--DGRVKLSDFGFCAQVSkevPRRKSLV--GTPY 480
Cdd:cd14193  92 IIDENYNLTELDTILFikQICEGIQYMHQMYILHLDLKPENILCVSreANQVKIIDFGLARRYK---PREKLRVnfGTPE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd14193 169 FLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILAcQWDFEDEEFADISEEAKDFISKLLIKEKSW 248
                       250
                ....*....|...
gi 5031975  560 RATAAELLKHPFL 572
Cdd:cd14193 249 RMSASEALKHPWL 261
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
321-572 1.04e-25

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: 106.93  E-value: 1.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFI-----KIGEGSTGIV--CIAtvRSSGKLVAVKKMDLRKQQ---RRELLFNEVVIMRDYQHENVVEMYNSYLVGDE 390
Cdd:cd14198   5 FNNFYiltskELGRGKFAVVrqCIS--KSTGQEYAAKFLKKRRRGqdcRAEILHEIAVLELAKSNPRVVNLHEVYETTSE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVT---HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQ 464
Cdd:cd14198  83 IILILEYAAGGEIFNLCVpdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  465 VSKEVPRRKsLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSP 543
Cdd:cd14198 163 IGHACELRE-IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQvNVDYSEETFSSVSQ 241
                       250       260
                ....*....|....*....|....*....
gi 5031975  544 SLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14198 242 LATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
317-578 1.31e-25

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: 108.21  E-value: 1.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYlDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ----RREllFNEVVIMRDYQHENVVEMYNSYLVG---- 388
Cdd:cd07878  14 PERY-QNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSlihaRRT--YRELRLLKHMKHENVIGLLDVFTPAtsie 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  389 --DELWVVMEFLeGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS 466
Cdd:cd07878  91 nfNEVYLVTNLM-GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQAD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVprrKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---------------- 529
Cdd:cd07878 170 DEM---TGYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEvvgtpspevlkkisse 246
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975  530 -------NLPPR-LKNLHKV----SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPP 578
Cdd:cd07878 247 harkyiqSLPHMpQQDLKKIfrgaNPLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDP 307
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
319-572 1.42e-25

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: 106.13  E-value: 1.42e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  319 SYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELlFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd14107   2 SVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARA-FQERDILARLSHRRLTCLLDQFETRKTLILILELC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSKEVPRRkSL 475
Cdd:cd14107  81 SSEELLDrLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEITPSEHQF-SK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPRLKNLHKVSPSLKGFLDRLLV 554
Cdd:cd14107 160 YGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATlLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQ 239
                       250
                ....*....|....*...
gi 5031975  555 RDPAQRATAAELLKHPFL 572
Cdd:cd14107 240 PDPEKRPSASECLSHEWF 257
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
327-572 1.70e-25

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: 106.65  E-value: 1.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGA-LT 404
Cdd:cd14174  10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGSiLA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFGF---------CAQVSkeVPRR 472
Cdd:cd14174  90 HIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFDLgsgvklnsaCTPIT--TPEL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVGTPYWMAPELISRLP-----YGPEVDIWSLGIMVIEMVDGEPPYFNEPPL-------KAMKMIRDNLPPRL----- 535
Cdd:cd14174 168 TTPCGSAEYMAPEVVEVFTdeatfYDKRCDLWSLGVILYIMLSGYPPFVGHCGTdcgwdrgEVCRVCQNKLFESIqegky 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  536 ----KNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14174 248 efpdKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
326-571 1.72e-25

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: 106.59  E-value: 1.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlrKQQRRELL----FNEVVIMRDYQ-HENVVEMYNsyLVGDE----LWVVME 396
Cdd:cd07831   6 KIGEGTFSEVLKAQSRKTGKYYAIKCM---KKHFKSLEqvnnLREIQALRRLSpHPNILRLIE--VLFDRktgrLALVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLtHDGRVKLSDFGFCAQVSKEVPRRKsL 475
Cdd:cd07831  81 LMDMNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCRGIYSKPPYTE-Y 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNE-------------PPLKAMKMIRD------NLPP 533
Cdd:cd07831 159 ISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPlfPGTNEldqiakihdvlgtPDAEVLKKFRKsrhmnyNFPS 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031975  534 RL-----KNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07831 239 KKgtglrKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
327-572 1.78e-25

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 108.29  E-value: 1.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM-----DLRKQQRrelLFNEVVIMRDYQHENV---VEMYNSYLVG--DELWVVME 396
Cdd:cd07853   8 IGYGAFGVVWSVTDPRDGKRVALKKMpnvfqNLVSCKR---VFRELKMLCFFKHDNVlsaLDILQPPHIDpfEEIYVVTE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSL- 475
Cdd:cd07853  85 LMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGL-ARVEEPDESKHMTq 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 -VGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL---------------------- 531
Cdd:cd07853 164 eVVTQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLgtpsleamrsacegarahilrg 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 5031975  532 ---PPRLKNLHKVSPSLK----GFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07853 244 phkPPSLPVLYTLSSQATheavHLLCRMLVFDPDKRISAADALAHPYL 291
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
290-572 2.09e-25

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: 108.94  E-value: 2.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  290 RSPQREPQRVSH--EQFRAALQLVvdpGDPRSYLDNF--IK-IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRE 361
Cdd:cd05624  41 HSPLRRDKYVSEflEWAKPFTQLV---KEMQLHRDDFeiIKvIGRGAFGEVAVVKMKNTERIYAMKilnKWEMLKRAETA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  362 LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVT--HTRMNEEQIAAVCLAVLQALSVLHAQGVIHR 439
Cdd:cd05624 118 CFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSkfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHR 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  440 DIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL-VGTPYWMAPELISRL-----PYGPEVDIWSLGIMVIEMVDGEP 513
Cdd:cd05624 198 DIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVaVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGET 277
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  514 PYFNEPPLKAMKMI-----RDNLPPRLKNlhkVSPSLKGFLDRLLV---RDPAQRATaAELLKHPFL 572
Cdd:cd05624 278 PFYAESLVETYGKImnheeRFQFPSHVTD---VSEEAKDLIQRLICsreRRLGQNGI-EDFKKHAFF 340
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
322-575 2.28e-25

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 107.06  E-value: 2.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKI---GEGSTGIVCIATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd06650   5 DDFEKIselGAGNGGVVFKVSHKPSGLVMARKLIHLEiKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKSL 475
Cdd:cd06650  85 MDGGSLDQVLKKAgRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA--NSF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGE----PPYFNE--------------------------------- 518
Cdd:cd06650 163 VGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRypipPPDAKElelmfgcqvegdaaetpprprtpgrplssygmd 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031975  519 --PPLKAMKM---IRDNLPPRLKNLhKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06650 243 srPPMAIFELldyIVNEPPPKLPSG-VFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRS 303
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
326-571 2.95e-25

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: 105.64  E-value: 2.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ-RRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd07836   7 KLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEgTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKDLKK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 481
Cdd:cd07836  87 YMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSNEVVTLWY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELI--SRLpYGPEVDIWSLGIMVIEMVDGEPPYF----NEPPLKAMKMI---RDNLPPRLKNLHKVSPSLK------ 546
Cdd:cd07836 167 RAPDVLlgSRT-YSTSIDIWSVGCIMAEMITGRPLFPgtnnEDQLLKIFRIMgtpTESTWPGISQLPEYKPTFPryppqd 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  547 -------------GFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07836 246 lqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
317-572 3.04e-25

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: 106.91  E-value: 3.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLdNFIKIGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRELL----FNEVVIMRDYQHENVV---EMYNSYLVGD 389
Cdd:cd07879  14 PERYT-SLKQVGSGAYGSVCSAIDKRTGEKVAIKK--LSRPFQSEIFakraYRELTLLKHMQHENVIgllDVFTSAVSGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  390 EL---WVVMEFLEGGaLTDIVTHtRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS 466
Cdd:cd07879  91 EFqdfYLVMPYMQTD-LQKIMGH-PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHAD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVprrKSLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGE-----------------------PPYFNEPPLK 522
Cdd:cd07879 169 AEM---TGYVVTRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKtlfkgkdyldqltqilkvtgvpgPEFVQKLEDK 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  523 AMKMIRDNLP--PRlKNLH----KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07879 246 AAKSYIKSLPkyPR-KDFStlfpKASPQAVDLLEKMLELDVDKRLTATEALEHPYF 300
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
326-521 3.43e-25

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 105.66  E-value: 3.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVrsSGKLVAVKKM----DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14158  22 KLGEGGFGVVFKGYI--NDKNVAVKKLaamvDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTD----------IVTHTRMNEEQIAAvclavlQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC---AQVSKE 468
Cdd:cd14158 100 SLLDrlaclndtppLSWHMRCKIAQGTA------NGINYLHENNHIHRDIKSANILLDETFVPKISDFGLArasEKFSQT 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  469 VPRRKsLVGTPYWMAPELIsRLPYGPEVDIWSLGIMVIEMVDGEPP--YFNEPPL 521
Cdd:cd14158 174 IMTER-IVGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPPvdENRDPQL 226
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
317-578 3.88e-25

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: 107.05  E-value: 3.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYlDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ--RRELLFNEVVIMRDYQHENVVEMYNSYLVG------ 388
Cdd:cd07877  16 PERY-QNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSiiHAKRTYRELRLLKHMKHENVIGLLDVFTPArsleef 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  389 DELWVVMEFLeGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE 468
Cdd:cd07877  95 NDVYLVTHLM-GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDE 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VprrKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDG-----------------------EPPYFNEPPLKAM 524
Cdd:cd07877 174 M---TGYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLTGrtlfpgtdhidqlklilrlvgtpGAELLKKISSESA 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  525 KMIRDNLP--PRLkNLHKV----SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPP 578
Cdd:cd07877 251 RNYIQSLTqmPKM-NFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDP 309
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
327-572 6.09e-25

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: 105.27  E-value: 6.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRE----LLFNEVVIMRDYQHENVVEMYNsyLVGDELWVVMEFLEGGA 402
Cdd:cd07864  15 IGEGTYGQVYKAKDKDTGELVALKK--VRLDNEKEgfpiTAIREIKILRQLNHRSVVNLKE--IVTDKQDALDFKKDKGA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LT---DIVTHTRM----------NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV 469
Cdd:cd07864  91 FYlvfEYMDHDLMgllesglvhfSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYNSEE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PR-RKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEP--------------------------------PY 515
Cdd:cd07864 171 SRpYTNKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPifqanqelaqlelisrlcgspcpavwpdviklPY 250
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  516 FNEppLKAMKMIRDNLPPRLKNLHKVSPSLkgfLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07864 251 FNT--MKPKKQYRRRLREEFSFIPTPALDL---LDHMLTLDPSKRCTAEQALNSPWL 302
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
322-572 6.97e-25

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: 104.29  E-value: 6.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNF-------IKIGEGSTGIVCIATVRSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd14113   3 DNFdsfysevAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFGFCAQVSKeVP 470
Cdd:cd14113  82 LEMADQGRLLDyVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNT-TY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPRLKNLHKVSPSLKGFL 549
Cdd:cd14113 161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETcLNICRLDFSFPDDYFKGVSQKAKDFV 240
                       250       260
                ....*....|....*....|...
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14113 241 CFLLQMDPAKRPSAALCLQEQWL 263
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
326-569 7.48e-25

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: 104.69  E-value: 7.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGstGIVCIATVR--SSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGD-----ELWVVMEFL 398
Cdd:cd13986   7 LLGEG--GFSFVYLVEdlSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaggkkEVYLLLPYY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVT-----HTRMNEEQIAAVCLAVLQALSVLHAQ---GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd13986  85 KRGSLQDEIErrlvkGTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSMNPARIEIE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSLV---------GTPYWMAPELISRLPYG---PEVDIWSLGIMVIEMVDGEPPYfnEPPLK-----AMKMIRDNLPP 533
Cdd:cd13986 165 GRREALalqdwaaehCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPF--ERIFQkgdslALAVLSGNYSF 242
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031975  534 RLKNLHkvSPSLKGFLDRLLVRDPAQRATAAELLKH 569
Cdd:cd13986 243 PDNSRY--SEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
325-574 7.97e-25

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: 105.92  E-value: 7.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKLVAVKKM----DLRKQQRRELlfNEVVIMRDYQHENVVE-----MYNSYLVGDELWVVM 395
Cdd:cd07858  11 KPIGRGAYGIVCSAKNSETNEKVAIKKIanafDNRIDAKRTL--REIKLLRHLDHENVIAikdimPPPHREAFNDVYIVY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEggalTD----IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 471
Cdd:cd07858  89 ELMD----TDlhqiIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKSLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEP-----PYFNEPPL-------------------KAMKM 526
Cdd:cd07858 165 MTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPlfpgkDYVHQLKLitellgspseedlgfirneKARRY 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  527 IRdNLP--PR--LKNLH-KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd07858 245 IR-SLPytPRqsFARLFpHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLAS 296
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
323-573 9.26e-25

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 105.83  E-value: 9.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   323 NFIK-IGEGSTGIVCIATVRSSG-KLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:PTZ00426  33 NFIRtLGTGSFGRVILATYKNEDfPPVAIKRFEkskIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEF 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   398 LEGGaltDIVTHTRMNEEQIAAV-CLAVLQALSV---LHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKevpRRK 473
Cdd:PTZ00426 113 VIGG---EFFTFLRRNKRFPNDVgCFYAAQIVLIfeyLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDT---RTY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   474 SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF-NEPPLKAMKMIRD--NLPPRLKNlhkvspSLKGFLD 550
Cdd:PTZ00426 187 TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYaNEPLLIYQKILEGiiYFPKFLDN------NCKHLMK 260
                        250       260
                 ....*....|....*....|....*...
gi 5031975   551 RLLVRDPAQR-----ATAAELLKHPFLA 573
Cdd:PTZ00426 261 KLLSHDLTKRygnlkKGAQNVKEHPWFG 288
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
327-571 1.44e-24

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: 104.74  E-value: 1.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM---DLRK-------QQRRELLFNEvviMRDYqhenVVEMYNSYLVGDELWVVME 396
Cdd:cd05597   9 IGRGAFGEVAVVKLKSTEKVYAMKILnkwEMLKraetacfREERDVLVNG---DRRW----ITKLHYAFQDENYLYLVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGG-ALTDIVTHTRMNEEQIAAVCLA--VLqALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK 473
Cdd:cd05597  82 YYCGGdLLTLLSKFEDRLPEEMARFYLAemVL-AIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SL-VGTPYWMAPELISRLP-----YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-----RDNLPPrlkNLHKVS 542
Cdd:cd05597 161 SVaVGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnhkeHFSFPD---DEDDVS 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 5031975  543 PSLKGFLDRLLVrDPAQR---ATAAELLKHPF 571
Cdd:cd05597 238 EEAKDLIRRLIC-SRERRlgqNGIDDFKKHPF 268
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
326-572 1.46e-24

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: 103.16  E-value: 1.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14191   9 RLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 --IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHD--GRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 481
Cdd:cd14191  89 riIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLIDFGL-ARRLENAGSLKVLFGTPEF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNepplkamkmirDNLPPRLKNL------------HKVSPSLKGFL 549
Cdd:cd14191 168 VAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG-----------DNDNETLANVtsatwdfddeafDEISDDAKDFI 236
                       250       260
                ....*....|....*....|...
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14191 237 SNLLKKDMKARLTCTQCLQHPWL 259
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
326-572 1.61e-24

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: 103.40  E-value: 1.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLrKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14104   7 ELGRGQFGIVHRCVETSSKKTYMAKFVKV-KGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL-LTHDGR-VKLSDFGFCAQVsKEVPRRKSLVGTPYW 481
Cdd:cd14104  86 RITTARfeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyCTRRGSyIKIIEFGQSRQL-KPGDKFRLQYTSAEF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRdNLPPRLKN--LHKVSPSLKGFLDRLLVRDPAQ 559
Cdd:cd14104 165 YAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIR-NAEYAFDDeaFKNISIEALDFVDRLLVKERKS 243
                       250
                ....*....|...
gi 5031975  560 RATAAELLKHPFL 572
Cdd:cd14104 244 RMTAQEALNHPWL 256
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
327-572 1.76e-24

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 104.80  E-value: 1.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYN------SYLVGDELWVVMEFL 398
Cdd:cd07850   8 IGSGAQGIVCAAYDTVTGQNVAIKKLSrpFQNVTHAKRAYRELVLMKLVNHKNIIGLLNvftpqkSLEEFQDVYLVMELM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTdiVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGT 478
Cdd:cd07850  88 DANLCQ--VIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAGTSFMMTPYVVT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGE----------------------PPYF-------------NEPPLKA 523
Cdd:cd07850 165 RYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTvlfpgtdhidqwnkiieqlgtpSDEFmsrlqptvrnyveNRPKYAG 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031975  524 M---KMIRDNL-PPRLKNLHKVSPSL-KGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07850 245 YsfeELFPDVLfPPDSEEHNKLKASQaRDLLSKMLVIDPEKRISVDDALQHPYI 298
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
327-586 2.48e-24

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: 103.92  E-value: 2.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMR---DYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKalkKGDIIARDEVESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFVMEYAAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GAL-----TDIVTHTRmneEQIAAVClaVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL 475
Cdd:cd05589  87 GDLmmhihEDVFSEPR---AVFYAAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTSTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY--------FNEpplkamkMIRDNLP-PRLknlhkVSPSLK 546
Cdd:cd05589 162 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFpgddeeevFDS-------IVNDEVRyPRF-----LSTEAI 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031975  547 GFLDRLLVRDPAQR-----ATAAELLKHPF---------LAKAGPPaSIVPLMR 586
Cdd:cd05589 230 SIMRRLLRKNPERRlgaseRDAEDVKKQPFfrnidwealLARKIKP-PFVPTIK 282
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
327-578 2.52e-24

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: 104.73  E-value: 2.52e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVG------DELWVVMEFL 398
Cdd:cd07876  29 IGSGAQGIVCAAFDTVLGINVAVKKLSrpFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQksleefQDVYLVMELM 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTdiVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVgT 478
Cdd:cd07876 109 DANLCQ--VIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVV-T 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY---------------FNEPPLKAMKMIRDNLPPRLKN---LHK 540
Cdd:cd07876 186 RYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFqgtdhidqwnkvieqLGTPSAEFMNRLQPTVRNYVENrpqYPG 265
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  541 VS----------PS-----------LKGFLDRLLVRDPAQRATAAELLKHPFL--------AKAGPP 578
Cdd:cd07876 266 ISfeelfpdwifPSeserdklktsqARDLLSKMLVIDPDKRISVDEALRHPYItvwydpaeAEAPPP 332
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
327-572 2.55e-24

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: 102.56  E-value: 2.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCI-----ATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd14076   9 LGEGEFGKVKLgwplpKANHRSGVQVAIKlirRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR-RKSLV 476
Cdd:cd14076  89 SGGELFDYILARRRLKDSVACRLFAQLiSGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGDlMSTSC 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELI-SRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPL----KAMKMIRDNLPPRLKNLHKVSPSLKGFLD 550
Cdd:cd14076 169 GSPCYAAPELVvSDSMYaGRKADIWSCGVILYAMLAGYLPFDDDPHNpngdNVPRLYRYICNTPLIFPEYVTPKARDLLR 248
                       250       260
                ....*....|....*....|..
gi 5031975  551 RLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14076 249 RILVPNPRKRIRLSAIMRHAWL 270
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
321-572 2.56e-24

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 104.75  E-value: 2.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFIK---IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd05627   1 LDDFESlkvIGRGAFGEVRLVQKKDTGHIYAMKilrKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGG-ALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK------ 467
Cdd:cd05627  81 MEFLPGGdMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKahrtef 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 --------------------------EVPRRK---SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNE 518
Cdd:cd05627 161 yrnlthnppsdfsfqnmnskrkaetwKKNRRQlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031975  519 PPLKAMKMI---RDNL--PPRLknlhKVSPSLKGFLDRLLVrDPAQR---ATAAELLKHPFL 572
Cdd:cd05627 241 TPQETYRKVmnwKETLvfPPEV----PISEKAKDLILRFCT-DAENRigsNGVEEIKSHPFF 297
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
327-573 3.67e-24

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 104.55  E-value: 3.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMdLRKQQRRELLFNEVVIMRDYQHEN----VVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05629   9 IGKGAFGEVRLVQKKDTGKIYAMKTL-LKSEMFKKDQLAHVKAERDVLAESdspwVVSLYYSFQDAQYLYLIMEFLPGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLA-VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK-------------- 467
Cdd:cd05629  88 LMTMLIKYDTFSEDVTRFYMAeCVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFHKqhdsayyqkllqgk 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 ------------------------------EVPRRK---SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPP 514
Cdd:cd05629 168 snknridnrnsvavdsinltmsskdqiatwKKNRRLmaySTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPP 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  515 YFNEPPLKAMKMI---RDNL--PprlKNLHkVSPSLKGFLDRLLVrDPAQ---RATAAELLKHPFLA 573
Cdd:cd05629 248 FCSENSHETYRKIinwRETLyfP---DDIH-LSVEAEDLIRRLIT-NAENrlgRGGAHEIKSHPFFR 309
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
327-569 4.62e-24

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: 101.63  E-value: 4.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRELLF-NEVVIMRDYQ-HENVVEMYNSYLVGDELWV-VMEFLEGGAL 403
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKF--VPKPSTKLKDFlREYNISLELSvHPHIIKTYDVAFETEDYYVfAQEYAPYGDL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL--THDGRVKLSDFGFCAQVSKEVPRRKSLvgTPY 480
Cdd:cd13987  79 FSIIPPQVgLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTRRVGSTVKRVSGT--IPY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 wMAPELISRLPYG-----PEVDIWSLGIMVIEMVDGEPPY--------FNEPPLKAMKMIRDNLPPRLKNLhkvSPSLKG 547
Cdd:cd13987 157 -TAPEVCEAKKNEgfvvdPSIDVWAFGVLLFCCLTGNFPWekadsddqFYEEFVRWQKRKNTAVPSQWRRF---TPKALR 232
                       250       260
                ....*....|....*....|..
gi 5031975  548 FLDRLLVRDPAQRATAAELLKH 569
Cdd:cd13987 233 MFKKLLAPEPERRCSIKEVFKY 254
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
327-573 5.00e-24

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: 104.71  E-value: 5.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05623  80 IGRGAFGEVAVVKLKNADKVFAMKilnKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDL 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVT--HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL-VGTPY 480
Cdd:cd05623 160 LTLLSkfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVaVGTPD 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPELISRLP-----YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-----RDNLPPRLKNlhkVSPSLKGFLD 550
Cdd:cd05623 240 YISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnhkeRFQFPTQVTD---VSENAKDLIR 316
                       250       260
                ....*....|....*....|....*
gi 5031975  551 RLLV-RDPAQRATAAELLK-HPFLA 573
Cdd:cd05623 317 RLICsREHRLGQNGIEDFKnHPFFV 341
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
323-581 5.07e-24

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: 103.63  E-value: 5.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIKIGEGSTGIVCIATVRSSGKLVAVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDEL------WVV 394
Cdd:cd07874  21 NLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTdiVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKS 474
Cdd:cd07874 101 MELMDANLCQ--VIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAGTSFMMTP 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD---------------------GEP-PYF-------------NEP 519
Cdd:cd07874 178 YVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRhkilfpgrdyidqwnkvieqlGTPcPEFmkklqptvrnyveNRP 257
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  520 PLKAM---KMIRDNLPPRLKNLHKVSPS-LKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASI 581
Cdd:cd07874 258 KYAGLtfpKLFPDSLFPADSEHNKLKASqARDLLSKMLVIDPAKRISVDEALQHPYINVWYDPAEV 323
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
375-567 5.42e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 106.03  E-value: 5.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   375 HENVVEMYNsylVGDE---LWVVMEFLEGGALTDIV-THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH 450
Cdd:NF033483  66 HPNIVSVYD---VGEDggiPYIVMEYVDGRTLKDYIrEHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   451 DGRVKLSDFGFC--------AQVSkevprrkSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK 522
Cdd:NF033483 143 DGRVKVTDFGIAralssttmTQTN-------SVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPVS 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5031975   523 -AMKMIRDNLP-PRLKNlHKVSPSlkgfLDRL----LVRDPAQR-ATAAELL 567
Cdd:NF033483 216 vAYKHVQEDPPpPSELN-PGIPQS----LDAVvlkaTAKDPDDRyQSAAEMR 262
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
327-586 7.26e-24

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: 102.69  E-value: 7.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCI---ATVRSSGKLVAVKKMD----LRKQQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd05614   8 LGTGAYGKVFLvrkVSGHDANKLYAMKVLRkaalVQKAKTVEHTRTERNVLEHVrQSPFLVTLHYAFQTDAKLHLILDYV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ-VSKEVPRRKSLV 476
Cdd:cd05614  88 SGGELfTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEfLTEEKERTYSFC 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYfnepPLKAMKMIRDNLPPRLKNLHKVSPSLKGF-----LD 550
Cdd:cd05614 168 GTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPF----TLEGEKNTQSEVSRRILKCDPPFPSFIGPvardlLQ 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031975  551 RLLVRDPAQRATAA-----ELLKHPF--------LAKAGPPASIVPLMR 586
Cdd:cd05614 244 KLLCKDPKKRLGAGpqgaqEIKEHPFfkgldweaLALRKVNPPFRPSIR 292
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
321-569 7.45e-24

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 102.92  E-value: 7.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   321 LDNFIkiGEGSTGIVCIATVRSSGKLVAVKKMDLRK-----QQRREL---------LFNEVVIMRDYQHENVVEMYNSYL 386
Cdd:PTZ00024  13 KGAHL--GEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvTKDRQLvgmcgihftTLRELKIMNEIKHENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   387 VGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF----- 461
Cdd:PTZ00024  91 EGDFINLVMDIMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLarryg 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   462 -------CAQVSKEVPRRK--SLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNE----------- 518
Cdd:PTZ00024 171 yppysdtLSKDETMQRREEmtSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPlfPGENEidqlgrifell 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031975   519 --------PPLKAMKMIRDNLPPRLKNLHKVSP----SLKGFLDRLLVRDPAQRATAAELLKH 569
Cdd:PTZ00024 251 gtpnednwPQAKKLPLYTEFTPRKPKDLKTIFPnasdDAIDLLQSLLKLNPLERISAKEALKH 313
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
327-572 8.19e-24

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: 101.05  E-value: 8.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRkqqrrELLFNEVVIMRDYQHENVVEMYNSYLV-GDELWVVMEFLEGGALTD 405
Cdd:cd14109  12 EKRAAQGAPFHVTERSTGRNFLAQLRYGD-----PFLMREVDIHNSLDHPNIVQMHDAYDDeKLAVTVIDNLASTIELVR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMN---EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDgRVKLSDFGfcaqVSKEVPRRK---SLVGTP 479
Cdd:cd14109  87 DNLLPGKDyytERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFG----QSRRLLRGKlttLIYGSP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLLVRDPA 558
Cdd:cd14109 162 EFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSgKWSFDSSPLGNISDDARDFIKKLLVYIPE 241
                       250
                ....*....|....
gi 5031975  559 QRATAAELLKHPFL 572
Cdd:cd14109 242 SRLTVDEALNHPWF 255
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
327-573 8.95e-24

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 102.55  E-value: 8.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD-----LRKQQRrelLFNEVVIMRDYQHENVVEMYNSYLVGD-----ELWVVME 396
Cdd:cd07859   8 IGKGSYGVVCSAIDTHTGEKVAIKKINdvfehVSDATR---ILREIKLLRLLRHPDIVEIKHIMLPPSrrefkDIYVVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR---K 473
Cdd:cd07859  85 LMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAifwT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRL--PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL--PP-----RLKN------- 537
Cdd:cd07859 165 DYVATRWYRAPELCGSFfsKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLgtPSpetisRVRNekarryl 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  538 --------------LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd07859 245 ssmrkkqpvpfsqkFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
328-515 9.28e-24

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: 100.42  E-value: 9.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  328 GEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRrellfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV 407
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKK--LLKIEK------EAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  408 THTR---MNEEQIAAVCLAVLQALSVLHAQG---VIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVprRKSLVGTPYW 481
Cdd:cd14060  74 NSNEseeMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTT--HMSLVGTFPW 151
                       170       180       190
                ....*....|....*....|....*....|....
gi 5031975  482 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14060 152 MAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
327-515 1.01e-23

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 101.05  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAVCLA--VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE---------------- 468
Cdd:cd14154  81 LKDMARPLPWAQRVRFAkdIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEErlpsgnmspsetlrhl 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031975  469 -VPRRK---SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEM---VDGEPPY 515
Cdd:cd14154 161 kSPDRKkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIigrVEADPDY 214
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
327-509 1.12e-23

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 100.79  E-value: 1.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR-------------- 471
Cdd:cd14222  81 LRADDpFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKpppdkpttkkrtlr 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  472 ------RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV 509
Cdd:cd14222 161 kndrkkRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
327-515 1.19e-23

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: 100.16  E-value: 1.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIAtvRSSGKlVAVKKMDLRKQQRRELL-F-NEVVIMRDYQHENVVeMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14062   1 IGSGSFGTVYKG--RWHGD-VAVKKLNVTDPTPSQLQaFkNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGSSLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DI--VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKE---VPRRKSLVGTP 479
Cdd:cd14062  77 KHlhVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGL-ATVKTRwsgSQQFEQPTGSI 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELIsRL----PYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14062 156 LWMAPEVI-RMqdenPYSFQSDVYAFGIVLYELLTGQLPY 194
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
327-527 2.08e-23

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 102.42  E-value: 2.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG-A 402
Cdd:cd05628   9 IGRGAFGEVRLVQKKDTGHVYAMKilrKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGdM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK------------EVP 470
Cdd:cd05628  89 MTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKahrtefyrnlnhSLP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 --------------------RRK---SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI 527
Cdd:cd05628 169 sdftfqnmnskrkaetwkrnRRQlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKV 248
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
319-571 2.34e-23

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: 100.85  E-value: 2.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  319 SYLDNF---IKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQqrRELL----FNEVVIMRDYQHENVVEMYN-SYLVGDE 390
Cdd:cd07866   5 SKLRDYeilGKLGEGTFGEVYKARQIKTGRVVALKKILMHNE--KDGFpitaLREIKILKKLKHPNVVPLIDmAVERPDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 -------LWVVMEFLE---GGALTDivTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG 460
Cdd:cd07866  83 skrkrgsVYMVTPYMDhdlSGLLEN--PSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  461 F------CAQVSKEVP---RRK--SLVGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEP--------------- 513
Cdd:cd07866 161 LarpydgPPPNPKGGGgggTRKytNLVVTRWYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRRPilqgksdidqlhlif 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  514 -----------PYFNEPPLKAMKMIRDNLPPRLK-NLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07866 241 klcgtpteetwPGWRSLPGCEGVHSFTNYPRTLEeRFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
327-572 3.54e-23

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: 99.29  E-value: 3.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLR---KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGD-ELWVVMEFLEGGA 402
Cdd:cd14163   8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVMELAEDGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLthDGR-VKLSDFGFCAQVSKEvpRR---KSLVG 477
Cdd:cd14163  88 VFDCVLHGgPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL--QGFtLKLTDFGFAKQLPKG--GRelsQTFCG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEV-DIWSLGIMVIEMVDGEPPY--FNEPPLKAMKMIRDNLPPRLknlhKVSPSLKGFLDRLLV 554
Cdd:cd14163 164 STAYAAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPFddTDIPKMLCQQQKGVSLPGHL----GVSRTCQDLLKRLLE 239
                       250
                ....*....|....*...
gi 5031975  555 RDPAQRATAAELLKHPFL 572
Cdd:cd14163 240 PDMVLRPSIEEVSWHPWL 257
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
325-515 4.49e-23

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: 101.65  E-value: 4.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKLVAVKKMD----LRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05600  17 TQVGQGGYGSVFLARKKDTGEICALKIMKkkvlFKLNEVNHVL-TERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTR-MNEEQ----IAAVCLAVlqalSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC------------- 462
Cdd:cd05600  96 GDFRTLLNNSGiLSEEHarfyIAEMFAAI----SSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAsgtlspkkiesmk 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  463 ------------------------AQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd05600 172 irleevkntafleltakerrniyrAMRKEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPF 248
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
320-545 4.79e-23

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: 99.38  E-value: 4.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVR----SSGKLVAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEM-YNSYLVGD-EL 391
Cdd:cd05038   5 HLKFIKQLGEGHFGSVELCRYDplgdNTGEQVAVKSLqpSGEEQHMSDFK-REIEILRTLDHEYIVKYkGVCESPGRrSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALTDIVTHTRMN---------EEQIAavclavlQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFc 462
Cdd:cd05038  84 RLIMEYLPSGSLRDYLQRHRDQidlkrlllfASQIC-------KGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  463 AQV---SKEVPRRKSLVGTP-YWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPpyFNEPPLKAMKMIRDNLPP---- 533
Cdd:cd05038 156 AKVlpeDKEYYYVKEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYELFTyGDP--SQSPPALFLRMIGIAQGQmivt 233
                       250
                ....*....|..
gi 5031975  534 RLKNLHKVSPSL 545
Cdd:cd05038 234 RLLELLKSGERL 245
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
343-571 5.77e-23

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 99.94  E-value: 5.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  343 SGKLVAVKKMDLR--KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTH---TRMNEEQI 417
Cdd:cd08226  24 TGTLVTVKITNLDncSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTyfpEGMNEALI 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  418 AAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY-------WMAPELISRL 490
Cdd:cd08226 104 GNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQRSKVVYDFPQfstsvlpWLSPELLRQD 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  491 PYGPEV--DIWSLGIMVIEMVDGEPPYFN---------------------------EPPLK---------------AMKM 526
Cdd:cd08226 184 LHGYNVksDIYSVGITACELARGQVPFQDmrrtqmllqklkgppyspldifpfpelESRMKnsqsgmdsgigesvaTSSM 263
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  527 IRDNLPPRLKN--LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd08226 264 TRTMTSERLQTpsSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSF 310
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
327-560 7.06e-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: 100.48  E-value: 7.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMdlrkqqRRELLFNEVVIMRDYQHENVVEM--YNSYLVG--------DELWVVME 396
Cdd:cd05617  23 IGRGSYAKVLLVRLKKNDQIYAMKVV------KKELVHDDEDIDWVQTEKHVFEQasSNPFLVGlhscfqttSRLFLVIE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALT-DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL 475
Cdd:cd05617  97 YVNGGDLMfHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTF 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY---FNEPPLKAMKMIRDNL---PPRLKNLHKVSPS--LKG 547
Cdd:cd05617 177 CGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVIlekPIRIPRFLSVKAShvLKG 256
                       250
                ....*....|...
gi 5031975  548 FLDrllvRDPAQR 560
Cdd:cd05617 257 FLN----KDPKER 265
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
326-572 9.33e-23

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: 98.65  E-value: 9.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE---G 400
Cdd:cd07861   7 KIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLSmdlK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd07861  87 KYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTHEVVTLW 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPE-LISRLPYGPEVDIWSLGIMVIEMV--------DGE-------------------------PPYFNEPPlkamKM 526
Cdd:cd07861 167 YRAPEvLLGSPRYSTPVDIWSIGTIFAEMAtkkplfhgDSEidqlfrifrilgtptediwpgvtslPDYKNTFP----KW 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  527 IRDNLPPRLKNLHKVSPSLkgfLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07861 243 KKGSLRTAVKNLDEDGLDL---LEKMLIYDPAKRISAKKALVHPYF 285
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
327-460 9.83e-23

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 94.05  E-value: 9.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HE-NVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKgLElNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  405 DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG 460
Cdd:cd13968  81 AYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
322-571 1.06e-22

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: 98.27  E-value: 1.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  322 DNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd07839   3 EKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEgvPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 ----------GGALTDIVTHTRMNEeqiaavclaVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV 469
Cdd:cd07839  83 qdlkkyfdscNGDIDPEIVKSFMFQ---------LLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYF-------------------NEPPLKAMKMIRD 529
Cdd:cd07839 154 RCYSAEVVTLWYRPPDvLFGAKLYSTSIDMWSAGCIFAELANAGRPLFpgndvddqlkrifrllgtpTEESWPGVSKLPD 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  530 NLP----PRLKNLHKVSPSL----KGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07839 234 YKPypmyPATTSLVNVVPKLnstgRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
326-566 1.10e-22

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 97.97  E-value: 1.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKqqrrellFN--EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd13991  13 RIGRGSFGEVHRMEDKQTGFQCAVKKVRLEV-------FRaeELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR-VKLSDFGFCAQV-----SKEVPRRKSLV 476
Cdd:cd13991  86 GQLIKEQgCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLdpdglGKSLFTGDYIP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPP---YFNEPplKAMKMIRDnlPPRLKnlhKVSPSLKGFLDRL- 552
Cdd:cd13991 166 GTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPwtqYYSGP--LCLKIANE--PPPLR---EIPPSCAPLTAQAi 238
                       250
                ....*....|....*..
gi 5031975  553 ---LVRDPAQRATAAEL 566
Cdd:cd13991 239 qagLRKEPVHRASAAEL 255
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
327-516 1.31e-22

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 97.72  E-value: 1.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTRMNEEQIAAVCLA--VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC------------AQVSKEVPRR 472
Cdd:cd14221  81 IKSMDSHYPWSQRVSFAkdIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdektqpegLRSLKKPDRK 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031975  473 K--SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEM---VDGEPPYF 516
Cdd:cd14221 161 KryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIigrVNADPDYL 209
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
326-572 1.61e-22

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 97.30  E-value: 1.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKkMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT- 404
Cdd:cd14110  10 EINRGRFSVVRQCEEKRSGQMLAAK-IIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLy 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE----VPRRKSLVGTpy 480
Cdd:cd14110  89 NLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGkvlmTDKKGDYVET-- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 wMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlpprLKNLHKVSPSLKG----FLDRLLVRD 556
Cdd:cd14110 167 -MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKG----KVQLSRCYAGLSGgavnFLKSTLCAK 241
                       250
                ....*....|....*.
gi 5031975  557 PAQRATAAELLKHPFL 572
Cdd:cd14110 242 PWGRPTASECLQNPWL 257
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
320-560 1.88e-22

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: 97.67  E-value: 1.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd05607   3 YFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDkkrLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQI-------AAVCLAVLQalsvLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV--SK 467
Cdd:cd05607  83 LMNGGDLKYHIYNVGERGIEMervifysAQITCGILH----LHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVkeGK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EVPRRkslVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMK--MIRDNLPPRLKNLHKV-SPS 544
Cdd:cd05607 159 PITQR---AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTP-FRDHKEKVSKeeLKRRTLEDEVKFEHQNfTEE 234
                       250
                ....*....|....*.
gi 5031975  545 LKGFLDRLLVRDPAQR 560
Cdd:cd05607 235 AKDICRLFLAKKPENR 250
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
327-575 2.00e-22

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: 98.18  E-value: 2.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNevviMRDYQHENVVEMY----NSYLVGDELWVVMEFLEGGA 402
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELH----WRASQCPHIVRIVdvyeNLYAGRKCLLIVMECLDGGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTH---TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH---DGRVKLSDFGFcaqvSKEVPRRKSLV 476
Cdd:cd14170  86 LFSRIQDrgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGF----AKETTSHNSLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 G---TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPL-------KAMKMIRDNLPPrlKNLHKVSPSLK 546
Cdd:cd14170 162 TpcyTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLaispgmkTRIRMGQYEFPN--PEWSEVSEEVK 239
                       250       260
                ....*....|....*....|....*....
gi 5031975  547 GFLDRLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd14170 240 MLIRNLLKTEPTQRMTITEFMNHPWIMQS 268
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
327-570 2.81e-22

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 97.11  E-value: 2.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRS-SGKLVAVKKM--DLRKQQRRELLFNEVVIMRDYQ---HENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd14052   8 IGSGEFSQVYKVSERVpTGKVYAVKKLkpNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELCEN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GAL----TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCaqVSKEVPRRKSLV 476
Cdd:cd14052  88 GSLdvflSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA--TVWPLIRGIERE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV-------DGEP------------PYFNEPPLKAMKMIRDNLPPRLKN 537
Cdd:cd14052 166 GDREYIAPEILSEHMYDKPADIFSLGLILLEAAanvvlpdNGDAwqklrsgdlsdaPRLSSTDLHSASSPSSNPPPDPPN 245
                       250       260       270
                ....*....|....*....|....*....|...
gi 5031975  538 LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14052 246 MPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
326-573 2.86e-22

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: 98.25  E-value: 2.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATV--RSSGKLVAVKKMD-------LRKQQRRELLFnevviMRDYQ-HENVVEMYNSYLVG----DEL 391
Cdd:cd07857   7 ELGQGAYGIVCSARNaeTSEEETVAIKKITnvfskkiLAKRALRELKL-----LRHFRgHKNITCLYDMDIVFpgnfNEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  392 WVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----FCAQVSK 467
Cdd:cd07857  82 YLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGlargFSENPGE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPY--------FNE-------PP---------LK 522
Cdd:cd07857 162 NAGFMTEYVATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRKPVFkgkdyvdqLNQilqvlgtPDeetlsrigsPK 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  523 AMKMIRD-NLPPRLK---NLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLA 573
Cdd:cd07857 242 AQNYIRSlPNIPKKPfesIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLA 296
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
319-572 6.96e-22

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: 96.18  E-value: 6.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  319 SYLdNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELL-FNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd07870   1 SYL-NLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTaIREASLLKGLKHANIVLLHDIIHTKETLTFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEVPRR--KS 474
Cdd:cd07870  80 MHTDLAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAR--AKSIPSQtySS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNEPPLKAMKM-------IRDN-------------- 530
Cdd:cd07870 158 EVVTLWYRPPDvLLGATDYSSALDIWGAGCIFIEMLQGQPafPGVSDVFEQLEKIwtvlgvpTEDTwpgvsklpnykpew 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 5031975  531 -LPPRLKNLHKV------SPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07870 238 fLPCKPQQLRVVwkrlsrPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
334-572 7.51e-22

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 96.94  E-value: 7.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  334 IVCIATVRSSGKLVAVKKMDLRKQQRRELLF--NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD-IVTHT 410
Cdd:cd08227  15 TVNLARYKPTGEYVTVRRINLEACTNEMVTFlqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDlICTHF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  411 R--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLS---------DFGFCAQVSKEVPRRKSLVgTP 479
Cdd:cd08227  95 MdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsnlsmiNHGQRLRVVHDFPKYSVKV-LP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 yWMAPELISR--LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK------------------------AMKMIRD---- 529
Cdd:cd08227 174 -WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQmlleklngtvpclldtttipaeelTMKPSRSgans 252
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031975  530 --------------NLPPRLKNLHKV-SPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd08227 253 glgesttvstprpsNGESSSHPYNRTfSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 310
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
350-571 8.18e-22

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 95.46  E-value: 8.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  350 KKMDLRKQQRRELlfnevVIMRDYQHENVVEMYNSYLVG-DELWVVMEFLEGGAL-TDIVTHTRMNEEQIAAVCLAVLQA 427
Cdd:cd13990  43 KKQNYIKHALREY-----EIHKSLDHPRIVKLYDVFEIDtDSFCTVLEYCDGNDLdFYLKQHKSIPEREARSIIMQVVSA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  428 LSVL--HAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSKEVPRRKSL------VGTPYWMAPELISRLPYGP-- 494
Cdd:cd13990 118 LKYLneIKPPIIHYDLKPGNILLHSGnvsGEIKITDFGLSKIMDDESYNSDGMeltsqgAGTYWYLPPECFVVGKTPPki 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  495 --EVDIWSLGIMVIEMVDGEPPY----------FNEPPLKAMKMIRDNLPprlknlhKVSPSLKGFLDRLLVRDPAQRAT 562
Cdd:cd13990 198 ssKVDVWSVGVIFYQMLYGRKPFghnqsqeailEENTILKATEVEFPSKP-------VVSSEAKDFIRRCLTYRKEDRPD 270

                ....*....
gi 5031975  563 AAELLKHPF 571
Cdd:cd13990 271 VLQLANDPY 279
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
327-571 1.44e-21

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 95.04  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGD-----ELWVVMEFLEG 400
Cdd:cd14037  11 LAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYIDSSANRSgngvyEVLLLMEYCKG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVT---HTRMNEEQIAAVCLAVLQALSVLHA--QGVIHRDIKSDSILLTHDGRVKLSDFGF-------------C 462
Cdd:cd14037  91 GGVIDLMNqrlQTGLTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGSattkilppqtkqgV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  463 AQVSKEVPRRKslvgTPYWMAPELI---SRLPYGPEVDIWSLGIMVIEMVdgeppYFNEP-----PLkAMKMIRDNLPPr 534
Cdd:cd14037 171 TYVEEDIKKYT----TLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLC-----FYTTPfeesgQL-AILNGNFTFPD- 239
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 5031975  535 lknLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14037 240 ---NSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
326-575 2.24e-21

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 95.50  E-value: 2.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd06649  12 ELGAGNGGVVTKVQHKPSGLIMARKLIHLEiKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHT-RMNEEQIAAVCLAVLQALSVLHAQ-GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKSLVGTPYWM 482
Cdd:cd06649  92 QVLKEAkRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA--NSFVGTRSYM 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVDGEPP-----------YFNEPPLKA---------------------------- 523
Cdd:cd06649 170 SPERLQGTHYSVQSDIWSMGLSLVELAIGRYPipppdakeleaIFGRPVVDGeegephsisprprppgrpvsghgmdsrp 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031975  524 -------MKMIRDNLPPRLKNlHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKA 575
Cdd:cd06649 250 amaifelLDYIVNEPPPKLPN-GVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKRS 307
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
327-571 2.28e-21

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: 95.57  E-value: 2.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMdlrkqqRRELLFNEVVIMRDYQHENVVEMYNSY--LVG--------DELWVVME 396
Cdd:cd05588   3 IGRGSYAKVLMVELKKTKRIYAMKVI------KKELVNDDEDIDWVQTEKHVFETASNHpfLVGlhscfqteSRLFFVIE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGaltDIVTHT----RMNEEQI----AAVCLAvlqaLSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE 468
Cdd:cd05588  77 FVNGG---DLMFHMqrqrRLPEEHArfysAEISLA----LNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY----FNEPPLKAM----------KMIRdnlPPR 534
Cdd:cd05588 150 GDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNPDQNTedylfqvileKPIR---IPR 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031975  535 LKNLhKVSPSLKGFLDrllvRDPAQRATA------AELLKHPF 571
Cdd:cd05588 227 SLSV-KAASVLKGFLN----KNPAERLGChpqtgfADIQSHPF 264
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
320-572 2.37e-21

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 93.91  E-value: 2.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSY---LVGDELWV- 393
Cdd:cd14033   2 FLKFNIEIGRGSFKTVYRGLDTETTVEVAWCELQTRKlsKGERQRFSEEVEMLKGLQHPNIVRFYDSWkstVRGHKCIIl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQG--VIHRDIKSDSILLTH-DGRVKLSDFGFCAQvsKEV 469
Cdd:cd14033  82 VTELMTSGTLKTYLKRFReMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLATL--KRA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRRKSLVGTPYWMAPELISRlPYGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPrlKNLHKVS-PSLKG 547
Cdd:cd14033 160 SFAKSVIGTPEFMAPEMYEE-KYDEAVDVYAFGMCILEMATSEYPYSEcQNAAQIYRKVTSGIKP--DSFYKVKvPELKE 236
                       250       260
                ....*....|....*....|....*
gi 5031975  548 FLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14033 237 IIEGCIRTDKDERFTIQDLLEHRFF 261
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
351-572 2.53e-21

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 93.77  E-value: 2.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   351 KMDLRKQQRRELlFNEV-----VIMRDyqHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV-THTRMNEeqiAAVCLAV 424
Cdd:PHA03390  42 KLFVQKIIKAKN-FNAIepmvhQLMKD--NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLkKEGKLSE---AEVKKII 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   425 LQ---ALSVLHAQGVIHRDIKSDSILLT-HDGRVKLSDFGFCaqvsKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWS 500
Cdd:PHA03390 116 RQlveALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLC----KIIGTPSCYDGTLDYFSPEKIKGHNYDVSFDWWA 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975   501 LGIMVIEMVDGEPPYFNEP----PLKAMKMIRDNLPPRLKNlhkVSPSLKGFLDRLLVRDPAQRATA-AELLKHPFL 572
Cdd:PHA03390 192 VGVLTYELLTGKHPFKEDEdeelDLESLLKRQQKKLPFIKN---VSKNANDFVQSMLKYNINYRLTNyNEIIKHPFL 265
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
327-571 4.03e-21

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: 93.66  E-value: 4.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHEN----VVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTGGdcpfIVCMTYAFQTPDKLCFILDLMN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrrKSLVGT 478
Cdd:cd05606  82 GGDLhYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKP--HASVGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PYWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDP 557
Cdd:cd05606 160 HGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDV 239
                       250
                ....*....|....*....
gi 5031975  558 AQR-----ATAAELLKHPF 571
Cdd:cd05606 240 SKRlgclgRGATEVKEHPF 258
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
323-578 4.97e-21

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 95.11  E-value: 4.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  323 NFIKIGEGSTGIVCIATVRSSGKLVAVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVG------DELWVV 394
Cdd:cd07875  28 NLKPIGSGAQGIVCAAYDAILERNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQksleefQDVYIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTdiVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKS 474
Cdd:cd07875 108 MELMDANLCQ--VIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAGTSFMMTP 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY---------------FNEPPLKAMKMIRDNLPPRLKN-- 537
Cdd:cd07875 185 YVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFpgtdhidqwnkvieqLGTPCPEFMKKLQPTVRTYVENrp 264
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975  538 ------LHKVSPSL----------------KGFLDRLLVRDPAQRATAAELLKHPFL--------AKAGPP 578
Cdd:cd07875 265 kyagysFEKLFPDVlfpadsehnklkasqaRDLLSKMLVIDASKRISVDEALQHPYInvwydpseAEAPPP 335
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
327-585 5.03e-21

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: 94.17  E-value: 5.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREllfNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQ---REVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGGELLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRM-NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFGFcaqvSKEVPRRKSLVGTP-- 479
Cdd:cd14180  91 RIKKKARfSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGF----ARLRPQGSRPLQTPcf 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 --YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY-------FNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFL 549
Cdd:cd14180 167 tlQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFqskrgkmFHNHAADIMHKIKEgDFSLEGEAWKGVSEEAKDLV 246
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFLaKAGPPASIVPLM 585
Cdd:cd14180 247 RGLLTVDPAKRLKLSELRESDWL-QGGSALSSTPLM 281
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
320-572 8.40e-21

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: 92.27  E-value: 8.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14108   3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSAR-RELALLAELDHKSIVRFHDAFEKRRVVIIVTELCH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG--RVKLSDFGFCAQVSKEVPRRKSLvG 477
Cdd:cd14108  82 EELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQYCKY-G 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPRLKNLHKVSPSLKGFLDRLLVRD 556
Cdd:cd14108 161 TPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNyNVAFEESMFKDLCREAKGFIIKVLVSD 240
                       250
                ....*....|....*.
gi 5031975  557 PAqRATAAELLKHPFL 572
Cdd:cd14108 241 RL-RPDAEETLEHPWF 255
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
327-570 8.59e-21

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: 93.06  E-value: 8.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVV-------EMynSYLVGDELWVVMEFL 398
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElSVKNKDRWCHEIQIMKKLNHPNVVkacdvpeEM--NFLVNDVPLLAMEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH-DGRV--KLSDFGFcaqvSKEVPR 471
Cdd:cd14039  79 SGGDLRKLLNKPEnccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEiNGKIvhKIIDLGY----AKDLDQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RK---SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF-NEPPLKAMKMIRDNLP--------------- 532
Cdd:cd14039 155 GSlctSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLhNLQPFTWHEKIKKKDPkhifaveemngevrf 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 5031975  533 ----PRLKNLHK--VSPsLKGFLDRLLVRDPAQRATAAEL-LKHP 570
Cdd:cd14039 235 sthlPQPNNLCSliVEP-MEGWLQLMLNWDPVQRGGGLDTdSKQP 278
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
326-515 1.11e-20

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: 91.74  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05041   2 KIGRGNFGDVYRGVLKPDNTEVAVKtcRETLPPDLKRKFL-QEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ-------VS---KEVPR 471
Cdd:cd05041  81 LTFLrkKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedgeytVSdglKQIPI 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031975  472 RkslvgtpyWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05041 161 K--------WTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPY 197
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
391-572 1.20e-20

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: 91.97  E-value: 1.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVTH---TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQ 464
Cdd:cd14172  76 LLIIMECMEGGELFSRIQErgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKE 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  465 VSKEVPRRKSLVgTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFN------EPPLKA-MKMIRDNLPPrlKN 537
Cdd:cd14172 156 TTVQNALQTPCY-TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSntgqaiSPGMKRrIRMGQYGFPN--PE 232
                       170       180       190
                ....*....|....*....|....*....|....*
gi 5031975  538 LHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14172 233 WAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
327-573 1.35e-20

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: 93.02  E-value: 1.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD----LRKQQRRELLFNEVVIMRDYQHEN--VVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSkkviVAKKEVAHTIGERNILVRTALDESpfIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTRMNEEQIAAVCLAVL-QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd05586  81 GELFWHLQKEGRFSEDRAKFYIAELvLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI---RDNLPprlKNLhkVSPSLKGFLDRLLVR 555
Cdd:cd05586 161 EYLAPEvLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIafgKVRFP---KDV--LSDEGRSFVKGLLNR 235
                       250       260
                ....*....|....*....|..
gi 5031975  556 DPAQR----ATAAELLKHPFLA 573
Cdd:cd05586 236 NPKHRlgahDDAVELKEHPFFA 257
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
327-533 1.77e-20

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 91.28  E-value: 1.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGK---LVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05033  12 IGGGEFGEVCSGSLKLPGKkeiDVAIKtlKSGYSDKQRLDFL-TEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTdivTHTRMNEEQIAAVCL-----AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKSLV 476
Cdd:cd05033  91 SLD---KFLRENDGKFTVTQLvgmlrGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFG----LSRRLEDSEATY 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  477 GT-----PY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPYFNEPPLKAMKMIRDN--LPP 533
Cdd:cd05033 164 TTkggkiPIrWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPYWDMSNQDVIKAVEDGyrLPP 229
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
327-585 1.97e-20

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: 92.41  E-value: 1.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRREllfNEVVIMRDYQ-HENVVEMYNSYlvGDEL--WVVMEFLEGGAL 403
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ---REIAALKLCEgHPNIVKLHEVY--HDQLhtFLVMELLKGGEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG---RVKLSDFGFcaqvSKEVPRRKSLVGTP 479
Cdd:cd14179  90 LErIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGF----ARLKPPDNQPLKTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 ----YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNE-------PPLKAMKMIRD-NLPPRLKNLHKVSPSLKG 547
Cdd:cd14179 166 cftlHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQgDFSFEGEAWKNVSQEAKD 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  548 FLDRLLVRDPAQRATAAELLKHPFLaKAGPPASIVPLM 585
Cdd:cd14179 246 LIQGLLTVDPNKRIKMSGLRYNEWL-QDGSQLSSNPLM 282
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
327-515 2.07e-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: 93.17  E-value: 2.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMdlrkqqRRELLFNEVVIMRDYQHENVVEMYNS--YLVG--------DELWVVME 396
Cdd:cd05618  28 IGRGSYAKVLLVRLKKTERIYAMKVV------KKELVNDDEDIDWVQTEKHVFEQASNhpFLVGlhscfqteSRLFFVIE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQIAAVCLAVLQ-ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL 475
Cdd:cd05618 102 YVNGGDLMFHMQRQRKLPEEHARFYSAEISlALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTF 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd05618 182 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
327-515 2.50e-20

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: 90.92  E-value: 2.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVK--KMDLRK--QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14061   2 IGVGGFGKVYRGIWR--GEEVAVKaaRQDPDEdiSVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQG---VIHRDIKSDSILLTH--------DGRVKLSDFGFCAQVSKEVpr 471
Cdd:cd14061  80 LNRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLAREWHKTT-- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  472 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14061 158 RMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
326-538 2.56e-20

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 91.28  E-value: 2.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVciatvrSSGKL---VAVKKMDLR--KQQRRELLFNEVVIMRDYQHENVVeMYNSYLVGDELWVVMEFLEG 400
Cdd:cd14151  15 RIGSGSFGTV------YKGKWhgdVAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDI--VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK--SLV 476
Cdd:cd14151  88 SSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQfeQLS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELI---SRLPYGPEVDIWSLGIMVIEMVDGEPPYFN----------------EPPLKAmkmIRDNLPPRLKN 537
Cdd:cd14151 168 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNinnrdqiifmvgrgylSPDLSK---VRSNCPKAMKR 244

                .
gi 5031975  538 L 538
Cdd:cd14151 245 L 245
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
327-563 2.63e-20

Catalytic domain of Transforming Growth Factor beta Receptor-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 receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-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: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 91.35  E-value: 2.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMDLRKQQRrelLFNEVVIMRD--YQHENVVEmynsYLVGD--------ELWVVME 396
Cdd:cd13998   3 IGKGRFGEVWKASLK--NEPVAVKIFSSRDKQS---WFREKEIYRTpmLKHENILQ----FIAADerdtalrtELWLVTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVI---------HRDIKSDSILLTHDGRVKLSDFG----FCA 463
Cdd:cd13998  74 FHPNGSL*DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIADFGlavrLSP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 QVSKEVPRRKSLVGTPYWMAPELI------SRLPYGPEVDIWSLGIMVIEMV-----------DGEPPYF----NEPPLK 522
Cdd:cd13998 154 STGEEDNANNGQVGTKRYMAPEVLegainlRDFESFKRVDIYAMGLVLWEMAsrctdlfgiveEYKPPFYsevpNHPSFE 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  523 AMKMI--RDNLPPRLKNLHKVSPSLKGF---LDRLLVRDPAQRATA 563
Cdd:cd13998 234 DMQEVvvRDKQRPNIPNRWLSHPGLQSLaetIEECWDHDAEARLTA 279
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
324-568 2.70e-20

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: 90.59  E-value: 2.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  324 FIK-IGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05059   8 FLKeLGSGQFGVVHLGKWRGKID-VAIKMIK-EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGC 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpRRKSLVGTPY 480
Cdd:cd05059  86 LLNYLRERRgkFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDD--EYTSSVGTKF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 ---WMAPELISRLPYGPEVDIWSLGIMVIEM-VDGEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLKGFLDRLLVRD 556
Cdd:cd05059 164 pvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVfSEGKMPYERFSNSEVVEHISQGY--RLYRPHLAPTEVYTIMYSCWHEK 241
                       250
                ....*....|..
gi 5031975  557 PAQRATAAELLK 568
Cdd:cd05059 242 PEERPTFKILLS 253
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
327-569 3.29e-20

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 90.24  E-value: 3.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKlVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGK-VMVMKELKRFDEQRSFL-KEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTH--TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVK---LSDFGFCAQVSKEV---PRRK---SL 475
Cdd:cd14065  79 LKSmdEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDEKtkkPDRKkrlTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEM---VDGEPPY------FNEPPLKAMKMIRDNLPPRLKNLHKVSPSLk 546
Cdd:cd14065 159 VGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIigrVPADPDYlprtmdFGLDVRAFRTLYVPDCPPSFLPLAIRCCQL- 237
                       250       260
                ....*....|....*....|...
gi 5031975  547 gfldrllvrDPAQRATAAELLKH 569
Cdd:cd14065 238 ---------DPEKRPSFVELEHH 251
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
356-569 3.66e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 92.75  E-value: 3.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   356 KQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQG 435
Cdd:PHA03212 123 KAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENR 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   436 VIHRDIKSDSILLTHDGRVKLSDFGF-CAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPP 514
Cdd:PHA03212 203 IIHRDIKAENIFINHPGDVCLGDFGAaCFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDS 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   515 YF--------------------------NEPPLKAMKMIRDNLP-------------PRLKNLHKVSPSLKGFLDRLLVR 555
Cdd:PHA03212 283 LFekdgldgdcdsdrqikliirrsgthpNEFPIDAQANLDEIYIglakkssrkpgsrPLWTNLYELPIDLEYLICKMLAF 362
                        250
                 ....*....|....
gi 5031975   556 DPAQRATAAELLKH 569
Cdd:PHA03212 363 DAHHRPSAEALLDF 376
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
350-574 3.87e-20

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 90.55  E-value: 3.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  350 KKMDLRKQQRREllfNEVVIMRDYQHENVVEMYNSY---LVGDELWV-VMEFLEGGALTDIVTHTR-MNEEQIAAVCLAV 424
Cdd:cd14031  46 RKLTKAEQQRFK---EEAEMLKGLQHPNIVRFYDSWesvLKGKKCIVlVTELMTSGTLKTYLKRFKvMKPKVLRSWCRQI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  425 LQALSVLHAQG--VIHRDIKSDSILLTH-DGRVKLSDFGFCAQVSKEVPrrKSLVGTPYWMAPELISRlPYGPEVDIWSL 501
Cdd:cd14031 123 LKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLMRTSFA--KSVIGTPEFMAPEMYEE-HYDESVDVYAF 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  502 GIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPrlKNLHKVS-PSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd14031 200 GMCMLEMATSEYPYSEcQNAAQIYRKVTSGIKP--ASFNKVTdPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
326-543 3.95e-20

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 90.86  E-value: 3.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVeMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14149  19 RIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFR-NEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYK 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 I--VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK--SLVGTPYW 481
Cdd:cd14149  97 HlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQveQPTGSILW 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  482 MAPELI---SRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPLKAMKMIRDNLPPRLKNLHKVSP 543
Cdd:cd14149 177 MAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYshINNRDQIIFMVGRGYASPDLSKLYKNCP 243
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
326-571 4.00e-20

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 91.58  E-value: 4.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIA--TVRSSGKLVAVKKMDLRKQQRREL---LFNEVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFL 398
Cdd:cd07842   7 CIGRGTYGRVYKAkrKNGKDGKEYAIKKFKGDKEQYTGIsqsACREIALLRELKHENVVSLVEVFLEHADksVYLLFDYA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTRMNEEQIAAVCL-----AVLQALSVLHAQGVIHRDIKSDSILLTHD----GRVKLSDFGF---CAQVS 466
Cdd:cd07842  87 EHDLWQIIKFHRQAKRVSIPPSMVksllwQILNGIHYLHSNWVLHRDLKPANILVMGEgperGVVKIGDLGLarlFNAPL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVPRRKSLVGTPYWMAPELI--SRlPYGPEVDIWSLGIMVIEMVDGEPPYFNEP-------PLKAMKMIR--------- 528
Cdd:cd07842 167 KPLADLDPVVVTIWYRAPELLlgAR-HYTKAIDIWAIGCIFAELLTLEPIFKGREakikksnPFQRDQLERifevlgtpt 245
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975  529 --------------------------DNLPPRLKNLHKvSPSLKGF--LDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07842 246 ekdwpdikkmpeydtlksdtkastypNSLLAKWMHKHK-KPDSQGFdlLRKLLEYDPTKRITAEEALEHPY 315
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
327-502 4.22e-20

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 90.65  E-value: 4.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVG--------DELWVVMEF 397
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGkeesdqgqAEYLLLTEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGaLTDIVTHTR----MNEEQIAAVCLAVLQALSVLHAQG--VIHRDIKSDSILLTHDGRVKLSDFGFC--------- 462
Cdd:cd14036  88 CKGQ-LVDFVKKVEapgpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSAtteahypdy 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  463 -------AQVSKEVPRrkslVGTPYWMAPELI---SRLPYGPEVDIWSLG 502
Cdd:cd14036 167 swsaqkrSLVEDEITR----NTTPMYRTPEMIdlySNYPIGEKQDIWALG 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
328-572 6.96e-20

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: 89.51  E-value: 6.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  328 GEGSTGIVCIATVRSSGKLVAVKKMDLRKQQrrELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV 407
Cdd:cd14112  14 GRFSVIVKAVDSTTETDAHCAVKIFEVSDEA--SEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQEDVFTRFS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  408 THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT--HDGRVKLSDFGFCAQVSKEVprRKSLVGTPYWMAPE 485
Cdd:cd14112  92 SNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKVSKLG--KVPVDGDTDWASPE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  486 LI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAmkMIRDNL---PPRLKNLHK-VSPSLKGFLDRLLVRDPAQR 560
Cdd:cd14112 170 FHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEE--ETKENVifvKCRPNLIFVeATQEALRFATWALKKSPTRR 247
                       250
                ....*....|..
gi 5031975  561 ATAAELLKHPFL 572
Cdd:cd14112 248 MRTDEALEHRWL 259
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
326-572 7.79e-20

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: 90.02  E-value: 7.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKkmDLRKQQRRELL----FNEVVIMR---DYQHENVVEMYN---SYLVGDELWVVM 395
Cdd:cd07863   7 EIGVGAYGTVYKARDPHSGHFVALK--SVRVQTNEDGLplstVREVALLKrleAFDHPNIVRLMDvcaTSRTDRETKVTL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EF----LEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 471
Cdd:cd07863  85 VFehvdQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMAL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKSLVgTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEP--------------------PYFNEPPLKaMKMIRDNL 531
Cdd:cd07863 165 TPVVV-TLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPlfcgnseadqlgkifdliglPPEDDWPRD-VTLPRGAF 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  532 PPRL-KNLHKVSPSL--KG--FLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07863 243 SPRGpRPVQSVVPEIeeSGaqLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
327-569 9.68e-20

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: 89.55  E-value: 9.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDL-RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVG---------DE--LWVV 394
Cdd:cd14048  14 LGRGGFGVVFEAKNKVDDCNYAVKRIRLpNNELAREKVLREVRALAKLDHPGIVRYFNAWLERppegwqekmDEvyLYIQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQ----ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP 470
Cdd:cd14048  94 MQLCRKENLKDWMNRRCTMESRELFVCLNIFKqiasAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTAMDQGEP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  471 RRKSL------------VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVdgeppyfnEPPLKAMKMIRD-------NL 531
Cdd:cd14048 174 EQTVLtpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI--------YSFSTQMERIRTltdvrklKF 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  532 PPRLKNLHkvsPSLKGFLDRLLVRDPAQRATAAELLKH 569
Cdd:cd14048 246 PALFTNKY---PEERDMVQQMLSPSPSERPEAHEVIEH 280
pknD PRK13184
serine/threonine-protein kinase PknD;
326-568 2.81e-19

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 92.14  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   326 KIGEGSTGIVCIATVRSSGKLVAVKKM--DLRKQQR-RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:PRK13184   9 LIGKGGMGEVYLAYDPVCSRRVALKKIreDLSENPLlKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   403 LTDIVTHTRMNE---------EQIAA---VCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcAQVSKE-- 468
Cdd:PRK13184  89 LKSLLKSVWQKEslskelaekTSVGAflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG--AAIFKKle 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   469 --------VPRRKSL----------VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDN 530
Cdd:PRK13184 167 eedlldidVDERNICyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRK---KGRKISYRD 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 5031975   531 --LPPRLKNLHK-VSPSLKGFLDRLLVRDPAQRATAAELLK 568
Cdd:PRK13184 244 viLSPIEVAPYReIPPFLSQIAMKALAVDPAERYSSVQELK 284
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
327-509 3.87e-19

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 87.19  E-value: 3.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK--KMDLRkqqrRELLFNEVVIMRDYQHENVVEmYNSYLVGDE-LWVVMEFLEGGAL 403
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKiyKNDVD----QHKIVREISLLQKLSHPNIVR-YLGICVKDEkLHPILEYVSGGCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTRMN---EEQIAAVClAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVK---LSDFGFcAQVSKEVP-----RR 472
Cdd:cd14156  76 EELLAREELPlswREKVELAC-DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGL-AREVGEMPandpeRK 153
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV 509
Cdd:cd14156 154 LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
325-517 3.91e-19

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 87.31  E-value: 3.91e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKlVAVKKmdLRKQQRRELLF-NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 403
Cdd:cd05112  10 QEIGSGQFGLVHLGYWLNKDK-VAIKT--IREGAMSEEDFiEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpRRKSLVGTPY- 480
Cdd:cd05112  87 SDYLRTQRglFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD--QYTSSTGTKFp 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 5031975  481 --WMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPYFN 517
Cdd:cd05112 165 vkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFsEGKIPYEN 204
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
327-572 3.93e-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: 88.97  E-value: 3.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHEN---VVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05633  13 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMNG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRrkSLVGTP 479
Cdd:cd05633  93 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPH--ASVGTH 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPA 558
Cdd:cd05633 171 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVS 250
                       250
                ....*....|....*....
gi 5031975  559 QR-----ATAAELLKHPFL 572
Cdd:cd05633 251 KRlgchgRGAQEVKEHSFF 269
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
327-519 6.30e-19

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 86.64  E-value: 6.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd05039  14 IGKGEFGDVMLGDYR--GQKVAVKCLK-DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVDY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VtHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGtpyWM 482
Cdd:cd05039  91 L-RSRgravITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQDGGKLPIK---WT 166
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEP 519
Cdd:cd05039 167 APEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIP 204
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
326-571 9.34e-19

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 87.21  E-value: 9.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK---KMDLRKQQRrellfnEVVIMRDYQ-HENVVEMYNsyLVGDELW----VVMEF 397
Cdd:cd14132  25 KIGRGKYSEVFEGINIGNNEKVVIKvlkPVKKKKIKR------EIKILQNLRgGPNIVKLLD--VVKDPQSktpsLIFEY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGgalTDIVT-HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR-VKLSDFGFcAQV---SKEVPRR 472
Cdd:cd14132  97 VNN---TDFKTlYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGL-AEFyhpGQEYNVR 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 kslVGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEPPYFN-----------------EPPLKAMKMIRDNLPPR 534
Cdd:cd14132 173 ---VASRYYKGPELLVDYQyYDYSLDMWSLGCMLASMIFRKEPFFHghdnydqlvkiakvlgtDDLYAYLDKYGIELPPR 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  535 LKNL------------------HKVSPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14132 250 LNDIlgrhskkpwerfvnsenqHLVTPEALDLLDKLLRYDHQERITAKEAMQHPY 304
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
318-527 1.11e-18

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: 86.49  E-value: 1.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  318 RSYLDNFIKIGEGSTGIVCI----ATVRSSGKLVAVKKMDLR-KQQRRELLFNEVVIMRDYQHENVVEMYN--SYLVGDE 390
Cdd:cd05080   3 KRYLKKIRDLGEGHFGKVSLycydPTNDGTGEMVAVKALKADcGPQHRSGWKQEIDILKTLYHENIVKYKGccSEQGGKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVP 470
Cdd:cd05080  83 LQLIMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFG----LAKAVP 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031975  471 ------RRKSLVGTP-YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYfNEPPLKAMKMI 527
Cdd:cd05080 159 egheyyRVREDGDSPvFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSS-QSPPTKFLEMI 221
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
326-578 1.31e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 90.18  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLR--KQQRRELLFNEVVIMRDYQHENVVEMYNSYL--VGDELWVVMEFLEGG 401
Cdd:PTZ00266   20 KIGNGRFGEVFLVKHKRTQEFFCWKAISYRglKEREKSQLVIEVNVMRELKHKNIVRYIDRFLnkANQKLYILMEFCDAG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    402 ALTDIVTHT-----RMNEEQIAAVCLAVLQALSVLH-------AQGVIHRDIKSDSILLT----HDGRV----------- 454
Cdd:PTZ00266  100 DLSRNIQKCykmfgKIEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLStgirHIGKItaqannlngrp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975    455 --KLSDFGFCAQVSKEvPRRKSLVGTPYWMAPELI--SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM--KMIR 528
Cdd:PTZ00266  180 iaKIGDFGLSKNIGIE-SMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQLisELKR 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5031975    529 D-NLPPRLKnlhkvSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPP 578
Cdd:PTZ00266  259 GpDLPIKGK-----SKELNILIKNLLNLSAKERPSALQCLGYQIIKNVGPP 304
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
326-513 1.46e-18

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: 86.24  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIA-TVRSSGKLVAVKKMDLRKQQRRELL--FNEVVIMR---DYQHENVVEMYNSYLVG-----DELWVV 394
Cdd:cd07862   8 EIGEGAYGKVFKArDLKNGGRFVALKRVRVQTGEEGMPLstIREVAVLRhleTFEHPNVVRLFDVCTVSrtdreTKLTLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALT--DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrR 472
Cdd:cd07862  88 FEHVDQDLTTylDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMA-L 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEP 513
Cdd:cd07862 167 TSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKP 207
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
326-571 1.51e-18

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: 86.43  E-value: 1.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKK----MD--------LRKQQRRELLFNEVVIMRDYQHENVVEMYNSylvgdELWV 393
Cdd:cd07837   8 KIGEGTYGKVYKARDKNTGKLVALKKtrleMEeegvpstaLREVSLLQMLSQSIYIVRLLDVEHVEENGKP-----LLYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTRMNEEQIAAVCLA-----VLQALSVLHAQGVIHRDIKSDSILLTHD-GRVKLSDFGFCAQVSK 467
Cdd:cd07837  83 VFEYLDTDLKKFIDSYGRGPHNPLPAKTIQsfmyqLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLGRAFTI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 EVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYF------------------NEPPLKAMKMIR 528
Cdd:cd07837 163 PIKSYTHEIVTLWYRAPEvLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPgdselqqllhifrllgtpNEEVWPGVSKLR 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  529 D-NLPPRLK--NLHKVSPSLK----GFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd07837 243 DwHEYPQWKpqDLSRAVPDLEpegvDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
326-576 1.73e-18

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: 86.21  E-value: 1.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELL-FNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEggalT 404
Cdd:cd07873   9 KLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD----K 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTH-----TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEVPRR--KSLVG 477
Cdd:cd07873  85 DLKQYlddcgNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR--AKSIPTKtySNEVV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI--------RDNLPPRLKN----------- 537
Cdd:cd07873 163 TLWYRPPDiLLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIfrilgtptEETWPGILSNeefksynypky 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  538 ----LHKVSPSLKG----FLDRLLVRDPAQRATAAELLKHPFLAKAG 576
Cdd:cd07873 243 radaLHNHAPRLDSdgadLLSKLLQFEGRKRISAEEAMKHPYFHSLG 289
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
326-576 2.12e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 86.03  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   326 KIGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRE----LLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEgg 401
Cdd:PLN00009   9 KIGEGTYGVVYKARDRVTNETIALKK--IRLEQEDEgvpsTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLD-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   402 alTDIVTHT------RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLthDGR---VKLSDFGFCAQVSKEVPRR 472
Cdd:PLN00009  85 --LDLKKHMdsspdfAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLI--DRRtnaLKLADFGLARAFGIPVRTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   473 KSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNE-------------------PPLKAMKMIRDN 530
Cdd:PLN00009 161 THEVVTLWYRAPEiLLGSRHYSTPVDIWSVGCIFAEMVNQKPlfPGDSEidelfkifrilgtpneetwPGVTSLPDYKSA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 5031975   531 LPP-RLKNLHKVSPSLK----GFLDRLLVRDPAQRATAAELLKHPFLAKAG 576
Cdd:PLN00009 241 FPKwPPKDLATVVPTLEpagvDLLSKMLRLDPSKRITARAALEHEYFKDLG 291
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
327-515 3.33e-18

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: 84.70  E-value: 3.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKM----DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14147  11 IGIGGFGKVYRGSWR--GELVAVKAArqdpDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQG---VIHRDIKSDSILLTHDGR--------VKLSDFGFCAQVSKEVpr 471
Cdd:cd14147  89 LSRALAGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIEnddmehktLKITDFGLAREWHKTT-- 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  472 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14147 167 QMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
318-583 3.35e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 87.40  E-value: 3.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   318 RSY-LDNFIkiGEGSTGIVCIATVRSSGKLVAVKKMdLRKQQRREllfNEVVIMRDYQHENVVEMYNSYLV----GDE-- 390
Cdd:PTZ00036  66 KSYkLGNII--GNGSFGVVYEAICIDTSEKVAIKKV-LQDPQYKN---RELLIMKNLNHINIIFLKDYYYTecfkKNEkn 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   391 --LWVVMEFLEGGALTDIVTHTRMNEEQ----IAAVCLAVLQALSVLHAQGVIHRDIKSDSILL---THDgrVKLSDFGf 461
Cdd:PTZ00036 140 ifLNVVMEFIPQTVHKYMKHYARNNHALplflVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIdpnTHT--LKLCDFG- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   462 CAQVSKEVPRRKSLVGTPYWMAPEL-ISRLPYGPEVDIWSLGIMVIEMVDGEPPY---------------FNEPPLKAMK 525
Cdd:PTZ00036 217 SAKNLLAGQRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFsgqssvdqlvriiqvLGTPTEDQLK 296
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975   526 MIRDN-----LPP-RLKNLHKVSPslKG-------FLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVP 583
Cdd:PTZ00036 297 EMNPNyadikFPDvKPKDLKKVFP--KGtpddainFISQFLKYEPLKRLNPIEALADPFFDDLRDPCIKLP 365
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
327-572 3.73e-18

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 85.91  E-value: 3.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFnEVVIM-------RDYQHeNVVEMYNSYLVGDELWVVMEFLe 399
Cdd:cd14225  51 IGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALV-EVKILdalrrkdRDNSH-NVIHMKEYFYFRNHLCITFELL- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTRMNEEQIAAV---CLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSKEVprrKS 474
Cdd:cd14225 128 GMNLYELIKKNNFQGFSLSLIrrfAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSSCYEHQRV---YT 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNEPPLKAMKMIRDNLPP----------RL------- 535
Cdd:cd14225 205 YIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPlfPGENEVEQLACIMEVLGLPPpelienaqrrRLffdskgn 284
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  536 -KNL-----HKVSPSLK--------------GFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14225 285 pRCItnskgKKRRPNSKdlasalktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
327-515 3.94e-18

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: 84.27  E-value: 3.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMDLRKQQ----RRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14148   2 IGVGGFGKVYKGLWR--GEEVAVKAARQDPDEdiavTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQG---VIHRDIKSDSILLTH--------DGRVKLSDFGFCAQVSKEVpr 471
Cdd:cd14148  80 LNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDFGLAREWHKTT-- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  472 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14148 158 KMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
326-517 4.35e-18

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 84.30  E-value: 4.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVciatvrSSGKL---VAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVeMYNSYLVGDELWVVMEFLEG 400
Cdd:cd14150   7 RIGTGSFGTV------FRGKWhgdVAVKILKVTEPTPEQLqaFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDI--VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLtHDG-RVKLSDFGFCAQVSK-------EVP 470
Cdd:cd14150  80 SSLYRHlhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFL-HEGlTVKIGDFGLATVKTRwsgsqqvEQP 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031975  471 RrkslvGTPYWMAPELIsRL----PYGPEVDIWSLGIMVIEMVDGEPPYFN 517
Cdd:cd14150 159 S-----GSILWMAPEVI-RMqdtnPYSFQSDVYAYGVVLYELMSGTLPYSN 203
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
327-566 4.65e-18

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk 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: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 84.26  E-value: 4.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVK--KMDLRKQQrrelLFNEVVIMRDYQHENVVEMYnSYLVGDE--LWVVMEFLEGGA 402
Cdd:cd05082  14 IGKGEFGDVMLGDYR--GNKVAVKciKNDATAQA----FLAEASVMTQLRHSNLVQLL-GVIVEEKggLYIVTEYMAKGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVT---HTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKSLVGTP 479
Cdd:cd05082  87 LVDYLRsrgRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFG----LTKEASSTQDTGKLP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 Y-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYfnepPLKAMKmirdNLPPRLKNLHKVS------PSLKGFLDR 551
Cdd:cd05082 163 VkWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY----PRIPLK----DVVPRVEKGYKMDapdgcpPAVYDVMKN 234
                       250
                ....*....|....*
gi 5031975  552 LLVRDPAQRATAAEL 566
Cdd:cd05082 235 CWHLDAAMRPSFLQL 249
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
327-572 5.13e-18

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: 85.48  E-value: 5.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHEN---VVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTGDcpfIVCMSYAFHTPDKLSFILDLMNG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GAL-TDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRrkSLVGTP 479
Cdd:cd14223  88 GDLhYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPH--ASVGTH 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  480 YWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPA 558
Cdd:cd14223 166 GYMAPEVLQKgVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVN 245
                       250
                ....*....|....*....
gi 5031975  559 QR-----ATAAELLKHPFL 572
Cdd:cd14223 246 RRlgcmgRGAQEVKEEPFF 264
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
327-515 6.83e-18

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: 83.93  E-value: 6.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKM----DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14146   2 IGVGGFGKVYRATWK--GQEVAVKAArqdpDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHT----------RMNEEQIAAVCLAVLQALSVLHAQGV---IHRDIKSDSILL----THDG----RVKLSDFGF 461
Cdd:cd14146  80 LNRALAAAnaapgprrarRIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLlekiEHDDicnkTLKITDFGL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5031975  462 CAQVSKEVprRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14146 160 AREWHRTT--KMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
389-588 8.14e-18

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 86.21  E-value: 8.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  389 DELWVVMEFLEGGALTDIVTHTRM-NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL-THDGRVKLSDFGFCAQVS 466
Cdd:COG5752 111 QRLYLVQEFIEGQTLAQELEKKGVfSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANIIRrRSDGKLVLIDFGVAKLLT 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 -KEVPRRKSLVGTPYWMAPELISRLPYgPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMKMI-RDNLPPRlknlHKVSPS 544
Cdd:COG5752 191 iTALLQTGTIIGTPEYMAPEQLRGKVF-PASDLYSLGVTCIYLLTGVSP-FDLFDVSEDRWVwRDFLPPG----TKVSDR 264
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031975  545 LKGFLDRLLVRDPAQR-ATAAELLK-----HPFLAKAGPPA-SIVPLMRQN 588
Cdd:COG5752 265 LGQILDKLLQNALKQRyQSATEVLQalkrqPPVSYSPIPVApTKLPIQAQP 315
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
317-528 8.21e-18

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 83.54  E-value: 8.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMyNSYLVGDELWVVME 396
Cdd:cd05073   9 PRESLKLEKKLGAGQFGEVWMATYNKHTK-VAVKTMK-PGSMSVEAFLAEANVMKTLQHDKLVKL-HAVVTKEPIYIITE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQIAAV---CLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRR 472
Cdd:cd05073  86 FMAKGSLLDFLKSDEGSKQPLPKLidfSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEdNEYTAR 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYfnePPLKAMKMIR 528
Cdd:cd05073 166 EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY---PGMSNPEVIR 219
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
326-510 8.72e-18

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 84.53  E-value: 8.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ--HENVVEMYNSYLVGDE------------- 390
Cdd:cd13977   7 EVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQrqHPNVIQLEECVLQRDGlaqrmshgssksd 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 -----------------------LWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL 447
Cdd:cd13977  87 lylllvetslkgercfdprsacyLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNIL 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031975  448 LTHdGR----VKLSDFGFCAQVSKEVPRRK-----------SLVGTPYWMAPElISRLPYGPEVDIWSLGIMVIEMVD 510
Cdd:cd13977 167 ISH-KRgepiLKVADFGLSKVCSGSGLNPEepanvnkhflsSACGSDFYMAPE-VWEGHYTAKADIFALGIIIWAMVE 242
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
342-527 9.50e-18

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: 83.91  E-value: 9.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  342 SSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYN-SYLVG-DELWVVMEFLEGGALTDIVT--HTRMNEEQI 417
Cdd:cd14205  31 NTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGvCYSAGrRNLRLIMEYLPYGSLRDYLQkhKERIDHIKL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  418 AAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKSL--VGTP-----YWMAPELISRL 490
Cdd:cd14205 111 LQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFG----LTKVLPQDKEYykVKEPgespiFWYAPESLTES 186
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031975  491 PYGPEVDIWSLGIMVIEMVDgeppyFNE----PPLKAMKMI 527
Cdd:cd14205 187 KFSVASDVWSFGVVLYELFT-----YIEksksPPAEFMRMI 222
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
325-574 9.83e-18

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 83.59  E-value: 9.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDE----LWVVMEFL 398
Cdd:cd14032   7 IELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKveRQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQG--VIHRDIKSDSILLTH-DGRVKLSDFGFCAQvsKEVPRRKS 474
Cdd:cd14032  87 TSGTLKTYLKRFKvMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL--KRASFAKS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRlPYGPEVDIWSLGIMVIEMVDGEPPYfnEPPLKAMKMIRDNL----PPRLKNLHkvSPSLKGFLD 550
Cdd:cd14032 165 VIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLEMATSEYPY--SECQNAAQIYRKVTcgikPASFEKVT--DPEIKEIIG 239
                       250       260
                ....*....|....*....|....
gi 5031975  551 RLLVRDPAQRATAAELLKHPFLAK 574
Cdd:cd14032 240 ECICKNKEERYEIKDLLSHAFFAE 263
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
327-533 1.93e-17

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 82.61  E-value: 1.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGK---LVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05065  12 IGAGEFGEVCRGRLKLPGKreiFVAIKtlKSGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVthtRMNEEQIAAVCL-----AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA--QVSKEVPRRKS 474
Cdd:cd05065  91 ALDSFL---RQNDGQFTVIQLvgmlrGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRflEDDTSDPTYTS 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  475 LVGTPY---WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPYFNEPPLKAMKMIRDN--LPP 533
Cdd:cd05065 168 SLGGKIpirWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWDMSNQDVINAIEQDyrLPP 232
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
326-572 1.93e-17

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: 83.14  E-value: 1.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELL-FNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGaLT 404
Cdd:cd07871  12 KLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDSD-LK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTH--TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEVPRR--KSLVGTPY 480
Cdd:cd07871  91 QYLDNcgNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLAR--AKSVPTKtySNEVVTLW 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 WMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNE---------------------PPLKAMKMIRDNLPP--RLK 536
Cdd:cd07871 169 YRPPDvLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGStvkeelhlifrllgtpteetwPGVTSNEEFRSYLFPqyRAQ 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5031975  537 NLHKVSPSLKG----FLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07871 249 PLINHAPRLDTdgidLLSSLLLYETKSRISAEAALRHSYF 288
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
324-568 2.34e-17

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: 82.22  E-value: 2.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  324 FIK-IGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05114   8 FMKeLGSGLFGVVRLGKWRAQYK-VAIKAIR-EGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGC 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR--MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd05114  86 LLNYLRQRRgkLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKFPV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  481 -WMAPELISRLPYGPEVDIWSLGIMVIEM-VDGEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLKGFLDRLLVRDPA 558
Cdd:cd05114 166 kWSPPEVFNYSKFSSKSDVWSFGVLMWEVfTEGKMPFESKSNYEVVEMVSRGH--RLYRPKLASKSVYEVMYSCWHEKPE 243
                       250
                ....*....|
gi 5031975  559 QRATAAELLK 568
Cdd:cd05114 244 GRPTFADLLR 253
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
10-55 3.21e-17

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 75.38  E-value: 3.21e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 5031975   10 EISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESArRPKPLVD 55
Cdd:cd01093   2 EISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSG-ITKEEQK 46
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
326-566 3.65e-17

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 81.70  E-value: 3.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRS--SGKL-VAVK--KMDLrKQQRRELLFNEVVIMRDYQHENVVEmynsyLVG----DELWVVME 396
Cdd:cd05056  13 CIGEGQFGDVYQGVYMSpeNEKIaVAVKtcKNCT-SPSVREKFLQEAYIMRQFDHPHIVK-----LIGviteNPVWIVME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVThTRMNEEQIAAVCLAVLQ---ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRK 473
Cdd:cd05056  87 LAPLGELRSYLQ-VNKYSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPYFNEPPLKAMKMI----RDNLPPrlknlhKVSPSLKG 547
Cdd:cd05056 166 SKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMLGVKPFQGVKNNDVIGRIengeRLPMPP------NCPPTLYS 239
                       250
                ....*....|....*....
gi 5031975  548 FLDRLLVRDPAQRATAAEL 566
Cdd:cd05056 240 LMTKCWAYDPSKRPRFTEL 258
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
327-516 4.82e-17

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk 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: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 81.74  E-value: 4.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRS-----SGKLVAVKKM------DLRKQQRREllfneVVIMRDYQHENVVEMYNSYLVGDELWVVM 395
Cdd:cd05049  13 LGEGAFGKVFLGECYNlepeqDKMLVAVKTLkdasspDARKDFERE-----AELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDI---------------VTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG 460
Cdd:cd05049  88 EYMEHGDLNKFlrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFG 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  461 FCAQV----------SKEVPRRkslvgtpyWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYF 516
Cdd:cd05049 168 MSRDIystdyyrvggHTMLPIR--------WMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWF 226
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
327-515 5.17e-17

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 80.82  E-value: 5.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKlVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGalt 404
Cdd:cd05085   4 LGKGNFGEVYKGTLKDKTP-VAVKtcKEDLPQELKIKFL-SEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 479
Cdd:cd05085  79 DFLSFLRkkkdeLKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQIP 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5031975  480 Y-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05085 159 IkWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPY 196
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
327-515 5.42e-17

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 80.98  E-value: 5.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKlVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI 406
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQ-VMALKMNTLSSNRANML-REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  407 VTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFGFCAQVSKEVPRRKSL--VGTPY 480
Cdd:cd14155  79 LDSNEpLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLAEKIPDYSDGKEKLavVGSPY 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEM---VDGEPPY 515
Cdd:cd14155 159 WMAPEVLRGEPYNEKADVFSYGIILCEIiarIQADPDY 196
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
321-538 6.02e-17

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: 81.24  E-value: 6.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  321 LDNFIKIGEGSTGIVCIAtvRSSGKlVAVK--KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRG--RWHGD-VAIKllNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLtHDGRVKLSDFGFCAQVSKEVPRRK--S 474
Cdd:cd14063  79 KGRTLYSLIheRKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGLFSLSGLLQPGRRedT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYW---MAPELI----------SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPP-------LKAMKMIRDNL--P 532
Cdd:cd14063 158 LVIPNGWlcyLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAesiiwqvGCGKKQSLSQLdiG 237

                ....*.
gi 5031975  533 PRLKNL 538
Cdd:cd14063 238 REVKDI 243
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
326-572 6.75e-17

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: 81.27  E-value: 6.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKkmDLRKQQRRELLFN---EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEgga 402
Cdd:cd07844   7 KLGEGSYATVYKGRSKLTGQLVALK--EIRLEHEEGAPFTairEASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 lTDIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEVPRR--KSL 475
Cdd:cd07844  82 -TDLKQYMDdcgggLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR--AKSVPSKtySNE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYfnepplKAMKMIRDNL----------------------- 531
Cdd:cd07844 159 VVTLWYRPPDvLLGSTEYSTSLDMWGVGCIFYEMATGRPLF------PGSTDVEDQLhkifrvlgtpteetwpgvssnpe 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  532 ---------PPRlkNLHKVSPSLKG------FLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07844 233 fkpysfpfyPPR--PLINHAPRLDRiphgeeLALKFLQYEPKKRISAAEAMKHPYF 286
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
344-515 6.98e-17

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: 80.86  E-value: 6.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  344 GKLVAVKKM----DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAA 419
Cdd:cd14145  29 GDEVAVKAArhdpDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVN 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  420 VCLAVLQALSVLHAQG---VIHRDIKSDSILLTH--------DGRVKLSDFGFCAQVSKEVprRKSLVGTPYWMAPELIS 488
Cdd:cd14145 109 WAVQIARGMNYLHCEAivpVIHRDLKSSNILILEkvengdlsNKILKITDFGLAREWHRTT--KMSAAGTYAWMAPEVIR 186
                       170       180
                ....*....|....*....|....*..
gi 5031975  489 RLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14145 187 SSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
326-562 7.00e-17

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: 81.55  E-value: 7.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKK----MDLRKQQRRELlfnEVVIMRDYQHENVV------EMYNSYLVGDELWVVM 395
Cdd:cd14038   1 RLGTGGFGNVLRWINQETGEQVAIKQcrqeLSPKNRERWCL---EIQIMKRLNHPNVVaardvpEGLQKLAPNDLPLLAM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH-DGRV--KLSDFGFcaqvSKE 468
Cdd:cd14038  78 EYCQGGDLRKYLNQFEnccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgEQRLihKIIDLGY----AKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRK---SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF-NEPPLKAMKMIR----------DNLP-- 532
Cdd:cd14038 154 LDQGSlctSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLpNWQPVQWHGKVRqksnedivvyEDLTga 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  533 -------PRLKNLHKV-SPSLKGFLDRLLVRDPAQRAT 562
Cdd:cd14038 234 vkfssvlPTPNNLNGIlAGKLERWLQCMLMWHPRQRGT 271
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
327-524 7.03e-17

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: 80.96  E-value: 7.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKM--DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLhsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTRMNEE-----QIAavcLAVLQALSVLH--AQGVIHRDIKSDSILLTHDGRVKLSDFGF--CAQVSKEVPRR--- 472
Cdd:cd13978  81 SLLEREIQDVPwslrfRII---HEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLskLGMKSISANRRrgt 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEV--DIWSLGIMVIEMVDGEPPYFNEP-PLKAM 524
Cdd:cd13978 158 ENLGGTPIYMAPEAFDDFNKKPTSksDVYSFAIVIWAVLTRKEPFENAInPLLIM 212
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
374-504 7.47e-17

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 80.61  E-value: 7.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  374 QHENVVEMYNS-----YLVGDELWV--VMEFLEGGALTDIVTHTRMNEE-QIAavcLAVLQALSVLHAQGVIHRDIKSDS 445
Cdd:cd13975  56 KHERIVSLHGSvidysYGGGSSIAVllIMERLHRDLYTGIKAGLSLEERlQIA---LDVVEGIRFLHSQGLVHRDIKLKN 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031975  446 ILLTHDGRVKLSDFGFCaqvSKEVPRRKSLVGTPYWMAPELISRlPYGPEVDIWSLGIM 504
Cdd:cd13975 133 VLLDKKNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFSG-KYDNSVDVYAFGIL 187
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
325-572 7.68e-17

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 81.25  E-value: 7.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSY---LVGDELWV-VMEFL 398
Cdd:cd14030  31 IEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKseRQRFKEEAGMLKGLQHPNIVRFYDSWestVKGKKCIVlVTELM 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQG--VIHRDIKSDSILLTH-DGRVKLSDFGFCAQvsKEVPRRKS 474
Cdd:cd14030 111 TSGTLKTYLKRFKvMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL--KRASFAKS 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRlPYGPEVDIWSLGIMVIEMVDGEPPYFN-EPPLKAMKMIRDNLPPrlKNLHKVS-PSLKGFLDRL 552
Cdd:cd14030 189 VIGTPEFMAPEMYEE-KYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRRVTSGVKP--ASFDKVAiPEVKEIIEGC 265
                       250       260
                ....*....|....*....|
gi 5031975  553 LVRDPAQRATAAELLKHPFL 572
Cdd:cd14030 266 IRQNKDERYAIKDLLNHAFF 285
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
344-537 1.12e-16

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 80.95  E-value: 1.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  344 GKLVAVKKMDLRKQQ--RRELLFNEVVIMRdyqHENVVEMYNSYLVG----DELWVVMEFLEGGALTDIVTHTRMNEEQI 417
Cdd:cd14142  28 GESVAVKIFSSRDEKswFRETEIYNTVLLR---HENILGFIASDMTSrnscTQLWLITHYHENGSLYDYLQRTTLDHQEM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  418 AAVCLAVLQALSVLHA-----QG---VIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV----PRRKSLVGTPYWMAPE 485
Cdd:cd14142 105 LRLALSAASGLVHLHTeifgtQGkpaIAHRDLKSKNILVKSNGQCCIADLGLAVTHSQETnqldVGNNPRVGTKRYMAPE 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031975  486 LI------SRLPYGPEVDIWSLGIMVIEMV----------DGEPPYF----NEPPLKAMKMI------RDNLPPRLKN 537
Cdd:cd14142 185 VLdetintDCFESYKRVDIYAFGLVLWEVArrcvsggiveEYKPPFYdvvpSDPSFEDMRKVvcvdqqRPNIPNRWSS 262
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
320-567 1.50e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 80.24  E-value: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  320 YLDNFIKI---GEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELL--FNEVVIMRDYQHENVVEMYNSYL--VGDELW 392
Cdd:cd14049   4 YLNEFEEIarlGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMkvLREVKVLAGLQHPNIVGYHTAWMehVQLMLY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  393 VVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSV--------------LHAQGVIHRDIKSDSILLT-HDGRVKLS 457
Cdd:cd14049  84 IQMQLCELSLWDWIVERNKRPCEEEFKSAPYTPVDVDVttkilqqllegvtyIHSMGIVHRDLKPRNIFLHgSDIHVRIG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  458 DFGF-CAQV------SKEVPRRKSL-----VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDgepPYFNE-PPLKAM 524
Cdd:cd14049 164 DFGLaCPDIlqdgndSTTMSRLNGLthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEmERAEVL 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 5031975  525 KMIRDNLPPrlKNLHKVSPSLKGFLDRLLVRDPAQRATAAELL 567
Cdd:cd14049 241 TQLRNGQIP--KSLCKRWPVQAKYIKLLTSTEPSERPSASQLL 281
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
422-572 1.52e-16

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 80.44  E-value: 1.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  422 LAVLQALSVLH-AQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG-----------TPYWMAPELISR 489
Cdd:cd14011 121 LQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILS 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  490 LPYGPEVDIWSLGIMVIEMV-DGEPPY-FNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELL 567
Cdd:cd14011 201 KTCDPASDMFSLGVLIYAIYnKGKPLFdCVNNLLSYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLS 280

                ....*
gi 5031975  568 KHPFL 572
Cdd:cd14011 281 KIPFF 285
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
327-541 1.79e-16

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 80.01  E-value: 1.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMDLRKQQ--RRELLFNEVVIMRdyqHENVVEMYNSYLVGD----ELWVVMEFLEG 400
Cdd:cd14056   3 IGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDswFRETEIYQTVMLR---HENILGFIAADIKSTgswtQLWLITEYHEH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQ--------GVIHRDIKSDSILLTHDGRVKLSDFG----FCAQVSKE 468
Cdd:cd14056  78 GSLYDYLQRNTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGlavrYDSDTNTI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRKSLVGTPYWMAPELISRlPYGPE-------VDIWSLGIMVIEMV----------DGEPPYF----NEPPLKAMKMI 527
Cdd:cd14056 158 DIPPNPRVGTKRYMAPEVLDD-SINPKsfesfkmADIYSFGLVLWEIArrceiggiaeEYQLPYFgmvpSDPSFEEMRKV 236
                       250       260
                ....*....|....*....|
gi 5031975  528 ------RDNLPPRLKNlHKV 541
Cdd:cd14056 237 vcveklRPPIPNRWKS-DPV 255
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
326-572 1.83e-16

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 80.70  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEG--STgiVCIATVRSSGKLVAVKkmdLRKQQR--RELLFNEVVIMR--------DYQHENVVEMYNSYLV----GD 389
Cdd:cd14136  17 KLGWGhfST--VWLCWDLQNKRFVALK---VVKSAQhyTEAALDEIKLLKcvreadpkDPGREHVVQLLDDFKHtgpnGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  390 ELWVVMEFLeGGALTDIVTHTRMNEEQIAAV-CLA--VLQALSVLHAQ-GVIHRDIKSDSILLTHDG-RVKLSDFGFCAQ 464
Cdd:cd14136  92 HVCMVFEVL-GPNLLKLIKRYNYRGIPLPLVkKIArqVLQGLDYLHTKcGIIHTDIKPENVLLCISKiEVKIADLGNACW 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  465 VSKevpRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGE----------------------------PP-- 514
Cdd:cd14136 171 TDK---HFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDylfdphsgedysrdedhlaliiellgriPRsi 247
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031975  515 ---------YFNEP----PLKAMKM--IRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14136 248 ilsgkysreFFNRKgelrHISKLKPwpLEDVLVEKYKWSKEEAKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
326-583 1.99e-16

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: 80.42  E-value: 1.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELL-FNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEggalT 404
Cdd:cd07872  13 KLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD----K 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEVPRR--KSLVG 477
Cdd:cd07872  89 DLKQYMDdcgniMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR--AKSVPTKtySNEVV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  478 TPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPY-----------------------------------FNEPPL 521
Cdd:cd07872 167 TLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEMASGRPLFpgstvedelhlifrllgtpteetwpgissndefknYNFPKY 246
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031975  522 KAMKMIrdNLPPRLKnlhkvSPSLKgFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVP 583
Cdd:cd07872 247 KPQPLI--NHAPRLD-----TEGIE-LLTKFLQYESKKRISAEEAMKHAYFRSLGTRIHSLP 300
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
327-515 2.27e-16

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 79.69  E-value: 2.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIV---CIATVRSSGKL--VAVKKMDLRK--QQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd05032  14 LGQGSFGMVyegLAKGVVKGEPEtrVAIKTVNENAsmRERIEFL-NEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTRMNEEQIAAV-----------CLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE 468
Cdd:cd05032  93 KGDLKSYLRSRRPEAENNPGLgpptlqkfiqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIYET 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 VPRRKSLVGT-PY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05032 173 DYYRKGGKGLlPVrWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPY 222
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
327-574 2.70e-16

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 79.20  E-value: 2.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGK---LVAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05064  13 LGTGRFGELCRGCLKLPSKrelPVAIHTLraGCSDKQRRGFL-AEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVthtRMNEEQIAAVCL-----AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE----VPRR 472
Cdd:cd05064  92 ALDSFL---RKHEGQLVAGQLmgmlpGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQEDKSEaiytTMSG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  473 KSLVgtpYWMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLKGFLDR 551
Cdd:cd05064 169 KSPV---LWAAPEAIQYHHFSSASDVWSFGIVMWEvMSYGERPYWDMSGQDVIKAVEDGF--RLPAPRNCPNLLHQLMLD 243
                       250       260
                ....*....|....*....|...
gi 5031975  552 LLVRDPAQRATAAELlkHPFLAK 574
Cdd:cd05064 244 CWQKERGERPRFSQI--HSILSK 264
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
315-531 3.18e-16

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: 79.74  E-value: 3.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  315 GDPRSYlDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELL-FNEVVIMRDYQHENVVEMYNSYLVGDELWV 393
Cdd:cd07869   2 GKADSY-EKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTaIREASLLKGLKHANIVLLHDIIHTKETLTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  394 VMEFLEGGALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEVPRR 472
Cdd:cd07869  81 VFEYVHTDLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR--AKSVPSH 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031975  473 --KSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYfnepplKAMKMIRDNL 531
Cdd:cd07869 159 tySNEVVTLWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQGVAAF------PGMKDIQDQL 214
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
326-570 3.77e-16

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 78.98  E-value: 3.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIV--CIAtvRSSGKLVAVKKmdlRKQQRRELLFNEVVIMRDY------QHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14051   7 KIGSGEFGSVykCIN--RLDGCVYAIKK---SKKPVAGSVDEQNALNEVYahavlgKHPHVVRYYSAWAEDDHMIIQNEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LEGGALTDIVTH-----TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRV------------------ 454
Cdd:cd14051  82 CNGGSLADAISEnekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPvsseeeeedfegeednpe 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  455 ------KLSDFGFCAQVSKevPRRKSlvGTPYWMAPELI----SRLpygPEVDIWSLGIMVIEMVDGEPPYFNEPplkAM 524
Cdd:cd14051 162 snevtyKIGDLGHVTSISN--PQVEE--GDCRFLANEILqenySHL---PKADIFALALTVYEAAGGGPLPKNGD---EW 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  525 KMIRD-NLPPrlknLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14051 232 HEIRQgNLPP----LPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
330-520 3.88e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 80.31  E-value: 3.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   330 GSTGIVCIATVRSSGKLVAVKKmdlrKQQRRELLfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEggalTDIVTH 409
Cdd:PHA03209  77 GSEGRVFVATKPGQPDPVVLKI----GQKGTTLI--EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS----SDLYTY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   410 TRMNEEQI---AAVCL--AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfCAQVSKEVPRRKSLVGTPYWMAP 484
Cdd:PHA03209 147 LTKRSRPLpidQALIIekQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPVVAPAFLGLAGTVETNAP 225
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 5031975   485 ELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPP 520
Cdd:PHA03209 226 EVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPP 261
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
327-523 4.00e-16

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: 78.34  E-value: 4.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKK---MDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVG-DELWVVMEFLEGGA 402
Cdd:cd14064   1 IGSGSFGKVYKGRCR--NKIVAIKRyraNTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR--MNEEQIAAVCLAVLQALSVLH--AQGVIHRDIKSDSILLTHDGRVKLSDFG---FCAQVSKEVPRRKSl 475
Cdd:cd14064  79 LFSLLHEQKrvIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGesrFLQSLDEDNMTKQP- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031975  476 vGTPYWMAPELISRLP-YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA 523
Cdd:cd14064 158 -GNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPFAHLKPAAA 205
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
316-515 4.16e-16

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 78.38  E-value: 4.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  316 DPRSYldNFIK-IGEGSTGIVCIATVRssGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 394
Cdd:cd05113   2 DPKDL--TFLKeLGTGQFGVVKYGKWR--GQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHT--RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvpRR 472
Cdd:cd05113  78 TEYMANGCLLNYLREMrkRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDD--EY 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  473 KSLVGTPY---WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05113 156 TSSVGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
325-566 4.25e-16

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 78.55  E-value: 4.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  325 IKIGEGSTGIVCIATVRS-SGKL--VAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYnSYLVGDELWVVMEFLE 399
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMkSGKEveVAVKtlKQEHEKAGKKEFL-REASVMAQLDHPCIVRLI-GVCKGEPLMLVMELAP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTD-IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPrrkslVGT 478
Cdd:cd05060  79 LGPLLKyLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFG----MSRALG-----AGS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  479 PY------------WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSL 545
Cdd:cd05060 150 DYyrattagrwplkWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGE--RLPRPEECPQEI 227
                       250       260
                ....*....|....*....|.
gi 5031975  546 KGFLDRLLVRDPAQRATAAEL 566
Cdd:cd05060 228 YSIMLSCWKYRPEDRPTFSEL 248
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
317-568 4.32e-16

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, 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. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 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: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 78.66  E-value: 4.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSG-----KLVAVKKMDLRKQQRRELLFN-EVVIMRDYQHENVVEMYNSYLVGDE 390
Cdd:cd05046   3 PRSNLQEITTLGRGEFGEVFLAKAKGIEeeggeTLVLVKALQKTKDENLQSEFRrELDMFRKLSHKNVVRLLGLCREAEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVTHTRMNEE----------QIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG 460
Cdd:cd05046  83 HYMILEYTDLGDLKQFLRATKSKDEklkppplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  461 FCAQV-SKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYF---NEPPLKAMKMIRDNLPPrl 535
Cdd:cd05046 163 LSKDVyNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYglsDEEVLNRLQAGKLELPV-- 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 5031975  536 knlHKVSPS-LKGFLDRLLVRDPAQRATAAELLK 568
Cdd:cd05046 241 ---PEGCPSrLYKLMTRCWAVNPKDRPSFSELVS 271
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
317-568 4.59e-16

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR 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: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 79.00  E-value: 4.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKL------VAVK--KMDLRKQQRRELLfNEVVIMRDY-QHENVVEMYNSYLV 387
Cdd:cd05053  10 PRDRLTLGKPLGEGAFGQVVKAEAVGLDNKpnevvtVAVKmlKDDATEKDLSDLV-SEMEMMKMIgKHKNIINLLGACTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  388 GDELWVVMEFLEGGALTD-----------------IVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH 450
Cdd:cd05053  89 DGPLYVVVEYASKGNLREflrarrppgeeaspddpRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  451 DGRVKLSDFGFCAQVSKEVPRRKSLVG-TPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMI 527
Cdd:cd05053 169 DNVMKIADFGLARDIHHIDYYRKTTNGrLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  528 RDNLppRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLK 568
Cdd:cd05053 249 KEGH--RMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
310-572 4.68e-16

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: 79.53  E-value: 4.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  310 LVVDPGDprsYLDNFIKI----GEGSTGIVCIATVRSSGKLVAVKKmdLRKQQR-RELLFNEVVIMRDYQHE------NV 378
Cdd:cd14134   2 LIYKPGD---LLTNRYKIlrllGEGTFGKVLECWDRKRKRYVAVKI--IRNVEKyREAAKIEIDVLETLAEKdpngksHC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  379 VEMYNSYLVGDELWVVMEFLeGGALTDIVTHTRM---NEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH----- 450
Cdd:cd14134  77 VQLRDWFDYRGHMCIVFELL-GPSLYDFLKKNNYgpfPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvk 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  451 --------------DGRVKLSDFGfCAQVSKEvpRRKSLVGTPYWMAPELISRLPYGPEVDIWSLG-IMV---------- 505
Cdd:cd14134 156 vynpkkkrqirvpkSTDIKLIDFG-SATFDDE--YHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGcILVelytgellfq 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  506 ----------IEMVDGEPP--------------YFNEPPL------KAMKMIRDNLPPRLKNLHKVSPSLKGFLD---RL 552
Cdd:cd14134 233 thdnlehlamMERILGPLPkrmirrakkgakyfYFYHGRLdwpegsSSGRSIKRVCKPLKRLMLLVDPEHRLLFDlirKM 312
                       330       340
                ....*....|....*....|
gi 5031975  553 LVRDPAQRATAAELLKHPFL 572
Cdd:cd14134 313 LEYDPSKRITAKEALKHPFF 332
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
326-515 5.63e-16

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: 77.99  E-value: 5.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIAtvRSSGKLVAVK--KMDLRKQQrrelLFNEVVIMRDYQHENVVEMYNSYLvGDELWVVMEFLEGGAL 403
Cdd:cd05083  13 IIGEGEFGAVLQG--EYMGQKVAVKniKCDVTAQA----FLEETAVMTKLQHKNLVRLLGVIL-HNGLYIVMELMSKGNL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVtHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKSLVGTP 479
Cdd:cd05083  86 VNFL-RSRgralVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG----LAKVGSMGVDNSRLP 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5031975  480 Y-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05083 161 VkWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
10-63 6.06e-16

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 72.34  E-value: 6.06e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975     10 EISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESA-RRPKPLVDPACITSIQ 63
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGiTEDEQKENPKAVLDVL 55
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
327-572 8.51e-16

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 77.58  E-value: 8.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFN------EVVIMRDY----QHENVVEMYNSYLVGDELWVVME 396
Cdd:cd14101   8 LGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLPGvnpvpnEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 F-LEGGALTDIVTHTRMNEEQIA-AVCLAVLQALSVLHAQGVIHRDIKSDSILL-THDGRVKLSDFGFCAQVSKEVprRK 473
Cdd:cd14101  88 RpQHCQDLFDYITERGALDESLArRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGATLKDSM--YT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  474 SLVGTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEpplkamkmiRDNLPPRLKNLHKVSPSLKGFLDRL 552
Cdd:cd14101 166 DFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERD---------TDILKAKPSFNKRVSNDCRSLIRSC 236
                       250       260
                ....*....|....*....|
gi 5031975  553 LVRDPAQRATAAELLKHPFL 572
Cdd:cd14101 237 LAYNPSDRPSLEQILLHPWM 256
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
327-533 9.05e-16

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 77.60  E-value: 9.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGK---LVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05066  12 IGAGEFGEVCSGRLKLPGKreiPVAIKtlKAGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTdivTHTRMNEEQIAAVCL-----AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 476
Cdd:cd05066  91 SLD---AFLRKHDGQFTVIQLvgmlrGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTR 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031975  477 GTPY---WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPYFNEPPLKAMKMIRD--NLPP 533
Cdd:cd05066 168 GGKIpirWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWEMSNQDVIKAIEEgyRLPA 230
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
358-517 9.70e-16

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: 77.54  E-value: 9.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  358 QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVI 437
Cdd:cd14027  33 EHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVI 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  438 HRDIKSDSILLTHDGRVKLSDFGFC-----AQVSKEVPRRKSLV--------GTPYWMAPELISRLPYGP--EVDIWSLG 502
Cdd:cd14027 113 HKDLKPENILVDNDFHIKIADLGLAsfkmwSKLTKEEHNEQREVdgtakknaGTLYYMAPEHLNDVNAKPteKSDVYSFA 192
                       170
                ....*....|....*
gi 5031975  503 IMVIEMVDGEPPYFN 517
Cdd:cd14027 193 IVLWAIFANKEPYEN 207
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
411-569 1.22e-15

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 77.83  E-value: 1.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  411 RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL---THdgRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELI 487
Cdd:cd13974 128 RLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLnkrTR--KITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVL 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  488 SRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPprlkNLHKVSPSLKGFLDRLLVRDPAQRATA 563
Cdd:cd13974 206 SGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAaeyTIP----EDGRVSENTVCLIRKLLVLNPQKRLTA 281

                ....*.
gi 5031975  564 AELLKH 569
Cdd:cd13974 282 SEVLDS 287
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
326-571 1.43e-15

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 76.93  E-value: 1.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGivciaTVRSSGKL----VAVKKMdLRkqQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd13982   8 VLGYGSEG-----TIVFRGTFdgrpVAVKRL-LP--EFFDFADREVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 gALTDIVT--HTRMNEEQIAAVCLAVLQ----ALSVLHAQGVIHRDIKSDSILLTHD-----GRVKLSDFGFCAQVS--- 466
Cdd:cd13982  80 -SLQDLVEspRESKLFLRPGLEPVRLLRqiasGLAHLHSLNIVHRDLKPQNILISTPnahgnVRAMISDFGLCKKLDvgr 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  467 KEVPRRKSLVGTPYWMAPELIS-RLPYGP--EVDIWSLG-IMVIEMVDGEPPyFNEPPLKAMKMIRD--NLPPRLKNLHK 540
Cdd:cd13982 159 SSFSRRSGVAGTSGWIAPEMLSgSTKRRQtrAVDIFSLGcVFYYVLSGGSHP-FGDKLEREANILKGkySLDKLLSLGEH 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 5031975  541 VsPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd13982 238 G-PEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
344-563 1.59e-15

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 77.05  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  344 GKLVAVKKMDLRKQQRRELLFnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDI--VTHTRMNEEQIAAVC 421
Cdd:cd13992  25 GRTVAIKHITFSRTEKRTILQ-ELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVllNREIKMDWMFKSSFI 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  422 LAVLQALSVLHAQ-GVIHRDIKSDSILLthDGR--VKLSDFGFCAQVSKEVPRRKSLVGTPY---WMAPELISRLPYG-- 493
Cdd:cd13992 104 KDIVKGMNYLHSSsIGYHGRLKSSNCLV--DSRwvVKLTDFGLRNLLEEQTNHQLDEDAQHKkllWTAPELLRGSLLEvr 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  494 --PEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPRLKNLH----KVSPSLKGFLDRLLVRDPAQRATA 563
Cdd:cd13992 182 gtQKGDVYSFAIILYEILFRSDPFALEREVAIvEKVISGGNKPFRPELAvlldEFPPRLVLLVKQCWAENPEKRPSF 258
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
327-515 2.35e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 77.49  E-value: 2.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD-----LRKQQrrellfNEVVIMRDYQHE-----NVVEMYNSYLVGDELWVVME 396
Cdd:cd14211   7 LGRGTFGQVVKCWKRGTNEIVAIKILKnhpsyARQGQ------IEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGaLTDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEV 469
Cdd:cd14211  81 MLEQN-LYDFLKQNKfspLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSASHVSKAV 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  470 PrrKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14211 160 C--STYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY 203
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
345-519 3.45e-15

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 76.21  E-value: 3.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  345 KLVAVKKMDLrkQQRRELLfNEVVIMRDY--QHENVVEMYNSYLVG----DELWVVMEFLEGGALTDIVTHTRMNEEQIA 418
Cdd:cd14053  19 RLVAVKIFPL--QEKQSWL-TEREIYSLPgmKHENILQFIGAEKHGesleAEYWLITEFHERGSLCDYLKGNVISWNELC 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  419 AVCLAVLQALSVLHAQ----------GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSL--VGTPYWMAPE- 485
Cdd:cd14053  96 KIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGDTHgqVGTRRYMAPEv 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  486 LISRLPYGPE----VDIWSLGIMVIEMV------DGEPPYFNEP 519
Cdd:cd14053 176 LEGAINFTRDaflrIDMYAMGLVLWELLsrcsvhDGPVDEYQLP 219
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
317-538 3.73e-15

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 76.16  E-value: 3.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGK-----LVAVKKMDLRKQQRRELLF-NEVVIMRDYQHENVVEMYNSYLVGDE 390
Cdd:cd05061   4 SREKITLLRELGQGSFGMVYEGNARDIIKgeaetRVAVKTVNESASLRERIEFlNEASVMKGFTCHHVVRLLGVVSKGQP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  391 LWVVMEFLEGGALTDIVTHTRMNEE--------------QIAAvclAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKL 456
Cdd:cd05061  84 TLVVMELMAHGDLKSYLRSLRPEAEnnpgrppptlqemiQMAA---EIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  457 SDFGFCAQVSKEVPRRKSLVG-TPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRD---- 529
Cdd:cd05061 161 GDFGMTRDIYETDYYRKGGKGlLPVrWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDggyl 240
                       250
                ....*....|...
gi 5031975  530 ----NLPPRLKNL 538
Cdd:cd05061 241 dqpdNCPERVTDL 253
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
330-516 4.13e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 77.58  E-value: 4.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   330 GSTGIVCIATVR--SSGKLVAVKKMDLRKQQRREllfneVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV 407
Cdd:PHA03207 103 GSEGEVFVCTKHgdEQRKKVIVKAVTGGKTPGRE-----IDILKTISHRAIINLIHAYRWKSTVCMVMPKYKCDLFTYVD 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   408 THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV--SKEVPRRKSLVGTPYWMAPE 485
Cdd:PHA03207 178 RSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLdaHPDTPQCYGWSGTLETNSPE 257
                        170       180       190
                 ....*....|....*....|....*....|.
gi 5031975   486 LISRLPYGPEVDIWSLGIMVIEMVDGEPPYF 516
Cdd:PHA03207 258 LLALDPYCAKTDIWSAGLVLFEMSVKNVTLF 288
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
327-575 4.18e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 76.97  E-value: 4.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHEN-VVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14226  21 IGKGSFGQVVKAYDHVEQEWVAIKiiknKKAFLNQAQIEVRLLELMNKHDTENKYyIVRLKRHFMFRNHLCLVFELLSYN 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 aLTDIVTHTRMNeeqiaAVCLAV--------LQALSVLHAQ--GVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSKEV 469
Cdd:cd14226 101 -LYDLLRNTNFR-----GVSLNLtrkfaqqlCTALLFLSTPelSIIHCDLKPENILLCNPKRsaIKIIDFGSSCQLGQRI 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  470 PRrksLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEP--PYFNE-------------PP-------------- 520
Cdd:cd14226 175 YQ---YIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPlfSGANEvdqmnkivevlgmPPvhmldqapkarkff 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  521 ---------LKAMKMIRDNLPP---RLKNL-----------------HKVSPSLKgFLD---RLLVRDPAQRATAAELLK 568
Cdd:cd14226 252 eklpdgtyyLKKTKDGKKYKPPgsrKLHEIlgvetggpggrragepgHTVEDYLK-FKDlilRMLDYDPKTRITPAEALQ 330

                ....*..
gi 5031975  569 HPFLAKA 575
Cdd:cd14226 331 HSFFKRT 337
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
318-509 4.25e-15

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: 76.12  E-value: 4.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  318 RSYLDNFIKIGEGSTGIV--CIATVR--SSGKLVAVKKmdLRKQQRREL---LFNEVVIMRDYQHENVVEmYNSYLV--- 387
Cdd:cd05079   3 KRFLKRIRDLGEGHFGKVelCRYDPEgdNTGEQVAVKS--LKPESGGNHiadLKKEIEILRNLYHENIVK-YKGICTedg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  388 GDELWVVMEFLEGGALTDIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA-- 463
Cdd:cd05079  80 GNGIKLIMEFLPSGSLKEYLprNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKai 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  464 QVSKEVPRRKSLVGTP-YWMAPELISRLPYGPEVDIWSLGIMVIEMV 509
Cdd:cd05079 160 ETDKEYYTVKDDLDSPvFWYAPECLIQSKFYIASDVWSFGVTLYELL 206
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
327-529 4.52e-15

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 75.78  E-value: 4.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGK---LVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd05063  13 IGAGEFGEVFRGILKMPGRkevAVAIKtlKPGYTEKQRQDFL-SEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHT--RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVG-- 477
Cdd:cd05063  92 ALDKYLRDHdgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGL-SRVLEDDPEGTYTTSgg 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  478 -TPY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPYFNEPPLKAMKMIRD 529
Cdd:cd05063 171 kIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYWDMSNHEVMKAIND 225
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
327-515 4.57e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 76.61  E-value: 4.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFnEVVIMRDYQHENV-----VEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14229   8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI-EVGILARLSNENAdefnfVRAYECFQHRNHTCLVFEMLEQN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 aLTDIVTHTRMNEEQ---IAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT----HDGRVKLSDFGFCAQVSKEVPrrKS 474
Cdd:cd14229  87 -LYDFLKQNKFSPLPlkvIRPILQQVATALKKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHVSKTVC--ST 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14229 164 YLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY 204
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
326-517 4.87e-15

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 75.35  E-value: 4.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA- 402
Cdd:cd05084   3 RIGRGNFGEVFSGRLRADNTPVAVKscRETLPPDLKAKFL-QEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDf 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTH-TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS----------KEVPR 471
Cdd:cd05084  82 LTFLRTEgPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEdgvyaatggmKQIPV 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  472 RkslvgtpyWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFN 517
Cdd:cd05084 162 K--------WTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYAN 200
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
350-572 4.92e-15

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 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. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 75.27  E-value: 4.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  350 KKMDLRKQQRRELLFNEVVImrdyQHENVVEMYNSYL--VGDELWVVM--EFLEGGALTDIVTHTR-----MNEEQIAAV 420
Cdd:cd13984  33 KIFKAQEEKIRAVFDNLIQL----DHPNIVKFHRYWTdvQEEKARVIFitEYMSSGSLKQFLKKTKknhktMNEKSWKRW 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  421 CLAVLQALSVLHA--QGVIHRDIKSDSILLTHDGRVKLSDFGFCAqVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDI 498
Cdd:cd13984 109 CTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDA-IHNHVKTCREEHRNLHFFAPEYGYLEDVTTAVDI 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  499 WSLGIMVIEMV------DGEPPYFNEPPL-KAMKMIRDNLpprlknlhkvspsLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd13984 188 YSFGMCALEMAaleiqsNGEKVSANEEAIiRAIFSLEDPL-------------QKDFIRKCLSVAPQDRPSARDLLFHPV 254

                .
gi 5031975  572 L 572
Cdd:cd13984 255 L 255
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
327-515 6.19e-15

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 75.99  E-value: 6.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMD-LRKQQRRELLFNEVVIMRDYQHENVVEMYNSY--LVGDELWVVMEFLEGGAL 403
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNnLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEeeLTTRHKVLVMELCPCGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  404 TDIVTHTR----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSIL--LTHDGRV--KLSDFGfCAQVSKEVPRRKSL 475
Cdd:cd13988  81 YTVLEEPSnaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFG-AARELEDDEQFVSL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5031975  476 VGTPYWMAPELISRL--------PYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd13988 160 YGTEEYLHPDMYERAvlrkdhqkKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
327-519 8.61e-15

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 75.00  E-value: 8.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIAtvRSSGKlVAVK--KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 404
Cdd:cd14152   8 IGQGRWGKVHRG--RWHGE-VAIRllEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRTLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIV--THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLtHDGRVKLSDFGF--CAQVSKEvPRRKSLVGTP- 479
Cdd:cd14152  85 SFVrdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVQE-GRRENELKLPh 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  480 ---YWMAPELI---------SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP 519
Cdd:cd14152 163 dwlCYLAPEIVremtpgkdeDCLPFSKAADVYAFGTIWYELQARDWPLKNQP 214
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
327-572 9.01e-15

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 74.62  E-value: 9.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFN------EVVIMRDYQH--ENVVEMYNSYLVGDELWVVMEFL 398
Cdd:cd14100   8 LGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPNgtrvpmEIVLLKKVGSgfRGVIRLLDWFERPDSFVLVLERP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EG-GALTDIVTHTRMNEEQIA-AVCLAVLQALSVLHAQGVIHRDIKSDSILLT-HDGRVKLSDFGFCAQVSKEVprRKSL 475
Cdd:cd14100  88 EPvQDLFDFITERGALPEELArSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKDTV--YTDF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  476 VGTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPY-FNEPPLKAMKMIRdnlpprlknlHKVSPSLKGFLDRLL 553
Cdd:cd14100 166 DGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFeHDEEIIRGQVFFR----------QRVSSECQHLIKWCL 235
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14100 236 ALRPSDRPSFEDIQNHPWM 254
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
326-515 1.07e-14

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 74.39  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKlVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd05148  13 KLGSGYFGEVWEGLWKNRVR-VAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLLA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVthtRMNEEQIAAV------CLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTP 479
Cdd:cd05148  92 FL---RSPEGQVLPVaslidmACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGL-ARLIKEDVYLSSDKKIP 167
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5031975  480 Y-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05148 168 YkWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPY 205
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
327-568 1.13e-14

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: 74.45  E-value: 1.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVcIATVRSSGKLVAVKKMDLRKQQRRELLFN-EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd14664   1 IGRGGAGTV-YKGVMPNGTLVAVKRLKGEGTQGGDHGFQaEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTRMNEEQI-----AAVCLAVLQALSVLH---AQGVIHRDIKSDSILLTHDGRVKLSDFGFCA-QVSKEVPRRKSLV 476
Cdd:cd14664  80 LLHSRPESQPPLdwetrQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKlMDDKDSHVMSSVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  477 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMKMIRD---NLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14664 160 GSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRP-FDEAFLDDGVDIVDwvrGLLEEKKVEALVDPDLQGVYKLEE 238
                       250       260
                ....*....|....*....|....*..
gi 5031975  554 VR------------DPAQRATAAELLK 568
Cdd:cd14664 239 VEqvfqvallctqsSPMERPTMREVVR 265
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
327-572 1.57e-14

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 73.84  E-value: 1.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKmdLRKQQRRE-------LLFNEVVIMRDY--QHENVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14102   8 LGSGGFGTVYAGSRIADGLPVAVKH--VVKERVTEwgtlngvMVPLEIVLLKKVgsGFRGVIKLLDWYERPDGFLIVMER 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 LE-GGALTDIVTHT-RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILL-THDGRVKLSDFGFCAQVSKEVprRKS 474
Cdd:cd14102  86 PEpVKDLFDFITEKgALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFGSGALLKDTV--YTD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPYWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLkamkmirdnLPPRLKNLHKVSPSLKGFLDRLL 553
Cdd:cd14102 164 FDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEEI---------LRGRLYFRRRVSPECQQLIKWCL 234
                       250
                ....*....|....*....
gi 5031975  554 VRDPAQRATAAELLKHPFL 572
Cdd:cd14102 235 SLRPSDRPTLEQIFDHPWM 253
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
363-573 1.93e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 75.89  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   363 LFNEVVIMRDYQHENVVEMY-------NSYLVGDEL-WVVMEFLEGGAL----TDIVTHTRMNEEQIaavclavLQALSV 430
Cdd:PHA03210 210 LENEILALGRLNHENILKIEeilrseaNTYMITQKYdFDLYSFMYDEAFdwkdRPLLKQTRAIMKQL-------LCAVEY 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   431 LHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE-VPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV 509
Cdd:PHA03210 283 IHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKErEAFDYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDML 362
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   510 ---------DGEPPY----------------FNEPPLKAMKMIRD--------NLPPRLKNLHkVSPSLKGFLDRLLVRD 556
Cdd:PHA03210 363 shdfcpigdGGGKPGkqllkiidslsvcdeeFPDPPCKLFDYIDSaeidhaghSVPPLIRNLG-LPADFEYPLVKMLTFD 441
                        250
                 ....*....|....*..
gi 5031975   557 PAQRATAAELLKHPFLA 573
Cdd:PHA03210 442 WHLRPGAAELLALPLFS 458
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
317-515 3.04e-14

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 73.15  E-value: 3.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd05072   5 PRESIKLVKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSVQAFL-EEANLMKTLQHDKLVRLYAVVTKEEPIYIITE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTH---TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRR 472
Cdd:cd05072  83 YMAKGSLLDFLKSdegGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEdNEYTAR 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05072 163 EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY 206
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
317-538 3.38e-14

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 73.00  E-value: 3.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVME 396
Cdd:cd05067   5 PRETLKLVERLGAGQFGEVWMGYYNGHTK-VAIKSLK-QGSMSPDAFLAEANLMKQLQHQRLVRLY-AVVTQEPIYIITE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHT---RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKEVPRR 472
Cdd:cd05067  82 YMENGSLVDFLKTPsgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIeDNEYTAR 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYfnePPLKAMKMIR-----------DNLPPRLKNL 538
Cdd:cd05067 162 EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPY---PGMTNPEVIQnlergyrmprpDNCPEELYQL 236
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
326-515 4.97e-14

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 72.37  E-value: 4.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIAT-VRSSGKL--VAVK--KMD-LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLvGDELWVVMEFLE 399
Cdd:cd05040   2 KLGDGSFGVVRRGEwTTPSGKViqVAVKclKSDvLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVL-SSPLMMVTELAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDivthtRMNEEQ----IAAVCLAVLQ---ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE---- 468
Cdd:cd05040  81 LGSLLD-----RLRKDQghflISTLCDYAVQianGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNedhy 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031975  469 --VPRRKslvgTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05040 156 vmQEHRK----VPFaWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPW 202
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
327-515 5.33e-14

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 73.58  E-value: 5.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFnEVVIMRDYQHENV-----VEMYNSYLVGDELWVVMEFLEGG 401
Cdd:cd14228  23 LGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQI-EVSILSRLSSENAdeynfVRSYECFQHKNHTCLVFEMLEQN 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 aLTDIVTHTRMNE---EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT----HDGRVKLSDFGFCAQVSKEVPrrKS 474
Cdd:cd14228 102 -LYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHVSKAVC--ST 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031975  475 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14228 179 YLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY 219
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
327-563 5.41e-14

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 72.78  E-value: 5.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVrsSGKLVAVKkmdLRKQQRRELLFNEVVIMR--DYQHENVVemynSYLVGDE------LW---VVM 395
Cdd:cd14054   3 IGQGRYGTVWKGSL--DERPVAVK---VFPARHRQNFQNEKDIYElpLMEHSNIL----RFIGADErptadgRMeylLVL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  396 EFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQ---------GVIHRDIKSDSILLTHDGRVKLSDFGFCAQV- 465
Cdd:cd14054  74 EYAPKGSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLr 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  466 -SKEVPRR------KSL--VGTPYWMAPELI----------SRLpygPEVDIWSLGIMVIE-------MVDGEP------ 513
Cdd:cd14054 154 gSSLVRGRpgaaenASIseVGTLRYMAPEVLegavnlrdceSAL---KQVDVYALGLVLWEiamrcsdLYPGESvppyqm 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  514 PYFNE----PPLKAMKMI------RDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATA 563
Cdd:cd14054 231 PYEAElgnhPTFEDMQLLvsrekaRPKFPDAWKENSLAVRSLKETIEDCWDQDAEARLTA 290
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
342-508 6.62e-14

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: 72.23  E-value: 6.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  342 SSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYN-SYLVG-DELWVVMEFLEGGALTDIV--THTRMNEEQI 417
Cdd:cd05081  31 NTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGvSYGPGrRSLRLVMEYLPSGCLRDFLqrHRARLDASRL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  418 AAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPRRKS--LVGTP-----YWMAPELISRL 490
Cdd:cd05081 111 LLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFG----LAKLLPLDKDyyVVREPgqspiFWYAPESLSDN 186
                       170
                ....*....|....*...
gi 5031975  491 PYGPEVDIWSLGIMVIEM 508
Cdd:cd05081 187 IFSRQSDVWSFGVVLYEL 204
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
327-515 9.10e-14

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 72.82  E-value: 9.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMR-------DYqheNVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd14227  23 LGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARlstesadDY---NFVRAYECFQHKNHTCLVFEMLE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGaLTDIVTHTRMNE---EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR----VKLSDFGFCAQVSKEVPrr 472
Cdd:cd14227 100 QN-LYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRqpyrVKVIDFGSASHVSKAVC-- 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 515
Cdd:cd14227 177 STYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY 219
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
374-572 9.17e-14

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: 71.22  E-value: 9.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  374 QHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR 453
Cdd:cd14022  43 AHSNINQITEIILGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  454 --VKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELI--SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD 529
Cdd:cd14022 123 trVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  530 ---NLPPRLknlhkvSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14022 203 gqfNIPETL------SPKAKCLIRSILRREPSERLTSQEILDHPWF 242
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
347-515 1.30e-13

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 71.29  E-value: 1.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  347 VAVKKmdLRK----QQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQ------ 416
Cdd:cd05044  29 VAVKT--LRKgatdQEKAEFL-KEAHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDLLSYLRAARPTAFTpplltl 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  417 --IAAVCLAVLQALSVLHAQGVIHRDIKSDSILLT----HDGRVKLSDFGFCAQVSKEVPRRKSLVGT-PY-WMAPELIS 488
Cdd:cd05044 106 kdLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSskdyRERVVKIGDFGLARDIYKNDYYRKEGEGLlPVrWMAPESLV 185
                       170       180
                ....*....|....*....|....*...
gi 5031975  489 RLPYGPEVDIWSLGIMVIE-MVDGEPPY 515
Cdd:cd05044 186 DGVFTTQSDVWAFGVLMWEiLTLGQQPY 213
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
326-572 1.32e-13

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 72.28  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK----KMDLRKQQRREL----LFNEVVIMRDYQHenVVEMYNSYLVGDELWVVMEF 397
Cdd:cd14212   6 LLGQGTFGQVVKCQDLKTNKLVAVKvlknKPAYFRQAMLEIailtLLNTKYDPEDKHH--IVRLLDHFMHHGHLCIVFEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  398 L-------------EGGALTDIVTHTRmneeQIaavclavLQALSVLHAQGVIHRDIKSDSILLTHD--GRVKLSDFGfc 462
Cdd:cd14212  84 LgvnlyellkqnqfRGLSLQLIRKFLQ----QL-------LDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFG-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  463 aqvSKEVPRRK--SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIE-------------------MVD--GEPP----- 514
Cdd:cd14212 151 ---SACFENYTlyTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAElflglplfpgnseynqlsrIIEmlGMPPdwmle 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  515 ------------------------------------------YFNEPPLKAMKM---IRDNLPPRLKNLHKVSPSLKGFL 549
Cdd:cd14212 228 kgkntnkffkkvaksggrstyrlktpeefeaenncklepgkrYFKYKTLEDIIMnypMKKSKKEQIDKEMETRLAFIDFL 307
                       330       340
                ....*....|....*....|...
gi 5031975  550 DRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14212 308 KGLLEYDPKKRWTPDQALNHPFI 330
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
375-572 1.53e-13

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: 70.68  E-value: 1.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  375 HENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRV 454
Cdd:cd14024  44 HEGVCSVLEVVIGQDRAYAFFSRHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRT 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  455 KLSDFGF--CAQVSKEVPRRKSLVGTPYWMAPELI-SRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD- 529
Cdd:cd14024 124 KLVLVNLedSCPLNGDDDSLTDKHGCPAYVGPEILsSRRSYsGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRg 203
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031975  530 --NLPPRLknlhkvSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14024 204 afSLPAWL------SPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
326-534 1.59e-13

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 71.35  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRssGKLVAVKKMDLRKQQR--RELLFNEVVIMRdyqHENVVEMYNSYLVGD----ELWVVMEFLE 399
Cdd:cd14144   2 SVGKGRYGEVWKGKWR--GEKVAVKIFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHA-----QG---VIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 471
Cdd:cd14144  77 NGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLHTeifgtQGkpaIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 ----RKSLVGTPYWMAPELISRL-------PYgPEVDIWSLGIMVIEMV----------DGEPPYF----NEPPLKAMKM 526
Cdd:cd14144 157 vdlpPNTRVGTKRYMAPEVLDESlnrnhfdAY-KMADMYSFGLVLWEIArrcisggiveEYQLPYYdavpSDPSYEDMRR 235
                       250
                ....*....|....
gi 5031975  527 I------RDNLPPR 534
Cdd:cd14144 236 VvcverrRPSIPNR 249
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
427-572 1.83e-13

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: 71.48  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  427 ALSVLHAQGVIHRDIKSDSILLTHDGRV-KLSDFGFCAQVSK-EVprrkslvgTPY-----WMAPELISRLPYGPEVDIW 499
Cdd:cd14135 117 ALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFGSASDIGEnEI--------TPYlvsrfYRAPEIILGLPYDYPIDMW 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  500 SLGIMVIEM---------------------VDGEPP------------YFNE------------PPLKAMKMIRDNLPPR 534
Cdd:cd14135 189 SVGCTLYELytgkilfpgktnnhmlklmmdLKGKFPkkmlrkgqfkdqHFDEnlnfiyrevdkvTKKEVRRVMSDIKPTK 268
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  535 --LKNLHKVSPS----------LKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14135 269 dlKTLLIGKQRLpdedrkkllqLKDLLDKCLMLDPEKRITPNEALQHPFI 318
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
317-515 1.85e-13

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 71.36  E-value: 1.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGK-----LVAVKKMDLR-KQQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGD 389
Cdd:cd05055  33 PRNNLSFGKTLGAGAFGKVVEATAYGLSKsdavmKVAVKMLKPTaHSSEREALMSELKIMSHLgNHENIVNLLGACTIGG 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  390 ELWVVMEFLEGGaltDIVTHTRMNEEQIAA----VCLA--VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA 463
Cdd:cd05055 113 PILVITEYCCYG---DLLNFLRRKRESFLTledlLSFSyqVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLAR 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  464 QV---SKEVPRRKSLVGTPyWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05055 190 DImndSNYVVKGNARLPVK-WMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPY 244
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
327-570 2.57e-13

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: 70.34  E-value: 2.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIAtvRSSGKLVAVKKMDLRKQQRRE---------------------LLFNEVVIMRDYQHENVVemynsY 385
Cdd:cd14000   2 LGDGGFGSVYRA--SYKGEPVAVKIFNKHTSSNFAnvpadtmlrhlratdamknfrLLRQELTVLSHLHHPSIV-----Y 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  386 LVG---DELWVVMEFLEGGALTDIVTH--------TRMNEEQIAavcLAVLQALSVLHAQGVIHRDIKSDSILL-----T 449
Cdd:cd14000  75 LLGigiHPLMLVLELAPLGSLDHLLQQdsrsfaslGRTLQQRIA---LQVADGLRYLHSAMIIYRDLKSHNVLVwtlypN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  450 HDGRVKLSDFGFCAQVSKEvpRRKSLVGTPYWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR 528
Cdd:cd14000 152 SAIIIKIADYGISRQCCRM--GAKGSEGTPGFRAPEIARGnVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIH 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5031975  529 DNLPPRLKNLHKVSPS-LKGFLDRLLVRDPAQRATAA---ELLKHP 570
Cdd:cd14000 230 GGLRPPLKQYECAPWPeVEVLMKKCWKENPQQRPTAVtvvSILNSP 275
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
326-516 3.69e-13

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 70.45  E-value: 3.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATV-----RSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05093  12 ELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIVTH--------------TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV- 465
Cdd:cd05093  92 GDLNKFLRAhgpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVy 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031975  466 SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYF 516
Cdd:cd05093 172 STDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWY 224
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
317-562 4.62e-13

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 69.74  E-value: 4.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd05068   6 DRKSLKLLRKLGSGQFGEVWEGLWNNTTP-VAVKTLKPGTMDPEDFL-REAQIMKKLRHPKLIQLYAVCTLEEPIYIITE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTH--TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKS 474
Cdd:cd05068  84 LMKHGSLLEYLQGkgRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGL-ARVIKVEDEYEA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  475 LVGTPY---WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRDNLppRLKNLHKVSPSLKGFLD 550
Cdd:cd05068 163 REGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQVERGY--RMPCPPNCPPQLYDIML 240
                       250
                ....*....|..
gi 5031975  551 RLLVRDPAQRAT 562
Cdd:cd05068 241 ECWKADPMERPT 252
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
348-567 4.83e-13

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 70.12  E-value: 4.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  348 AVKKMDLRKQQRRELLFN-----EVVIMRDYQHENVVEmYNSY--LVGDELWVVMEFLeGGALTDIVtHTRMNEE----- 415
Cdd:cd14001  32 AVKKINSKCDKGQRSLYQerlkeEAKILKSLNHPNIVG-FRAFtkSEDGSLCLAMEYG-GKSLNDLI-EERYEAGlgpfp 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  416 --QIAAVCLAVLQALSVLHAQG-VIHRDIKSDSILLTHDGR-VKLSDFGFCAQVSKEVPRRKS----LVGTPYWMAPELI 487
Cdd:cd14001 109 aaTILKVALSIARALEYLHNEKkILHGDIKSGNVLIKGDFEsVKLCDFGVSLPLTENLEVDSDpkaqYVGTEPWKAKEAL 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  488 SR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA----MKMIRDN---------LPPRLK-NLHKVSPSLKGFLDRL 552
Cdd:cd14001 189 EEgGVITDKADIFAYGLVLWEMMTLSVPHLNLLDIEDddedESFDEDEedeeayygtLGTRPAlNLGELDDSYQKVIELF 268
                       250
                ....*....|....*...
gi 5031975  553 LV---RDPAQRATAAELL 567
Cdd:cd14001 269 YActqEDPKDRPSAAHIV 286
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
327-534 5.54e-13

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 69.78  E-value: 5.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRssGKLVAVKKMDLRKQQR--RELLFNEVVIMRdyqHENVVemynSYLVGD--------ELWVVME 396
Cdd:cd14143   3 IGKGRFGEVWRGRWR--GEDVAVKIFSSREERSwfREAEIYQTVMLR---HENIL----GFIAADnkdngtwtQLWLVSD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLH-----AQG---VIHRDIKSDSILLTHDGRVKLSDFGFC-----A 463
Cdd:cd14143  74 YHEHGSLFDYLNRYTVTVEGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDLKSKNILVKKNGTCCIADLGLAvrhdsA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 QVSKEVPRRKSlVGTPYWMAPELIS------RLPYGPEVDIWSLGIMVIEMV----------DGEPPYFN----EPPLKA 523
Cdd:cd14143 154 TDTIDIAPNHR-VGTKRYMAPEVLDdtinmkHFESFKRADIYALGLVFWEIArrcsiggiheDYQLPYYDlvpsDPSIEE 232
                       250
                ....*....|....*..
gi 5031975  524 MK------MIRDNLPPR 534
Cdd:cd14143 233 MRkvvceqKLRPNIPNR 249
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
350-572 6.55e-13

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: 69.39  E-value: 6.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  350 KKMDLRKQQRRELLFNEVVImrdyQHENVVEMYNSYLVGDE----LWVVMEFLEGGALTDIV-----THTRMNEEQIAAV 420
Cdd:cd14034  48 KNFKLQEEKVKAVFDNLIQL----EHLNIVKFHKYWADVKEnrarVIFITEYMSSGSLKQFLkktkkNHKTMNEKAWKRW 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  421 CLAVLQALSVLHA--QGVIHRDIKSDSILLTHDGRVKLSDFGfCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDI 498
Cdd:cd14034 124 CTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQKNLHFFAPEYGEVANVTTAVDI 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  499 WSLGIMVIEMV------DGEPPYFNEPPLK-AMKMIRDnlpprlknlhkvsPSLKGFLDRLLVRDPAQRATAAELLKHPF 571
Cdd:cd14034 203 YSFGMCALEMAvleiqgNGESSYVPQEAINsAIQLLED-------------PLQREFIQKCLEVDPSKRPTARELLFHQA 269

                .
gi 5031975  572 L 572
Cdd:cd14034 270 L 270
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
347-538 6.97e-13

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 69.27  E-value: 6.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  347 VAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTR--MNEEQIAAVCL 422
Cdd:cd14153  25 VAIRLIDIERDNEEQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKvvLDVNKTRQIAQ 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  423 AVLQALSVLHAQGVIHRDIKSDSILLThDGRVKLSDFG-FCAQVSKEVPRRKSLVGTPY-W---MAPELI---------S 488
Cdd:cd14153 105 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlFTISGVLQAGRREDKLRIQSgWlchLAPEIIrqlspeteeD 183
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5031975  489 RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNL 538
Cdd:cd14153 184 KLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSQI 233
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
317-566 7.64e-13

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 69.48  E-value: 7.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIAtvRSSGKL-------VAVK--KMDLRKQQRRELlFNEVVIMRDYQHENVVEMYNSYLV 387
Cdd:cd05050   3 PRNNIEYVRDIGQGAFGRVFQA--RAPGLLpyepftmVAVKmlKEEASADMQADF-QREAALMAEFDHPNIVKLLGVCAV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  388 GDELWVVMEFLEGGALTDIVTH-----------------------TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSD 444
Cdd:cd05050  80 GKPMCLLFEYMAYGDLNEFLRHrspraqcslshstssarkcglnpLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  445 SILLTHDGRVKLSDFGFCAQV----------SKEVPRRkslvgtpyWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEP 513
Cdd:cd05050 160 NCLVGENMVVKIADFGLSRNIysadyykaseNDAIPIR--------WMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQ 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031975  514 PYFNEPPLKAMKMIRD--------NLPPRLKNLHKVSPSlkgfldrllvRDPAQRATAAEL 566
Cdd:cd05050 232 PYYGMAHEEVIYYVRDgnvlscpdNCPLELYNLMRLCWS----------KLPSDRPSFASI 282
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
327-572 7.94e-13

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 69.70  E-value: 7.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFN-------EVVIMRDYQHENVVEMYNSY-LVGDELWVVMEFL 398
Cdd:cd14041  14 LGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDSFCTVLEYC 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  399 EGGALT-DIVTHTRMNEEQIAAVCLAVLQALSVLHA--QGVIHRDIKSDSILL---THDGRVKLSDFGFCAQVSKE---- 468
Cdd:cd14041  94 EGNDLDfYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIKITDFGLSKIMDDDsyns 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  469 ---VPRRKSLVGTPYWMAPE--LISRLP--YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLK-------AMKMIRDNLPPR 534
Cdd:cd14041 174 vdgMELTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQdilqentILKATEVQFPPK 253
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  535 lknlHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14041 254 ----PVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
326-566 8.44e-13

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 69.22  E-value: 8.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIA-----TVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05092  12 ELGEGAFGKVFLAechnlLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRH 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALT----------------DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ 464
Cdd:cd05092  92 GDLNrflrshgpdakildggEGQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSRD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  465 V-SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMI---RDNLPPRlknl 538
Cdd:cd05092 172 IySTDYYRVGGRTMLPIrWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECItqgRELERPR---- 247
                       250       260
                ....*....|....*....|....*...
gi 5031975  539 hKVSPSLKGFLDRLLVRDPAQRATAAEL 566
Cdd:cd05092 248 -TCPPEVYAIMQGCWQREPQQRHSIKDI 274
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
327-514 9.03e-13

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 69.08  E-value: 9.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSgkLVAVKKM----DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd14159   1 IGEGGFGCVYQAVMRNT--EYAVKRLkedsELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDivthtRMNEeQIAAVCLAVLQALSV----------LH--AQGVIHRDIKSDSILLTHDGRVKLSDFG---FC----- 462
Cdd:cd14159  79 LED-----RLHC-QVSCPCLSWSQRLHVllgtaraiqyLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGlarFSrrpkq 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  463 AQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPP 514
Cdd:cd14159 153 PGMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
317-515 1.00e-12

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes 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 (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 68.94  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVME 396
Cdd:cd05069  10 PRESLRLDVKLGQGCFGEVWMGTWNGTTK-VAIKTLK-PGTMMPEAFLQEAQIMKKLRHDKLVPLY-AVVSEEPIYIVTE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTH---TRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRR 472
Cdd:cd05069  87 FMGKGSLLDFLKEgdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEdNEYTAR 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPY 515
Cdd:cd05069 167 QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPY 210
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
326-577 1.26e-12

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 68.50  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIA-----TVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 400
Cdd:cd05094  12 ELGEGAFGKVFLAecynlSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKH 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  401 GALTDIV-----------------THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA 463
Cdd:cd05094  92 GDLNKFLrahgpdamilvdgqprqAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  464 QV-SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRDNlppRLKNLHK 540
Cdd:cd05094 172 DVySTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIECITQG---RVLERPR 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5031975  541 VSPslKGFLDRLL---VRDPAQRATAAELLKHPF-LAKAGP 577
Cdd:cd05094 249 VCP--KEVYDIMLgcwQREPQQRLNIKEIYKILHaLGKATP 287
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
327-568 1.39e-12

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET 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: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 68.45  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATV-----RSSGKLVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 399
Cdd:cd05045   8 LGEGEFGKVVKATAfrlkgRAGYTTVAVKmlKENASSSELRDLL-SEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTR-------------------------MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRV 454
Cdd:cd05045  87 YGSLRSFLRESRkvgpsylgsdgnrnssyldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRKM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  455 KLSDFGFCAQVSKE---VPRRKSLVGTPyWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRDN 530
Cdd:cd05045 167 KISDFGLSRDVYEEdsyVKRSKGRIPVK-WMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLFNLLKTG 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5031975  531 LppRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLK 568
Cdd:cd05045 246 Y--RMERPENCSEEMYNLMLTCWKQEPDKRPTFADISK 281
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
327-541 1.51e-12

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: 68.07  E-value: 1.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVcIATVRSSGKLVAVKKMDLRKQQRRELLFN---------------------EVVIMRDYQHENVVemynsY 385
Cdd:cd14067   1 LGQGGSGTV-IYRARYQGQPVAVKRFHIKKCKKRTDGSAdtmlkhlraadamknfsefrqEASMLHSLQHPCIV-----Y 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  386 LVG---DELWVVMEFLEGGALTDIVTHTRMNEEQIA-------AVCLAVLQALSVLHAQGVIHRDIKSDSILL-THDGR- 453
Cdd:cd14067  75 LIGisiHPLCFALELAPLGSLNTVLEENHKGSSFMPlghmltfKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwSLDVQe 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  454 ---VKLSDFGFCAQVSKEvpRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDN 530
Cdd:cd14067 155 hinIKLSDYGISRQSFHE--GALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
                       250
                ....*....|.
gi 5031975  531 LPPRLKNLHKV 541
Cdd:cd14067 233 IRPVLGQPEEV 243
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
416-507 1.58e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 69.92  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975   416 QIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC--AQVSKEVPRRKSLVGTPYWMAPELISRLPYG 493
Cdd:PHA03211 261 QVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAAcfARGSWSTPFHYGIAGTVDTNAPEVLAGDPYT 340
                         90
                 ....*....|....
gi 5031975   494 PEVDIWSLGIMVIE 507
Cdd:PHA03211 341 PSVDIWSAGLVIFE 354
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
366-572 1.66e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 68.93  E-value: 1.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  366 EVVIMRDYQHENVVEMYNSYL--VGDELWVVMEFLEGGALTDIVTH--TRMNEE-------QIAAVCLAVLQALSVLHAQ 434
Cdd:cd07868  64 EIALLRELKHPNVISLQKVFLshADRKVWLLFDYAEHDLWHIIKFHraSKANKKpvqlprgMVKSLLYQILDGIHYLHAN 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  435 GVIHRDIKSDSILLTHD----GRVKLSDFGFCAQVS---KEVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVI 506
Cdd:cd07868 144 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  507 EMVDGEP-------------PY--------FNEPPLKA----------------MKMIRDNLPP-----RLKNLHKVSPS 544
Cdd:cd07868 224 ELLTSEPifhcrqediktsnPYhhdqldriFNVMGFPAdkdwedikkmpehstlMKDFRRNTYTncsliKYMEKHKVKPD 303
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  545 LKGF--LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07868 304 SKAFhlLQKLLTMDPIKRITSEQAMQDPYF 333
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
317-515 2.04e-12

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src 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: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 67.79  E-value: 2.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVME 396
Cdd:cd05071   7 PRESLRLEVKLGQGCFGEVWMGTWNGTTR-VAIKTLK-PGTMSPEAFLQEAQVMKKLRHEKLVQLY-AVVSEEPIYIVTE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIV---THTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRR 472
Cdd:cd05071  84 YMSKGSLLDFLkgeMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEdNEYTAR 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEM-VDGEPPY 515
Cdd:cd05071 164 QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELtTKGRVPY 207
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
326-551 2.15e-12

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 67.67  E-value: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMdlRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEfLEGGALT 404
Cdd:cd14017   7 KIGGGGFGEIYKVRDVVDGEEVAMKVE--SKSQPKQVLKMEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMT-LLGPNLA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHT---RMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLthdGR-------VKLSDFGFCAQV---SKEVPR 471
Cdd:cd14017  84 ELRRSQprgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAI---GRgpsdertVYILDFGLARQYtnkDGEVER 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  472 RKS----LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFN----EPPLKAMKMIRD-----NLPPRLKNL 538
Cdd:cd14017 161 PPRnaagFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKlkdkEEVGKMKEKIDHeellkGLPKEFFQI 240
                       250
                ....*....|...
gi 5031975  539 HKVSPSLKgFLDR 551
Cdd:cd14017 241 LKHIRSLS-YFDT 252
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
326-570 3.04e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 67.36  E-value: 3.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIV---------CIATVRSSGKLVAvKKMDlRKQQRRELLFNEVVimrdYQHENVVEMYNSYLVGDELWVVME 396
Cdd:cd14138  12 KIGSGEFGSVfkcvkrldgCIYAIKRSKKPLA-GSVD-EQNALREVYAHAVL----GQHSHVVRYYSAWAEDDHMLIQNE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVT--HTRMN---EEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH-----------------DGRV 454
Cdd:cd14138  86 YCNGGSLADAISenYRIMSyftEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRtsipnaaseegdedewaSNKV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  455 --KLSDFGFCAQVSKevPRRKSlvGTPYWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDNL 531
Cdd:cd14138 166 ifKIGDLGHVTRVSS--PQVEE--GDSRFLANEVLQEnYTHLPKADIFALALTVVCAAGAEPLPTNG---DQWHEIRQGK 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 5031975  532 PPRLKNLhkVSPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14138 239 LPRIPQV--LSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
366-572 3.23e-12

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 67.79  E-value: 3.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  366 EVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLEGGALTDIVTH---------TRMNEEQIAAVCLAVLQALSVLHAQ 434
Cdd:cd07867  49 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEHDLWHIIKFHraskankkpMQLPRSMVKSLLYQILDGIHYLHAN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  435 GVIHRDIKSDSILLTHD----GRVKLSDFGFCAQVS---KEVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVI 506
Cdd:cd07867 129 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  507 EMVDGEP-------------PYFNE-----------PPLKAMKMIRD--NLPPRLKNL----------------HKVSPS 544
Cdd:cd07867 209 ELLTSEPifhcrqediktsnPFHHDqldrifsvmgfPADKDWEDIRKmpEYPTLQKDFrrttyansslikymekHKVKPD 288
                       250       260       270
                ....*....|....*....|....*....|
gi 5031975  545 LKGF--LDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd07867 289 SKVFllLQKLLTMDPTKRITSEQALQDPYF 318
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
314-568 3.51e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 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: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 67.34  E-value: 3.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  314 PGDPRSYL--DNFI---KIGEGSTGIVCIATVRSSGK-------LVAVK--KMDLRKQQRRELLfNEVVIMRDY-QHENV 378
Cdd:cd05098   3 PEDPRWELprDRLVlgkPLGEGCFGQVVLAEAIGLDKdkpnrvtKVAVKmlKSDATEKDLSDLI-SEMEMMKMIgKHKNI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  379 VEMYNSYLVGDELWVVMEFLEGGALTDIVTHTR-----------------MNEEQIAAVCLAVLQALSVLHAQGVIHRDI 441
Cdd:cd05098  82 INLLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycynpshnpeeqLSSKDLVSCAYQVARGMEYLASKKCIHRDL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  442 KSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT-PY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNE 518
Cdd:cd05098 162 AARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRlPVkWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGV 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031975  519 PPLKAMKMirdnlpprLKNLHKVS-PSLKGFLDRLLVRD-----PAQRATAAELLK 568
Cdd:cd05098 242 PVEELFKL--------LKEGHRMDkPSNCTNELYMMMRDcwhavPSQRPTFKQLVE 289
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
326-570 3.55e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 67.26  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKmdlrkqQRREL--LFNEVVIMRDY-------QHENVVEMYNSYLVGDELWVVME 396
Cdd:cd14139   7 KIGVGEFGSVYKCIKRLDGCVYAIKR------SMRPFagSSNEQLALHEVyahavlgHHPHVVRYYSAWAEDDHMIIQNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTR-----MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRV----------------- 454
Cdd:cd14139  81 YCNGGSLQDAISENTksgnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQSssgvgeevsneedefls 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  455 -----KLSDFGFCAQVSKevPRRKSlvGTPYWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKmiR 528
Cdd:cd14139 161 anvvyKIGDLGHVTSINK--PQVEE--GDSRFLANEILQEdYRHLPKADIFALGLTVALAAGAEPLPTNGAAWHHIR--K 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 5031975  529 DNLPPRLknlHKVSPSLKGFLDRLLVRDPAQRATAAELLKHP 570
Cdd:cd14139 235 GNFPDVP---QELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
317-529 4.14e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 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: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 67.35  E-value: 4.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGK-------LVAVKKM-DLRKQQRRELLFNEVVIMRDY-QHENVVEMYNSYLV 387
Cdd:cd05101  22 PRDKLTLGKPLGEGCFGQVVMAEAVGIDKdkpkeavTVAVKMLkDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  388 GDELWVVMEFLEGGALTDIVTH------------TRMNEEQ-----IAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTH 450
Cdd:cd05101 102 DGPLYVIVEYASKGNLREYLRArrppgmeysydiNRVPEEQmtfkdLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  451 DGRVKLSDFGFCAQVSKEVPRRKSLVGT-PY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMI 527
Cdd:cd05101 182 NNVMKIADFGLARDINNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKLL 261

                ..
gi 5031975  528 RD 529
Cdd:cd05101 262 KE 263
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
326-515 4.61e-12

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 66.68  E-value: 4.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd05052  13 KLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFL-KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVThtRMNEEQIAAVCL-----AVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd05052  92 YLR--ECNREELNAVVLlymatQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPI 169
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 5031975  481 -WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05052 170 kWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPY 206
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
326-479 4.66e-12

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 66.71  E-value: 4.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKLVAVK--KMDLRKQQrrelLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLeGGA 402
Cdd:cd14016   7 KIGSGSFGEVYLGIDLKTGEEVAIKieKKDSKHPQ----LEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDLL-GPS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVT--HTRMNEEQIAavCLAV--LQALSVLHAQGVIHRDIKSDSILL---THDGRVKLSDFGFCA----QVSKE-VP 470
Cdd:cd14016  82 LEDLFNkcGRKFSLKTVL--MLADqmISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKkyrdPRTGKhIP 159
                       170
                ....*....|.
gi 5031975  471 RR--KSLVGTP 479
Cdd:cd14016 160 YRegKSLTGTA 170
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
326-515 5.33e-12

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 66.09  E-value: 5.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNsyLVGDE-LWVVMEFLEGGALT 404
Cdd:cd14203   2 KLGQGCFGEVWMGTWNGTTK-VAIKTLK-PGTMSPEAFLEEAQIMKKLRHDKLVQLYA--VVSEEpIYIVTEFMSKGSLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRRKSLVGTPY 480
Cdd:cd14203  78 DFLKDGEgkyLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEdNEYTARQGAKFPIK 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 5031975  481 WMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPY 515
Cdd:cd14203 158 WTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPY 193
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
344-538 5.42e-12

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 66.57  E-value: 5.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  344 GKLVAVKKM-DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL------------------T 404
Cdd:cd05090  34 AQLVAIKTLkDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLheflimrsphsdvgcssdE 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  405 DIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKEVPRRKSLVGTPY-WM 482
Cdd:cd05090 114 DGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIySSDYYRVQNKSLLPIrWM 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031975  483 APELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIR--------DNLPPRLKNL 538
Cdd:cd05090 194 PPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRkrqllpcsEDCPPRMYSL 258
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
327-515 5.69e-12

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 66.40  E-value: 5.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVR----SSGKlVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDEL------WVV 394
Cdd:cd05035   7 LGEGEFGSVMEAQLKqddgSQLK-VAVKTMKVDIHTYSEIeeFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppspMVI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  395 MEFLEGGALTDIVTHTRMNE-------EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-S 466
Cdd:cd05035  86 LPFMKHGDLHSYLLYSRLGGlpeklplQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIyS 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 5031975  467 KEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPY 515
Cdd:cd05035 166 GDYYRQGRISKMPVkWIALESLADNVYTSKSDVWSFGVTMWEiATRGQTPY 216
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
314-529 6.12e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 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: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 66.97  E-value: 6.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  314 PGDP-----RSYLDNFIKIGEGSTGIVCIATV------RSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDY-QHENVV 379
Cdd:cd05100   2 PADPkwelsRTRLTLGKPLGEGCFGQVVMAEAigidkdKPNKPVTVAVKMLKDDATDKDLsdLVSEMEMMKMIgKHKNII 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  380 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTR------------MNEEQIA-----AVCLAVLQALSVLHAQGVIHRDIK 442
Cdd:cd05100  82 NLLGACTQDGPLYVLVEYASKGNLREYLRARRppgmdysfdtckLPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  443 SDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT-PY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEP 519
Cdd:cd05100 162 ARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 241
                       250
                ....*....|
gi 5031975  520 PLKAMKMIRD 529
Cdd:cd05100 242 VEELFKLLKE 251
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
375-564 8.32e-12

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 66.25  E-value: 8.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  375 HENVVEMYNSYLVGDEL----WVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHA----QG-----VIHRDI 441
Cdd:cd14055  54 HENILQFLTAEERGVGLdrqyWLITAYHENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSdrtpCGrpkipIAHRDL 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  442 KSDSILLTHDGRVKLSDFGFCAQVSKEVpRRKSL-----VGTPYWMAPELISR------LPYGPEVDIWSLGIMVIEMV- 509
Cdd:cd14055 134 KSSNILVKNDGTCVLADFGLALRLDPSL-SVDELansgqVGTARYMAPEALESrvnledLESFKQIDVYSMALVLWEMAs 212
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031975  510 ---------DGEPPYFN----EPPLKAMKMI------RDNLPPRLKNlHKVSPSLKGFLDRLLVRDPAQRATAA 564
Cdd:cd14055 213 rceasgevkPYELPFGSkvreRPCVESMKDLvlrdrgRPEIPDSWLT-HQGMCVLCDTITECWDHDPEARLTAS 285
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
326-515 1.11e-11

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 65.00  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRSSGKlVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 405
Cdd:cd05034   2 KLGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSPEAFL-QEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  406 IVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKE---VPRRkslvGTP 479
Cdd:cd05034  80 YLRTGEgraLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGL-ARLIEDdeyTARE----GAK 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 5031975  480 Y---WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05034 155 FpikWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPY 194
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
327-515 1.11e-11

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 65.80  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKL--VAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDEL------WVVME 396
Cdd:cd05075   8 LGEGEFGSVMEGQLNQDDSVlkVAVKTMKIAICTRSEMedFLSEAVCMKEFDHPNVMRLIGVCLQNTESegypspVVILP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTRMNE-------EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKE 468
Cdd:cd05075  88 FMKHGDLHSFLLYSRLGDcpvylptQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIyNGD 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031975  469 VPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05075 168 YYRQGRISKMPVkWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPY 216
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
326-568 1.47e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 65.45  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVCIATVRssGKLVAVKKMDLRKQQR--RELLFNEVVIMRdyqHENVVEMYNSYLVGD----ELWVVMEFLE 399
Cdd:cd14220   2 QIGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  400 GGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQ--------GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK---- 467
Cdd:cd14220  77 NGSLYDFLKCTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSdtne 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  468 -EVPrRKSLVGTPYWMAPEL----ISRLPYGPEV--DIWSLGIMVIEMV----------DGEPPYF----NEPPLKAMKM 526
Cdd:cd14220 157 vDVP-LNTRVGTKRYMAPEVldesLNKNHFQAYImaDIYSFGLIIWEMArrcvtggiveEYQLPYYdmvpSDPSYEDMRE 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  527 I--RDNLPPRLKNLHKVSPSLKGFLDRL---LVRDPAQRATAAELLK 568
Cdd:cd14220 236 VvcVKRLRPTVSNRWNSDECLRAVLKLMsecWAHNPASRLTALRIKK 282
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
11-43 1.52e-11

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 59.14  E-value: 1.52e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 5031975      11 ISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLI 43
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFTGLPTEWKSLL 33
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
415-569 2.44e-11

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 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: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 65.39  E-value: 2.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  415 EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPR--RKSLVGTPY-WMAPELISRLP 491
Cdd:cd05103 179 EDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKD-PDyvRKGDARLPLkWMAPETIFDRV 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  492 YGPEVDIWSLGIMVIEMVD-GEPPYfnePPLKamkmIRDNLPPRLKNLHKV------SPSLKGFLDRLLVRDPAQRATAA 564
Cdd:cd05103 258 YTIQSDVWSFGVLLWEIFSlGASPY---PGVK----IDEEFCRRLKEGTRMrapdytTPEMYQTMLDCWHGEPSQRPTFS 330

                ....*
gi 5031975  565 ELLKH 569
Cdd:cd05103 331 ELVEH 335
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
374-572 3.22e-11

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: 63.60  E-value: 3.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  374 QHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR 453
Cdd:cd13976  43 SHPNISGVHEVIAGETKAYVFFERDHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  454 VKLSDFGFCAQVSKEvPRRKSL---VGTPYWMAPELI-SRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR 528
Cdd:cd13976 123 TKLRLESLEDAVILE-GEDDSLsdkHGCPAYVSPEILnSGATYsGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIR 201
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5031975  529 D---NLPPRLknlhkvSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd13976 202 RgqfAIPETL------SPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
347-519 3.62e-11

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 63.97  E-value: 3.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  347 VAVKKM-DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLvGDELWVVMEFLEGGALTDIVTH--TRMNEEQIAAVCLA 423
Cdd:cd05057  39 VAIKVLrEETGPKANEEILDEAYVMASVDHPHLVRLLGICL-SSQVQLITQLMPLGCLLDYVRNhrDNIGSQLLLNWCVQ 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  424 VLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG-TPY-WMAPELISRLPYGPEVDIWSL 501
Cdd:cd05057 118 IAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGkVPIkWMALESIQYRIYTHKSDVWSY 197
                       170
                ....*....|....*....
gi 5031975  502 GIMVIE-MVDGEPPYFNEP 519
Cdd:cd05057 198 GVTVWElMTFGAKPYEGIP 216
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
327-515 3.63e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 63.91  E-value: 3.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLV--AVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTRMNE-----------------EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqv 465
Cdd:cd05047  83 LLDFLRKSRVLEtdpafaianstastlssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  466 SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05047 161 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 212
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
363-568 5.39e-11

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 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: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 64.22  E-value: 5.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  363 LFNEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTH------------TRMNEEQIA-----AVCLAV 424
Cdd:cd05099  64 LISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRArrppgpdytfdiTKVPEEQLSfkdlvSCAYQV 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  425 LQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG-TPY-WMAPELISRLPYGPEVDIWSLG 502
Cdd:cd05099 144 ARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGrLPVkWMAPEALFDRVYTHQSDVWSFG 223
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031975  503 IMVIEMVD-GEPPYFNEPPLKAMKMIRDNlpPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLK 568
Cdd:cd05099 224 ILMWEIFTlGGSPYPGIPVEELFKLLREG--HRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVE 288
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
336-509 7.97e-11

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 63.13  E-value: 7.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  336 CIATVRSSGKLVAVKKMDLRKQQ----RRELlFNevviMRDYQHENVVEMYNSYLVGD----ELWVVMEFLEGGALTDIV 407
Cdd:cd14140  10 CVWKAQLMNEYVAVKIFPIQDKQswqsEREI-FS----TPGMKHENLLQFIAAEKRGSnlemELWLITAFHDKGSLTDYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  408 THTRMNEEQIAAVCLAVLQALSVLHAQ-----------GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVP--RRKS 474
Cdd:cd14140  85 KGNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPpgDTHG 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031975  475 LVGTPYWMAPELI------SRLPYgPEVDIWSLGIMVIEMV 509
Cdd:cd14140 165 QVGTRRYMAPEVLegainfQRDSF-LRIDMYAMGLVLWELV 204
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
375-572 8.97e-11

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: 62.37  E-value: 8.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  375 HENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGR- 453
Cdd:cd14023  44 HRNITGIVEVILGDTKAYVFFEKDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERt 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  454 -VKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPY--GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDN 530
Cdd:cd14023 124 qLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG 203
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031975  531 ---LPprlknlHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 572
Cdd:cd14023 204 qfcIP------DHVSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
327-515 9.90e-11

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 62.49  E-value: 9.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKL---VAVKKMD-LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDEL-WVVMEFLEGG 401
Cdd:cd05058   3 IGKGHFGCVYHGTLIDSDGQkihCAVKSLNrITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSpLVVLPYMKHG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHTRMNE--EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKEV--PRRKSLV 476
Cdd:cd05058  83 DLRNFIRSETHNPtvKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIyDKEYysVHNHTGA 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5031975  477 GTPY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPPY 515
Cdd:cd05058 163 KLPVkWMALESLQTQKFTTKSDVWSFGVLLWElMTRGAPPY 203
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
327-515 1.06e-10

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 63.09  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  327 IGEGSTGIVCIATVRSSGKLV--AVKKMD--LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 402
Cdd:cd05088  15 IGEGNFGQVLKARIKKDGLRMdaAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  403 LTDIVTHTR-----------------MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqv 465
Cdd:cd05088  95 LLDFLRKSRvletdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5031975  466 SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05088 173 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 224
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
317-515 1.40e-10

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 62.39  E-value: 1.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  317 PRSYLDNFIKIGEGSTGIVCIATVRSSGKlVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVME 396
Cdd:cd05070   7 PRESLQLIKRLGNGQFGEVWMGTWNGNTK-VAIKTLK-PGTMSPESFLEEAQIMKKLKHDKLVQLY-AVVSEEPIYIVTE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  397 FLEGGALTDIVTHTR---MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS-KEVPRR 472
Cdd:cd05070  84 YMSKGSLLDFLKDGEgraLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEdNEYTAR 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 5031975  473 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV-DGEPPY 515
Cdd:cd05070 164 QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPY 207
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
326-515 1.45e-10

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 61.90  E-value: 1.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  326 KIGEGSTGIVC--IATVRSSGKLVAVK--KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVMEFLEGG 401
Cdd:cd05116   2 ELGSGNFGTVKkgYYQMKKVVKTVAVKilKNEANDPALKDELLREANVMQQLDNPYIVRMI-GICEAESWMLVMEMAELG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  402 ALTDIVTHTR-MNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 480
Cdd:cd05116  81 PLNKFLQKNRhVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKW 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 5031975  481 ---WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 515
Cdd:cd05116 161 pvkWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPY 199
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
415-568 2.07e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 62.33  E-value: 2.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  415 EQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEvPR--RKSLVGTPY-WMAPELISRLP 491
Cdd:cd14207 180 EDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKN-PDyvRKGDARLPLkWMAPESIFDKI 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  492 YGPEVDIWSLGIMVIEMVD-GEPPYfnePPLKAMKMIRDNLPP--RLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLK 568
Cdd:cd14207 259 YSTKSDVWSYGVLLWEIFSlGASPY---PGVQIDEDFCSKLKEgiRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVE 335
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
345-590 2.12e-10

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 62.00  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  345 KLVAVKKMDLRKQQRRELLFN-------EVVIMRDYQHENVVEMYNSY-LVGDELWVVMEFLEGGALT-DIVTHTRMNEE 415
Cdd:cd14040  32 RYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDfYLKQHKLMSEK 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  416 QIAAVCLAVLQALSVLH--AQGVIHRDIKSDSILL---THDGRVKLSDFGFCAQVSKE------VPRRKSLVGTPYWMAP 484
Cdd:cd14040 112 EARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgMDLTSQGAGTYWYLPP 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031975  485 E--LISRLP--YGPEVDIWSLGIMVIEMVDGEPPYFNEPplKAMKMIRDNLPPRLKNLH-----KVSPSLKGFLDRLLVR 555
Cdd:cd14040 192 EcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQ--SQQDILQENTILKATEVQfpvkpVVSNEAKAFIRRCLAY 269
                       250       260       270
                ....*....|....*....|....*....|....*
gi 5031975  556 DPAQRATAAELLKHPFLakagppasiVPLMRQNRT 590
Cdd:cd14040 270 RKEDRFDVHQLASDPYL---------LPHMRRSNS 295
 
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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