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Conserved domains on  [gi|17865613|sp|Q63802|]
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RecName: Full=Wee1-like protein kinase; AltName: Full=Wee1A kinase

Protein Classification

wee1-like protein kinase( domain architecture ID 10197647)

wee1-like protein kinase is an atypical tyrosine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates; although functionally a tyrosine kinase, in sequence and structure it most closely resembles serine/threonine kinases such as Chk1 and cAMP kinases

CATH:  1.10.510.10
EC:  2.7.10.2
Gene Symbol:  WEE1
Gene Ontology:  GO:0005524|GO:0006468|GO:0004713
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
292-567 0e+00

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: 608.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHM 371
Cdd:cd14138   1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEEGDEDDW 451
Cdd:cd14138  81 LIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDEW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 ISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLP 531
Cdd:cd14138 161 ASNKVIFKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPTNGDQWHEIRQGKLP 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd14138 241 RIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHSV 276
 
Name Accession Description Interval E-value
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
292-567 0e+00

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: 608.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHM 371
Cdd:cd14138   1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEEGDEDDW 451
Cdd:cd14138  81 LIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDEW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 ISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLP 531
Cdd:cd14138 161 ASNKVIFKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPTNGDQWHEIRQGKLP 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd14138 241 RIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHSV 276
Pkinase pfam00069
Protein kinase domain;
298-568 1.44e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 185.53  E-value: 1.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   378 CNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRyihsmslvhmdikpsnifisrtsipnavseegdeddwisnkvm 457
Cdd:pfam00069  80 VEGGSLFDLLSEK----GAFSEREAKFIMKQILEGLE------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   458 fkigdlghvtRISSPQVEEGDSRFLANEVLQENYsHLPKADIFALALTVVC-AAGAEPLP---RNGDQWHEIRQG-RLPR 532
Cdd:pfam00069 113 ----------SGSSLTTFVGTPWYMAPEVLGGNP-YGPKVDVWSLGCILYElLTGKPPFPginGNEIYELIIDQPyAFPE 181
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 17865613   533 IPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:pfam00069 182 LPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
298-565 4.75e-43

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 155.38  E-value: 4.75e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI-KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwiSNKVm 457
Cdd:smart00220  79 CEGGDLFDLLKKRGR----LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE-----------------DGHV- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    458 fKIGDLG----------HVTRISSPQveegdsrFLANEVLQEN-YSHlpKADIFAL-ALTVVCAAGAEPLPRNGDQWHEI 525
Cdd:smart00220 137 -KLADFGlarqldpgekLTTFVGTPE-------YMAPEVLLGKgYGK--AVDIWSLgVILYELLTGKPPFPGDDQLLELF 206
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 17865613    526 RQGRLPRIPQ-----VLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:smart00220 207 KKIGKPKPPFpppewDISPEAKDLIRKLLVKDPEKRLTAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
301-560 1.57e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 128.59  E-value: 1.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFrREARALARL-NHPNIVRVYDVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegdeddwisnkvmfK 459
Cdd:COG0515  91 GESLADLLRRRGP----LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV-------------------K 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISSPQVEEGDSR-----FLANEVLQ-ENYShlPKADIFALALTV-VCAAGAEPLPRNGDQ--WHEIRQGRL 530
Cdd:COG0515 148 LIDFGIARALGGATLTQTGTVvgtpgYMAPEQARgEPVD--PRSDVYSLGVTLyELLTGRPPFDGDSPAelLRAHLREPP 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 531 PRIPQV---LSQELTELLKVMIHPDPERRPSAM 560
Cdd:COG0515 226 PPPSELrpdLPPALDAIVLRALAKDPEERYQSA 258
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
288-578 6.64e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 79.48  E-value: 6.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  288 SNMKSRYTTEFHELEK---IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAlREVyahAVL--GQHPHVVRYF 362
Cdd:PLN00034  63 SGSAPSAAKSLSELERvnrIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQIC-REI---EILrdVNHPNVVKCH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  363 SAWAEDDHMLIQNEYCNGGSLadavsENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI-SRTSIpna 441
Cdd:PLN00034 139 DMFDHNGEIQVLLEFMDGGSL-----EGTHIAD---EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLInSAKNV--- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  442 vseegdeddwisnkvmfKIGDLGhVTRISSPQVEEGDSR-----FLANEVLQENYSHLP----KADIFALALTVV-CAAG 511
Cdd:PLN00034 208 -----------------KIADFG-VSRILAQTMDPCNSSvgtiaYMSPERINTDLNHGAydgyAGDIWSLGVSILeFYLG 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613  512 AEPLP--RNGDqWHE----IRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQ 578
Cdd:PLN00034 270 RFPFGvgRQGD-WASlmcaICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQG 341
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
301-436 1.37e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 51.33  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgsvDEQNAL----REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:NF033483  12 GERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDLA---RDPEFVarfrREAQSAASL-SHPNIVSVYDVGEDGGIPYIVME 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  377 YCNGGSLADAVSENYRvMSYfTEAElkDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:NF033483  88 YVDGRTLKDYIREHGP-LSP-EEAV--EIMIQILSALEHAHRNGIVHRDIKPQNILITKD 143
 
Name Accession Description Interval E-value
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
292-567 0e+00

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: 608.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHM 371
Cdd:cd14138   1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEEGDEDDW 451
Cdd:cd14138  81 LIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDEW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 ISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLP 531
Cdd:cd14138 161 ASNKVIFKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPTNGDQWHEIRQGKLP 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd14138 241 RIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHSV 276
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
297-567 0e+00

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: 560.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14051   1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVYAHAVLGKHPHVVRYYSAWAEDDHMIIQNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEE-----GDEDDW 451
Cdd:cd14051  81 YCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSEEEeedfeGEEDNP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 ISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLP 531
Cdd:cd14051 161 ESNEVTYKIGDLGHVTSISNPQVEEGDCRFLANEILQENYSHLPKADIFALALTVYEAAGGGPLPKNGDEWHEIRQGNLP 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 532 RIPQvLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd14051 241 PLPQ-CSPEFNELLRSMIHPDPEKRPSAAALLQHPV 275
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
297-567 1.64e-156

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: 451.30  E-value: 1.64e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14139   1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR--TSIPNAVSEEGDEDDW-IS 453
Cdd:cd14139  81 YCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHkmQSSSGVGEEVSNEEDEfLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 NKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRI 533
Cdd:cd14139 161 ANVVYKIGDLGHVTSINKPQVEEGDSRFLANEILQEDYRHLPKADIFALGLTVALAAGAEPLPTNGAAWHHIRKGNFPDV 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 17865613 534 PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd14139 241 PQELPESFSSLLKNMIQPDPEQRPSATALARHTV 274
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
297-566 2.11e-134

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: 394.06  E-value: 2.11e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseegdeddwISNKV 456
Cdd:cd13997  81 LCENGSLQDALEELSP-ISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIF-------------------ISNKG 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRI-SSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQ 535
Cdd:cd13997 141 TCKIGDFGLATRLeTSGDVEEGDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQGKLPLPPG 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 536 -VLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd13997 221 lVLSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
298-565 2.23e-67

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: 220.64  E-value: 2.23e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CnGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvm 457
Cdd:cd14050  83 C-DTSLQQYCEETHSL----PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGV------------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQV---EEGDSRFLANEVLQENYShlPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLP-RI 533
Cdd:cd14050 139 CKLGDFGLVVELDKEDIhdaQEGDPRYMAPELLQGSFT--KAADIFSLGITILELACNLELPSGGDGWHQLRQGYLPeEF 216
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 534 PQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14050 217 TAGLSPELRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
292-560 4.85e-56

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: 191.35  E-value: 4.85e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHM 371
Cdd:cd13996   2 SRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEK-SSASEKVLREVKALAKL-NHPNIVRYYTAWVEEPPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVsENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddw 451
Cdd:cd13996  80 YIQMELCEGGTLRDWI-DRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDL------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isnkvMFKIGDLGHVTRISSPQVEE------------------GDSRFLANEVLQ-ENYSHlpKADIFALA-----LTVV 507
Cdd:cd13996 146 -----QVKIGDFGLATSIGNQKRELnnlnnnnngntsnnsvgiGTPLYASPEQLDgENYNE--KADIYSLGiilfeMLHP 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 508 CAAGAEPLPRNGDqwheIRQGRLPriPQVLSQELTE--LLKVMIHPDPERRPSAM 560
Cdd:cd13996 219 FKTAMERSTILTD----LRNGILP--ESFKAKHPKEadLIQSLLSKNPEERPSAE 267
Pkinase pfam00069
Protein kinase domain;
298-568 1.44e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 185.53  E-value: 1.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   378 CNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRyihsmslvhmdikpsnifisrtsipnavseegdeddwisnkvm 457
Cdd:pfam00069  80 VEGGSLFDLLSEK----GAFSEREAKFIMKQILEGLE------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   458 fkigdlghvtRISSPQVEEGDSRFLANEVLQENYsHLPKADIFALALTVVC-AAGAEPLP---RNGDQWHEIRQG-RLPR 532
Cdd:pfam00069 113 ----------SGSSLTTFVGTPWYMAPEVLGGNP-YGPKVDVWSLGCILYElLTGKPPFPginGNEIYELIIDQPyAFPE 181
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 17865613   533 IPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:pfam00069 182 LPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
304-566 1.03e-48

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: 169.37  E-value: 1.03e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVdEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKL-LEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFKIGDL 463
Cdd:cd00180  79 KDLLKENKGPLS---EEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT-------------------VKLADF 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 GHVTRISSPQVEEGDSRFL-----ANEVLQENYSHLPKADIFALALTVVCAagaeplprngdqwheirqgrlpripqvls 538
Cdd:cd00180 137 GLAKDLDSDDSLLKTTGGTtppyyAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------- 187
                       250       260
                ....*....|....*....|....*...
gi 17865613 539 QELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd00180 188 EELKDLIRRMLQYDPKKRPSAKELLEHL 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
298-566 6.90e-48

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: 169.52  E-value: 6.90e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKR-LDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ-----HPHVVRYFSAWAEDDHM 371
Cdd:cd14052   2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLEEV---SILREltldgHDNIVQLIDSWEYHGHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddw 451
Cdd:cd14052  79 YIQTELCENGSLDVFLSELGL-LGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITF---------EGT---- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isnkvmFKIGDLGHVTRISSPQ-VE-EGDSRFLANEVLQE-NYSHlpKADIFALALTVVCAAGAEPLPRNGDQWHEIRQG 528
Cdd:cd14052 145 ------LKIGDFGMATVWPLIRgIErEGDREYIAPEILSEhMYDK--PADIFSLGLILLEAAANVVLPDNGDAWQKLRSG 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 529 RLPRIPQ------------------------VLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14052 217 DLSDAPRlsstdlhsasspssnpppdppnmpILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
298-565 4.75e-43

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 155.38  E-value: 4.75e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI-KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwiSNKVm 457
Cdd:smart00220  79 CEGGDLFDLLKKRGR----LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE-----------------DGHV- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    458 fKIGDLG----------HVTRISSPQveegdsrFLANEVLQEN-YSHlpKADIFAL-ALTVVCAAGAEPLPRNGDQWHEI 525
Cdd:smart00220 137 -KLADFGlarqldpgekLTTFVGTPE-------YMAPEVLLGKgYGK--AVDIWSLgVILYELLTGKPPFPGDDQLLELF 206
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 17865613    526 RQGRLPRIPQ-----VLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:smart00220 207 KKIGKPKPPFpppewDISPEAKDLIRKLLVKDPEKRLTAEEALQH 251
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
291-565 2.20e-42

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: 154.45  E-value: 2.20e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 291 KSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPlAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDH 370
Cdd:cd14046   1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLR-SESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDD 450
Cdd:cd14046  79 LYIQMEYCEKSTLRDLIDSG----LFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFL-------------DSNG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 WIsnkvmfKIGDLGHVT---------------RISSPQVEEGDSR-------FLANEVLQENYSHL-PKADIFALAltVV 507
Cdd:cd14046 142 NV------KIGDFGLATsnklnvelatqdinkSTSAALGSSGDLTgnvgtalYVAPEVQSGTKSTYnEKVDMYSLG--II 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 508 CAAGAEPLPRNGDQWHEIRQGRLPRI------PQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14046 214 FFEMCYPFSTGMERVQILTALRSVSIefppdfDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
298-559 3.87e-40

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: 147.61  E-value: 3.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKR------SKKplagsvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHM 371
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEidlsnmSEK------EREEALNEVKLLSKL-KHPNIVKYYESFEENGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddw 451
Cdd:cd08215  75 CIVMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKD--------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isNKVmfKIGDLG--HV---------TRISSPQveegdsrFLANEVLQEN-YSHlpKADIFAL--------ALTVvcaag 511
Cdd:cd08215 140 --GVV--KLGDFGisKVlesttdlakTVVGTPY-------YLSPELCENKpYNY--KSDIWALgcvlyelcTLKH----- 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 512 aeplPRNGDQWHE----IRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd08215 202 ----PFEANNLPAlvykIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSA 249
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
292-565 2.65e-38

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: 142.63  E-value: 2.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHM 371
Cdd:cd14047   2 ERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK------LNNEKAEREVKALAKL-DHPNIVRYNGCWDGFDYD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 ----------------LIQNEYCNGGSLADAVSENYRVMSYFTEAElkDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsr 435
Cdd:cd14047  75 petsssnssrsktkclFIQMEFCEKGTLESWIEKRNGEKLDKVLAL--EIFEQITKGVEYIHSKKLIHRDLKPSNIFL-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 436 tsipnavSEEGdeddwisnKVmfKIGDLGHVTRISSP---QVEEGDSRFLANEVLQ-ENYSHlpKADIFALALTV----- 506
Cdd:cd14047 151 -------VDTG--------KV--KIGDFGLVTSLKNDgkrTKSKGTLSYMSPEQISsQDYGK--EVDIYALGLILfellh 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 507 VCAAGAEplprNGDQWHEIRQGRLPriPQVLSQELTE--LLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14047 212 VCDSAFE----KSKFWTDLRNGILP--DIFDKRYKIEktIIKKMLSKKPEDRPNASEILRT 266
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
302-568 1.20e-37

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: 140.73  E-value: 1.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPlAGSVDEQNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVKEVELS-GDSEEELEALeREIRILSSL-KHPNIVRYLGTERTENTLNIFLEYVPG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVsENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKI 460
Cdd:cd06606  84 GSLASLL-KKFGK---LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILV-------------DSDGVV------KL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQVEEGDS------RFLANEVL-QENYShlPKADIFALALTVV-CAAGAEPLPRNGDQ----WHEIRQG 528
Cdd:cd06606 141 ADFGCAKRLAEIATGEGTKslrgtpYWMAPEVIrGEGYG--RAADIWSLGCTVIeMATGKPPWSELGNPvaalFKIGSSG 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 529 RLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06606 219 EPPPIPEHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
297-565 1.72e-35

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: 134.25  E-value: 1.72e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKrsKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIK--KINLESKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGdeddwisnkv 456
Cdd:cd05122  78 FCSGGSLKDLLKNTNKT---LTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILL---------TSDG---------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPQVEE---GDSRFLANEVL-QENYShlPKADIFALALTVV-CAAGAEPLPRNGDQ--WHEIRQGR 529
Cdd:cd05122 136 EVKLIDFGLSAQLSDGKTRNtfvGTPYWMAPEVIqGKPYG--FKADIWSLGITAIeMAEGKPPYSELPPMkaLFLIATNG 213
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 530 LP--RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd05122 214 PPglRNPKKWSKEFKDFLKKCLQKDPEKRPTAEQLLKH 251
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
301-560 8.05e-35

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: 132.71  E-value: 8.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQN-ALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd14014   5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRErFLREARALARL-SHPNIVRVYDVGEDDGRPYIVMEYVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegdeddwisnkvmfK 459
Cdd:cd14014  84 GGSLADLLRERGP----LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRV-------------------K 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISSPQVEEGDSR-----FLANEVLQENYSHlPKADIFALALTV-VCAAGAepLPRNGDQWHEIRQG----- 528
Cdd:cd14014 141 LTDFGIARALGDSGLTQTGSVlgtpaYMAPEQARGGPVD-PRSDIYSLGVVLyELLTGR--PPFDGDSPAAVLAKhlqea 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 17865613 529 --RLPRIPQVLSQELTELLKVMIHPDPERRPSAM 560
Cdd:cd14014 218 ppPPSPLNPDVPPALDAIILRALAKDPEERPQSA 251
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
298-568 1.59e-34

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: 131.74  E-value: 1.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKcVKRL-DGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd08530   2 FKVLKKLGKGSYGSVYK-VKRLsDNQVYALKEVNLGSLSQKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkv 456
Cdd:cd08530  80 YAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL------------------ 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mFKIGDLGhVTRISSPQV---EEGDSRFLANEVLQEN-YSHlpKADIFAL-ALTVVCAAGAEPLprNGDQWHEIRQ---- 527
Cdd:cd08530 142 -VKIGDLG-ISKVLKKNLaktQIGTPLYAAPEVWKGRpYDY--KSDIWSLgCLLYEMATFRPPF--EARTMQELRYkvcr 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 528 GRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd08530 216 GKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSPAV 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
297-568 1.29e-32

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: 126.37  E-value: 1.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAV-SENYRVMsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnk 455
Cdd:cd08529  80 YAENGDLHSLIkSQRGRPL---PEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL-------------DKGDNV--- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGhVTRISSPQVE-----EGDSRFLANEVLQEN-YSHlpKADIFALALTVV-CAAGAEPLPRN--GDQWHEIR 526
Cdd:cd08529 141 ---KIGDLG-VAKILSDTTNfaqtiVGTPYYLSPELCEDKpYNE--KSDVWALGCVLYeLCTGKHPFEAQnqGALILKIV 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 527 QGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd08529 215 RGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTELLRNPSL 256
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
297-568 9.41e-32

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: 124.19  E-value: 9.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKcVKRL-DGCIYAIK---------RSKKPLagsVDEQNALREVyahavlgQHPHVVRYFsawa 366
Cdd:cd08217   1 DYEVLETIGKGSFGTVRK-VRRKsDGKILVWKeidygkmseKEKQQL---VSEVNILREL-------KHPNIVRYY---- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 367 edDH--------MLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIH-----SMSLVHMDIKPSNIFI 433
Cdd:cd08217  66 --DRivdranttLYIVMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 434 SRtsipnavseegdeddwisnKVMFKIGD------LGHVTRISSPQVeeGDSRFLANEVLQEN-YShlPKADIFALAltv 506
Cdd:cd08217 144 DS-------------------DNNVKLGDfglarvLSHDSSFAKTYV--GTPYYMSPELLNEQsYD--EKSDIWSLG--- 197
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 507 vC-----AAGAEP-LPRNGDQWHE-IRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd08217 198 -CliyelCALHPPfQAANQLELAKkIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
301-560 1.57e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 128.59  E-value: 1.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFrREARALARL-NHPNIVRVYDVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegdeddwisnkvmfK 459
Cdd:COG0515  91 GESLADLLRRRGP----LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV-------------------K 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISSPQVEEGDSR-----FLANEVLQ-ENYShlPKADIFALALTV-VCAAGAEPLPRNGDQ--WHEIRQGRL 530
Cdd:COG0515 148 LIDFGIARALGGATLTQTGTVvgtpgYMAPEQARgEPVD--PRSDVYSLGVTLyELLTGRPPFDGDSPAelLRAHLREPP 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 531 PRIPQV---LSQELTELLKVMIHPDPERRPSAM 560
Cdd:COG0515 226 PPPSELrpdLPPALDAIVLRALAKDPEERYQSA 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
298-568 3.25e-31

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: 122.32  E-value: 3.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMR---LRKQNKELIINEILIMKEC-KHPNIVDYYDSYLVGDELWVVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddwisnkvm 457
Cdd:cd06614  78 MDGGSLTDIITQNP---VRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSK---------DGS---------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEE----GDSRFLANEV-LQENYShlPKADIFALALTVVCAAGAEPlPRNGDQ----WHEIRQG 528
Cdd:cd06614 136 VKLADFGFAAQLTKEKSKRnsvvGTPYWMAPEViKRKDYG--PKVDIWSLGIMCIEMAEGEP-PYLEEPplraLFLITTK 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 529 RLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06614 213 GIPPLknPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
302-559 8.10e-31

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: 121.43  E-value: 8.10e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd05117   6 KVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVMELCTGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeddwisnkvmfKIG 461
Cdd:cd05117  85 ELFDRIVKK----GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPI----------------KII 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGHVTRISSPQVEE---GDSRFLANEVLQEN-YShlPKADIFAL-ALTVVCAAGAEPLPRNGDQ--WHEIRQGRL---P 531
Cdd:cd05117 145 DFGLAKIFEEGEKLKtvcGTPYYVAPEVLKGKgYG--KKCDIWSLgVILYILLCGYPPFYGETEQelFEKILKGKYsfdS 222
                       250       260
                ....*....|....*....|....*...
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd05117 223 PEWKNVSEEAKDLIKRLLVVDPKKRLTA 250
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
296-566 1.43e-30

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: 120.45  E-value: 1.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKrsKKPLAGsvDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIK--VVPVEE--DLQEIIKEI---SILKQcdSPYIVKYYGSYFKNTDLWI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwis 453
Cdd:cd06612  76 VMEYCGAGSVSDIMKITNKT---LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL---------NEEGQ------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGhvtrISSPQVEEGDSR--------FLANEVLQE-NYSHlpKADIFALALTVVCAAGAEPlPRNGdqWHE 524
Cdd:cd06612 138 ----AKLADFG----VSGQLTDTMAKRntvigtpfWMAPEVIQEiGYNN--KADIWSLGITAIEMAEGKP-PYSD--IHP 204
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 525 IRQ----GRLP----RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd06612 205 MRAifmiPNKPpptlSDPEKWSPEFNDFVKKCLVKDPEERPSAIQLLQHP 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
303-565 3.37e-30

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: 119.71  E-value: 3.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLAGSV-DEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06626   7 KIGEGTFGKVYTAVNLDTGELMAMKeirfqDNDPKTIKEIaDEMKVLEGL-------DHPNLVRYYGVEVHREEVYIFME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADaVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKV 456
Cdd:cd06626  80 YCQEGTLEE-LLRHGRILD---EAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLD------------------SNGL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MfKIGDLGHVTRISSP---------QVEEGDSRFLANEVLQENYS--HLPKADIFALALTVV-CAAGAEPLPRNGDQW-- 522
Cdd:cd06626 138 I-KLGDFGSAVKLKNNtttmapgevNSLVGTPAYMAPEVITGNKGegHGRAADIWSLGCVVLeMATGKRPWSELDNEWai 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 523 -HEIRQGRLPRIPQ--VLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06626 217 mYHVGMGHKPPIPDslQLSPEGKDFLSRCLESDPKKRPTASELLDH 262
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
292-565 5.73e-30

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: 119.59  E-value: 5.73e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVYAHAVLgQHPHVVRYFSAWAE---- 367
Cdd:cd14048   2 SRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREK-VLREVRALAKL-DHPGIVRYFNAWLErppe 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 -------DDHMLIQNEYCNGGSLADAVSENYRVMS--YFTeaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsi 438
Cdd:cd14048  80 gwqekmdEVYLYIQMQLCRKENLKDWMNRRCTMESreLFV---CLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSL--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 439 pnavseegdeDDWIsnkvmfKIGDLGHVTRISSPQVEE----------------GDSRFLANEVLQEN-YSHlpKADIFA 501
Cdd:cd14048 154 ----------DDVV------KVGDFGLVTAMDQGEPEQtvltpmpayakhtgqvGTRLYMSPEQIHGNqYSE--KVDIFA 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 502 LALTVVcaagaEPLPRNGDQWHEIR---QGRLPRIPQVLSQELTE---LLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14048 216 LGLILF-----ELIYSFSTQMERIRtltDVRKLKFPALFTNKYPEerdMVQQMLSPSPSERPEAHEVIEH 280
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
304-558 1.76e-28

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: 114.17  E-value: 1.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKcvKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd13999   1 IGSGSFGEVYK--GKWRGTDVAIKKLKVEDDNDELLKEFRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSENYRVMSYFTeaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKIGDL 463
Cdd:cd13999  78 YDLLHKKKIPLSWSL---RLKIALDIARGMNYLHSPPIIHRDLKSLNILL-------------DENFTV------KIADF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 GhVTRISSPQVEE-----GDSRFLANEVLQ-ENYSHlpKADIFALAltVVC---AAGAEP---LPRNGDQWHEIRQGRLP 531
Cdd:cd13999 136 G-LSRIKNSTTEKmtgvvGTPRWMAPEVLRgEPYTE--KADVYSFG--IVLwelLTGEVPfkeLSPIQIAAAVVQKGLRP 210
                       250       260
                ....*....|....*....|....*..
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd13999 211 PIPPDCPPELSKLIKRCWNEDPEKRPS 237
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
292-562 9.04e-28

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: 113.37  E-value: 9.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHM 371
Cdd:cd14049   2 SRYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGL-QHPNIVGYHTAWMEHVQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 L--IQNEYCNgGSLADAVSENYRVMSYFTEAE----------LKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIP 439
Cdd:cd14049  81 MlyIQMQLCE-LSLWDWIVERNKRPCEEEFKSapytpvdvdvTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 440 NAVSEEGdeddWISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHL-PKADIFALAltVVCAAGAEPLPRN 518
Cdd:cd14049 160 VRIGDFG----LACPDILQDGNDSTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYdFKSDMYSIG--VILLELFQPFGTE 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 519 GDQWHEIRQGRLPRIPQVLSQ---ELTELLKVMIHPDPERRPSAMVL 562
Cdd:cd14049 234 MERAEVLTQLRNGQIPKSLCKrwpVQAKYIKLLTSTEPSERPSASQL 280
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
304-568 9.73e-28

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: 112.63  E-value: 9.73e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPlagSVDEQNALREVYAHAVLG---------QHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVELP---SVSAENKDRKKSMLDALQreiallrelQHENIVQYLGSSSDANHLNIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLAdAVSENYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI-SRTSIpnAVSEEGdeddwIS 453
Cdd:cd06628  85 LEYVPGGSVA-TLLNNY---GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVdNKGGI--KISDFG-----IS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 NKVMFKIgdLGHVTRISSPQVeEGDSRFLANEVLQENySHLPKADIFALA-LTVVCAAGAEPLPrNGDQWHEI-RQGR-- 529
Cdd:cd06628 154 KKLEANS--LSTKNNGARPSL-QGSVFWMAPEVVKQT-SYTRKADIWSLGcLVVEMLTGTHPFP-DCTQMQAIfKIGEna 228
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 530 LPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06628 229 SPTIPSNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
301-565 2.35e-27

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: 111.07  E-value: 2.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14003   5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENKIYLVMEYASG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKI 460
Cdd:cd14003  84 GELFDYIVNNGR----LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-------------DKNGNL------KI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLG----------HVTRISSPQveegdsrFLANEVLQENYSHLPKADIFALALTV-VCAAGAepLPRNGDQ----WHEI 525
Cdd:cd14003 141 IDFGlsnefrggslLKTFCGTPA-------YAAPEVLLGRKYDGPKADVWSLGVILyAMLTGY--LPFDDDNdsklFRKI 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 526 RQGRLPrIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14003 212 LKGKYP-IPSHLSPDARDLIRRMLVVDPSKRITIEEILNH 250
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
297-565 3.20e-27

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: 110.86  E-value: 3.20e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsVDEQNALREVYAH-AVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK------LEPGDDFEIIQQEiSMLKEcrHPNIVAYFGSYLRRDKLWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAvsenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwis 453
Cdd:cd06613  75 VMEYCGGGSLQDI----YQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILL---------TEDGD------ 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQEN----YSHlpKADIFALALTVVCAAGAEPlPRNGdqWHEI 525
Cdd:cd06613 136 ----VKLADFGVSAQLTATIAKRksfiGTPYWMAPEVAAVErkggYDG--KCDIWALGITAIELAELQP-PMFD--LHPM 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 526 RQ----GRLPRIPQVL------SQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06613 207 RAlfliPKSNFDPPKLkdkekwSPDFHDFIKKCLTKNPKKRPTATKLLQH 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
303-565 4.43e-27

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: 110.76  E-value: 4.43e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVYAhAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd06623   8 VLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQ-LLRELKT-LRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMS-LVHMDIKPSNIFISRTsipNAVseegdeddwisnkvmfKIG 461
Cdd:cd06623  86 LADLLKKV----GKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSK---GEV----------------KIA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGhVTRISSPQVEEGDS-----------RFLAnevlqENYSHlpKADIFALALTVV-CAAGAEPL--PRNGDQW---HE 524
Cdd:cd06623 143 DFG-ISKVLENTLDQCNTfvgtvtymspeRIQG-----ESYSY--AADIWSLGLTLLeCALGKFPFlpPGQPSFFelmQA 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 525 IRQGRLPRIP-QVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06623 215 ICDGPPPSLPaEEFSPEFRDFISACLQKDPKKRPSAAELLQH 256
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
304-565 4.98e-27

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: 110.57  E-value: 4.98e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNA---LREVyahAVLG--QHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVkqlEQEI---ALLSklRHPNIVQYYGTEREEDNLYIFLEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnkvMF 458
Cdd:cd06632  85 PGGSIHKLLQR----YGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNG-------------------VV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLG---HVTRISSPQVEEGDSRFLANEVL-QENYSHLPKADIFALALTVV-CAAGAEPlprngdqWHEI-------- 525
Cdd:cd06632 142 KLADFGmakHVEAFSFAKSFKGSPYWMAPEVImQKNSGYGLAVDIWSLGCTVLeMATGKPP-------WSQYegvaaifk 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 526 --RQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06632 215 igNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLEH 256
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
298-565 9.01e-26

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: 106.74  E-value: 9.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ---NALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDetvDANREAKLLSKL-DHPAIVKFHDSFVEKESFCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwisn 454
Cdd:cd08222  81 TEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN------------------ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvMFKIGDLGhVTRISSPQVEE-----GDSRFLANEVLQ-ENYSHlpKADIFALA--LTVVCA-----AGAEPLprngDQ 521
Cdd:cd08222 143 --VIKVGDFG-ISRILMGTSDLattftGTPYYMSPEVLKhEGYNS--KSDIWSLGciLYEMCClkhafDGQNLL----SV 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 522 WHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd08222 214 MYKIVEGETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEILKI 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
303-559 9.41e-26

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: 106.97  E-value: 9.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSK-KPLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd08224   7 KIGKGQFSVVYRARCLLDGRLVALKKVQiFEMMDAKARQDCLKEI---DLLQQlnHPNIIKYLASFIENNELNIVLELAD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFK 459
Cdd:cd08224  84 AGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGV-------------------VK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGhVTRISSPQVEEGDSR-----FLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPLPRNG----DQWHEIRQGR 529
Cdd:cd08224 145 LGDLG-LGRFFSSKTTAAHSLvgtpyYMSPERIREQGYDF-KSDIWSLGcLLYEMAALQSPFYGEKmnlySLCKKIEKCE 222
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 530 LPRIPQVL-SQELTELLKVMIHPDPERRPSA 559
Cdd:cd08224 223 YPPLPADLySQELRDLVAACIQPDPEKRPDI 253
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
298-566 1.11e-25

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: 107.23  E-value: 1.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFY-SWEECMNLREVKSLRKLNEHPNIVKLKEVFRENDELYFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGgSLADAVSEnyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseegdeddwISNKVM 457
Cdd:cd07830  80 MEG-NLYQLMKD--RKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLL-------------------VSGPEV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLG---HVtRISSPQVEEGDSR-FLANEVL--QENYSHlpKADIFALA---------------------LTVVCAA 510
Cdd:cd07830 138 VKIADFGlarEI-RSRPPYTDYVSTRwYRAPEILlrSTSYSS--PVDIWALGcimaelytlrplfpgsseidqLYKICSV 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 511 GAEPLPRNGDQWHEIRQG---RLPRIPQVL--------SQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd07830 215 LGTPTKQDWPEGYKLASKlgfRFPQFAPTSlhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQHP 281
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
297-589 1.29e-25

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: 106.95  E-value: 1.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKrsKKPLAGSVDE-QNALREVYahaVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd06609   2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIK--VIDLEEAEDEiEDIQQEIQ---FLSQcdSPYITKYYGSFLKGSKLWI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSenyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwis 453
Cdd:cd06609  77 IMEYCGGGSVLDLLK-----PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILL---------SEEGD------ 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVL-QENYSHlpKADIFALALTVVCAAGAEPlPRNGdqWHEIRQG 528
Cdd:cd06609 137 ----VKLADFGVSGQLTSTMSKRntfvGTPFWMAPEVIkQSGYDE--KADIWSLGITAIELAKGEP-PLSD--LHPMRVL 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 529 RL-PR--IPQVLSQELTELLKVMIH----PDPERRPSAMVLVKHSVLLSASRKSAEQLRIELnAEKFK 589
Cdd:cd06609 208 FLiPKnnPPSLEGNKFSKPFKDFVElclnKDPKERPSAKELLKHKFIKKAKKTSYLTLLIER-IKKWK 274
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
304-566 5.35e-25

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: 104.94  E-value: 5.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKP------------LAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAW--AE 367
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSrlrkrregkndrGKIKNALDDVRREI---AIMKKldHPNIVRLYEVIddPE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIQNEYCNGGSL----ADAVSENyrvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavs 443
Cdd:cd14008  78 SDKLYLVLEYCEGGPVmeldSGDRVPP------LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTA-------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 444 eegdeddwiSNKVmfKIGDLGhvtriSSPQVEEGDSR---------FLANEVLQENYS--HLPKADIFALALTVVCAAGA 512
Cdd:cd14008 144 ---------DGTV--KISDFG-----VSEMFEDGNDTlqktagtpaFLAPELCDGDSKtySGKAADIWALGVTLYCLVFG 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 513 EpLPRNGD----QWHEIRQGRLP-RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14008 208 R-LPFNGDnileLYEAIQNQNDEfPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHP 265
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
297-566 7.86e-25

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: 104.09  E-value: 7.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDH-MLIQ 374
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKViSKSQLQKSGLEHQLRREIEIQSHL-RHPNILRLYGYFEDKKRiYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 nEYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwisn 454
Cdd:cd14007  80 -EYAPNGELYKELKKQKR----FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILL---------GSNGE------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDLGhvtriSSpqVEEGDSR---------FLANEVLqENYSHLPKADIFALAltVVC---AAGAEPLPRNGDQ- 521
Cdd:cd14007 139 ---LKLADFG-----WS--VHAPSNRrktfcgtldYLPPEMV-EGKEYDYKVDIWSLG--VLCyelLVGKPPFESKSHQe 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 522 -WHEIRQGRLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14007 206 tYKRIQNVDI-KFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLNHP 250
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
301-558 3.05e-24

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 102.22  E-value: 3.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    301 LEKIGSGEFGSVFKCV-KRLDGCIY---AIKRSKKPlAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:smart00219   4 GKKLGEGAFGEVYKGKlKGKGGKKKvevAVKTLKED-ASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    377 YCNGGSLADAVSENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKV 456
Cdd:smart00219  82 YMEGGDLLSYLRKN---RPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG------------------ENLV 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    457 MfKIGDLG-----HVTRISSPQVEEGDSRFLANEVLQEN-YSHlpKADIFALALTV--VCAAGAEPLPR--NGDQWHEIR 526
Cdd:smart00219 141 V-KISDFGlsrdlYDDDYYRKRGGKLPIRWMAPESLKEGkFTS--KSDVWSFGVLLweIFTLGEQPYPGmsNEEVLEYLK 217
                          250       260       270
                   ....*....|....*....|....*....|..
gi 17865613    527 QGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:smart00219 218 NGYRLPQPPNCPPELYDLMLQCWAEDPEDRPT 249
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
301-558 3.99e-24

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: 101.86  E-value: 3.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    301 LEKIGSGEFGSVFKCV-KRLDGCIY---AIKRSKKPlAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:smart00221   4 GKKLGEGAFGEVYKGTlKGKGDGKEvevAVKTLKED-ASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    377 YCNGGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKV 456
Cdd:smart00221  82 YMPGGDLLDYLRKNRPKE--LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG------------------ENLV 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613    457 MfKIGDLGhVTRisspQVEEGDS----------RFLANEVLQEN-YSHlpKADIFALALTV--VCAAGAEPLPRNGDQ-- 521
Cdd:smart00221 142 V-KISDFG-LSR----DLYDDDYykvkggklpiRWMAPESLKEGkFTS--KSDVWSFGVLLweIFTLGEEPYPGMSNAev 213
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 17865613    522 WHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:smart00221 214 LEYLKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRPT 250
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
304-559 5.50e-24

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: 101.19  E-value: 5.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPlagSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKR---DKKKEAVLREISILNQL-QHPRIIQLHEAYESPTELVLILELCSGGEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdeDDWISNKVmfKIGDL 463
Cdd:cd14006  77 LDRLAERGSL----SEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILL---------------ADRPSPQI--KIIDF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 GHVTRIsSPQVEE----GDSRFLANEVLQENYSHLPkADIFAL-ALTVVCAAGAEPLPRNGDQwhE----IRQGRL---P 531
Cdd:cd14006 136 GLARKL-NPGEELkeifGTPEFVAPEIVNGEPVSLA-TDMWSIgVLTYVLLSGLSPFLGEDDQ--EtlanISACRVdfsE 211
                       250       260
                ....*....|....*....|....*...
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd14006 212 EYFSSVSQEAKDFIRKLLVKEPRKRPTA 239
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
302-565 6.10e-24

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: 101.46  E-value: 6.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKC-VKRLDGCIY--AIKRSKKPlAGSVDEQNALREVYAHAVLGqHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd00192   1 KKLGEGAFGEVYKGkLKGGDGKTVdvAVKTLKED-ASESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSENYRVM-----SYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiS 453
Cdd:cd00192  79 EGGDLLDFLRKSRPVFpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVG------------------E 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 NKVMfKIGDLGhVTRisspQVEEGDS-----------RFLANEVLQEN-YSHlpKADIFALALTV--VCAAGAEPLPrnG 519
Cdd:cd00192 141 DLVV-KISDFG-LSR----DIYDDDYyrkktggklpiRWMAPESLKDGiFTS--KSDVWSFGVLLweIFTLGATPYP--G 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 520 DQWHEIRQ-----GRLPRiPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd00192 211 LSNEEVLEylrkgYRLPK-PENCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
297-565 6.40e-24

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: 101.78  E-value: 6.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQiVKRKVAGNDKNLQLFqREINILKSL-EHPGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdEDDwisn 454
Cdd:cd14098  80 MEYVEGGDLMDFIMAWGAI----PEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQ------------DDP---- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kVMFKIGDLGHVTRISSPQVEE---GDSRFLANEVLQENYSHLP-----KADIFALALTV-VCAAGAepLPRNGDQ---- 521
Cdd:cd14098 140 -VIVKISDFGLAKVIHTGTFLVtfcGTMAYLAPEILMSKEQNLQggysnLVDMWSVGCLVyVMLTGA--LPFDGSSqlpv 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 522 WHEIRQGRLPRIPQV---LSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14098 217 EKRIRKGRYTQPPLVdfnISEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
298-568 1.11e-23

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: 100.80  E-value: 1.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDG--C-IYAIKRSKKPLAgsvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSehCvIKEIDLTKMPVK---EKEASKKEVILLAKM-KHPNIVTFFASFQENGRLFIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSN 454
Cdd:cd08225  78 MEYCDGGDLMKRINRQRGVL--FSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLS------------------KN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 KVMFKIGDLGhVTRISSPQVE-----EGDSRFLANEVLQeNYSHLPKADIFALA--LTVVCAAGAeplPRNGDQWHE--- 524
Cdd:cd08225 138 GMVAKLGDFG-IARQLNDSMElaytcVGTPYYLSPEICQ-NRPYNNKTDIWSLGcvLYELCTLKH---PFEGNNLHQlvl 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17865613 525 -IRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd08225 213 kICQGYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
302-566 2.21e-23

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: 99.94  E-value: 2.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14099   7 KFLGKGGFAKCYEVTDMSTGKVYAGKVvPKSSLTKPKQREKLKSEIKIHRSL-KHPNIVKFHDCFEDEENVYILLELCSN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDdwisNKVmfKI 460
Cdd:cd14099  86 GSLMELL----KRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL-------------DEN----MNV--KI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPqvEE------GDSRFLANEVLQENYSHLPKADIFALAltVVCAA---GAEPL--PRNGDQWHEIRQGR 529
Cdd:cd14099 143 GDFGLAARLEYD--GErkktlcGTPNYIAPEVLEKKKGHSFEVDIWSLG--VILYTllvGKPPFetSDVKETYKRIKKNE 218
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 530 LpRIPQ--VLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14099 219 Y-SFPShlSISDEAKDLIRSMLQPDPTKRPSLDEILSHP 256
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
298-576 7.37e-22

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 95.91  E-value: 7.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIID--LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwisnkvm 457
Cdd:cd06641  84 LGGGSALDLLEP-----GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL---------SEHGE---------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTVVCAAGAEPlPRNgdQWHEIR------Q 527
Cdd:cd06641 140 VKLADFGVAGQLTDTQIKRn*fvGTPFWMAPEVIKQS-AYDSKADIWSLGITAIELARGEP-PHS--ELHPMKvlflipK 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17865613 528 GRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSA 576
Cdd:cd06641 216 NNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTS 264
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
298-565 1.18e-21

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: 95.09  E-value: 1.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKML-SHKNVVRFYGHRREGEFQYLFLEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRVMSYFTEAELKDLLlqvgRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDwisnkvM 457
Cdd:cd14069  82 ASGGELFDKIEPDVGMPEDVAQFYFQQLM----AGLKYLHSCGITHRDIKPENLLL-------------DEND------N 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEE------GDSRFLANEVLQENYSHLPKADIFALA-LTVVCAAGAEP--LPRNGDQ----WHE 524
Cdd:cd14069 139 LKISDFGLATVFRYKGKERllnkmcGTLPYVAPELLAKKKYRAEPVDVWSCGiVLFAMLAGELPwdQPSDSCQeysdWKE 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17865613 525 IR---QGRLPRIPQ-VLSqelteLLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14069 219 NKktyLTPWKKIDTaALS-----LLRKILTENPNKRITIEDIKKH 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
302-564 1.43e-21

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: 94.72  E-value: 1.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQN-----ALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd13993   6 SPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDfqklpQLREIDLHRRVSRHPNIITLHDVFETEVAIYIVLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvmsYFTEAEL-KDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseeGDEDDwisnk 455
Cdd:cd13993  86 YCPNGDLFEAITENRI---YVGKTELiKNVFLQLIDAVKHCHSLGIYHRDIKPENILLS-----------QDEGT----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmFKIGDLGHVTRIS-SPQVEEGDSRFLANEVLQENYSHLP-----KADIFALA---LTVVCAAGAEPLPRNGDQWHEIR 526
Cdd:cd13993 147 --VKLCDFGLATTEKiSMDFGVGSEFYMAPECFDEVGRSLKgypcaAGDIWSLGiilLNLTFGRNPWKIASESDPIFYDY 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 527 QGRLPRIPQV---LSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd13993 225 YLNSPNLFDVilpMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
298-576 2.20e-21

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 94.73  E-value: 2.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDE-QNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06640   6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIID--LEEAEDEiEDIQQEI---TVLSQcdSPYVTKYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwisn 454
Cdd:cd06640  81 MEYLGGGSALDLLRA-----GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLL---------SEQGD------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTVVCAAGAEplPRNGDQwHEIR---- 526
Cdd:cd06640 140 ---VKLADFGVAGQLTDTQIKRntfvGTPFWMAPEVIQQS-AYDSKADIWSLGITAIELAKGE--PPNSDM-HPMRvlfl 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 527 --QGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSA 576
Cdd:cd06640 213 ipKNNPPTLVGDFSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTS 264
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
301-567 4.01e-21

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: 93.58  E-value: 4.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFK--CVKRLDGCiyAIKR---SKKPLagSVDEqnALREVYAHAvLGQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd06610   6 IEVIGSGATAVVYAayCLPKKEKV--AIKRidlEKCQT--SMDE--LRKEIQAMS-QCNHPNVVSYYTSFVVGDELWLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnk 455
Cdd:cd06610  79 PLLSGGSLLDIMKSSYP-RGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL-------------GEDGSV--- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGhvtrISSPQVEEGDSR------------FLANEVLQENYSHLPKADIFALALTVV-CAAGAEPLprngdqw 522
Cdd:cd06610 142 ---KIADFG----VSASLATGGDRTrkvrktfvgtpcWMAPEVMEQVRGYDFKADIWSFGITAIeLATGAAPY------- 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 523 HE---------IRQGRLPRIP-----QVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd06610 208 SKyppmkvlmlTLQNDPPSLEtgadyKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKF 266
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
297-592 4.95e-21

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: 93.85  E-value: 4.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALRevyahavLGQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEiEILLR-------YGQHPNIITLRDVYDDGNSVYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADavsenyRVMS--YFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavSEEGDEDDwis 453
Cdd:cd14091  74 ELLRGGELLD------RILRqkFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYA--------DESGDPES--- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGHVTRIsspQVEEG-------DSRFLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPLPRN-GDQWHE 524
Cdd:cd14091 137 ----LRICDFGFAKQL---RAENGllmtpcyTANFVAPEVLKKQGYDA-ACDIWSLGvLLYTMLAGYTPFASGpNDTPEV 208
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 525 IrqgrLPRIPQ-----------VLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLRIELNAEKFKNSL 592
Cdd:cd14091 209 I----LARIGSgkidlsggnwdHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVKGAV 283
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
298-558 5.84e-21

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: 92.94  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   298 FHELEKIGSGEFGSVFKCV----KRLDGCIYAIKRSKkPLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHM 371
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLK-EGADEEEREDFLEEA---SIMKKldHPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   372 LIQNEYCNGGSLADAVSENYRVMSyfteaeLKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegde 448
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRKLT------LKDLLsmaLQIAKGMEYLESKNFVHRDLAARNCLVSE------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   449 ddwisNKVMfKIGDLGhVTRisspQVEEGDS-----------RFLANEVLQEN-YSHlpKADIFALALTV--VCAAGAEP 514
Cdd:pfam07714 138 -----NLVV-KISDFG-LSR----DIYDDDYyrkrgggklpiKWMAPESLKDGkFTS--KSDVWSFGVLLweIFTLGEQP 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 17865613   515 LP--RNGDQWHEIRQG-RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:pfam07714 205 YPgmSNEEVLEFLEDGyRLPQ-PENCPDELYDLMKQCWAYDPEDRPT 250
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
293-568 7.17e-21

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: 92.86  E-value: 7.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEFHEL-EKI--GSGEFGSVFKCVKRLDGCIYAIKrsKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDD 369
Cdd:cd06624   2 EYEYEYDESgERVvlGKGTFGVVYAARDLSTQVRIAIK--EIPERDSREVQPLHEEIALHSRL-SHKNIVQYLGSVSEDG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAV-------SENYRVMSYFTEaelkdlllQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnav 442
Cdd:cd06624  79 FFKIFMEQVPGGSLSALLrskwgplKDNENTIGYYTK--------QILEGLKYLHDNKIVHRDIKGDNVLVNTYS----- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 443 seeGdeddwisnkvMFKIGDLGHVTRIS--SPQVE--EGDSRFLANEVL-QENYSHLPKADIFALALTVV-CAAGAEPLP 516
Cdd:cd06624 146 ---G----------VVKISDFGTSKRLAgiNPCTEtfTGTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIeMATGKPPFI 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 517 RNGD-QWHEIRQGRL---PRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06624 213 ELGEpQAAMFKVGMFkihPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
297-568 7.71e-21

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: 92.57  E-value: 7.71e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd08218   1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEV---AVLSKmkHPNIVQYQESFEENGNLYIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisn 454
Cdd:cd08218  78 MDYCDGGDLYKRINAQRGVL--FPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGI---------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDLGhVTRISSPQVEE-----GDSRFLANEVLqENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWH---EIR 526
Cdd:cd08218 140 ---IKLGDFG-IARVLNSTVELartciGTPYYLSPEIC-ENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNlvlKII 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 527 QGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd08218 215 RGSYPPVPSRYSYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
297-566 9.67e-21

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: 92.11  E-value: 9.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHML-IQN 375
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKL-KHPNIVSYKESFEGEDGFLyIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnk 455
Cdd:cd08223  80 GFCEGGDLYTRLKEQKGVL--LEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNI----------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmFKIGDLG-----------HVTRISSPQveegdsrFLANEVLQEN-YSHlpKADIFALA------LTVVCAAGAEPLpr 517
Cdd:cd08223 141 --IKVGDLGiarvlesssdmATTLIGTPY-------YMSPELFSNKpYNH--KSDVWALGccvyemATLKHAFNAKDM-- 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17865613 518 nGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd08223 208 -NSLVYKILEGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRILRQP 255
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
297-568 1.54e-20

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: 91.57  E-value: 1.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSS-AVEDSRKEAVLLAKM-KHPNIVAFKESFEADGHLYIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwiSNKV 456
Cdd:cd08219  79 YCDGGDLMQKIKLQRGKL--FPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQ-----------------NGKV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLGHVTRISSPQVEE----GDSRFLANEVLqENYSHLPKADIFALA--LTVVCAAGAeplPRNGDQWH----EIR 526
Cdd:cd08219 140 --KLGDFGSARLLTSPGAYActyvGTPYYVPPEIW-ENMPYNNKSDIWSLGciLYELCTLKH---PFQANSWKnlilKVC 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 527 QGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd08219 214 QGSYKPLPSHYSYELRSLIKQMFKRNPRSRPSATTILSRGSL 255
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
338-568 3.43e-20

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: 90.57  E-value: 3.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 338 DEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIH 417
Cdd:cd08221  42 ERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQL--FPEEVVLWYLYQIVSAVSHIH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 418 SMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFKIGDLGHVTRISSP-QVEE---GDSRFLANEVLQ-ENYS 492
Cdd:cd08221 119 KAGILHRDIKTLNIFLTKADL-------------------VKLGDFGISKVLDSEsSMAEsivGTPYYMSPELVQgVKYN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 493 HlpKADIFA--------LALTVVCAAgAEPLprngDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd08221 180 F--KSDIWAvgcvlyelLTLKRTFDA-TNPL----RLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLE 252

                ....
gi 17865613 565 HSVL 568
Cdd:cd08221 253 RPLL 256
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
304-559 4.40e-20

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: 90.74  E-value: 4.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK---RSKKPLAGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDLYAIKvikKRDMIRKNQVDSVLAERNILSQA---QNPFVVKLYYSFQGKKNLYLVMEYLPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLAdAVSENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAV----SEEGDEDDWISNKV 456
Cdd:cd05579  78 GDLY-SLLEN---VGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTdfglSKVGLVRRQIKLSI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPqveeGDSRFLANEVLqENYSHLPKADIFALA------LTvvcaagAEPlPRNGDQWHE----IR 526
Cdd:cd05579 154 QKKSNGAPEKEDRRIV----GTPDYLAPEIL-LGQGHGKTVDWWSLGvilyefLV------GIP-PFHAETPEEifqnIL 221
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 527 QGRLPRiPQV--LSQELTELLKVMIHPDPERRPSA 559
Cdd:cd05579 222 NGKIEW-PEDpeVSDEAKDLISKLLTPDPEKRLGA 255
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
301-488 4.51e-20

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: 90.34  E-value: 4.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLagSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14114   7 LEELGTGAFGVVHRCTERATGNNFAAKFIMTPH--ESDKETVRKEIQIMNQL-HHPKLINLHDAFEDDNEMVLILEFLSG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwiSNKVmfKI 460
Cdd:cd14114  84 GELFERIAAEHYKMS---EAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKR---------------SNEV--KL 143
                       170       180       190
                ....*....|....*....|....*....|.
gi 17865613 461 GDLGHVTRISSPQ---VEEGDSRFLANEVLQ 488
Cdd:cd14114 144 IDFGLATHLDPKEsvkVTTGTAEFAAPEIVE 174
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
302-565 4.56e-20

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: 89.98  E-value: 4.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKR---SKKPlagsVDEQNALR-EVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd06627   6 DLIGRGAFGSVYKGLNLNTGEFVAIKQislEKIP----KSDLKSVMgEIDLLKKL-NHPNIVKYIGSVKTKDSLYIILEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddwisnkvm 457
Cdd:cd06627  81 VENGSLASIIKKFGK----FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTK---------DGL---------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTVVcaagaEPL---PRNGDQ-----WHEI 525
Cdd:cd06627 138 VKLADFGVATKLNEVEKDEnsvvGTPYWMAPEVIEMS-GVTTASDIWSVGCTVI-----ELLtgnPPYYDLqpmaaLFRI 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 526 RQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06627 212 VQDDHPPLPENISPELRDFLLQCFQKDPTLRPSAKELLKH 251
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
304-559 5.10e-20

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: 90.08  E-value: 5.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPlagSVDEQNALREVYAHAVLGQHPHVVRYFS-AWAEDDHMLIQNEYCNGGS 382
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKP---STKLKDFLREYNISLELSVHPHIIKTYDvAFETEDYYVFAQEYAPYGD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisNKVmfKIGD 462
Cdd:cd13987  78 LFSIIPPQVGL----PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDC---------------RRV--KLCD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSP-QVEEGDSRFLANEVLQ----ENYSHLPKADIFALALTVVC----------AAGAEPLPRNGDQWHEIRQ 527
Cdd:cd13987 137 FGLTRRVGSTvKRVSGTIPYTAPEVCEakknEGFVVDPSIDVWAFGVLLFCcltgnfpwekADSDDQFYEEFVRWQKRKN 216
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 528 GRLPRIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd13987 217 TAVPSQWRRFTPKALRMFKKLLAPEPERRCSI 248
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
298-576 8.79e-20

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: 89.73  E-value: 8.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDE-QNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06642   6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIID--LEEAEDEiEDIQQEI---TVLSQcdSPYITRYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwisn 454
Cdd:cd06642  81 MEYLGGGSALDLLKP-----GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLL---------SEQGD------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENYSHLpKADIFALALTVVCAAGAEplPRNGDqWHEIR---- 526
Cdd:cd06642 140 ---VKLADFGVAGQLTDTQIKRntfvGTPFWMAPEVIKQSAYDF-KADIWSLGITAIELAKGE--PPNSD-LHPMRvlfl 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 527 --QGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSA 576
Cdd:cd06642 213 ipKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTS 264
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
302-557 1.54e-19

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: 88.64  E-value: 1.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKI---GSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd08220   3 EKIrvvGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSML-HHPNIIEYYESFLEDKALMIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSEnyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwisNKVMF 458
Cdd:cd08220  82 PGGTLFEYIQQ--RKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNK------------------KRTVV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGhVTRISSpqveegdSRFLANEV----------LQENYSHLPKADIFALA--LTVVC----AAGAEPLPRngdQW 522
Cdd:cd08220 142 KIGDFG-ISKILS-------SKSKAYTVvgtpcyispeLCEGKPYNQKSDIWALGcvLYELAslkrAFEAANLPA---LV 210
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 523 HEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRP 557
Cdd:cd08220 211 LKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRP 245
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
298-438 1.65e-19

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: 89.08  E-value: 1.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDE---QNALREVyahAVLG--QHPHVVRYFSAWAEDDHML 372
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRL---DNEEEgipSTALREI---SLLKelKHPNIVKLLDVIHTENKLY 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 373 IQNEYCNGgSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSI 438
Cdd:cd07829  75 LVFEYCDQ-DLKKYLDKRPGPLP---PNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGV 136
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
303-586 1.86e-19

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: 89.32  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIK----RSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd06644  19 ELGDGAFGKVYKAKNKETGALAAAKvietKSEEELEDYMVEIEILATC-------NHPYIVKLLGAFYWDGKLWIMIEFC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSENYRVMsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwisnkvmF 458
Cdd:cd06644  92 PGGAVDAIMLELDRGL---TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLL---------TLDGD----------I 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGhVTRISSPQVEEGDS-----RFLANEVLQ-ENYSHLP---KADIFALALTVVCAAGAEPlPRngdqwHEIRQGR 529
Cdd:cd06644 150 KLADFG-VSAKNVKTLQRRDSfigtpYWMAPEVVMcETMKDTPydyKADIWSLGITLIEMAQIEP-PH-----HELNPMR 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 530 L---------PRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSA-SRKSAEQLRIELNAE 586
Cdd:cd06644 223 VllkiaksepPTLsqPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVtSNRPLRELVAEAKAE 291
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
302-557 2.66e-19

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: 88.16  E-value: 2.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKK-PLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd08228   8 KKIGRGQFSEVYRATCLLDRKPVALKKVQIfEMMDAKARQDCVKEI---DLLKQlnHPNVIKYLDSFIEDNELNIVLELA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmF 458
Cdd:cd08228  85 DAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV-------------------V 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQVEE----GDSRFLANEVLQENYSHLpKADIFALALTVVCAAGAEPlPRNGDQW------HEIRQG 528
Cdd:cd08228 146 KLGDLGLGRFFSSKTTAAhslvGTPYYMSPERIHENGYNF-KSDIWSLGCLLYEMAALQS-PFYGDKMnlfslcQKIEQC 223
                       250       260       270
                ....*....|....*....|....*....|
gi 17865613 529 RLPRIP-QVLSQELTELLKVMIHPDPERRP 557
Cdd:cd08228 224 DYPPLPtEHYSEKLRELVSMCIYPDPDQRP 253
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
304-556 3.74e-19

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: 87.28  E-value: 3.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEqNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEiSRKKLNKKLQE-NLESEI---AILKSikHPNIVRLYDVQKTEDFIYLVLEYCAG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseeGDEDDWisnkvMFKI 460
Cdd:cd14009  77 GDLSQYIRKRGRL----PEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLS-----------TSGDDP-----VLKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQVEE---GDSRFLANEVLQ-ENYShlPKADIFAL-ALTVVCAAGAEPLP-RNGDQWHE-IRQGRL--- 530
Cdd:cd14009 137 ADFGFARSLQPASMAEtlcGSPLYMAPEILQfQKYD--AKADLWSVgAILFEMLVGKPPFRgSNHVQLLRnIERSDAvip 214
                       250       260
                ....*....|....*....|....*.
gi 17865613 531 PRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14009 215 FPIAAQLSPDCKDLLRRLLRRDPAER 240
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
302-565 3.76e-19

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: 87.71  E-value: 3.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGS-VFKcvKRLDGCIYAIKRSkkpLAGSVDEqnALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd13982   7 KVLGYGSEGTiVFR--GTFDGRPVAVKRL---LPEFFDF--ADREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 gSLADAVsENYRVMSYF--TEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAV----SEEGdeddwISN 454
Cdd:cd13982  80 -SLQDLV-ESPRESKLFlrPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVramiSDFG-----LCK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 KVMFKIGDLGHVTRISspqveeGDSRFLANEVLQENYSHLPKA--DIFALALTV--VCAAGAEPLPRNGDQWHEIRQGR- 529
Cdd:cd13982 153 KLDVGRSSFSRRSGVA------GTSGWIAPEMLSGSTKRRQTRavDIFSLGCVFyyVLSGGSHPFGDKLEREANILKGKy 226
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 530 -LPRIPQVLSQ--ELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd13982 227 sLDKLLSLGEHgpEAQDLIERMIDFDPEKRPSAEEVLNH 265
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
285-557 4.06e-19

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: 88.16  E-value: 4.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 285 ITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKK-PLAGSVDEQNALREVYAHAVLgQHPHVVRYFS 363
Cdd:cd08229  13 ALRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDAKARADCIKEIDLLKQL-NHPNVIKYYA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 364 AWAEDDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavs 443
Cdd:cd08229  92 SFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGV----- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 444 eegdeddwisnkvmFKIGDLG----HVTRISSPQVEEGDSRFLANEVLQENYSHLpKADIFALALTVVCAAGAEPlPRNG 519
Cdd:cd08229 167 --------------VKLGDLGlgrfFSSKTTAAHSLVGTPYYMSPERIHENGYNF-KSDIWSLGCLLYEMAALQS-PFYG 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17865613 520 DQWH------EIRQGRLPRIPQ-VLSQELTELLKVMIHPDPERRP 557
Cdd:cd08229 231 DKMNlyslckKIEQCDYPPLPSdHYSEELRQLVNMCINPDPEKRP 275
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
297-566 4.67e-19

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: 87.40  E-value: 4.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDEQNA-LREVyahAVL--GQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd06605   2 DLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIR--LEIDEALQKQiLREL---DVLhkCNSPYIVGFYGAFYSEGDISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLaDAVsenYRVMSYFTEAELKDLLLQVGRGLRYIHS-MSLVHMDIKPSNIFI-SRTSIpnavseegdeddw 451
Cdd:cd06605  77 CMEYMDGGSL-DKI---LKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVnSRGQV------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isnkvmfKIGDLGHVTRI--SSPQVEEGDSRFLANEVLQ-ENYSHlpKADIFALALTVV-CAAGAEPLPRNG-------- 519
Cdd:cd06605 140 -------KLCDFGVSGQLvdSLAKTFVGTRSYMAPERISgGKYTV--KSDIWSLGLSLVeLATGRFPYPPPNakpsmmif 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17865613 520 DQWHEIRQGRLPRIPQ-VLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd06605 211 ELLSYIVDEPPPLLPSgKFSPDFQDFVSQCLQKDPTERPSYKELMEHP 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
304-566 5.02e-19

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: 87.41  E-value: 5.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKC----------VKRLDGCIYAIKRSKkplagsvdEQNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHML 372
Cdd:cd06625   8 LGQGAFGQVYLCydadtgrelaVKQVEIDPINTEASK--------EVKALeCEIQLLKNL-QHERIVQYYGCLQDEKSLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNGGSLADAVSeNYRVMsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisRTSIPNAvseegdeddwi 452
Cdd:cd06625  79 IFMEYMPGGSVKDEIK-AYGAL---TENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL--RDSNGNV----------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 snkvmfKIGDLGHVTRISSPQVEEGDSRF------LANEVLQ-ENYSHlpKADIFALALTVVCAAGAEPlPrngdqWHEI 525
Cdd:cd06625 142 ------KLGDFGASKRLQTICSSTGMKSVtgtpywMSPEVINgEGYGR--KADIWSVGCTVVEMLTTKP-P-----WAEF 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 526 R----------QGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd06625 208 EpmaaifkiatQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEELLSHS 258
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
301-566 7.00e-19

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: 86.52  E-value: 7.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDEQNALREVYAHAVLG---QHPHVVRYFSA--WAEDDHMLIQN 375
Cdd:cd05118   4 LRKIGEGAFGTVWLARDKVTGEKVAIKKIK---NDFRHPKAALREIKLLKHLNdveGHPNIVKLLDVfeHRGGNHLCLVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCnGGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavSEEGDeddwisnk 455
Cdd:cd05118  81 ELM-GMNLYELIKDYPRG---LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILIN--------LELGQ-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmFKIGDLGhVTRISSPQ--VEEGDSRFL-ANEVLQENYSHLPKADIFALALTVVCAAGAEPL---PRNGDQWHEIRqgR 529
Cdd:cd05118 141 --LKLADFG-LARSFTSPpyTPYVATRWYrAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLfpgDSEVDQLAKIV--R 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 530 LPRIPQVLSqelteLLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd05118 216 LLGTPEALD-----LLSKMLKYDPAKRITASQALAHP 247
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
301-569 1.13e-18

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: 86.58  E-value: 1.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKR----SKKplagsvDEQNALREVYAHAVLgQHPHVVRYFsawaedDHMLIQNE 376
Cdd:cd13986   5 QRLLGEGGFSFVYLVEDLSTGRLYALKKilchSKE------DVKEAMREIENYRLF-NHPNILRLL------DSQIVKEA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 -----------YCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSM---SLVHMDIKPSNIFISrtsipnav 442
Cdd:cd13986  72 ggkkevylllpYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLS-------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 443 seegDEDDWIsnkvmfkIGDLGHVTRisSPQVEEGDSRFLANEVLQENYSHLP-----------------KADIFALALT 505
Cdd:cd13986 144 ----EDDEPI-------LMDLGSMNP--ARIEIEGRREALALQDWAAEHCTMPyrapelfdvkshctideKTDIWSLGCT 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 506 VVCAA-GAEPLPR---NGDQWHEIRQGRLPRIPQ--VLSQELTELLKVMIHPDPERRPSAMVLVKHSVLL 569
Cdd:cd13986 211 LYALMyGESPFERifqKGDSLALAVLSGNYSFPDnsRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDL 280
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
296-508 1.84e-18

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: 86.34  E-value: 1.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCV-KRLDGCIYAIKRSKK------PLAGSvDEQNALREVYAHAVLgQHPHVVRYFSAWAED 368
Cdd:cd14096   1 ENYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKadlssdNLKGS-SRANILKEVQIMKRL-SHPNIVKLLDFQESD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIQNEYCNGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT----SIPNAVSE 444
Cdd:cd14096  79 EYYYIVLELADGGEIFHQIVR----LTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIpfipSIVKLRKA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 445 EGDEDdwisnKV---------------MFKIGDLG--HVTRISSPQVEEGDSRFLANEVL-QENYSHlpKADIFALA--- 503
Cdd:cd14096 155 DDDET-----KVdegefipgvggggigIVKLADFGlsKQVWDSNTKTPCGTVGYTAPEVVkDERYSK--KVDMWALGcvl 227

                ....*
gi 17865613 504 LTVVC 508
Cdd:cd14096 228 YTLLC 232
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
304-565 3.22e-18

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: 84.85  E-value: 3.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPlagsVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRF----DEQRSFLKEVKLMRRL-SHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSENYRVMSYFTEAELKdllLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIP-NAVseegdeddwisnkvmfkIGD 462
Cdd:cd14065  76 EELLKSMDEQLPWSQRVSLA---KDIASGMAYLHSKNIIHRDLNSKNCLVREANRGrNAV-----------------VAD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQVEEGDSR----------FLANEVLQ-ENYSHlpKADIFALALtVVCA------AGAEPLPRNGDQWHEI 525
Cdd:cd14065 136 FGLAREMPDEKTKKPDRKkrltvvgspyWMAPEMLRgESYDE--KVDVFSFGI-VLCEiigrvpADPDYLPRTMDFGLDV 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 526 rQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14065 213 -RAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHH 251
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
296-568 3.59e-18

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: 84.71  E-value: 3.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEK--IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ---HPHVVRYFSAWAEDDH 370
Cdd:cd14106   6 NEVYTVEStpLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEI---AVLELckdCPRVVNLHEVYETRSE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseEGDedd 450
Cdd:cd14106  83 LILILELAAGGELQTLLDEEEC----LTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFP------LGD--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnkvmFKIGDLGhVTRISSPQVE----EGDSRFLANEVLqeNYSHLPKA-DIFALA-LTVVCAAGAEPLprNGDQWHE 524
Cdd:cd14106 150 -------IKLCDFG-ISRVIGEGEEireiLGTPDYVAPEIL--SYEPISLAtDMWSIGvLTYVLLTGHSPF--GGDDKQE 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 525 ----IRQGRL---PRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14106 218 tflnISQCNLdfpEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
304-559 4.08e-18

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: 84.69  E-value: 4.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSkkpLAGSVDEQN-ALREVYAHAVLGQHPHVVRYFSAWAEDDH----MLIQNEYC 378
Cdd:cd13985   8 LGEGGFSYVYLAHDVNTGRRYALKRM---YFNDEEQLRvAIKEIEIMKRLCGHPNIVQYYDSAILSSEgrkeVLLLMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 nGGSLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMS--LVHMDIKPSNIFisrtsipnavseegdeddwISNKV 456
Cdd:cd13985  85 -PGSLVDILEKSPP--SPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENIL-------------------FSNTG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPQVEEGDsRFLANEVLQEN-------------YSHLP---KADIFALA--LTVVCaagAEPLPRN 518
Cdd:cd13985 143 RFKLCDFGSATTEHYPLERAEE-VNIIEEEIQKNttpmyrapemidlYSKKPigeKADIWALGclLYKLC---FFKLPFD 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 519 GDQWHEIRQGRLPrIPQ--VLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd13985 219 ESSKLAIVAGKYS-IPEqpRYSPELHDLIRHMLTPDPAERPDI 260
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
303-565 4.78e-18

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: 84.30  E-value: 4.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSKKP-LAGS----VDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14095   7 VIGDGNFAVVKECRDKATDKEYALKIIDKAkCKGKehmiENEVAILRRV-------KHPNIVQLIEEYDTDTELYLVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegDEDDWISnkvm 457
Cdd:cd14095  80 VKGGDLFDAITSSTK----FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVE-----------HEDGSKS---- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEE-GDSRFLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPL-PRNGDQ---WHEIRQGRLP 531
Cdd:cd14095 141 LKLADFGLATEVKEPLFTVcGTPTYVAPEILAETGYGL-KVDIWAAGvITYILLCGFPPFrSPDRDQeelFDLILAGEFE 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 532 RIPQV---LSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14095 220 FLSPYwdnISDSAKDLISRMLVVDPEKRYSAGQVLDH 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
297-574 6.93e-18

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: 84.40  E-value: 6.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIK---RSKKPLAgsvdEQNALREVyAHAVLGQHPHVVRYFSAW-AEDDHML 372
Cdd:cd06621   2 KIVELSSLGEGAGGSVTKCRLRNTKTIFALKtitTDPNPDV----QKQILREL-EINKSCASPYIVKYYGAFlDEQDSSI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 -IQNEYCNGGSLaDAVSENYRVMSYFT-EAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdedd 450
Cdd:cd06621  77 gIAMEYCEGGSL-DSIYKKVKKKGGRIgEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTR--------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnKVMFKIGDLGhvtrISSPQVEEGDSRF------LANEVLQ-ENYShlPKADIFALALTVV-CAAGAEPLPRNGDQ- 521
Cdd:cd06621 141 ----KGQVKLCDFG----VSGELVNSLAGTFtgtsyyMAPERIQgGPYS--ITSDVWSLGLTLLeVAQNRFPFPPEGEPp 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 522 ------WHEIRQGRLPRIPQ------VLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRK 574
Cdd:cd06621 211 lgpielLSYIVNMPNPELKDepengiKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKK 275
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
302-442 1.35e-17

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: 83.11  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsvDEQNALREVYAHAVLGQHPHVVR----YFSAWAEDDHMLIQNEY 377
Cdd:cd14089   7 QVLGLGINGKVLECFHKKTGEKFALKVLR-------DNPKARREVELHWRASGCPHIVRiidvYENTYQGRKCLLVVMEC 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 378 CNGGSLADAVSEnyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSiPNAV 442
Cdd:cd14089  80 MEGGELFSRIQE--RADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKG-PNAI 141
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
304-567 1.46e-17

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: 83.25  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLAGSVDEqnALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKqvsfcRNSSSEQEEVVE--AIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSeNYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnkVMF 458
Cdd:cd06630  86 AGGSVASLLS-KY---GAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTG------------------QRL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQVEEGDSR--------FLANEVLQ-ENYSHlpKADIFALALTVVCAAGAEPlPRNGD--QWH---- 523
Cdd:cd06630 144 RIADFGAAARLASKGTGAGEFQgqllgtiaFMAPEVLRgEQYGR--SCDVWSVGCVIIEMATAKP-PWNAEkiSNHlali 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 524 -EIRQG-RLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd06630 221 fKIASAtTPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELLKHPV 266
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
302-608 2.68e-17

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: 82.77  E-value: 2.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREvyahavLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14175   7 ETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLR------YGQHPNIITLKDVYDDGKHVYLVTELMRGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnaVSEEGDEDDwisnkvmFKIG 461
Cdd:cd14175  81 ELLDKILRQ----KFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILY--------VDESGNPES-------LRIC 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGHVTRIsspQVEEG-------DSRFLANEVLQ-ENYSHlpKADIFALA-LTVVCAAGAEPLPRN-GDQWHEIrqgrLP 531
Cdd:cd14175 142 DFGFAKQL---RAENGllmtpcyTANFVAPEVLKrQGYDE--GCDIWSLGiLLYTMLAGYTPFANGpSDTPEEI----LT 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 532 RIP-----------QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLRIElnaekfknsllQKELKKA 600
Cdd:cd14175 213 RIGsgkftlsggnwNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQ-----------DVQLVKG 281

                ....*...
gi 17865613 601 QMAAKVAA 608
Cdd:cd14175 282 AMAATYSA 289
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
295-566 4.00e-17

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: 82.06  E-value: 4.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 295 TTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPL--AGSVDEQNALREVYAHA-VLGQ--HPHVVRYFSAWAEDD 369
Cdd:cd14084   5 RKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftIGSRREINKPRNIETEIeILKKlsHPCIIKIEDFFDAED 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseeGDED 449
Cdd:cd14084  85 DYYIVLELMEGGELFDRVVSNKR----LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLS-----------SQEE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 DWIsnkvmFKIGDLGH---VTRISSPQVEEGDSRFLANEVL----QENYShlPKADIFALALTV-VCAAGAEPLPRNGDQ 521
Cdd:cd14084 150 ECL-----IKITDFGLskiLGETSLMKTLCGTPTYLAPEVLrsfgTEGYT--RAVDCWSLGVILfICLSGYPPFSEEYTQ 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 522 W---HEIRQGRLPRIPQV---LSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14084 223 MslkEQILSGKYTFIPKAwknVSEEAKDLVKKMLVVDPSRRPSIEEALEHP 273
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
296-564 4.05e-17

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: 82.14  E-value: 4.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDE-QNALREV--YAHAVLGQHPHVVRYFSAWAEDDHML 372
Cdd:cd06917   1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLN--LDTDDDDvSDIQKEValLSQLKLGQPKNIIKYYGSYLKGPSLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNGGSL-----ADAVSENYRVMSyfteaeLKDLLLqvgrGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegd 447
Cdd:cd06917  79 IIMDYCEGGSIrtlmrAGPIAERYIAVI------MREVLV----ALKFIHKDGIIHRDIKAANILVTNT----------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwisNKVM---------FKIGDLGHVTRISSPQveegdsrFLANEVLQENYSHLPKADIFALALTVVCAAGAEPlPRN 518
Cdd:cd06917 138 ------GNVKlcdfgvaasLNQNSSKRSTFVGTPY-------WMAPEVITEGKYYDTKADIWSLGITTYEMATGNP-PYS 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 519 GDQWHE----IRQGRLPRIP-QVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd06917 204 DVDALRavmlIPKSKPPRLEgNGYSPLLKEFVAACLDEEPKDRLSADELLK 254
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
301-559 6.41e-17

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: 81.28  E-value: 6.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRldGCIYAIKRSKKPLAGSVDEQNALREVyaHAVLGQHPHVVRYF---SAWAEDDHMLIQNEY 377
Cdd:cd13979   8 QEPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAEL--NAARLRHENIVRVLaaeTGTDFASLGLIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegdeddwisnkvm 457
Cdd:cd13979  84 CGNGTLQQLIYEGSEPLPL---AHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVC------------------ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 fKIGDLGHVTRISSPQVEE-------GDSRFLANEVL-QENYShlPKADIFALALTVVCAAGAEpLPRNGDQWH------ 523
Cdd:cd13979 143 -KLCDFGCSVKLGEGNEVGtprshigGTYTYRAPELLkGERVT--PKADIYSFGITLWQMLTRE-LPYAGLRQHvlyavv 218
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 524 --EIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd13979 219 akDLRPDLSGLEDSEFGQRLRSLISRCWSAQPAERPNA 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
304-566 1.06e-16

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: 80.38  E-value: 1.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14185   8 IGDGNFAVVKECRHWNENQEYAMKiIDKSKLKGKEDMIESEILIIKSL---SHPNIVKLFEVYETEKEIYLILEYVRGGD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegDEDDWISnkvmFKIGD 462
Cdd:cd14185  85 LFDAIIESVK----FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQH-----------NPDKSTT----LKLAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQVEE-GDSRFLANEVLQENYSHLpKADIFALALTV-VCAAGAEPL---PRNGDQWHEIRQ-GRLPRIPQV 536
Cdd:cd14185 146 FGLAKYVTGPIFTVcGTPTYVAPEILSEKGYGL-EVDMWAAGVILyILLCGFPPFrspERDQEELFQIIQlGHYEFLPPY 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 537 ---LSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14185 225 wdnISEAAKDLISRLLVVDPEKRYTAKQVLQHP 257
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
301-565 1.09e-16

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: 81.19  E-value: 1.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKrSKKPLAgSVDEQ-----NALREvyahavLGQHPHVVRYFSAWAEDDHML--- 372
Cdd:cd06639  27 IETIGKGTYGKVYKVTNKKDGSLAAVK-ILDPIS-DVDEEieaeyNILRS------LPNHPNVVKFYGMFYKADQYVggq 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 --IQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavSEEGdedd 450
Cdd:cd06639  99 lwLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT--------TEGG---- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnkvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVL----QENYSHLPKADIFALALTVV-CAAGAEPLPrngdQ 521
Cdd:cd06639 167 -------VKLVDFGVSAQLTSARLRRntsvGTPFWMAPEVIaceqQYDYSYDARCDVWSLGITAIeLADGDPPLF----D 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 522 WHEIRQ-GRLPRI-------PQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06639 236 MHPVKAlFKIPRNppptllnPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEH 287
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
297-565 1.14e-16

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: 80.12  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14078   3 KYYELhETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGD-DLPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnk 455
Cdd:cd14078  81 EYCPGGELFDYIVAKDRL----SEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLL-------------DEDQNL--- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGHVTRISSPQVEE-----GDSRFLANEVLQENYSHLPKADIFALAL---TVVCAAgaepLPRNGDQ----WH 523
Cdd:cd14078 141 ---KLIDFGLCAKPKGGMDHHletccGSPAYAAPELIQGKPYIGSEADVWSMGVllyALLCGF----LPFDDDNvmalYR 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 524 EIRQGRLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14078 214 KIQSGKY-EEPEWLSPSSKLLLDQMLQVDPKKRITVKELLNH 254
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
301-565 1.17e-16

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: 80.82  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd07833   6 LGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREV---KVLRQlrHENIVNLKEAFRRKGRLYLVFEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 nGGSLADAVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmF 458
Cdd:cd07833  83 -ERTLLELLEASPGGLPP---DAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGV-------------------L 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRIS----SPQVEEGDSR-FLANEVLQENYSHLPKADIFALALTVVCAAGAEPL-PRNG--DQWHEIRQ--G 528
Cdd:cd07833 140 KLCDFGFARALTarpaSPLTDYVATRwYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLfPGDSdiDQLYLIQKclG 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 529 RLP-----------------------------RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd07833 220 PLPpshqelfssnprfagvafpepsqpeslerRYPGKVSSPALDFLKACLRMDPKERLTCDELLQH 285
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
304-563 1.33e-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: 79.88  E-value: 1.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRldGCIYAIKRSKKPLAGSVDEQNAL-REVyahAVLGQ--HPHVVRYFSAWAED-DHMLIQNEYCN 379
Cdd:cd14064   1 IGSGSFGKVYKGRCR--NKIVAIKRYRANTYCSKSDVDMFcREV---SILCRlnHPCVIQFVGACLDDpSQFAIVTQYVS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRVMSyfTEAELKdLLLQVGRGLRYIHSMS--LVHMDIKPSNIFIsrtsipnavseegDEDdwiSNKVM 457
Cdd:cd14064  76 GGSLFSLLHEQKRVID--LQSKLI-IAVDVAKGMEYLHNLTqpIIHRDLNSHNILL-------------YED---GHAVV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQV--EEGDSRFLANEVLQENYSHLPKADIFALALTV-------VCAAGAEPLPRNGDQ-WHEIRq 527
Cdd:cd14064 137 ADFGESRFLQSLDEDNMtkQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLwelltgeIPFAHLKPAAAAADMaYHHIR- 215
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 528 grlPRIPQVLSQELTELLKVMIHPDPERRPSAMVLV 563
Cdd:cd14064 216 ---PPIGYSIPKPISSLLMRGWNAEPESRPSFVEIV 248
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
304-576 1.46e-16

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: 80.56  E-value: 1.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKR----SKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIiqieSEEELEDFMVEIDILSEC-------KHPNIVGLYEAYFYENKLWILIEFCD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddwisnkvmFK 459
Cdd:cd06611  86 GGALDSIMLELERG---LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTL---------DGD----------VK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLG-----------HVTRISSPQveegdsrFLANEVLQ-ENYSHLP---KADIFALALTVVCAAGAEPlPRNgdQWHE 524
Cdd:cd06611 144 LADFGvsaknkstlqkRDTFIGTPY-------WMAPEVVAcETFKDNPydyKADIWSLGITLIELAQMEP-PHH--ELNP 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 525 IR------QGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSA 576
Cdd:cd06611 214 MRvllkilKSEPPTLdqPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKA 273
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
301-580 1.52e-16

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: 80.56  E-value: 1.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAiKRSKKPLAGSVDEQNALREVY-AHAVlgQHPHVVRYFSAW-AEDDHMLIQNEYC 378
Cdd:cd06620  10 LKDLGAGNGGSVSKVLHIPTGTIMA-KKVIHIDAKSSVRKQILRELQiLHEC--HSPYIVSFYGAFlNENNNIIICMEYM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLaDAVsenYRVMSYFTEAELKDLLLQVGRGLRYIHSM-SLVHMDIKPSNIFisrtsipnavseegdeddwISNKVM 457
Cdd:cd06620  87 DCGSL-DKI---LKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNIL-------------------VNSKGQ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGhVTR--ISS-PQVEEGDSRFLANEVLQ-ENYShlPKADIFALALTVV-CAAGAEPLPRNGDQW---------- 522
Cdd:cd06620 144 IKLCDFG-VSGelINSiADTFVGTSTYMSPERIQgGKYS--VKSDVWSLGLSIIeLALGEFPFAGSNDDDdgyngpmgil 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 523 ---HEIRQGRLPRIPQ--VLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLR 580
Cdd:cd06620 221 dllQRIVNEPPPRLPKdrIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASDVDLR 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
301-567 1.56e-16

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: 80.39  E-value: 1.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgSVDEQNALREVYAHAVLGQHPHVVRYfsawaeDDHMLIQNEycng 380
Cdd:cd07831   4 LGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFK-SLEQVNNLREIQALRRLSPHPNILRL------IEVLFDRKT---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLA---DAVSEN-YRVMS----YFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdeddwi 452
Cdd:cd07831  73 GRLAlvfELMDMNlYELIKgrkrPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI------------------- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 sNKVMFKIGDLGHVTRISS--PQVEEGDSR-FLANEVLQENYSHLPKADIFALALTVVCAAGAEPL-PrnG----DQWHE 524
Cdd:cd07831 134 -KDDILKLADFGSCRGIYSkpPYTEYISTRwYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLfP--GtnelDQIAK 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 525 I---------------------------RQGR-LPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSV 567
Cdd:cd07831 211 IhdvlgtpdaevlkkfrksrhmnynfpsKKGTgLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
302-565 1.71e-16

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: 79.93  E-value: 1.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSkkPLAGSVDEQnALREVYAHAVLGqHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14107   8 EEIGRGTFGFVKRVTHKGNGECCAAKFI--PLRSSTRAR-AFQERDILARLS-HRRLTCLLDQFETRKTLILILELCSSE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVsenYRvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnaVSEEgDEDdwisnkvmFKIG 461
Cdd:cd14107  84 ELLDRL---FL-KGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM--------VSPT-RED--------IKIC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGHVTRISS--PQVEE-GDSRFLANEVLQENysHLPKA-DIFALA-LTVVCAAGAEPLPRNGDQ--WHEIRQGRL---- 530
Cdd:cd14107 143 DFGFAQEITPseHQFSKyGSPEFVAPEIVHQE--PVSAAtDIWALGvIAYLSLTCHSPFAGENDRatLLNVAEGVVswdt 220
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 531 PRIPQvLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14107 221 PEITH-LSEDAKDFIKRVLQPDPEKRPSASECLSH 254
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
304-491 1.75e-16

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: 79.58  E-value: 1.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK--RSKKPlagsVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKfiKCRKA----KDREDVRNEIEIMNQL-RHPRLLQLYDAFETPREMVLVMEYVAGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAV-SENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIF-ISRTsipnavseegdeddwiSNKVmfK 459
Cdd:cd14103  76 ELFERVvDDDFEL----TERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRT----------------GNQI--K 133
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17865613 460 IGDLGHVTRI---SSPQVEEGDSRFLANEVLqeNY 491
Cdd:cd14103 134 IIDFGLARKYdpdKKLKVLFGTPEFVAPEVV--NY 166
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
297-487 1.79e-16

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: 80.45  E-value: 1.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCnGGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnkv 456
Cdd:cd07832  81 YM-LSSLSEVLRDEERP---LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG------------------- 137
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17865613 457 MFKIGDLG-------HVTRISSPQVeeGDSRFLANEVL 487
Cdd:cd07832 138 VLKIADFGlarlfseEDPRLYSHQV--ATRWYRAPELL 173
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
297-556 1.92e-16

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: 79.67  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKR----LDGCIYAIkrSKKPLAGSV----DEQNALREVyahavlgQHPHVVRYFSAWAED 368
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRHKekhdLEVAVKCI--NKKNLAKSQtllgKEIKILKEL-------KHENIVALYDFQEIA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIQNEYCNGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS----RTSIPNAVSe 444
Cdd:cd14202  74 NSVYLVMEYCNGGDLADYL----HTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggRKSNPNNIR- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 445 egdeddwisnkvmFKIGDLGHVTRISSPQVEE---GDSRFLANEV-LQENYShlPKADIFALALTVV-CAAGAEPL---- 515
Cdd:cd14202 149 -------------IKIADFGFARYLQNNMMAAtlcGSPMYMAPEViMSQHYD--AKADLWSIGTIIYqCLTGKAPFqass 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 516 PRNGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14202 214 PQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGLLQRNQKDR 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
298-560 4.94e-16

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


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 78.49  E-value: 4.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRldGCI--YAIK---RSKKPlagsvdeqNALREV-YAHAVlgQHPHVVRyFSAWAE-DDH 370
Cdd:cd14010   2 YVLYDEIGRGKHSVVYKGRRK--GTIefVAIKcvdKSKRP--------EVLNEVrLTHEL--KHPNVLK-FYEWYEtSNH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI-------------SRts 437
Cdd:cd14010  69 LWLVVEYCTGGDLETLLRQDGN----LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLdgngtlklsdfglAR-- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 438 ipnavsEEGDEDDWISNKVMfkigDLGHVTRISSPQVEEGDSRFLANEVLQEnYSHLPKADIFALAltvvCAAgaeplpr 517
Cdd:cd14010 143 ------REGEILKELFGQFS----DEGNVNKVSKKQAKRGTPYYMAPELFQG-GVHSFASDLWALG----CVL------- 200
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 518 ngdqwHEIRQGRLPripqVLSQELTELLKVMIHPDPERRPSAM 560
Cdd:cd14010 201 -----YEMFTGKPP----FVAESFTELVEKILNEDPPPPPPKV 234
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
297-521 5.07e-16

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: 78.68  E-value: 5.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGS----VDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHM 371
Cdd:cd14105   5 DFYDIgEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsrrgVSREDIEREVSILRQV-LHPNIITLHDVFENKTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAvseegdeddw 451
Cdd:cd14105  84 VLILELVAGGELFDFLAEK----ESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIP---------- 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 452 isnkvMFKIGDLGHVTRISSPQVEE---GDSRFLANEVLqeNYSHL-PKADIFALA-LTVVCAAGAEPLPRNGDQ 521
Cdd:cd14105 150 -----RIKLIDFGLAHKIEDGNEFKnifGTPEFVAPEIV--NYEPLgLEADMWSIGvITYILLSGASPFLGDTKQ 217
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
297-515 5.33e-16

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: 78.52  E-value: 5.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGS----VDEQNALREVyahAVLG--QHPHVVRYFSAWAEDD 369
Cdd:cd14194   5 DYYDTgEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgVSREDIEREV---SILKeiQHPNVITLHEVYENKT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegded 449
Cdd:cd14194  82 DVILILELVAGGELFDFLAEK----ESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVP---------- 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 450 dwisnKVMFKIGDLGHVTRISSPQVEE---GDSRFLANEVLqeNYSHLP-KADIFALA-LTVVCAAGAEPL 515
Cdd:cd14194 148 -----KPRIKIIDFGLAHKIDFGNEFKnifGTPEFVAPEIV--NYEPLGlEADMWSIGvITYILLSGASPF 211
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
302-568 6.36e-16

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: 78.43  E-value: 6.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLAD-AVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnAVSEEGDeddwisnkvmFKI 460
Cdd:cd14198  94 EIFNlCVPDLAEMVS---ENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLS------SIYPLGD----------IKI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRI-SSPQVEE--GDSRFLANEVLqeNYSHLPKA-DIFALA-LTVVCAAGAEPLPrnGDQwheiRQGRLPRIPQ 535
Cdd:cd14198 155 VDFGMSRKIgHACELREimGTPEYLAPEIL--NYDPITTAtDMWNIGvIAYMLLTHESPFV--GED----NQETFLNISQ 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 536 V-----------LSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14198 227 VnvdyseetfssVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
288-578 6.64e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 79.48  E-value: 6.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  288 SNMKSRYTTEFHELEK---IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAlREVyahAVL--GQHPHVVRYF 362
Cdd:PLN00034  63 SGSAPSAAKSLSELERvnrIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQIC-REI---EILrdVNHPNVVKCH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  363 SAWAEDDHMLIQNEYCNGGSLadavsENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI-SRTSIpna 441
Cdd:PLN00034 139 DMFDHNGEIQVLLEFMDGGSL-----EGTHIAD---EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLInSAKNV--- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  442 vseegdeddwisnkvmfKIGDLGhVTRISSPQVEEGDSR-----FLANEVLQENYSHLP----KADIFALALTVV-CAAG 511
Cdd:PLN00034 208 -----------------KIADFG-VSRILAQTMDPCNSSvgtiaYMSPERINTDLNHGAydgyAGDIWSLGVSILeFYLG 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613  512 AEPLP--RNGDqWHE----IRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQ 578
Cdd:PLN00034 270 RFPFGvgRQGD-WASlmcaICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQG 341
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
292-504 7.01e-16

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: 78.03  E-value: 7.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEfhELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDD 369
Cdd:cd14193   2 SYYNVN--KEEILGGGRFGQVHKCEEKSSGLKLAAKIIK--ARSQKEKEEVKNEI---EVMNQlnHANLIQLYDAFESRN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLAD-AVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIF-ISRTsipnavseegd 447
Cdd:cd14193  75 DIVLVMEYVDGGELFDrIIDENYNL----TELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSRE----------- 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwiSNKVmfKIGDLGHVTRISSPQ---VEEGDSRFLANEVLQENYSHLPkADIFALAL 504
Cdd:cd14193 140 -----ANQV--KIIDFGLARRYKPREklrVNFGTPEFLAPEVVNYEFVSFP-TDMWSLGV 191
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
296-579 8.19e-16

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: 78.52  E-value: 8.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIK---RSKKplagsvdeqNALREVYAHAVLGQHPHVVRYFSAWAEDDHM 371
Cdd:cd14178   2 TDGYEIkEDIGIGSYSVCKRCVHKATSTEYAVKiidKSKR---------DPSEEIEILLRYGQHPNIITLKDVYDDGKFV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnaVSEEGDEDDw 451
Cdd:cd14178  73 YLVMELMRGGELLDRILRQ----KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILY--------MDESGNPES- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isnkvmFKIGDLGHVTRIsspQVEEG-------DSRFLANEVLQENySHLPKADIFALA-LTVVCAAGAEPLPrNG--DQ 521
Cdd:cd14178 140 ------IRICDFGFAKQL---RAENGllmtpcyTANFVAPEVLKRQ-GYDAACDIWSLGiLLYTMLAGFTPFA-NGpdDT 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 522 WHEIrqgrLPRIPQ-----------VLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQL 579
Cdd:cd14178 209 PEEI----LARIGSgkyalsggnwdSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSQNQL 273
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
304-565 1.07e-15

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: 77.36  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLagsvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd14188   9 LGKGGFAKCYEMTDLTTNKVYAAKiiphsRVSKPH----QREKIDKEIELHRIL-HHKHVVQFYHYFEDKENIYILLEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwisnkVMF 458
Cdd:cd14188  84 SRRSMAHIL----KARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEN-------------------MEL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTV-VCAAGAEPLPRNG--DQWHEIRQGRLp 531
Cdd:cd14188 141 KVGDFGLAARLEPLEHRRrticGTPNYLSPEVLNKQ-GHGCESDIWALGCVMyTMLLGRPPFETTNlkETYRCIREARY- 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14188 219 SLPSSLLAPAKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
289-568 1.34e-15

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: 77.27  E-value: 1.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 289 NMKSRYTtefhELEKIGSGEFGSVFKCVKRLDGCIYAIKR------SKKPLAgsVDEQNALREvyahavlGQHPHVVRYF 362
Cdd:cd06647   4 DPKKKYT----RFEKIGQGASGTVYTAIDVATGQEVAIKQmnlqqqPKKELI--INEILVMRE-------NKNPNIVNYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 363 SAWAEDDHMLIQNEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtSIPNAV 442
Cdd:cd06647  71 DSYLVGDELWVVMEYLAGGSLTDVVTE-----TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL---GMDGSV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 443 seegdeddwisnkvmfKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTVVCAAGAEPLPRN 518
Cdd:cd06647 143 ----------------KLTDFGFCAQITPEQSKRstmvGTPYWMAPEVVTRK-AYGPKVDIWSLGIMAIEMVEGEPPYLN 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 519 GD---QWHEIRQGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06647 206 ENplrALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
301-559 1.76e-15

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: 76.88  E-value: 1.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKrldgciyaiKRSKKPLAGSV------DEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd14110   8 QTEINRGRFSVVRQCEE---------KRSGQMLAAKIipykpeDKQLVLREYQVLRRL-SHPRIAQLHSAYLSPRHLVLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNavseegdeddwisn 454
Cdd:cd14110  78 EELCSGPELLYNLAER----NSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITE---KN-------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvMFKIGDLGHVTRISSPQVEEGDSRF-----LANEVLQENySHLPKADIFALALTVVCAAGAE-PLPRNG--DQWHEIR 526
Cdd:cd14110 137 --LLKIVDLGNAQPFNQGKVLMTDKKGdyvetMAPELLEGQ-GAGPQTDIWAIGVTAFIMLSADyPVSSDLnwERDRNIR 213
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 527 QG--RLPRIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd14110 214 KGkvQLSRCYAGLSGGAVNFLKSTLCAKPWGRPTA 248
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
302-568 2.07e-15

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: 76.50  E-value: 2.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYA---IKRSKKPlagSVDEQNALREVyahAVLG--QHPHVVRYFSAWAED--DHMLIQ 374
Cdd:cd13983   7 EVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLP---KAERQRFKQEI---EILKslKHPNIIKFYDSWESKskKEVIFI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSM--SLVHMDIKPSNIFISRTsipnavseegdeddwi 452
Cdd:cd13983  81 TELMTSGTLKQYLKRFKRL----KLKVIKSWCRQILEGLNYLHTRdpPIIHRDLKCDNIFINGN---------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 SNKVmfKIGDLGHVT--RISSPQVEEGDSRFLANEVLQENYShlPKADIFALALTVV-----------CAAGAEPLPRng 519
Cdd:cd13983 141 TGEV--KIGDLGLATllRQSFAKSVIGTPEFMAPEMYEEHYD--EKVDIYAFGMCLLematgeypyseCTNAAQIYKK-- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 520 dqwheIRQGRLPR-IPQVLSQELTELLKVMIHPdPERRPSAMVLVKHSVL 568
Cdd:cd13983 215 -----VTSGIKPEsLSKVKDPELKDFIEKCLKP-PDERPSARELLEHPFF 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
297-568 3.95e-15

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: 76.20  E-value: 3.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCV--KRLDGCIYAIKRSKKPLAGSV----DEQNALREVyahavlgQHPHVVRYFSAWAEDDH 370
Cdd:cd14201   7 EYSRKDLVGHGAFAVVFKGRhrKKTDWEVAIKSINKKNLSKSQillgKEIKILKEL-------QHENIVALYDVQEMPNS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdedd 450
Cdd:cd14201  80 VFLVMEYCNGGDLADYL----QAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSS-------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wiSNKVMFKIGDLGHVTRISSPQVEE---GDSRFLANEV-LQENYShlPKADIFALALTVV-CAAGAEPLPRNGDQ---- 521
Cdd:cd14201 148 --VSGIRIKIADFGFARYLQSNMMAAtlcGSPMYMAPEViMSQHYD--AKADLWSIGTVIYqCLVGKPPFQANSPQdlrm 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 522 WHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14201 224 FYEKNKNLQPSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
304-565 4.25e-15

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: 75.84  E-value: 4.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-------RSKKPLAGsvDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14184   9 IGDGNFAVVKECVERSTGKEFALKiidkakcCGKEHLIE--NEVSILRRV-------KHPNIIMLIEEMDTPAELYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsIPNAVSEegdeddwisnkv 456
Cdd:cd14184  80 LVKGGDLFDAITSSTK----YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCE--YPDGTKS------------ 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mFKIGDLGHVTRISSPQVEE-GDSRFLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPLPRNG----DQWHEIRQGRL 530
Cdd:cd14184 142 -LKLGDFGLATVVEGPLYTVcGTPTYVAPEIIAETGYGL-KVDIWAAGvITYILLCGFPPFRSENnlqeDLFDQILLGKL 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 531 pRIPQVLSQELT----ELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14184 220 -EFPSPYWDNITdsakELISHMLQVNVEARYTAEQILSH 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
302-558 4.86e-15

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: 75.40  E-value: 4.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDG-CIYAIK-RSKKPLAGSVDEqNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSGArEVVAVKcVSKSSLNKASTE-NLLTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwiSNKVMFK 459
Cdd:cd14121  79 GGDLSRFIRSRRTL----PESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSS-----------------RYNPVLK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLG---HVTRISSPQVEEGDSRFLANE-VLQENYShlPKADIFALALTVV-CAAGAEPL-PRNGDQWHE-IRQGR--- 529
Cdd:cd14121 138 LADFGfaqHLKPNDEAHSLRGSPLYMAPEmILKKKYD--ARVDLWSVGVILYeCLFGRAPFaSRSFEELEEkIRSSKpie 215
                       250       260
                ....*....|....*....|....*....
gi 17865613 530 LPRIPQvLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14121 216 IPTRPE-LSADCRDLLLRLLQRDPDRRIS 243
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
301-565 5.51e-15

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: 75.82  E-value: 5.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKrSKKPLAgSVDEQ-----NALRevyahaVLGQHPHVVRYFSAWAEDD-----H 370
Cdd:cd06638  23 IETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPIH-DIDEEieaeyNILK------ALSDHPNVVKFYGMYYKKDvkngdQ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavSEEGdedd 450
Cdd:cd06638  95 LWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLT--------TEGG---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnkvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVL----QENYSHLPKADIFALALTVV-CAAGAEPLPrngdQ 521
Cdd:cd06638 163 -------VKLVDFGVSAQLTSTRLRRntsvGTPFWMAPEVIaceqQLDSTYDARCDVWSLGITAIeLGDGDPPLA----D 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 522 WHEIRQ-GRLPR-------IPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06638 232 LHPMRAlFKIPRnppptlhQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
274-591 7.37e-15

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: 75.53  E-value: 7.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 274 EDETRPAKRITITESNMKSRYTtefhELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvdEQNALREVYAHAVL- 352
Cdd:cd06656   1 DEEILEKLRSIVSVGDPKKKYT----RFEKIGQGASGTVYTAIDIATGQEVAIKQMNL-------QQQPKKELIINEILv 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 353 ---GQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPS 429
Cdd:cd06656  70 mreNKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTE-----TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 430 NIFISRTSipnavseegdeddwisnkvMFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALT 505
Cdd:cd06656 145 NILLGMDG-------------------SVKLTDFGFCAQITPEQSKRstmvGTPYWMAPEVVTRK-AYGPKVDIWSLGIM 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 506 VVCAAGAEPLPRNGD---QWHEIRQGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLR 580
Cdd:cd06656 205 AIEMVEGEPPYLNENplrALYLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPL 284
                       330
                ....*....|.
gi 17865613 581 IELNAEKFKNS 591
Cdd:cd06656 285 IIAAKEAIKNS 295
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
304-559 7.58e-15

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: 75.04  E-value: 7.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKR--LDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLG--QHPHVVRYFS-AWAEDDHMLIQNEYC 378
Cdd:cd13994   1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESKRKDYVKRLTSEYIISSklHHPNIVKVLDlCQDLHGKWCLVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVsENYRVMSyFTEAELkdLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmF 458
Cdd:cd13994  81 PGGDLFTLI-EKADSLS-LEEKDC--FFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV-------------------L 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQVEE--------GDSRFLANEVLQEN-YSHLPkADIFALALTVVC-AAGAEP--LPRNGD------ 520
Cdd:cd13994 138 KLTDFGTAEVFGMPAEKEspmsaglcGSEPYMAPEVFTSGsYDGRA-VDVWSCGIVLFAlFTGRFPwrSAKKSDsaykay 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 521 --QWHEIRQGRLPRIPQVLSqELTELLKVMIHPDPERRPSA 559
Cdd:cd13994 217 ekSGDFTNGPYEPIENLLPS-ECRRLIYRMLHPDPEKRITI 256
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
304-556 7.69e-15

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: 74.71  E-value: 7.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFK--CVKRLDGCIyAIKR-SKKPLAGSVD----EQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14120   1 IGHGAFAVVFKgrHRKKPDLPV-AIKCiTKKNLSKSQNllgkEIKILKEL-------SHENVVALLDCQETSSSVYLVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeddwiSNKV 456
Cdd:cd14120  73 YCNGGDLADYLQA----KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPS----------PNDI 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGH----------VTRISSPQveegdsrFLANEVLQ-ENYShlPKADIFALAlTVV--CAAGAEPL----PRNG 519
Cdd:cd14120 139 RLKIADFGFarflqdgmmaATLCGSPM-------YMAPEVIMsLQYD--AKADLWSIG-TIVyqCLTGKAPFqaqtPQEL 208
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 520 DQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14120 209 KAFYEKNANLRPNIPSGTSPALKDLLLGLLKRNPKDR 245
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
297-565 1.30e-14

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: 74.29  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIK--LEPGDDFSLIQQEIFMVKEC-KHCNIVAYFGSYLSREKLWICME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAvsenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwisnkv 456
Cdd:cd06646  87 YCGGGSLQDI----YHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILL---------TDNGD--------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mFKIGDLGHVTRISSPQVEE----GDSRFLANEV--LQEN--YSHLpkADIFALALTVVCAAGAEPLPRNgdqWHEIRQG 528
Cdd:cd06646 145 -VKLADFGVAAKITATIAKRksfiGTPYWMAPEVaaVEKNggYNQL--CDIWAVGITAIELAELQPPMFD---LHPMRAL 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 529 RL--------PRIPQVL--SQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06646 219 FLmsksnfqpPKLKDKTkwSSTFHNFVKISLTKNPKKRPTAERLLTH 265
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
304-565 1.75e-14

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: 73.88  E-value: 1.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-------RSKKPLAGsvDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14183  14 IGDGNFAVVKECVERSTGREYALKiinkskcRGKEHMIQ--NEVSILRRV-------KHPNIVLLIEEMDMPTELYLVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavSEEGDEDdwisnkv 456
Cdd:cd14183  85 LVKGGDLFDAITSTNK----YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYE-------HQDGSKS------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mFKIGDLGHVTRISSPQVEE-GDSRFLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPLPRNGDQ----WHEIRQGRL 530
Cdd:cd14183 147 -LKLGDFGLATVVDGPLYTVcGTPTYVAPEIIAETGYGL-KVDIWAAGvITYILLCGFPPFRGSGDDqevlFDQILMGQV 224
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 531 ----PRIPQVlSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14183 225 dfpsPYWDNV-SDSAKELITMMLQVDVDQRYSALQVLEH 262
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
299-566 1.92e-14

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: 73.87  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEK-IGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14665   2 YELVKdIGSGNFGVARLMRDKQTKELVAVKYIER---GEKIDENVQREIINHRSL-RHPNIVRFKEVILTPTHLAIVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNavseegdeddwisnkvm 457
Cdd:cd14665  78 AAGGELFERICNAGR----FSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPR----------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRI---SSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTV-VCAAGAEPL-----PRNGDQWHEIRQG 528
Cdd:cd14665 137 LKICDFGYSKSSvlhSQPKSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLyVMLVGAYPFedpeePRNFRKTIQRILS 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 529 RLPRIPQV--LSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14665 217 VQYSIPDYvhISPECRHLISRIFVADPATRITIPEIRNHE 256
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
293-611 2.04e-14

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: 75.06  E-value: 2.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHML 372
Cdd:cd14176  16 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK------SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnaVSEEGDEDDwi 452
Cdd:cd14176  90 VVTELMKGGELLDKILRQ----KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY--------VDESGNPES-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 snkvmFKIGDLGHVTRIsspQVEEG-------DSRFLANEVLQENySHLPKADIFALA-LTVVCAAGAEPLPrNG--DQW 522
Cdd:cd14176 156 -----IRICDFGFAKQL---RAENGllmtpcyTANFVAPEVLERQ-GYDAACDIWSLGvLLYTMLTGYTPFA-NGpdDTP 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 523 HEIrqgrLPRIP-----------QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLrielnaekfkNS 591
Cdd:cd14176 226 EEI----LARIGsgkfslsggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQL----------NR 291
                       330       340
                ....*....|....*....|
gi 17865613 592 LLQKELKKAQMAAKVAAEER 611
Cdd:cd14176 292 QDAPHLVKGAMAATYSALNR 311
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
296-520 2.07e-14

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: 73.50  E-value: 2.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELE-KIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd14191   1 SDFYDIEeRLGSGKFGQVFRLVEKKTKKVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLAD-AVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnAVSEEGDEddwis 453
Cdd:cd14191  78 LEMVSGGELFErIIDEDFEL----TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIM--------CVNKTGTK----- 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 454 nkvmFKIGDLGHVTRISSP---QVEEGDSRFLANEVLqeNYSHLPKA-DIFALAltVVC---AAGAEPLPRNGD 520
Cdd:cd14191 141 ----IKLIDFGLARRLENAgslKVLFGTPEFVAPEVI--NYEPIGYAtDMWSIG--VICyilVSGLSPFMGDND 206
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
298-566 2.30e-14

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: 73.95  E-value: 2.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRskkpLAGSVDEQN----ALREVYAHAVLgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd07847   3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKK----FVESEDDPVikkiALREIRMLKQL-KHPNLVNLIEVFRRKRKLHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGgSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwis 453
Cdd:cd07847  78 VFEYCDH-TVLNELEKNPRGVP---EHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQ--------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGHVTRISSPQVEEGD---SR-FLANEVLQENYSHLPKADIFALALTVVCAAGAEPL-PRNG--DQWHEIR 526
Cdd:cd07847 139 ----IKLCDFGFARILTGPGDDYTDyvaTRwYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLwPGKSdvDQLYLIR 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 527 Q--GRL-PRIPQVLSQelTELLKVMIHPDPERR-PSAMVLVKHS 566
Cdd:cd07847 215 KtlGDLiPRHQQIFST--NQFFKGLSIPEPETRePLESKFPNIS 256
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
274-591 2.42e-14

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: 73.99  E-value: 2.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 274 EDETRPAKRITITESNMKSRYTtefhELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvdEQNALREVYAHAVL- 352
Cdd:cd06654   2 DEEILEKLRSIVSVGDPKKKYT----RFEKIGQGASGTVYTAMDVATGQEVAIRQMNL-------QQQPKKELIINEILv 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 353 ---GQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPS 429
Cdd:cd06654  71 mreNKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTE-----TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 430 NIFISRTSipnavseegdeddwisnkvMFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALT 505
Cdd:cd06654 146 NILLGMDG-------------------SVKLTDFGFCAQITPEQSKRstmvGTPYWMAPEVVTRK-AYGPKVDIWSLGIM 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 506 VVCAAGAEPLPRNGD---QWHEIRQGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLR 580
Cdd:cd06654 206 AIEMIEGEPPYLNENplrALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPL 285
                       330
                ....*....|.
gi 17865613 581 IELNAEKFKNS 591
Cdd:cd06654 286 IAAAKEATKNN 296
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
297-566 2.50e-14

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: 73.50  E-value: 2.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVD----------EQNALREVyahavlgQHPHVVRYFSAW 365
Cdd:cd14195   5 DHYEMgEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrgvsreeierEVNILREI-------QHPNIITLHDIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAvsee 445
Cdd:cd14195  78 ENKTDVVLILELVSGGELFDFLAEK----ESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNP---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 446 gdeddwisnkvMFKIGDLGHVTRISSPQVEE---GDSRFLANEVLqeNYSHLP-KADIFALA-LTVVCAAGAEPLprngd 520
Cdd:cd14195 150 -----------RIKLIDFGIAHKIEAGNEFKnifGTPEFVAPEIV--NYEPLGlEADMWSIGvITYILLSGASPF----- 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 521 qWHEIRQGRLPRIPQV-----------LSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14195 212 -LGETKQETLTNISAVnydfdeeyfsnTSELAKDFIRRLLVKDPKKRMTIAQSLEHS 267
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
297-557 2.79e-14

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: 73.31  E-value: 2.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFK-CVKRLDGCIYAIKR--SKKPLAG--SVDEQNALREVYAH-AVLGQ---HPHVVRYFSAWAE 367
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKvRKKSNGQTLLALKEinMTNPAFGrtEQERDKSVGDIISEvNIIKEqlrHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIH-SMSLVHMDIKPSNIFISrtsipnavseeg 446
Cdd:cd08528  81 NDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLG------------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 447 dEDDwisnKVMfkIGDLGhVTRISSPQVEE-----GDSRFLANEVLQeNYSHLPKADIFALALTVVCAAGAEPlPRNGDQ 521
Cdd:cd08528 149 -EDD----KVT--ITDFG-LAKQKGPESSKmtsvvGTILYSCPEIVQ-NEPYGEKADIWALGCILYQMCTLQP-PFYSTN 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 522 W----HEIRQGRLPRIPQVL-SQELTELLKVMIHPDPERRP 557
Cdd:cd08528 219 MltlaTKIVEAEYEPLPEGMySDDITFVIRSCLTPDPEARP 259
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
301-566 3.09e-14

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: 72.99  E-value: 3.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKC--VKRLDGCIYAIKRSKKPLAGSVDEQNAL-REVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14080   5 GKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKFLpREL---EILRKlrHPNIIQVYSIFERGSKVFIFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVseegdeddwisnk 455
Cdd:cd14080  82 EYAEHGDLLEYIQKRGAL----SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDS---NNNV------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGHVTRISSPQVEE------GDSRFLANEVLQENYSHLPKADIFALAL---TVVCAAgaepLP---RNGDQWH 523
Cdd:cd14080 142 ---KLSDFGFARLCPDDDGDVlsktfcGSAAYAAPEILQGIPYDPKKYDIWSLGVilyIMLCGS----MPfddSNIKKML 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 524 EIRQGR---LPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14080 215 KDQQNRkvrFPSSVKKLSPECKDLIDQLLEPDPTKRATIEEILNHP 260
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
301-565 3.28e-14

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: 73.25  E-value: 3.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIK-------------RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAE 367
Cdd:cd14077   6 VKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglkkeREKRLEKEISRDIRTIREAALSSLL-NHPHICRLRDFLRT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIQNEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegd 447
Cdd:cd14077  85 PNHYYMLFEYVDGGQLLDYIISHGKL----KEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSG---------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwisnkvMFKIGDLGhVTRISSPQVEE----GDSRFLANEVLQENYSHLPKADIFALALTV---VCaaGAEPL-PRNG 519
Cdd:cd14077 151 ---------NIKIIDFG-LSNLYDPRRLLrtfcGSLYFAAPELLQAQPYTGPEVDVWSFGVVLyvlVC--GKVPFdDENM 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 520 DQWHE-IRQGRLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14077 219 PALHAkIKKGKV-EYPSYLSSECKSLISRMLVVDPKKRATLEQVLNH 264
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
298-436 3.81e-14

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: 73.46  E-value: 3.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ-----HPHVVRYF--SAWAEDDH 370
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREI---ALLKQlesfeHPNVVRLLdvCHGPRTDR 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 371 ---MLIQNEYCNGgSLADAVSenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd07838  78 elkLTLVFEHVDQ-DLATYLD--KCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSD 143
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
298-568 4.24e-14

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: 72.69  E-value: 4.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDG---CIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHpHVVRYFSAWAEDDHMLIQ 374
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGeevALKIIKNNKDYLDQSLDEIRLLELLNKKDKADKY-HIVRLKDVFYFKNHLCIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCnGGSLADAVSENyrVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI---SRTSIpnavseegdeddw 451
Cdd:cd14133  80 FELL-SQNLYEFLKQN--KFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasySRCQI------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isnkvmfKIGDLG---HVTRISSPQVEegdSRFL-ANEV-LQENYSHlpKADIFALALTVVCAAGAEPLPRNGDQwheir 526
Cdd:cd14133 144 -------KIIDFGsscFLTQRLYSYIQ---SRYYrAPEViLGLPYDE--KIDMWSLGCILAELYTGEPLFPGASE----- 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 527 QGRLPRIPQVLS--------------QELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14133 207 VDQLARIIGTIGippahmldqgkaddELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
299-556 4.85e-14

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: 72.44  E-value: 4.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEK-IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSV--DEQnALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14663   2 YELGRtLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmVEQ-IKREIAIMKLL-RHPNIVELHEVMATKTKIFFVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnk 455
Cdd:cd14663  80 ELVTGGELFSKIAKNGR----LKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLL-------------DEDGNL--- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGhVTRISSPQVEE-------GDSRFLANEVLQENYSHLPKADIFALALTV-VCAAGAEPL--PRNGDQWHEI 525
Cdd:cd14663 140 ---KISDFG-LSALSEQFRQDgllhttcGTPNYVAPEVLARRGYDGAKADIWSCGVILfVLLAGYLPFddENLMALYRKI 215
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 526 RQGRlPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14663 216 MKGE-FEYPRWFSPGAKSLIKRILDPNPSTR 245
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
296-566 5.45e-14

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: 73.13  E-value: 5.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd14177   3 TDVYELkEDIGVGSYSVCKRCIHRATNMEFAVKIIDK------SKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnaVSEEGDEDDwisn 454
Cdd:cd14177  77 TELMKGGELLDRILRQ----KFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILY--------MDDSANADS---- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDLGHVTRISSpqvEEG-------DSRFLANEVL-QENYShlPKADIFALA-LTVVCAAGAEPLPrNG--DQWH 523
Cdd:cd14177 141 ---IRICDFGFAKQLRG---ENGllltpcyTANFVAPEVLmRQGYD--AACDIWSLGvLLYTMLAGYTPFA-NGpnDTPE 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17865613 524 EIrqgrLPRIPQ-----------VLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14177 212 EI----LLRIGSgkfslsggnwdTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHS 261
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
274-568 5.46e-14

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: 73.22  E-value: 5.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 274 EDETRPAKRITITESNMKSRYTtefhELEKIGSGEFGSVFKCVKRLDGCIYAIKR---SKKPlagsvDEQNALREVYAHA 350
Cdd:cd06655   1 DEEIMEKLRTIVSIGDPKKKYT----RYEKIGQGASGTVFTAIDVATGQEVAIKQinlQKQP-----KKELIINEILVMK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 351 VLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSN 430
Cdd:cd06655  72 EL-KNPNIVNFLDSFLVGDELFVVMEYLAGGSLTDVVTE-----TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDN 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 431 IFISRtsipnavseEGDeddwisnkvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTV 506
Cdd:cd06655 146 VLLGM---------DGS----------VKLTDFGFCAQITPEQSKRstmvGTPYWMAPEVVTRK-AYGPKVDIWSLGIMA 205
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 507 VCAAGAEPLPRNGD---QWHEIRQGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06655 206 IEMVEGEPPYLNENplrALYLIATNGTPELqnPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFL 272
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
300-556 5.93e-14

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: 72.29  E-value: 5.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 300 ELEK-IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVyahAVLG--QHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14081   4 RLGKtLGKGQTGLVKLAKHCVTGQKVAIKiVNKEKLSKESVLMKVEREI---AIMKliEHPNVLKLYDVYENKKYLYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdeDDWisNK 455
Cdd:cd14081  81 EYVSGGELFDYLVKKGR----LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL---------------DEK--NN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VmfKIGDLGhvtrISSPQVEE-------GDSRFLANEVLQ-ENYsHLPKADI-------FALaltvvcAAGAepLPRNGD 520
Cdd:cd14081 140 I--KIADFG----MASLQPEGslletscGSPHYACPEVIKgEKY-DGRKADIwscgvilYAL------LVGA--LPFDDD 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 521 Q----WHEIRQGRlPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14081 205 NlrqlLEKVKRGV-FHIPHFISPDAQDLLRRMLEVNPEKR 243
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
298-565 6.07e-14

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: 72.04  E-value: 6.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEK-IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14071   1 FYDIERtIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKML-NHPHIIKLYQVMETKDMLYLVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkv 456
Cdd:cd14071  80 YASNGEIFDYLAQHGRM----SEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL-------------DANMNI---- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLGHVTRISSPQVEE---GDSRFLANEVLQENYSHLPKADIFALALTV---VCAAgaepLPRNGDQWHEIRQ--- 527
Cdd:cd14071 139 --KIADFGFSNFFKPGELLKtwcGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLyvlVCGA----LPFDGSTLQTLRDrvl 212
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 528 -GRLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14071 213 sGRF-RIPFFMSTDCEHLIRRMLVLDPSKRLTIEQIKKH 250
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
297-568 6.58e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 75.54  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   297 EFHELEKIGSGEFGSVFKCV-KRLDG--CIYAI------KRSKKPLagsVDEQNALREVyahavlgQHPHVVRYFSAW-- 365
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFLVKhKRTQEffCWKAIsyrglkEREKSQL---VIEVNVMREL-------KHKNIVRYIDRFln 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   366 AEDDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMS-------LVHMDIKPSNIFISrTSI 438
Cdd:PTZ00266   84 KANQKLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLS-TGI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   439 PNaVSEEGDEDDWISNKVMFKIGDLGHVTRISSPQVEE---GDSRFLANE-VLQENYSHLPKADIFALALTV--VCaAGA 512
Cdd:PTZ00266  163 RH-IGKITAQANNLNGRPIAKIGDFGLSKNIGIESMAHscvGTPYYWSPElLLHETKSYDDKSDMWALGCIIyeLC-SGK 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613   513 EPLPR--NGDQW-HEIRQGrlPRIP-QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:PTZ00266  241 TPFHKanNFSQLiSELKRG--PDLPiKGKSKELNILIKNLLNLSAKERPSALQCLGYQII 298
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
304-565 8.62e-14

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: 71.88  E-value: 8.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLagsvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd14189   9 LGKGGFARCYEMTDLATNKTYAVKviphsRVAKPH----QREKIVNEIELHRDL-HHKHVVKFSHHFEDAENIYIFLELC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAvsenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwisnkVMF 458
Cdd:cd14189  84 SRKSLAHI----WKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINEN-------------------MEL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALA---LTVVCaaGAEPLPRNG--DQWHEIRQGR 529
Cdd:cd14189 141 KVGDFGLAARLEPPEQRKkticGTPNYLAPEVLLRQ-GHGPESDVWSLGcvmYTLLC--GNPPFETLDlkETYRCIKQVK 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 530 LPrIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14189 218 YT-LPASLSLPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
304-566 9.63e-14

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: 71.52  E-value: 9.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLAGsvdEQNALREVyahAVLGQ--HPHVVRYFSAWAEDD--HMLIQ 374
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKilkkrKLRRIPNG---EANVKREI---QILRRlnHRNVIKLVDVLYNEEkqKLYMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGG--SLADAVSEN----YRVMSYFTeaelkdlllQVGRGLRYIHSMSLVHMDIKPSNIFIS---RTSIPN-AVSE 444
Cdd:cd14119  75 MEYCVGGlqEMLDSAPDKrlpiWQAHGYFV---------QLIDGLEYLHSQGIIHKDIKPGNLLLTtdgTLKISDfGVAE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 445 EGDeddwisnkvMFKIGDLGHVTRIS----SPQVEEGDSRFlanevlqenysHLPKADIFALALTVV-CAAGAEPLprNG 519
Cdd:cd14119 146 ALD---------LFAEDDTCTTSQGSpafqPPEIANGQDSF-----------SGFKVDIWSAGVTLYnMTTGKYPF--EG 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 520 DQWHE----IRQGRLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14119 204 DNIYKlfenIGKGEY-TIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
304-556 1.02e-13

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: 71.39  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-------RSKKPLAGSVDEQNALREVYahavlgqHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKvlrkkeiIKRKEVEHTLNERNILERVN-------HPFIVKLHYAFQTEEKLYLVLD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkv 456
Cdd:cd05123  74 YVPGGELFSHLSKE----GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL-------------DSDGHI---- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLGhvtrISSPQVEEGDSRF--------LANEVLQEN-YSHlpKADIFAL-ALTVVCAAGAEPL--PRNGDQWHE 524
Cdd:cd05123 133 --KLTDFG----LAKELSSDGDRTYtfcgtpeyLAPEVLLGKgYGK--AVDWWSLgVLLYEMLTGKPPFyaENRKEIYEK 204
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 525 IRQGRLpRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05123 205 ILKSPL-KFPEYVSPEAKSLISGLLQKDPTKR 235
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
303-568 1.32e-13

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: 71.50  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14197  16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LAD-AVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnAVSEEGDeddwisnkvmFKIG 461
Cdd:cd14197  96 IFNqCVADREEA---FKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLT------SESPLGD----------IKIV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGhVTRI--SSPQVEE--GDSRFLANEVLqeNYSHLPKA-DIFALA-LTVVCAAGAEPLPRNGDQ--WHEIRQGRLPRI 533
Cdd:cd14197 157 DFG-LSRIlkNSEELREimGTPEYVAPEIL--SYEPISTAtDMWSIGvLAYVMLTGISPFLGDDKQetFLNISQMNVSYS 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 534 PQ---VLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14197 234 EEefeHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
298-556 1.88e-13

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: 70.75  E-value: 1.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSvRNVLNELEILQEL-EHPFLVNLWYSFQDEEDMYMVVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGdeddwisnkv 456
Cdd:cd05578  81 LLLGGDLRYHLQQKVK----FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---------DEQG---------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGhVTRISSPQvEEGDSR-----FLANEVLQ-ENYSHLpkADIFALALTVV-CAAGAEPLP-RNGDQWHEIRQG 528
Cdd:cd05578 138 HVHITDFN-IATKLTDG-TLATSTsgtkpYMAPEVFMrAGYSFA--VDWWSLGVTAYeMLRGKRPYEiHSRTSIEEIRAK 213
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 529 RL---PRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05578 214 FEtasVLYPAGWSEEAIDLINKLLERDPQKR 244
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
301-436 2.07e-13

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: 70.59  E-value: 2.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDEQNALREVYAH-AVL---GQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKK---SDMIAKNQVTNVKAErAIMmiqGESPYVAKLYYSFQSKDYLYLVME 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05611  78 YLNGGDCASLI----KTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT 133
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
302-573 2.56e-13

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: 70.91  E-value: 2.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14086   7 EELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGFHYLVFDLVTGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SL-ADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeddwisnkvmfKI 460
Cdd:cd14086  86 ELfEDIVAR-----EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAV----------------KL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQVE----EGDSRFLANEVLQENYSHLPkADIFALALTV-VCAAGAEPLPRNGDQ--WHEIRQGRL--- 530
Cdd:cd14086 145 ADFGLAIEVQGDQQAwfgfAGTPGYLSPEVLRKDPYGKP-VDIWACGVILyILLVGYPPFWDEDQHrlYAQIKAGAYdyp 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 531 -PRIPQVlSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASR 573
Cdd:cd14086 224 sPEWDTV-TPEAKDLINQMLTVNPAKRITAAEALKHPWICQRDR 266
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
299-520 2.90e-13

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: 70.33  E-value: 2.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14190   7 HSKEVLGGGKFGKVHTCTEKRTGLKLAAKVINK--QNSKDKEMVLLEI---QVMNQlnHRNLIQLYEAIETPNEIVLFME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLAD-AVSENYrvmsYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnK 455
Cdd:cd14190  82 YVEGGELFErIVDEDY----HLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRT-----------------G 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLGHVTRISSPQ---VEEGDSRFLANEVLqeNYSHLP-KADIFALA-LTVVCAAGAEPLPRNGD 520
Cdd:cd14190 141 HQVKIIDFGLARRYNPREklkVNFGTPEFLSPEVV--NYDQVSfPTDMWSMGvITYMLLSGLSPFLGDDD 208
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
293-558 3.36e-13

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: 70.39  E-value: 3.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEFHELekIGSGEFGSVFKCVKRLDGCIYAIKRSkkplagSVDEQNAL----REVYAHAVLGQHPHVVRYFSAWAED 368
Cdd:cd14037   2 SHHVTIEKY--LAEGGFAHVYLVKTSNGGNRAALKRV------YVNDEHDLnvckREIEIMKRLSGHKNIVGYIDSSANR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 D-----HMLIQNEYCNGGSLADAVseNYRVMSYFTEAELKDLLLQVGRGLRYIHSM--SLVHMDIKPSNIFISRTSIpna 441
Cdd:cd14037  74 SgngvyEVLLLMEYCKGGGVIDLM--NQRLQTGLTESEILKIFCDVCEAVAAMHYLkpPLIHRDLKVENVLISDSGN--- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 442 vseegdeddwisnkvmFKIGDLGHVTR-ISSPQVEEG----DSRFLANEVLQ-------ENYSHLP---KADIFALA--L 504
Cdd:cd14037 149 ----------------YKLCDFGSATTkILPPQTKQGvtyvEEDIKKYTTLQyrapemiDLYRGKPiteKSDIWALGclL 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 505 TVVCAAgAEPLPRNGDQwhEIRQGR--LPRIPQvLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14037 213 YKLCFY-TTPFEESGQL--AILNGNftFPDNSR-YSKRLHKLIRYMLEEDPEKRPN 264
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
291-568 3.87e-13

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: 70.00  E-value: 3.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 291 KSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGsvdeqnalREVYAHAvLG-----QHPHVVRYFSAW 365
Cdd:cd14113   2 KDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMK--------RDQVTHE-LGvlqslQHPQLVGLLDTF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQNEYCNGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavsee 445
Cdd:cd14113  73 ETPTSYILVLEMADQGRLLDYVVR----WGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQS--------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 446 gdeddwiSNKVMFKIGDLGHVTRI-SSPQVEE--GDSRFLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPLPRNGDQ 521
Cdd:cd14113 140 -------LSKPTIKLADFGDAVQLnTTYYIHQllGSPEFAAPEIILGNPVSL-TSDLWSIGvLTYVLLSGVSPFLDESVE 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 522 WHEIRQGRLP-RIP----QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14113 212 ETCLNICRLDfSFPddyfKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
304-556 4.54e-13

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: 70.33  E-value: 4.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHM-----LIQNEYC 378
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELS-VKNKDRWCHEIQIMKKL-NHPNVVKACDVPEEMNFLvndvpLLAMEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVS--ENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwISNKV 456
Cdd:cd14039  79 SGGDLRKLLNkpEN---CCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQE----------------INGKI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPQVEE---GDSRFLANEvLQENYSHLPKADIFALALTVV-CAAGAEPLPRNGD--QWHEIRQGRL 530
Cdd:cd14039 140 VHKIIDLGYAKDLDQGSLCTsfvGTLQYLAPE-LFENKSYTVTVDYWSFGTMVFeCIAGFRPFLHNLQpfTWHEKIKKKD 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17865613 531 PR-----------------IPQ------VLSQELTELLKVMIHPDPERR 556
Cdd:cd14039 219 PKhifaveemngevrfsthLPQpnnlcsLIVEPMEGWLQLMLNWDPVQR 267
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
297-565 4.61e-13

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: 70.07  E-value: 4.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06645  12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIK--LEPGEDFAVVQQEIIMMKDC-KHSNIVAYFGSYLRRDKLWICME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAvsenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnkv 456
Cdd:cd06645  89 FCGGGSLQDI----YHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNG------------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPQVEE----GDSRFLANEVL----QENYSHLpkADIFALALTVVCAAGAEPLPRNgdqWHEIRQG 528
Cdd:cd06645 146 HVKLADFGVSAQITATIAKRksfiGTPYWMAPEVAaverKGGYNQL--CDIWAVGITAIELAELQPPMFD---LHPMRAL 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 529 RL--------PRIPQVL--SQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06645 221 FLmtksnfqpPKLKDKMkwSNSFHHFVKMALTKNPKKRPTAEKLLQH 267
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
297-577 5.43e-13

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: 69.88  E-value: 5.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGqhPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06622   2 EIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVS--PYIVDFYGAFFIEGAVYMCME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLaDAVSENYRVMSYFTEAELKDLLLQVGRGLRYI-HSMSLVHMDIKPSNIFisrtsipnavseegdeddwISNK 455
Cdd:cd06622  80 YMDAGSL-DKLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVL-------------------VNGN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLG----HVTRISSPQVeeGDSRFLANEVLQ-----ENYSHLPKADIFALALTVV-CAAGAEPLPRNG-----D 520
Cdd:cd06622 140 GQVKLCDFGvsgnLVASLAKTNI--GCQSYMAPERIKsggpnQNPTYTVQSDVWSLGLSILeMALGRYPYPPETyanifA 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 521 QWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAE 577
Cdd:cd06622 218 QLSAIVDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVD 274
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
298-431 6.36e-13

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: 68.95  E-value: 6.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKK-PLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKdKIEDEQDMVRIRREIEIMSSL-NHPHIIRIYEVFENKDKIVIVME 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 377 YCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14073  82 YASGGELYDYISERRRL----PEREARRIFRQIVSAVHYCHKNGVVHRDLKLENI 132
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
298-434 6.64e-13

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: 69.20  E-value: 6.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIK------RSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHM 371
Cdd:cd14002   3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKfipkrgKSEKELRNLRQEIEILRKL-------NHPNIIEMLDSFETKKEF 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 372 LIQNEYCNGgsladavsENYRVMSY---FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd14002  76 VVVTEYAQG--------ELFQILEDdgtLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG 133
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
298-565 6.86e-13

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: 69.25  E-value: 6.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKrskkpLAGSV-DEQNALREVYAhaVL---GQHPHVVRYFSAW------AE 367
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARHKKTGQLAAIK-----IMDIIeDEEEEIKLEIN--ILrkfSNHPNIATFYGAFikkdppGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGD 447
Cdd:cd06608  81 DDQLWLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILL---------TEEAE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwisnkvmFKIGDLGhVTRISSPQVEE-----GDSRFLANEVL----QENYSHLPKADIFALALTVV-CAAGAEPLpr 517
Cdd:cd06608 152 ----------VKLVDFG-VSAQLDSTLGRrntfiGTPYWMAPEVIacdqQPDASYDARCDVWSLGITAIeLADGKPPL-- 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 518 nGDQ-----WHEIRQGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06608 219 -CDMhpmraLFKIPRNPPPTLksPEKWSKEFNDFISECLIKNYEQRPFTEELLEH 272
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
297-436 8.24e-13

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: 70.01  E-value: 8.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ---NALREVYAHAvlgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05573   2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIahvRAERDILADA---DSPWIVRLHYAFQDEDHLYL 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 374 QNEYCNGGSLADAVSeNYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05573  79 VMEYMPGGDLMNLLI-KYDV---FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDAD 137
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
298-565 9.02e-13

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: 68.63  E-value: 9.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEV---KFLRQlrHPNTIEYKGCYLREHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGgSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGdeddwisn 454
Cdd:cd06607  80 MEYCLG-SASDIVEVHKKPLQ---EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILL---------TEPG-------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvMFKIGDLGHVTRISSPQVEEGDSRFLANEVL----QENYSHlpKADIFALALTVVCAAGAEPLPRNGDQ----WHeIR 526
Cdd:cd06607 139 --TVKLADFGSASLVCPANSFVGTPYWMAPEVIlamdEGQYDG--KVDVWSLGITCIELAERKPPLFNMNAmsalYH-IA 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 527 QGRLPRIPQV-LSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06607 214 QNDSPTLSSGeWSDDFRNFVDSCLQKIPQDRPSAEDLLKH 253
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
298-435 1.12e-12

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: 69.00  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKEL-KHKNIVRLYDVLHSDKKLTLVFEY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CnggslaDAVSENY--RVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd07839  81 C------DQDLKKYfdSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINK 134
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
304-556 1.24e-12

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: 69.01  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvdEQNALR---EVYAHAVLgQHPHVVRY------FSAWAEDDHMLIQ 374
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPS--DKNRERwclEVQIMKKL-NHPNVVSArdvppeLEKLSPNDLPLLA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVS--ENYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIfisrtsipnaVSEEGDeddwi 452
Cdd:cd13989  78 MEYCSGGDLRKVLNqpENC---CGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENI----------VLQQGG----- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 sNKVMFKIGDLGHVTRISSPQVEE---GDSRFLANEVL-QENYSHlpKADIFALAlTVV--CAAGAEP-LP-RNGDQWHE 524
Cdd:cd13989 140 -GRVIYKLIDLGYAKELDQGSLCTsfvGTLQYLAPELFeSKKYTC--TVDYWSFG-TLAfeCITGYRPfLPnWQPVQWHG 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 525 IRQGRLPR-----------------------IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd13989 216 KVKQKKPEhicayedltgevkfsselpspnhLSSILKEYLESWLQLMLRWDPRQR 270
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
297-585 1.55e-12

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: 68.51  E-value: 1.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIK----RSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHM 371
Cdd:cd06643   5 DFWEIvGELGDGAFGKVYKAQNKETGILAAAKvidtKSEEELEDYMVEIDILASC-------DHPNIVKLLDAFYYENNL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddw 451
Cdd:cd06643  78 WILIEFCAGGAVDAVMLELERPL---TEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTL---------DGD---- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isnkvmFKIGDLGhVTRISSPQVEEGDS-----RFLANEVLQ-ENYSHLP---KADIFALALTVVCAAGAEPlPRngdqw 522
Cdd:cd06643 142 ------IKLADFG-VSAKNTRTLQRRDSfigtpYWMAPEVVMcETSKDRPydyKADVWSLGVTLIEMAQIEP-PH----- 208
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 523 HEIRQGRL---------PRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHS-VLLSASRKSAEQLRIELNA 585
Cdd:cd06643 209 HELNPMRVllkiaksepPTLaqPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPfVSVLVSNKPLRELIAEAKA 283
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
296-556 1.56e-12

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: 68.37  E-value: 1.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKP-------LAGSVDEQNALREVyahavlgQHPHVVRYFSAWAED 368
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAkiiklkqVEHVLNEKRILSEV-------RHPFIVNLLGSFQDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIQNEYCNGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDE 448
Cdd:cd05580  74 RNLYMVMEYVPGGELFSLL----RRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL-------------DS 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 DDWIsnkvmfKIGDLGHVTRisspqVEE------GDSRFLANEVLQeNYSHLPKADIFALA-LTVVCAAGAEPLPRNGDQ 521
Cdd:cd05580 137 DGHI------KITDFGFAKR-----VKDrtytlcGTPEYLAPEIIL-SKGHGKAVDWWALGiLIYEMLAGYPPFFDENPM 204
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 522 --WHEIRQGRLpRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05580 205 kiYEKILEGKI-RFPSFFDPDAKDLIKRLLVVDLTKR 240
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
303-569 1.67e-12

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: 67.85  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVfkcvkrldgCIYAIKRSKKPLAgsVDEQNAL----REVYAHAVL----GQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06648  14 KIGEGSTGIV---------CIATDKSTGRQVA--VKKMDLRkqqrRELLFNEVVimrdYQHPNIVEMYSSYLVGDELWVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisn 454
Cdd:cd06648  83 MEFLEGGALTDIVTH-----TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG----------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvMFKIGDLGHVTRISS--PQVEE--GDSRFLANEVL-QENYShlPKADIFALALTVVCAAGAEPlPRNGDQ----WHEI 525
Cdd:cd06648 141 --RVKLSDFGFCAQVSKevPRRKSlvGTPYWMAPEVIsRLPYG--TEVDIWSLGIMVIEMVDGEP-PYFNEPplqaMKRI 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 526 RQGRLPRI--PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLL 569
Cdd:cd06648 216 RDNEPPKLknLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
298-565 1.75e-12

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: 67.96  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLG--QHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREV---DILKhvNHAHIIHLEEVFETPKRMYLVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNavseegdeddwiSNK 455
Cdd:cd14097  80 ELCEDGELKELLLRK----GFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDN------------NDK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLGHVTR---ISSPQVEE--GDSRFLANEVLQ-ENYSHlpKADIFALALTVVCAAGAEPLPRNGDQ---WHEIR 526
Cdd:cd14097 144 LNIKVTDFGLSVQkygLGEDMLQEtcGTPIYMAPEVISaHGYSQ--QCDIWSIGVIMYMLLCGEPPFVAKSEeklFEEIR 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 527 QGRL-------PRIPQVLSQELTELLKVmihpDPERRPSAMVLVKH 565
Cdd:cd14097 222 KGDLtftqsvwQSVSDAAKNVLQQLLKV----DPAHRMTASELLDN 263
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
304-556 1.92e-12

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: 67.94  E-value: 1.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKlDKKRIKKKKGETMALNEKIILEKV-SSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVsenYRV-MSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKIG 461
Cdd:cd05577  80 LKYHI---YNVgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL-------------DDHGHV------RIS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLG---HVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVV-CAAGAEPLPRNGDQW--HEIRQGRLP---R 532
Cdd:cd05577 138 DLGlavEFKGGKKIKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYeMIAGRSPFRQRKEKVdkEELKRRTLEmavE 217
                       250       260
                ....*....|....*....|....
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05577 218 YPDSFSPEARSLCEGLLQKDPERR 241
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
293-437 1.99e-12

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: 68.30  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEfhelEKIGSGEFGSVFKCVKRLDGCIYAIKR---SKKplagsvdEQNalREVYahaVLGQ--HPHVVR---YFSA 364
Cdd:cd14137   5 SYTIE----KVIGSGSFGVVYQAKLLETGEVVAIKKvlqDKR-------YKN--RELQ---IMRRlkHPNIVKlkyFFYS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 365 WAEDDHMLIQN---EYcnggsladaVSEN-YRVMSYFTEAELK-DLLL------QVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14137  69 SGEKKDEVYLNlvmEY---------MPETlYRVIRHYSKNKQTiPIIYvklysyQLFRGLAYLHSLGICHRDIKPQNLLV 139

                ....
gi 17865613 434 SRTS 437
Cdd:cd14137 140 DPET 143
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
304-565 2.33e-12

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: 67.50  E-value: 2.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPlagsVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKMNTLS----SNRANMLREVQLMNRL-SHPNILRFMGVCVHQGQLHALTEYINGGNL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSENyRVMSYFTEAELKdllLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegDEDDWISnkvmfKIGDL 463
Cdd:cd14155  76 EQLLDSN-EPLSWTVRVKLA---LDIARGLSYLHSKGIFHRDLTSKNCLIKR-----------DENGYTA-----VVGDF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 GHVTRIssPQVEEGDSR--------FLANEVLQ-ENYSHlpKADIFALALT---VVCAAGAEP--LPRNGD---QWHEIr 526
Cdd:cd14155 136 GLAEKI--PDYSDGKEKlavvgspyWMAPEVLRgEPYNE--KADVFSYGIIlceIIARIQADPdyLPRTEDfglDYDAF- 210
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 527 QGRLPRIPQVLSQELTELLKVmihpDPERRPSAMVLVKH 565
Cdd:cd14155 211 QHMVGDCPPDFLQLAFNCCNM----DPKSRPSFHDIVKT 245
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
297-556 2.52e-12

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: 68.55  E-value: 2.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVL--GQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05633   6 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIMLSLVstGDCPFIVCMTYAFHTPDKLCF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDEddwis 453
Cdd:cd05633  86 ILDLMNGGDLHYHLSQH----GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---------DEHGHV----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmfKIGDLGHVTRIS--SPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVV-CAAGAEPLPRNGDQ-WHEIRQGR 529
Cdd:cd05633 148 -----RISDLGLACDFSkkKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFkLLRGHSPFRQHKTKdKHEIDRMT 222
                       250       260       270
                ....*....|....*....|....*....|
gi 17865613 530 LP---RIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05633 223 LTvnvELPDSFSPELKSLLEGLLQRDVSKR 252
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
304-564 3.11e-12

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: 67.08  E-value: 3.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRldGCIYAIKrskkpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVK-----IIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADaVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMS---LVHMDIKPSNIFIsrtsipnavseegdeddwISNKVMFKI 460
Cdd:cd14058  74 YN-VLHGKEPKPIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLL------------------TNGGTVLKI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQ-VEEGDSRFLANEVLQ-ENYSHlpKADIFALALTVvcaagAEPLPR----------NGDQWHEIRQG 528
Cdd:cd14058 135 CDFGTACDISTHMtNNKGSAAWMAPEVFEgSKYSE--KCDVFSWGIIL-----WEVITRrkpfdhiggpAFRIMWAVHNG 207
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 529 RLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd14058 208 ERPPLIKNCPKPIESLMTRCWSKDPEKRPSMKEIVK 243
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
301-565 3.50e-12

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: 67.45  E-value: 3.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ--HPHVV----------RYFSAWAED 368
Cdd:cd07846   6 LGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREI---KMLKQlrHENLVnlievfrrkkRWYLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIQN--EYCNGgsladavsenyrvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseeg 446
Cdd:cd07846  83 DHTVLDDleKYPNG----------------LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGV-------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 447 deddwisnkvmFKIGDLGHVTRISSPQVEEGD---SR-FLANEVLQENYSHLPKADIFALALTVVCAAGAEPL-PRNG-- 519
Cdd:cd07846 139 -----------VKLCDFGFARTLAAPGEVYTDyvaTRwYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLfPGDSdi 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 520 DQWHEI--RQGRLP----------------RIPQV------------LSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd07846 208 DQLYHIikCLGNLIprhqelfqknplfagvRLPEVkeveplerrypkLSGVVIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
302-437 3.59e-12

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: 67.49  E-value: 3.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSkkplagsVDEQNALREVYAHAVLGQHPHVVRYFSAWAED----------DHM 371
Cdd:cd14171  12 QKLGTGISGPVRVCVKKSTGERFALKIL-------LDRPKARTEVRLHMMCSGHPNIVQIYDVYANSvqfpgessprARL 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 372 LIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTS 437
Cdd:cd14171  85 LIVMELMEGGELFDRISQH----RHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNS 146
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
293-472 4.40e-12

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: 67.21  E-value: 4.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTefheLEKIGSGEFGSVFKCVKRLDGCIYAIKRSKK-PLAGSVDEQN--ALREVyahAVLG--QHPHVVRYFSAWAE 367
Cdd:cd07841   1 RYEK----GKKLGEGTYAVVYKARDKETGRIVAIKKIKLgERKEAKDGINftALREI---KLLQelKHPNIIGLLDVFGH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIQNEYCNGgslaD--AVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavsee 445
Cdd:cd07841  74 KSNINLVFEFMET----DleKVIKDKSIV--LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA----------- 136
                       170       180
                ....*....|....*....|....*..
gi 17865613 446 gdeddwiSNKVMfKIGDLGHVTRISSP 472
Cdd:cd07841 137 -------SDGVL-KLADFGLARSFGSP 155
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
303-553 5.56e-12

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: 66.91  E-value: 5.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALrEVYAHAVLgQHPHVVRY------FSAWAEDDHMLIQNE 376
Cdd:cd14038   1 RLGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCL-EIQIMKRL-NHPNVVAArdvpegLQKLAPNDLPLLAME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVS--ENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIfisrtsipnaVSEEGDEddwisn 454
Cdd:cd14038  79 YCQGGDLRKYLNqfENCCGLR---EGAILTLLSDISSALRYLHENRIIHRDLKPENI----------VLQQGEQ------ 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 KVMFKIGDLGHVTRISSPQVEE---GDSRFLANEVL-QENYShlPKADIFALA-LTVVCAAGAEPLPRNGD--QWH-EIR 526
Cdd:cd14038 140 RLIHKIIDLGYAKELDQGSLCTsfvGTLQYLAPELLeQQKYT--VTVDYWSFGtLAFECITGFRPFLPNWQpvQWHgKVR 217
                       250       260
                ....*....|....*....|....*...
gi 17865613 527 QGRLPRIpqVLSQELTELLKVMIH-PDP 553
Cdd:cd14038 218 QKSNEDI--VVYEDLTGAVKFSSVlPTP 243
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
304-433 7.23e-12

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: 66.14  E-value: 7.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRlDGCIYAIKRsKKPLAGSVDEQNALREVyahAVLG--QHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14066   1 IGSGGFGTVYKGVLE-NGTVVAVKR-LNEMNCAASKKEFLTEL---EMLGrlRHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 382 SLADAVSENyRVMSYFTEAELKDLLLQVGRGLRYIHSMS---LVHMDIKPSNIFI 433
Cdd:cd14066  76 SLEDRLHCH-KGSPPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILL 129
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
301-558 7.33e-12

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: 66.22  E-value: 7.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRlDGCIYAIKrSKKPlaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05072  12 VKKLGAGQFGEVWMGYYN-NSTKVAVK-TLKP--GTMSVQAFLEEANLMKTL-QHDKLVRLYAVVTKEEPIYIITEYMAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAV--SENYRVMSyfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwisnkVMF 458
Cdd:cd05072  87 GSLLDFLksDEGGKVLL----PKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSES-------------------LMC 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQ--VEEGDS---RFLANEVLqeNY-SHLPKADI--FALALTVVCAAGAEPLP--RNGDQWHEIRQG 528
Cdd:cd05072 144 KIADFGLARVIEDNEytAREGAKfpiKWTAPEAI--NFgSFTIKSDVwsFGILLYEIVTYGKIPYPgmSNSDVMSALQRG 221
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 529 -RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05072 222 yRMPR-MENCPDELYDIMKTCWKEKAEERPT 251
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
304-558 7.34e-12

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: 66.00  E-value: 7.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKplagSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKN----DVDQHKIVREISLLQKL-SHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseEGDEDDWISNKVMFKIGDL 463
Cdd:cd14156  76 EELLAREELPLSW---REKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTP-------RGREAVVTDFGLAREVGEM 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 ghvtRISSPQVE---EGDSRFLANEVLQ-ENYSHlpKADIFALALtVVC------AAGAEPLPRNGDQWHEIR--QGRLP 531
Cdd:cd14156 146 ----PANDPERKlslVGSAFWMAPEMLRgEPYDR--KVDVFSFGI-VLCeilariPADPEVLPRTGDFGLDVQafKEMVP 218
                       250       260
                ....*....|....*....|....*..
gi 17865613 532 RIPqvlsQELTELLKVMIHPDPERRPS 558
Cdd:cd14156 219 GCP----EPFLDLAASCCRMDAFKRPS 241
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
298-565 8.12e-12

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: 66.60  E-value: 8.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06633  23 FVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQL-KHPNTIEYKGCYLKDHTAWLVME 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGgSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVseegdeddwisnkv 456
Cdd:cd06633 102 YCLG-SASDLLEVHKKPLQ---EVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE---PGQV-------------- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLGHVTRISSPQVEEGDSRFLANEVL--QENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIP 534
Cdd:cd06633 161 --KLADFGSASIASPANSFVGTPYWMAPEVIlaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSP 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 535 QVLSQELTELLKVMI----HPDPERRPSAMVLVKH 565
Cdd:cd06633 239 TLQSNEWTDSFRGFVdyclQKIPQERPSSAELLRH 273
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
293-438 8.77e-12

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: 66.62  E-value: 8.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKK-------PLAGsvdeqnaLREVYAHAVLgQHPHVVRYFSAW 365
Cdd:cd07845   4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMdnerdgiPISS-------LREITLLLNL-RHPNIVELKEVV 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 366 AED--DHMLIQNEYCNggslADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSI 438
Cdd:cd07845  76 VGKhlDSIFLVMEYCE----QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC 146
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
304-563 9.45e-12

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: 65.88  E-value: 9.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRldGCIYAIKRSKKPLAG--SVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14061   2 IGVGGFGKVYRGIWR--GEEVAVKAARQDPDEdiSVTLENVRQEARLFWML-RHPNIIALRGVCLQPPNLCLVMEYARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSeNYRVmsyfTEAELKDLLLQVGRGLRYIHS---MSLVHMDIKPSNIFISrtsipnavseEGDEDDWISNKVMf 458
Cdd:cd14061  79 ALNRVLA-GRKI----PPHVLVDWAIQIARGMNYLHNeapVPIIHRDLKSSNILIL----------EAIENEDLENKTL- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLG------HVTRISSPqveeGDSRFLANEVLQEN-YS------------------HLPKADIFALALTVVCAAGAE 513
Cdd:cd14061 143 KITDFGlarewhKTTRMSAA----GTYAWMAPEVIKSStFSkasdvwsygvllwelltgEVPYKGIDGLAVAYGVAVNKL 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 514 PLPrngdqwheirqgrlprIPQVLSQELTELLKVMIHPDPERRPS-AMVLV 563
Cdd:cd14061 219 TLP----------------IPSTCPEPFAQLMKDCWQPDPHDRPSfADILK 253
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
304-556 9.47e-12

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: 66.61  E-value: 9.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVL--GQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIMLSLVstGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKI 460
Cdd:cd14223  88 GDLHYHLSQH----GVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL-------------DEFGHV------RI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRIS--SPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVV-CAAGAEPLPRNGDQ-WHEIRQGRLP---RI 533
Cdd:cd14223 145 SDLGLACDFSkkKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFkLLRGHSPFRQHKTKdKHEIDRMTLTmavEL 224
                       250       260
                ....*....|....*....|...
gi 17865613 534 PQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14223 225 PDSFSPELRSLLEGLLQRDVNRR 247
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
298-435 1.03e-11

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: 66.05  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRskkplagsVDEQN--------ALREVyahAVLGQ--HPHVVRYFSAWAE 367
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKK--------IRMENekegfpitAIREI---KLLQKldHPNVVRLKEIVTS 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 368 DDHMLIQN------EYC----NGgsLADavsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd07840  70 KGSAKYKGsiymvfEYMdhdlTG--LLD------NPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINN 139
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
301-566 1.08e-11

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: 65.56  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGsVFKCVK-RLDGCIYAIK---RSKKplagsVDEqNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14662   5 VKDIGSGNFG-VARLMRnKETKELVAVKyieRGLK-----IDE-NVQREIINHRSL-RHPNIIRFKEVVLTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNavseegdeddwisnkv 456
Cdd:cd14662  77 YAAGGELFERICNAGR----FSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPR---------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mFKIGDLGHVTRI---SSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTV-VCAAGAEPL-----PRNgdqwheIRQ 527
Cdd:cd14662 137 -LKICDFGYSKSSvlhSQPKSTVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLyVMLVGAYPFedpddPKN------FRK 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17865613 528 gRLPRIPQV---------LSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14662 210 -TIQRIMSVqykipdyvrVSQDCRHLLSRIFVANPAKRITIPEIKNHP 256
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
324-566 1.16e-11

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 65.46  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 324 YAIKRSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFS----------AWaeddHMLIQNEYCNGGSLADAVSenyRV 393
Cdd:cd14012  33 FKTSNGKKQIQLLEKELESLKKL-------RHPNLVSYLAfsierrgrsdGW----KVYLLTEYAPGGSLSELLD---SV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 394 MSYFTEAeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeddwisnkvmfKIGDLGHVTRISS-- 471
Cdd:cd14012  99 GSVPLDT-ARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIV----------------KLTDYSLGKTLLDmc 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 472 ---PQVEEGDSRFLANEVLQENYSHLPKADIFALALtVVCAAGaeplprNG-DQWHEIRQGRLPRIPQVLSQELTELLKV 547
Cdd:cd14012 162 srgSLDEFKQTYWLPPELAQGSKSPTRKTDVWDLGL-LFLQML------FGlDVLEKYTSPNPVLVSLDLSASLQDFLSK 234
                       250
                ....*....|....*....
gi 17865613 548 MIHPDPERRPSAMVLVKHS 566
Cdd:cd14012 235 CLSLDPKKRPTALELLPHE 253
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
304-556 1.28e-11

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: 65.54  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALRE---VYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNErimLSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfK 459
Cdd:cd05606  82 GGDLHYHLSQH----GVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL-------------DEHGHV------R 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISS--PQVEEGDSRFLANEVLQENYSHLPKADIFALALTVV-CAAGAEPL-PRNGDQWHEIRQGRL---PR 532
Cdd:cd05606 139 ISDLGLACDFSKkkPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYkLLKGHSPFrQHKTKDKHEIDRMTLtmnVE 218
                       250       260
                ....*....|....*....|....
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05606 219 LPDSFSPELKSLLEGLLQRDVSKR 242
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
294-565 1.97e-11

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: 64.72  E-value: 1.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 294 YTTefheLEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKP--LAGSVDEQNALREVYAH-AVLGQ-----HPHVVRYFSAW 365
Cdd:cd14004   2 YTI----LKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKEriLVDTWVRDRKLGTVPLEiHILDTlnkrsHPNIVKLLDFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQNE-YCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavse 444
Cdd:cd14004  78 EDDEFYYLVMEkHGSGMDLFDFIERKPNM----DEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVIL----------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 445 egDEDDWIsnkvmfKIGDLGHVTRISSPQ--VEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGDqw 522
Cdd:cd14004 143 --DGNGTI------KLIDFGSAAYIKSGPfdTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYNIE-- 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 523 hEIRQGRLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14004 213 -EILEADL-RIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTD 253
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
292-515 2.26e-11

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: 64.60  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 292 SRYTTEFHELekIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSVDEQNALREVyahAVLGQHPHV--VRYFSAWAEDD 369
Cdd:cd14192   2 SYYAVCPHEV--LGGGRFGQVHKCTELSTGLTLAAKIIK--VKGAKEREEVKNEI---NIMNQLNHVnlIQLYDAFESKT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAVS-ENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnAVSEEGDE 448
Cdd:cd14192  75 NLTLIMEYVDGGELFDRITdESYQL----TELDAILFTRQICEGVHYLHQHYILHLDLKPENIL--------CVNSTGNQ 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 449 ddwisnkvmFKIGDLGhVTRISSP----QVEEGDSRFLANEVLQENYSHLPkADIFALA-LTVVCAAGAEPL 515
Cdd:cd14192 143 ---------IKIIDFG-LARRYKPreklKVNFGTPEFLAPEVVNYDFVSFP-TDMWSVGvITYMLLSGLSPF 203
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
296-565 3.11e-11

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 64.24  E-value: 3.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEK--IGSGEFGSVFKCVKRLDGciyaikrSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDH--- 370
Cdd:cd14172   2 TDDYKLSKqvLGLGVNGKVLECFHRRTG-------QKCALKLLYDSPKARREVEHHWRASGGPHIVHILDVYENMHHgkr 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 -MLIQNEYCNGGSLADAVSEnyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavSEEGDed 449
Cdd:cd14172  75 cLLIIMECMEGGELFSRIQE--RGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYT--------SKEKD-- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 dwisnkVMFKIGDLG---HVTRISSPQVEEGDSRFLANEVL-QENYSHlpKADIFALA-LTVVCAAGAEPLPRNGDQW-- 522
Cdd:cd14172 143 ------AVLKLTDFGfakETTVQNALQTPCYTPYYVAPEVLgPEKYDK--SCDMWSLGvIMYILLCGFPPFYSNTGQAis 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 523 ----HEIRQGRL----PRIPQVlSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14172 215 pgmkRRIRMGQYgfpnPEWAEV-SEEAKQLIRHLLKTDPTERMTITQFMNH 264
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
299-433 3.56e-11

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: 64.85  E-value: 3.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEK-IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFsawaeddHMLIQNEY 377
Cdd:cd07834   2 YELLKpIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHL-KHENIIGLL-------DILRPPSP 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLadavsenYRVMSYF--------------TEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07834  74 EEFNDV-------YIVTELMetdlhkvikspqplTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILV 136
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
297-435 3.84e-11

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: 64.16  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREvyaHAVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd05581   2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVlDKRHIIKEKKVKYVTIE---KEVLSRlaHPGIVKLYYTFQDESKLYF 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 374 QNEYCNGGSLADAV----SENYRVMSYFTeAELKDlllqvgrGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05581  79 VLEYAPNGDLLEYIrkygSLDEKCTRFYT-AEIVL-------ALEYLHSKGIIHRDLKPENILLDE 136
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
302-565 4.05e-11

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: 63.94  E-value: 4.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIK--------------RSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAE 367
Cdd:cd06629   7 ELIGKGTYGRVYLAMNATTGEMLAVKqvelpktssdradsRQKTVVDALKSEIDTLKDL-------DHPNIVQYLGFEET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIQNEYCNGGSladaVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnaVSEEGd 447
Cdd:cd06629  80 EDYFSIFLEYVPGGS----IGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNIL---------VDLEG- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwisnkvMFKIGDLG------HVTRISSPQVEEGDSRFLANEVLQEN---YShlPKADIFALALTVV-CAAGAEPLPR 517
Cdd:cd06629 146 ---------ICKISDFGiskksdDIYGNNGATSMQGSVFWMAPEVIHSQgqgYS--AKVDIWSLGCVVLeMLAGRRPWSD 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17865613 518 NgDQWHEI----RQGRLPRIPQ--VLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd06629 215 D-EAIAAMfklgNKRSAPPVPEdvNLSPEALDFLNACFAIDPRDRPTAAELLSH 267
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
304-565 4.32e-11

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: 63.89  E-value: 4.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRskkpLAGSVDEQNALREVYAHAVLGQ------HPHVVRYFSAW--AEDDHMLIQN 375
Cdd:cd06653  10 LGRGAFGEVYLCYDADTGRELAVKQ----VPFDPDSQETSKEVNALECEIQllknlrHDRIVQYYGCLrdPEEKKLSIFV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisRTSIPNAvseegdeddwisnk 455
Cdd:cd06653  86 EYMPGGSVKDQL----KAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL--RDSAGNV-------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGHVTRISSPQVE-------EGDSRFLANEVLQ-ENYSHlpKADIFALALTVVCAAGAEPlprngdQWHEIR- 526
Cdd:cd06653 146 ---KLGDFGASKRIQTICMSgtgiksvTGTPYWMSPEVISgEGYGR--KADVWSVACTVVEMLTEKP------PWAEYEa 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17865613 527 ---------QGRLPRIPQVLSQELTELLKvMIHPDPERRPSAMVLVKH 565
Cdd:cd06653 215 maaifkiatQPTKPQLPDGVSDACRDFLR-QIFVEEKRRPTAEFLLRH 261
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
296-438 4.73e-11

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: 64.26  E-value: 4.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR----SKK---PLAgsvdeqnALREVYAHAVLgQHPHVVRyfsawaed 368
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKilmhNEKdgfPIT-------ALREIKILKKL-KHPNVVP-------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 dhmLIQNEYCNGGSLADAVSENYRVMSY---------------FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07866  72 ---LIDMAVERPDKSKRKRGSVYMVTPYmdhdlsgllenpsvkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILI 148

                ....*
gi 17865613 434 SRTSI 438
Cdd:cd07866 149 DNQGI 153
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
399-565 5.27e-11

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: 63.88  E-value: 5.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 399 EAELKDLLLQVGRGLRYIH-SMSLVHMDIKPSNIFISRtsipnavseegdEDDWisnkvmfKIGDLGHVTRISSPQVEEG 477
Cdd:cd14011 113 DVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINS------------NGEW-------KLAGFDFCISSEQATDQFP 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 478 DSR---------------FLANEVLQENySHLPKADIFALALTV--VCAAGAePLPRNGDQWHEIRQ----------GRL 530
Cdd:cd14011 174 YFReydpnlpplaqpnlnYLAPEYILSK-TCDPASDMFSLGVLIyaIYNKGK-PLFDCVNNLLSYKKnsnqlrqlslSLL 251
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17865613 531 PRIPQvlsqELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14011 252 EKVPE----ELRDHVKTLLNVTPEVRPDAEQLSKI 282
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
298-599 5.57e-11

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: 64.30  E-value: 5.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06635  27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRI-KHPNSIEYKGCYLREHTAWLVME 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGgSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVseegdeddwisnkv 456
Cdd:cd06635 106 YCLG-SASDLLEVHKKPLQ---EIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE---PGQV-------------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLGHVTRISSPQVEEGDSRFLANEVL--QENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIP 534
Cdd:cd06635 165 --KLADFGSASIASPANSFVGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESP 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 535 QVLSQELTELLKVMI----HPDPERRPSAMVLVKHSVLLsasRKSAEQLRIEL-----NAEKFKNSLLQKELKK 599
Cdd:cd06635 243 TLQSNEWSDYFRNFVdsclQKIPQDRPTSEELLKHMFVL---RERPETVLIDLiqrtkDAVRELDNLQYRKMKK 313
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
297-434 5.92e-11

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: 63.14  E-value: 5.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRldGCIYAIKRSKkplagsvDEQNALREVYAHAVLG---QHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05039   7 DLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLK-------DDSTAAQAFLAEASVMttlRHPNLVQLLGVVLEGNGLYI 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 374 QNEYCNGGSLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd05039  78 VTEYMAKGSLVDYLRSRGR--AVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVS 136
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
303-572 8.45e-11

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: 63.47  E-value: 8.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVfkcvkrldgCIYAIKRSKKPLAGSVDE--QNALREVYAHAVL----GQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06659  28 KIGEGSTGVV---------CIAREKHSGRQVAVKMMDlrKQQRRELLFNEVVimrdYQHPNVVEMYKSYLVGEELWVLME 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwISNKV 456
Cdd:cd06659  99 YLQGGALTDIVSQ-----TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLT-----------------LDGRV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLGHVTRISS--PQVEE--GDSRFLANEVLQENySHLPKADIFALALTVVCAAGAEPlPRNGDQ----WHEIRQG 528
Cdd:cd06659 157 --KLSDFGFCAQISKdvPKRKSlvGTPYWMAPEVISRC-PYGTEVDIWSLGIMVIEMVDGEP-PYFSDSpvqaMKRLRDS 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 529 RLPRIPQV--LSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSAS 572
Cdd:cd06659 233 PPPKLKNShkASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTG 278
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
300-558 1.03e-10

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: 62.82  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 300 ELEKI---GSGEFGSVFKCVKRLDG-------CIYAIKRSKKPLAgsvdEQNALREVYAHAVLGqHPHVVRYFSAWAEDD 369
Cdd:cd05057   8 ELEKGkvlGSGAFGTVYKGVWIPEGekvkipvAIKVLREETGPKA----NEEILDEAYVMASVD-HPHLVRLLGICLSSQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIqNEYCNGGSLADAVSENyrvmsyftEAELKDLLL-----QVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVse 444
Cdd:cd05057  83 VQLI-TQLMPLGCLLDYVRNH--------RDNIGSQLLlnwcvQIAKGMSYLEEKRLVHRDLAARNVLVKT---PNHV-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 445 egdeddwisnkvmfKIGDLGhVTRISSP-----QVEEGDS--RFLANEVLQEN-YSHlpKADIFALALTV--VCAAGAEP 514
Cdd:cd05057 149 --------------KITDFG-LAKLLDVdekeyHAEGGKVpiKWMALESIQYRiYTH--KSDVWSYGVTVweLMTFGAKP 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 515 ---LPRNGDQWHEIRQGRLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05057 212 yegIPAVEIPDLLEKGERLPQ-PPICTIDVYMVLVKCWMIDAESRPT 257
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
294-558 1.05e-10

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: 62.55  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 294 YTTEFHELEKIGSGEFGSVFKCV--KRLDGCIYAIKrskkPLAGSVDEQNALREvYAHAVLGQHPHVVRYFSAWAEDDHM 371
Cdd:cd14112   1 PTGRFSFGSEIFRGRFSVIVKAVdsTTETDAHCAVK----IFEVSDEASEAVRE-FESLRTLQHENVQRLIAAFKPSNFA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEycnggSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI-FISRTSIPNAVSEEGDEDd 450
Cdd:cd14112  76 YLVME-----KLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNImFQSVRSWQVKLVDFGRAQ- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnkvmfKIGDLGHVTrisspqvEEGDSRFLANEVLQENYSHLPKADIFAL-ALTVVCAAGAEPLPRNGDQWHEIRQG- 528
Cdd:cd14112 150 --------KVSKLGKVP-------VDGDTDWASPEFHNPETPITVQSDIWGLgVLTFCLLSGFHPFTSEYDDEEETKENv 214
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 529 -----RLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14112 215 ifvkcRPNLIFVEATQEALRFATWALKKSPTRRMR 249
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
290-433 1.15e-10

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: 62.28  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 290 MKSRYttEFheLEKIGSGEFGSVFKCVKRlDGCIYAIKRSKKPLAGsvDEQNAL---REVYAHAVLgQHPHVVRYFSAWA 366
Cdd:cd14161   1 LKHRY--EF--LETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIK--DEQDLLhirREIEIMSSL-NHPHIISVYEVFE 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 367 EDDHMLIQNEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14161  73 NSSKIVIVMEYASRGDLYDYISERQRL----SELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL 135
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
297-515 1.20e-10

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: 62.67  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGS----VDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDD 369
Cdd:cd14196   5 DFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREV---SILRQvlHPNIITLHDVYENRT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAvseegded 449
Cdd:cd14196  82 DVVLILELVSGGELFDFLAQK----ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIP-------- 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 450 dwisnkvMFKIGDLGHVTRISSpQVE----EGDSRFLANEVLqeNYSHLP-KADIFALA-LTVVCAAGAEPL 515
Cdd:cd14196 150 -------HIKLIDFGLAHEIED-GVEfkniFGTPEFVAPEIV--NYEPLGlEADMWSIGvITYILLSGASPF 211
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
304-563 1.42e-10

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: 62.63  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCvkRLDGCIYAIKRSKK------------------PLAGSVDEQNALREVYAHAVLGQHPHVVrYFSAW 365
Cdd:cd14000   2 LGDGGFGSVYRA--SYKGEPVAVKIFNKhtssnfanvpadtmlrhlRATDAMKNFRLLRQELTVLSHLHHPSIV-YLLGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQnEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAvsee 445
Cdd:cd14000  79 GIHPLMLVL-ELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSA---- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 446 gdeddwisnkVMFKIGDLGhVTRISSPQ---VEEGDSRFLANEVLQENYSHLPKADIFALALTV--VCAAGAeplPRNGD 520
Cdd:cd14000 154 ----------IIIKIADYG-ISRQCCRMgakGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLyeILSGGA---PMVGH 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 521 QWHEIRQGRLPRIPQVLSQ-------ELTELLKVMIHPDPERRPSAMVLV 563
Cdd:cd14000 220 LKFPNEFDIHGGLRPPLKQyecapwpEVEVLMKKCWKENPQQRPTAVTVV 269
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
291-492 1.79e-10

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: 62.00  E-value: 1.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 291 KSRYttEFHELekIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVD----EQNALREVyahavlgQHPHVVRYFSAW 365
Cdd:cd14083   2 RDKY--EFKEV--LGTGAFSEVVLAEDKATGKLVAIKcIDKKALKGKEDslenEIAVLRKI-------KHPNIVQLLDIY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavsee 445
Cdd:cd14083  71 ESKSHLYLVMELVTGGELFDRIVEK----GSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSP--------- 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17865613 446 gDEDdwisNKVMfkIGDLGhvtrISSPQVEE------GDSRFLANEVL-QENYS 492
Cdd:cd14083 138 -DED----SKIM--ISDFG----LSKMEDSGvmstacGTPGYVAPEVLaQKPYG 180
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
303-566 1.86e-10

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: 61.94  E-value: 1.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVK-----RLDGCIYAIKRSKKplagsVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDH----MLI 373
Cdd:cd14033   8 EIGRGSFKTVYRGLDtettvEVAWCELQTRKLSK-----GERQRFSEEVEMLKGL-QHPNIVRFYDSWKSTVRghkcIIL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAvsenyrvMSYFTEAELKDLL---LQVGRGLRYIHSMS--LVHMDIKPSNIFISRtsiPNAvseegde 448
Cdd:cd14033  82 VTELMTSGTLKTY-------LKRFREMKLKLLQrwsRQILKGLHFLHSRCppILHRDLKCDNIFITG---PTG------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 ddwisnkvMFKIGDLGHVT--RISSPQVEEGDSRFLANEVLQENYSHlpKADIFALALTVVCAAGAE-PLP--RNGDQ-W 522
Cdd:cd14033 145 --------SVKIGDLGLATlkRASFAKSVIGTPEFMAPEMYEEKYDE--AVDVYAFGMCILEMATSEyPYSecQNAAQiY 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17865613 523 HEIRQGRLP-RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14033 215 RKVTSGIKPdSFYKVKVPELKEIIEGCIRTDKDERFTIQDLLEHR 259
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
299-431 2.03e-10

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: 62.32  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKplagsvdeQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14092   9 LREEALGDGSFSVCRKCVHKKTGQEFAVKiVSRR--------LDTSREVQLLRLCQGHPNIVKLHEVFQDELHTYLVMEL 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17865613 378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14092  81 LRGGELLERIRKKKR----FTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENL 130
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
301-438 2.04e-10

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: 62.39  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIkrsKKPLAGSVDEQ---NALREVYAHAVLgQHPHVVRyfsawaeddhmLIqnEY 377
Cdd:cd07865  17 LAKIGQGTFGEVFKARHRKTGQIVAL---KKVLMENEKEGfpiTALREIKILQLL-KHENVVN-----------LI--EI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNggSLADAVSEN----YRVMSY---------------FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSI 438
Cdd:cd07865  80 CR--TKATPYNRYkgsiYLVFEFcehdlagllsnknvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGV 157
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
302-568 2.11e-10

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: 61.68  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFkCVKRLDGCIYAIKR----SKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd06631   7 NVLGKGAYGTVY-CGLTSTGQLIAVKQveldTSDKEKAEKEYEKLQEEVDLLKTL-KHVNIVGYLGTCLEDNVVSIFMEF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsIPNAVseegdeddwisnkvm 457
Cdd:cd06631  85 VPGGSIASILAR----FGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIML----MPNGV--------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEEGDSRFL----------ANEVLQENySHLPKADIFALALTVVCAAGAEPLPRNGDQWHEI-- 525
Cdd:cd06631 142 IKLIDFGCAKRLCINLSSGSQSQLLksmrgtpywmAPEVINET-GHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIfa 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 526 ---RQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06631 221 igsGRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
304-568 2.45e-10

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: 61.73  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSV-----FKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL-REVYAHAVLGqHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14076   9 LGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENCQTSKImREINILKGLT-HPNIVRLLDVLKTKKYIGIVLEF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipNAVseegdeddwisnkvm 457
Cdd:cd14076  88 VSGGELFDYILAR----RRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNR--NLV--------------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 fkIGDLGHVTRISSPQVEE-----GDSRFLANE-VLQENYSHLPKADIFALALtVVCAAGAEPLPRNGDQwHEIRQGRLP 531
Cdd:cd14076 147 --ITDFGFANTFDHFNGDLmstscGSPCYAAPElVVSDSMYAGRKADIWSCGV-ILYAMLAGYLPFDDDP-HNPNGDNVP 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17865613 532 RI-----------PQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14076 223 RLyryicntplifPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
303-558 2.53e-10

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: 61.20  E-value: 2.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDE--QNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd14075   9 ELGSGNFSQVKLGIHQLTKEKVAIKILDK---TKLDQktQRLLsREISSMEKL-HHPNIIRLYEVVETLSKLHLVMEYAS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKvMFK 459
Cdd:cd14075  85 GGELYTKISTEGK----LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYA------------------SNN-CVK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISSPQVEE---GDSRFLANEVLQENYSHLPKADIFAL------ALTVVCAAGAEPLPRNGDQwheIRQGRL 530
Cdd:cd14075 142 VGDFGFSTHAKRGETLNtfcGSPPYAAPELFKDEHYIGIYVDIWALgvllyfMVTGVMPFRAETVAKLKKC---ILEGTY 218
                       250       260
                ....*....|....*....|....*...
gi 17865613 531 pRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14075 219 -TIPSYVSEPCQELIRGILQPVPSDRYS 245
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
298-436 2.92e-10

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: 61.86  E-value: 2.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKP---LAGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSemlEKEQVAHVRAERDILAEA---DNPWVVKLYYSFQDEENLYLI 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 375 NEYCNGGSLadavsenyrvMS------YFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05599  80 MEFLPGGDM----------MTllmkkdTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR 137
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
304-563 3.01e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 62.96  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  304 IGSGEFGSVFkCVKRL-DGCIYAIKRSKKPLAGSVDEQNALREVYA------HAVLGQHPHVVRYFSAWAEDDHML-IQN 375
Cdd:PTZ00283  40 LGSGATGTVL-CAKRVsDGEPFAVKVVDMEGMSEADKNRAQAEVCCllncdfFSIVKCHEDFAKKDPRNPENVLMIaLVL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  376 EYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNK 455
Cdd:PTZ00283 119 DYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLC------------------SNG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  456 VMfKIGDLGhVTRISSPQVEE-------GDSRFLANEVLQEN-YSHlpKADIFALALTVVcaagaEPL----PRNGDQWH 523
Cdd:PTZ00283 181 LV-KLGDFG-FSKMYAATVSDdvgrtfcGTPYYVAPEIWRRKpYSK--KADMFSLGVLLY-----ELLtlkrPFDGENME 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 17865613  524 EIRQ----GRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLV 563
Cdd:PTZ00283 252 EVMHktlaGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
355-568 3.05e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 62.73  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  355 HPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:PTZ00267 124 HFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  435 RTSIpnavseegdeddwisnkvmFKIGDLGHVTRIS-SPQVEEGDS-----RFLANEVLQ-ENYSHlpKADIFALALTVV 507
Cdd:PTZ00267 204 PTGI-------------------IKLGDFGFSKQYSdSVSLDVASSfcgtpYYLAPELWErKRYSK--KADMWSLGVILY 262
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613  508 caagaEPL----PRNGDQWHEIRQ----GRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:PTZ00267 263 -----ELLtlhrPFKGPSQREIMQqvlyGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
298-569 3.45e-10

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: 61.58  E-value: 3.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06634  17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKL-RHPNTIEYRGCYLREHTAWLVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGgSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGdeddwisnkv 456
Cdd:cd06634  96 YCLG-SASDLLEVHKKPLQ---EVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILL---------TEPG---------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPQVEEGDSRFLANEVL--QENYSHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIP 534
Cdd:cd06634 153 LVKLGDFGSASIMAPANSFVGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESP 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 535 QVLSQELTELLKVMI----HPDPERRPSAMVLVKHSVLL 569
Cdd:cd06634 233 ALQSGHWSEYFRNFVdsclQKIPQDRPTSDVLLKHRFLL 271
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
304-558 3.51e-10

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: 61.16  E-value: 3.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14148   2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWML-QHPNIIALRGVCLNPPHLCLVMEYARGGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVSeNYRVMSYFteaeLKDLLLQVGRGLRYIHSMSLV---HMDIKPSNIFISrtsipnavseEGDEDDWISNKVMfKI 460
Cdd:cd14148  81 NRALA-GKKVPPHV----LVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILIL----------EPIENDDLSGKTL-KI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLG------HVTRISSPqveeGDSRFLANEVLQENY-------------------SHLPKADIFALALTVVCAAGAEPL 515
Cdd:cd14148 145 TDFGlarewhKTTKMSAA----GTYAWMAPEVIRLSLfskssdvwsfgvllwelltGEVPYREIDALAVAYGVAMNKLTL 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 516 PrngdqwheirqgrlprIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14148 221 P----------------IPSTCPEPFARLLEECWDPDPHGRPD 247
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
297-492 3.67e-10

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: 61.20  E-value: 3.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELekIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSvdEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd14167   6 DFREV--LGTGAFSEVVLAEEKRTQKLVAIKcIAKKALEGK--ETSIENEI---AVLHKikHPNIVALDDIYESGGHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnaVSEEGDEDDWIS 453
Cdd:cd14167  79 IMQLVSGGELFDRIVEK----GFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLY--------YSLDEDSKIMIS 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17865613 454 NKVMFKIGDLGHVTRISSpqveeGDSRFLANEVL-QENYS 492
Cdd:cd14167 147 DFGLSKIEGSGSVMSTAC-----GTPGYVAPEVLaQKPYS 181
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
304-556 3.83e-10

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 61.59  E-value: 3.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLagsvdEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRM-----EANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKGGEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 AdavsENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegDEDDwisnKVMFKIGDL 463
Cdd:cd14179  90 L----ERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFT------------DESD----NSEIKIIDF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 GhVTRISSPQVEEGDS-----RFLANEVLQENySHLPKADIFALALTV-VCAAGAEPLPRNG---------DQWHEIRQG 528
Cdd:cd14179 150 G-FARLKPPDNQPLKTpcftlHYAAPELLNYN-GYDESCDLWSLGVILyTMLSGQVPFQCHDksltctsaeEIMKKIKQG 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 529 RLPRIPQV---LSQELTELLKVMIHPDPERR 556
Cdd:cd14179 228 DFSFEGEAwknVSQEAKDLIQGLLTVDPNKR 258
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
301-437 4.25e-10

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: 60.73  E-value: 4.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsVDEQNALR-EVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCn 379
Cdd:cd14017   5 VKKIGGGGFGEIYKVRDVVDGEEVAMKVESK-----SQPKQVLKmEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLL- 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 380 GGSLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTS 437
Cdd:cd14017  79 GPNLAELRRSQPRGK--FSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGP 134
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
301-433 4.27e-10

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: 61.52  E-value: 4.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQN---ALREVYAHAVlgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKhimAERNVLLKNV--KHPFLVGLHYSFQTTDKLYFVLDF 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 378 CNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05604  79 VNGGELFFHLQRE----RSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILL 130
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
301-564 5.01e-10

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: 60.61  E-value: 5.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14072   5 LKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKIL-NHPNIVKLFEVIETEKTLYLVMEYASG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKI 460
Cdd:cd14072  84 GEVFDYLVAHGRM----KEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL-------------DADMNI------KI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQVEE---GDSRFLANEVLQENYSHLPKADIFALAL---TVVCAAgaepLPRNGDQWHEIRQGRLP--- 531
Cdd:cd14072 141 ADFGFSNEFTPGNKLDtfcGSPPYAAPELFQGKKYDGPEVDVWSLGVilyTLVSGS----LPFDGQNLKELRERVLRgky 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 532 RIPQVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd14072 217 RIPFYMSTDCENLLKKFLVLNPSKRGTLEQIMK 249
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
298-556 5.24e-10

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: 60.78  E-value: 5.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFkCVKRLDGC----IYAIKRSKKPL----AGSVDEQNALREVYAHavLGQHPHVVRYFSAWAEDD 369
Cdd:cd05613   2 FELLKVLGTGAYGKVF-LVRKVSGHdagkLYAMKVLKKATivqkAKTAEHTRTERQVLEH--IRQSPFLVTLHYAFQTDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrTSIPNAVSEEGDED 449
Cdd:cd05613  79 KLHLILDYINGGELFTHLSQRER----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLD-SSGHVVLTDFGLSK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 DWISNKVMFKIGDLGHVTRISSPQVEEGDSrflanevlqenySHLPKADIFALA-LTVVCAAGAEPLPRNGDQWHEIRQG 528
Cdd:cd05613 154 EFLLDENERAYSFCGTIEYMAPEIVRGGDS------------GHDKAVDWWSLGvLMYELLTGASPFTVDGEKNSQAEIS 221
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 529 RL-----PRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05613 222 RRilksePPYPQEMSALAKDIIQRLLMKDPKKR 254
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
304-558 6.53e-10

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: 60.60  E-value: 6.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsVDEQ---NALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIR-----FDEEaqrNFLKEVKVMRSL-DHPNVLKFIGVLYKDKKLNLITEYIPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRVMSYFTEAEL-KDlllqVGRGLRYIHSMSLVHMDIKPSNIFIsRTSIPNAVSEEG----DEDDWISNK 455
Cdd:cd14154  75 GTLKDVLKDMARPLPWAQRVRFaKD----IASGMAYLHSMNIIHRDLNSHNCLV-REDKTVVVADFGlarlIVEERLPSG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLGHvtrISSPQVEE-----GDSRFLANEVLQ-ENYSHlpKADIFALALtVVCA----AGAEP--LPRNGD--- 520
Cdd:cd14154 150 NMSPSETLRH---LKSPDRKKrytvvGNPYWMAPEMLNgRSYDE--KVDIFSFGI-VLCEiigrVEADPdyLPRTKDfgl 223
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 521 QWHEIRQGRLPRIPQVlsqeLTELLKVMIHPDPERRPS 558
Cdd:cd14154 224 NVDSFREKFCAGCPPP----FFKLAFLCCDLDPEKRPP 257
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
304-556 8.49e-10

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: 60.79  E-value: 8.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEqnalrevYAHAVL-------GQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDE-------VAHTVTesrvlqnTRHPFLTALKYAFQTHDRLCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENyRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkv 456
Cdd:cd05595  76 YANGGELFFHLSRE-RV---FTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML-------------DKDGHI---- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLG----HVTRISSPQVEEGDSRFLANEVLQENySHLPKADIFALALTVvcaagaeplprngdqwHEIRQGRLP- 531
Cdd:cd05595 135 --KITDFGlckeGITDGATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVM----------------YEMMCGRLPf 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 532 -----------------RIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05595 196 ynqdherlfelilmeeiRFPRTLSPEAKSLLAGLLKKDPKQR 237
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
304-558 9.21e-10

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: 60.36  E-value: 9.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVK-RLDG----CIYAIKRSKKPLAGS-----VDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05045   8 LGEGEFGKVVKATAfRLKGragyTTVAVKMLKENASSSelrdlLSEFNLLKQV-------NHPHVIKLYGACSQDGPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSENYRV-------------MSYFTEAE----LKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05045  81 IVEYAKYGSLRSFLRESRKVgpsylgsdgnrnsSYLDNPDEraltMGDLIsfaWQISRGMQYLAEMKLVHRDLAARNVLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 434 SrtsipnavseEGdeddwisnKVMfKIGDLGhVTRisspQVEEGDS-----------RFLANEVLQEnYSHLPKADI--F 500
Cdd:cd05045 161 A----------EG--------RKM-KISDFG-LSR----DVYEEDSyvkrskgripvKWMAIESLFD-HIYTTQSDVwsF 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 501 ALALTVVCAAGAEPLPRNGDQ--WHEIRQG-RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05045 216 GVLLWEIVTLGGNPYPGIAPErlFNLLKTGyRMER-PENCSEEMYNLMLTCWKQEPDKRPT 275
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
302-431 1.02e-09

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: 59.67  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIY---AIKrSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQnEYC 378
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKSGKEvevAVK-TLKQEHEKAGKKEFLREASVMAQL-DHPCIVRLIGVCKGEPLMLVM-ELA 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 379 NGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd05060  78 PLGPLLKYLKKR----REIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNV 126
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
296-434 1.18e-09

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: 60.14  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQ-IIREL---KVLHEcnSPYIVGFYGAFYSDGEISI 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 374 QNEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHS-MSLVHMDIKPSNIFIS 434
Cdd:cd06615  77 CMEHMDGGSLDQVLKKAGRI----PENILGKISIAVLRGLTYLREkHKIMHRDVKPSNILVN 134
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
354-568 1.29e-09

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: 59.25  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSA--WAEDDHMLIqnEYCNGGSladaVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd13995  54 RHENIAELYGAllWEETVHLFM--EAGEGGS----VLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNI 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 432 FISRTS---IPNAVSEEGDEDdwisnkvmfkigdlghvtrISSPQVEEGDSRFLANEVLQENySHLPKADIFALALTVVC 508
Cdd:cd13995 128 VFMSTKavlVDFGLSVQMTED-------------------VYVPKDLRGTEIYMSPEVILCR-GHNTKADIYSLGATIIH 187
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 509 AAGAEP-----LPRNG-DQWHEIRQGRLP---RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd13995 188 MQTGSPpwvrrYPRSAyPSYLYIIHKQAPpleDIAQDCSPAMRELLEAALERNPNHRSSAAELLKHEAL 256
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
304-557 1.29e-09

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: 59.33  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCvkRLDGCIyAIKRSKKPLAGSVDEQNALREVyahAVLGQHPHV-VRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14062   1 IGSGSFGTVYKG--RWHGDV-AVKKLNVTDPTPSQLQAFKNEV---AVLRKTRHVnILLFMGYMTKPQLAIVTQWCEGSS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LadavsenYR---VM-SYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDdwisnkVMF 458
Cdd:cd14062  75 L-------YKhlhVLeTKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFL-------------HED------LTV 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVT---RIS-SPQVEE--GDSRFLANEV--LQENYSHLPKADIFALALtVVCAAGAEPLP----RNGDQ-WHEI 525
Cdd:cd14062 129 KIGDFGLATvktRWSgSQQFEQptGSILWMAPEVirMQDENPYSFQSDVYAFGI-VLYELLTGQLPyshiNNRDQiLFMV 207
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 526 RQGRL-PRIPQVLSQELTELLKVM---IHPDPERRP 557
Cdd:cd14062 208 GRGYLrPDLSKVRSDTPKALRRLMedcIKFQRDERP 243
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
296-607 1.35e-09

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: 59.84  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEK-IGSGEFGSVFKCVKRLDGCIYAIKRSKKplagSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHML 372
Cdd:cd14085   2 EDFFEIESeLGRGATSVVYRCRQKGTQKPYAVKKLKK----TVDKKIVRTEI---GVLLRlsHPNIIKLKEIFETPTEIS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrTSIPNAVseegdeddwi 452
Cdd:cd14085  75 LVLELVTGGELFDRIVEK----GYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYA-TPAPDAP---------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 snkvmFKIGDLGhVTRISSPQVEE----GDSRFLANEVLQeNYSHLPKADIFALA-LTVVCAAGAEPL-PRNGDQWHEIR 526
Cdd:cd14085 140 -----LKIADFG-LSKIVDQQVTMktvcGTPGYCAPEILR-GCAYGPEVDMWSVGvITYILLCGFEPFyDERGDQYMFKR 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 527 QGRL------PRIPQVlSQELTELLKVMIHPDPERRPSAMVLVKHSVLlsaSRKSAEQLRIELNAEKFKNSLLQKELkKA 600
Cdd:cd14085 213 ILNCdydfvsPWWDDV-SLNAKDLVKKLIVLDPKKRLTTQQALQHPWV---TGKAANFAHMDTAQKKLQEFNARRKL-KA 287

                ....*..
gi 17865613 601 QMAAKVA 607
Cdd:cd14085 288 AVKAVVA 294
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
297-565 1.38e-09

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 59.10  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14186   2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMiDKKAMQKAGMVQRVRNEVEIHCQL-KHPSILELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwisnK 455
Cdd:cd14186  81 EMCHNGEMSRYLKNRKKP---FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR-------------------N 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALALTVVCAAGAEPlPRNGDQwheiRQGRLP 531
Cdd:cd14186 139 MNIKIADFGLATQLKMPHEKHftmcGTPNYISPEIATRS-AHGLESDVWSLGCMFYTLLVGRP-PFDTDT----VKNTLN 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 532 RI-------PQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14186 213 KVvladyemPAFLSREAQDLIHQLLRKNPADRLSLSSVLDH 253
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
304-566 1.46e-09

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: 59.29  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSK-KPLAGSVD-EQNALR-EVYAHAVLgQHPHVVRYFSAW--AEDDHMLIQNEYC 378
Cdd:cd06652  10 LGQGAFGRVYLCYDADTGRELAVKQVQfDPESPETSkEVNALEcEIQLLKNL-LHERIVQYYGCLrdPQERTLSIFMEYM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisRTSIPNAvseegdeddwisnkvmf 458
Cdd:cd06652  89 PGGSIKDQL----KSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL--RDSVGNV----------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGHVTRISSPQVE-------EGDSRFLANEVLQ-ENYSHlpKADIFALALTVVCAAGAEPlprngdQWHEIR---- 526
Cdd:cd06652 146 KLGDFGASKRLQTICLSgtgmksvTGTPYWMSPEVISgEGYGR--KADIWSVGCTVVEMLTEKP------PWAEFEamaa 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 527 ------QGRLPRIPQVLSQELTELLKvMIHPDPERRPSAMVLVKHS 566
Cdd:cd06652 218 ifkiatQPTNPQLPAHVSDHCRDFLK-RIFVEAKLRPSADELLRHT 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
298-432 1.48e-09

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: 59.62  E-value: 1.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKK-PLAGSVDEQNALrevyahAVLG--QHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKsPLSRDSSLENEI------AVLKriKHENIVTLEDIYESTTHYYLV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 375 NEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIF 432
Cdd:cd14166  79 MQLVSGGELFDRILER----GVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLL 132
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
304-580 1.52e-09

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: 59.88  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLagsvdEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRM-----EANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSiPNAVseegdeddwisnkvmFKIGDL 463
Cdd:cd14180  89 LDRI----KKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADES-DGAV---------------LKVIDF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 GhVTRISSPQVEEGDS-----RFLANEVL-QENYSHLpkADIFALALTV-VCAAGAEPL---------PRNGDQWHEIRQ 527
Cdd:cd14180 149 G-FARLRPQGSRPLQTpcftlQYAAPELFsNQGYDES--CDLWSLGVILyTMLSGQVPFqskrgkmfhNHAADIMHKIKE 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 528 GRLP---RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQLR 580
Cdd:cd14180 226 GDFSlegEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPLM 281
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
304-565 1.55e-09

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: 59.20  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14116  13 LGKGKFGNVYLAREKQSKFILALKvLFKAQLEKAGVEHQLRREVEIQSHL-RHPNILRLYGYFHDATRVYLILEYAPLGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKVMfKIGD 462
Cdd:cd14116  92 VYRELQK----LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG------------------SAGEL-KIAD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQVEE--GDSRFLANEVLqENYSHLPKADIFALAltVVC---AAGAEPLPRNGdqwHEIRQGRLPRI---- 533
Cdd:cd14116 149 FGWSVHAPSSRRTTlcGTLDYLPPEMI-EGRMHDEKVDLWSLG--VLCyefLVGKPPFEANT---YQETYKRISRVeftf 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 534 PQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14116 223 PDFVTEGARDLISRLLKHNPSQRPMLREVLEH 254
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
301-558 1.57e-09

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: 59.13  E-value: 1.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSV----FKCVKRLdgCIYAIKRSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFsAWAEDDHMLIQNE 376
Cdd:cd05067  12 VERLGAGQFGEVwmgyYNGHTKV--AIKSLKQGSMSPDAFLAEANLMKQL-------QHQRLVRLY-AVVTQEPIYIITE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLAD--AVSENYRVMSYfteaELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwisn 454
Cdd:cd05067  82 YMENGSLVDflKTPSGIKLTIN----KLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDT------------------ 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kVMFKIGDLGHVTRISSPQ--VEEGDS---RFLANEVLqeNYSHLP-KADI--FALALTVVCAAGAEPLP--RNGDQWHE 524
Cdd:cd05067 140 -LSCKIADFGLARLIEDNEytAREGAKfpiKWTAPEAI--NYGTFTiKSDVwsFGILLTEIVTHGRIPYPgmTNPEVIQN 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 525 IRQG-RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05067 217 LERGyRMPR-PDNCPEELYQLMRLCWKERPEDRPT 250
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
298-598 1.79e-09

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: 59.62  E-value: 1.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL---REVYAHAVLGQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLmceKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSL-----ADAVSENyRVMSYFTEAELkdlllqvgrGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGded 449
Cdd:cd05589  81 MEYAAGGDLmmhihEDVFSEP-RAVFYAACVVL---------GLQFLHEHKIVYRDLKLDNLLLDT---------EG--- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 dwisnkvMFKIGD-------LGHVTRISSPQveeGDSRFLANEVLQENySHLPKADIFALA-LTVVCAAGAEPLPrnGDQ 521
Cdd:cd05589 139 -------YVKIADfglckegMGFGDRTSTFC---GTPEFLAPEVLTDT-SYTRAVDWWGLGvLIYEMLVGESPFP--GDD 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 522 WHEIRQGRLP---RIPQVLSQELTELLKVMIHPDPERRpsamvlvkhsvlLSASRKSAEQLRIELNaekFKN----SLLQ 594
Cdd:cd05589 206 EEEVFDSIVNdevRYPRFLSTEAISIMRRLLRKNPERR------------LGASERDAEDVKKQPF---FRNidweALLA 270

                ....
gi 17865613 595 KELK 598
Cdd:cd05589 271 RKIK 274
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
298-475 1.82e-09

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: 59.79  E-value: 1.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVdeQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEy 377
Cdd:cd07854   7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSV--KHALREIKIIRRL-DHDNIVKVYEVLGPSGSDLTEDV- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 cngGSLADaVSENYRVMSYFtEAELKDLL--------------LQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavs 443
Cdd:cd07854  83 ---GSLTE-LNSVYIVQEYM-ETDLANVLeqgplseeharlfmYQLLRGLKYIHSANVLHRDLKPANVFINT-------- 149
                       170       180       190
                ....*....|....*....|....*....|..
gi 17865613 444 eegdEDdwisnkVMFKIGDLGhVTRISSPQVE 475
Cdd:cd07854 150 ----ED------LVLKIGDFG-LARIVDPHYS 170
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
304-558 1.87e-09

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 58.79  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALR-EVYAHAVLGqHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14187  15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSmEIAIHRSLA-HQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LAdavsENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeDDwisnkVMFKIGD 462
Cdd:cd14187  94 LL----ELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLN--------------DD-----MEVKIGD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQVEE----GDSRFLANEVLQENySHLPKADIFALA-LTVVCAAGAEPLPRN--GDQWHEIRQGRLpRIPQ 535
Cdd:cd14187 151 FGLATKVEYDGERKktlcGTPNYIAPEVLSKK-GHSFEVDIWSIGcIMYTLLVGKPPFETSclKETYLRIKKNEY-SIPK 228
                       250       260
                ....*....|....*....|...
gi 17865613 536 VLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14187 229 HINPVAASLIQKMLQTDPTARPT 251
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
297-435 2.14e-09

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: 58.99  E-value: 2.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSV-------DEQNALREVyahavlgQHPHVVRYFSAWAEDD 369
Cdd:cd05612   2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLkqeqhvhNEKRVLKEV-------SHPFIIRLFWTEHDQR 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 370 HMLIQNEYCNGGSLADAVSENYRV---MSYFTEAELKDlllqvgrGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05612  75 FLYMLMEYVPGGELFSYLRNSGRFsnsTGLFYASEIVC-------ALEYLHSKEIVYRDLKPENILLDK 136
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
304-569 2.31e-09

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: 58.90  E-value: 2.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIY--AIKRSKKpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLAD------------AVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeD 449
Cdd:cd05047  82 NLLDflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVG--------------E 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 DWISnkvmfKIGDLGhVTRISSPQVEEG----DSRFLANEVLqeNYS-HLPKADI--FALALTVVCAAGAEPL--PRNGD 520
Cdd:cd05047 148 NYVA-----KIADFG-LSRGQEVYVKKTmgrlPVRWMAIESL--NYSvYTTNSDVwsYGVLLWEIVSLGGTPYcgMTCAE 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 521 QWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS-AMVLVKHSVLL 569
Cdd:cd05047 220 LYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSfAQILVSLNRML 269
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
281-434 2.47e-09

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: 59.19  E-value: 2.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 281 KRITITESNMKSRYttefHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREV--YAHAvlgQHPHV 358
Cdd:cd07880   4 QEVNKTIWEVPDRY----RDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELrlLKHM---KHENV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 359 VRYFSAWAEDDHMliqneycnggslaDAVSENYRVMSY-------------FTEAELKDLLLQVGRGLRYIHSMSLVHMD 425
Cdd:cd07880  77 IGLLDVFTPDLSL-------------DRFHDFYLVMPFmgtdlgklmkhekLSEDRIQFLVYQMLKGLKYIHAAGIIHRD 143

                ....*....
gi 17865613 426 IKPSNIFIS 434
Cdd:cd07880 144 LKPGNLAVN 152
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
298-464 2.49e-09

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: 59.22  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCV--KRLDGCIYAIKRSKkplaGSVDE-----QNALREVyahAVLG--QHPHVV---RYF--- 362
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFK----GDKEQytgisQSACREI---ALLRelKHENVVslvEVFleh 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 363 ---SAW-----AEDDHMLIQNEYcnggsladavSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07842  75 adkSVYllfdyAEHDLWQIIKFH----------RQAKRVS--IPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVM 142
                       170       180       190
                ....*....|....*....|....*....|
gi 17865613 435 RtsipnavseEGDEDDWIsnkvmfKIGDLG 464
Cdd:cd07842 143 G---------EGPERGVV------KIGDLG 157
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
297-472 2.76e-09

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: 58.77  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsVDEQ------NALREVyahAVL--GQHPHVVRYfsawaed 368
Cdd:cd07843   6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLK------MEKEkegfpiTSLREI---NILlkLQHPNIVTV------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIqneycngGSLADAVsenYRVMSY---------------FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFi 433
Cdd:cd07843  70 KEVVV-------GSNLDKI---YMVMEYvehdlkslmetmkqpFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLL- 138
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17865613 434 srtsipnavseegdeddwISNKVMFKIGDLGHVTRISSP 472
Cdd:cd07843 139 ------------------LNNRGILKICDFGLAREYGSP 159
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
304-558 2.84e-09

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: 58.42  E-value: 2.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsVDEQ---NALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIR-----CDEEtqkTFLTEVKVMRSL-DHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS--RTSIpnaVSEEGDEDDWISNKVM- 457
Cdd:cd14222  75 GTLKDFL----RADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKldKTVV---VADFGLSRLIVEEKKKp 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 ------FKIGDLGHVTRISSPQVeEGDSRFLANEVLQeNYSHLPKADIFALALtVVCA------AGAEPLPRNGDQWHEI 525
Cdd:cd14222 148 ppdkptTKKRTLRKNDRKKRYTV-VGNPYWMAPEMLN-GKSYDEKVDIFSFGI-VLCEiigqvyADPDCLPRTLDFGLNV 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 526 RQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14222 225 RLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPA 257
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
301-565 3.00e-09

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: 58.71  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKR---SKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14094   8 CEVIGKGPFSVVRRCIHRETGQQFAVKIvdvAKFTSSPGLSTEDLKREASICHML-KHPHIVELLETYSSDGMLYMVFEF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwiSNKVM 457
Cdd:cd14094  87 MDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK----------------ENSAP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQVEE----GDSRFLANEVLQENYSHLPkADIFALALTV-VCAAGAEPLPRNGDQWHE-IRQGRL- 530
Cdd:cd14094 151 VKLGGFGVAIQLGESGLVAggrvGTPHFMAPEVVKREPYGKP-VDVWGCGVILfILLSGCLPFYGTKERLFEgIIKGKYk 229
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 531 --PRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14094 230 mnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNH 266
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
303-558 3.02e-09

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: 58.29  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIK--RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14070   9 KLGEGSFAKVREGLHAVTGEKVAIKviDKKKAKKDSYVTKNLRREGRIQQMI-RHPNITQLLDILETENSYYLVMELCPG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWI-------S 453
Cdd:cd14070  88 GNLMHRIYDKKRL----EEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL-------------DENDNIklidfglS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 NKVMFKIGDLGHVTRISSPQveegdsrFLANEVLQENySHLPKADIFALALTVVCA-AGAEPL---PRNGDQWHE-IRQG 528
Cdd:cd14070 151 NCAGILGYSDPFSTQCGSPA-------YAAPELLARK-KYGPKVDVWSIGVNMYAMlTGTLPFtvePFSLRALHQkMVDK 222
                       250       260       270
                ....*....|....*....|....*....|
gi 17865613 529 RLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14070 223 EMNPLPTDLSPGAISFLRSLLEPDPLKRPN 252
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
286-433 3.40e-09

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 59.00  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  286 TESNMKSRYTtefhELEK-IGSGEFGSVFKCVKRLDGCIYAIKRSKK---PLAGSVDEQN---------ALREVYAHAVL 352
Cdd:PTZ00024   2 MSFSISERYI----QKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIieiSNDVTKDRQLvgmcgihftTLRELKIMNEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  353 gQHPHVVRYFSAWAEDDHMLIQNEYCNGgSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIF 432
Cdd:PTZ00024  78 -KHENIMGLVDVYVEGDFINLVMDIMAS-DLKKVVDRKIR----LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIF 151

                 .
gi 17865613  433 I 433
Cdd:PTZ00024 152 I 152
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
297-501 4.62e-09

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: 57.72  E-value: 4.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkPLAGSVDE-QNALRevyahaVLGQHPHV-VRYFSAWAEDDHMLIQ 374
Cdd:cd14150   1 EVSMLKRIGTGSFGTVFRGKWHGDVAVKILKVTE-PTPEQLQAfKNEMQ------VLRKTRHVnILLFMGFMTRPNFAII 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLadavsenYRVM----SYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavsEEGdedd 450
Cdd:cd14150  74 TQWCEGSSL-------YRHLhvteTRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFL----------HEG---- 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 451 wisnkVMFKIGDLGHVT---RIS-SPQVEE--GDSRFLANEV--LQENYSHLPKADIFA 501
Cdd:cd14150 133 -----LTVKIGDFGLATvktRWSgSQQVEQpsGSILWMAPEVirMQDTNPYSFQSDVYA 186
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
304-562 5.00e-09

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: 57.74  E-value: 5.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14146   2 IGVGGFGKVYRATWKGQEVAVKAARQDPDEDIKATAESVRQEAKLFSML-RHPNIIKLEGVCLEEPNLCLVMEFARGGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 ADAVS-----ENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLV---HMDIKPSNIFISrtsipnavseEGDEDDWISNK 455
Cdd:cd14146  81 NRALAaanaaPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLL----------EKIEHDDICNK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMfKIGDLG------HVTRISSPqveeGDSRFLANEVLQEnySHLPK-ADIFALALTVVCAAGAEpLPRNGDQWHEIRQG 528
Cdd:cd14146 151 TL-KITDFGlarewhRTTKMSAA----GTYAWMAPEVIKS--SLFSKgSDIWSYGVLLWELLTGE-VPYRGIDGLAVAYG 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 529 ------RLPrIPQVLSQELTELLKVMIHPDPERRPS-AMVL 562
Cdd:cd14146 223 vavnklTLP-IPSTCPEPFAKLMKECWEQDPHIRPSfALIL 262
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
296-521 5.42e-09

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: 57.60  E-value: 5.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIK----RSKKplagsvdEQNALREVYAHAVLgQHPHVVRYFSAWAEDDH 370
Cdd:cd14108   1 TDYYDIhKEIGRGAFSYLRRVKEKSSDLSFAAKfipvRAKK-------KTSARRELALLAEL-DHKSIVRFHDAFEKRRV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdedd 450
Cdd:cd14108  73 VIIVTELCHEELLERITKR-----PTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLM----------------- 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 451 WISNKVMFKIGDLGHVTRIS--SPQ-VEEGDSRFLANEVLqeNYSHLPKA-DIFALA-LTVVCAAGAEPLPRNGDQ 521
Cdd:cd14108 131 ADQKTDQVRICDFGNAQELTpnEPQyCKYGTPEFVAPEIV--NQSPVSKVtDIWPVGvIAYLCLTGISPFVGENDR 204
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
302-434 5.65e-09

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: 57.42  E-value: 5.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd14082   9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEV---AILQQlsHPGVVNLECMFETPERVFVVMEKLH 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 380 GGSLADAVS-ENYRVMSYFTeaelKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd14082  86 GDMLEMILSsEKGRLPERIT----KFLVTQILVALRYLHSKNIVHCDLKPENVLLA 137
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
298-568 6.07e-09

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: 57.71  E-value: 6.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKrskkPLAGSVDEQNALR-EVYAHAVLGQHPHVVRYFSAW------AEDDH 370
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK----VMDVTEDEEEEIKlEINMLKKYSHHRNIATYYGAFikksppGHDDQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeDD 450
Cdd:cd06636  94 LWLVMEFCGAGSVTDLVKNTKG--NALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV------DF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 WISNKVMFKIGDLGhvTRISSPQveegdsrFLANEVL--QEN----YSHlpKADIFALALTVV-CAAGAEPLPrngdQWH 523
Cdd:cd06636 166 GVSAQLDRTVGRRN--TFIGTPY-------WMAPEVIacDENpdatYDY--RSDIWSLGITAIeMAEGAPPLC----DMH 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 524 EIRQGRL-PRIP------QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06636 231 PMRALFLiPRNPppklksKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
302-504 6.98e-09

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: 57.45  E-value: 6.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKcvKRLDGCIYAIKrskkpLAGSVDEQNALRE--VYaHAVLGQHPHVVRYFSAWAEDDHMLIQ----N 375
Cdd:cd13998   1 EVIGKGRFGEVWK--ASLKNEPVAVK-----IFSSRDKQSWFREkeIY-RTPMLKHENILQFIAADERDTALRTElwlvT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADavsenYRVMSYFTEAELKDLLLQVGRGLRYIHS---------MSLVHMDIKPSNIFisrtsipnavseeg 446
Cdd:cd13998  73 AFHPNGSL*D-----YLSLHTIDWVSLCRLALSVARGLAHLHSeipgctqgkPAIAHRDLKSKNIL-------------- 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 447 deddwISNKVMFKIGDLGHVTRISS--------PQVEEGDSRFLANEVLQ-----ENYSHLPKADIFALAL 504
Cdd:cd13998 134 -----VKNDGTCCIADFGLAVRLSPstgeednaNNGQVGTKRYMAPEVLEgainlRDFESFKRVDIYAMGL 199
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
302-565 7.39e-09

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: 57.36  E-value: 7.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ-NALREVYAHAV-----LGQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14093   9 EILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEaEELREATRREIeilrqVSGHPNIIELHDVFESPTFIFLVF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnk 455
Cdd:cd14093  89 ELCRKGELFDYLTEVVT----LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL-------------DDNLNV--- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmfKIGDLGHVTRIsspqvEEGDS--------RFLANEVLQ-------ENYSHlpKADIFALAL---TVVCaaGAEPLpr 517
Cdd:cd14093 149 ---KISDFGFATRL-----DEGEKlrelcgtpGYLAPEVLKcsmydnaPGYGK--EVDMWACGVimyTLLA--GCPPF-- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 518 ngdqWHE--------IRQGRLP-RIPQV--LSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14093 215 ----WHRkqmvmlrnIMEGKYEfGSPEWddISDTAKDLISKLLVVDPKKRLTAEEALEH 269
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
298-433 8.46e-09

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: 57.57  E-value: 8.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAW-AEDDHMLiqne 376
Cdd:cd07852   9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRTFREIMFLQELNDHPNIIKLLNVIrAENDKDI---- 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 377 ycnggsladavsenYRVMSYFtEAEL-----KDLLL---------QVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07852  85 --------------YLVFEYM-ETDLhavirANILEdihkqyimyQLLKALKYLHSGGVIHRDLKPSNILL 140
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
304-558 8.48e-09

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: 57.08  E-value: 8.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHS-SPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 A---DAVSENyrvmsyfTEAELK-DLLLQVGRGLRYIHSMS--LVHMDIKPSNIFisrtsipnavseegdeddwISNKVM 457
Cdd:cd13978  80 KsllEREIQD-------VPWSLRfRIIHEIALGMNFLHNMDppLLHHDLKPENIL-------------------LDNHFH 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLG--HVTRISSPQVEEGDSR-------FLANEVLQE-NYSHLPKADIFALA-LTVVCAAGAEPLPRNGDQWHEIR 526
Cdd:cd13978 134 VKISDFGlsKLGMKSISANRRRGTEnlggtpiYMAPEAFDDfNKKPTSKSDVYSFAiVIWAVLTRKEPFENAINPLLIMQ 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 527 ---QGRLPRIPQV-------LSQELTELLKVMIHPDPERRPS 558
Cdd:cd13978 214 ivsKGDRPSLDDIgrlkqieNVQELISLMIRCWDGNPDARPT 255
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
303-568 8.63e-09

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: 57.36  E-value: 8.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKRSkkplagSVDEQNALREVYAHAVLGQ---HPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd06658  29 KIGEGSTGIVCIATEKHTGKQVAVKKM------DLRKQQRRELLFNEVVIMRdyhHENVVDMYNSYLVGDELWVVMEFLE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnkvMFK 459
Cdd:cd06658 103 GGALTDIVTH-----TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDG-------------------RIK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISS--PQVEE--GDSRFLANEVLqenySHLP---KADIFALALTVVCAAGAEPLPRNGDQWHEIRQGR--- 529
Cdd:cd06658 159 LSDFGFCAQVSKevPKRKSlvGTPYWMAPEVI----SRLPygtEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRdnl 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 530 LPRIPQV--LSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd06658 235 PPRVKDShkVSSVLRGFLDLMLVREPSQRATAQELLQHPFL 275
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
304-558 9.03e-09

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: 57.11  E-value: 9.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVfkcvkrLDGCIYAIKRSK----------KPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05055  43 LGAGAFGKV------VEATAYGLSKSDavmkvavkmlKPTAHSSEREALMSELKIMSHLGNHENIVNLLGACTIGGPILV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSENYRVMsyfteAELKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdedd 450
Cdd:cd05055 117 ITEYCCYGDLLNFLRRKRESF-----LTLEDLLsfsYQVAKGMAFLASKNCIHRDLAARNVLLTHGKI------------ 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnkvmFKIGDLGHVTRI--SSPQVEEGDSR----FLANEVLQEN-YSHLPKADIFALALTVVCAAGAEP---LPRNGD 520
Cdd:cd05055 180 -------VKICDFGLARDImnDSNYVVKGNARlpvkWMAPESIFNCvYTFESDVWSYGILLWEIFSLGSNPypgMPVDSK 252
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 521 QWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05055 253 FYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPT 290
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
298-437 9.13e-09

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: 56.85  E-value: 9.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLD-------GCIYAIKRskkpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDH 370
Cdd:cd14019   3 YRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKH----IYPTSSPSRILNELECLERLGGSNNVSGLITAFRNEDQ 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 371 MLIQNEYCNGGSLADavseNYRVMSYFteaELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTS 437
Cdd:cd14019  79 VVAVLPYIEHDDFRD----FYRKMSLT---DIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRET 138
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
297-558 9.82e-09

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: 56.97  E-value: 9.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL---EKIGSGEFGSVFKCVkrLDGCIYAIKRSKKPLAGSVDE--QNALREVYAHAVLgQHPHVVRYFSAWAEDDHM 371
Cdd:cd14145   4 DFSELvleEIIGIGGFGKVYRAI--WIGDEVAVKAARHDPDEDISQtiENVRQEAKLFAML-KHPNIIALRGVCLKEPNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSeNYRVMSYFteaeLKDLLLQVGRGLRYIHSMSLV---HMDIKPSNIFISRTsipnavSEEGDe 448
Cdd:cd14145  81 CLVMEFARGGPLNRVLS-GKRIPPDI----LVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEK------VENGD- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 ddwISNKVMfKIGDLG------HVTRISSPqveeGDSRFLANEVLQEnySHLPK-ADIFALALTVVCAAGAEpLPRNGDQ 521
Cdd:cd14145 149 ---LSNKIL-KITDFGlarewhRTTKMSAA----GTYAWMAPEVIRS--SMFSKgSDVWSYGVLLWELLTGE-VPFRGID 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 522 WHEIRQG------RLPrIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14145 218 GLAVAYGvamnklSLP-IPSTCPEPFARLMEDCWNPDPHSRPP 259
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
293-431 1.04e-08

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: 57.30  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTtefhELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREV--YAHAvlgQHPHVVRYFSAWAEDDH 370
Cdd:cd07851  16 RYQ----NLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELrlLKHM---KHENVIGLLDVFTPASS 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 371 -MLIQNEYCNGgSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd07851  89 lEDFQDVYLVT-HLMGADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNL 149
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
304-556 1.04e-08

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: 56.98  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPL------AGSVDEQ----------NALREVYAH-AVLGQ--HPHVVRYFS 363
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKiLSKKKLlkqagfFRRPPPRrkpgalgkplDPLDRVYREiAILKKldHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 364 AWAE--DDHMLIQNEYCNGGSLADAVSEN----YRVMSYFteaelKDLLLqvgrGLRYIHSMSLVHMDIKPSNIFIS--- 434
Cdd:cd14118  82 VLDDpnEDNLYMVFELVDKGAVMEVPTDNplseETARSYF-----RDIVL----GIEYLHYQKIIHRDIKPSNLLLGddg 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 435 RTSIPN-AVSEE--GDeDDWISNKVmfkigdlghvtrisspqveeGDSRFLANEVLQEN---YSHLPkADIFALALTVVC 508
Cdd:cd14118 153 HVKIADfGVSNEfeGD-DALLSSTA--------------------GTPAFMAPEALSESrkkFSGKA-LDIWAMGVTLYC 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 509 -AAGAEP-LPRNGDQWHE-IRQGRLpRIPQ--VLSQELTELLKVMIHPDPERR 556
Cdd:cd14118 211 fVFGRCPfEDDHILGLHEkIKTDPV-VFPDdpVVSEQLKDLILRMLDKNPSER 262
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
298-432 1.05e-08

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: 56.98  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAG---SVDEQNA-LREVyahavlgQHPHVVRYFSAWAEDDHML 372
Cdd:cd14168  12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKcIPKKALKGkesSIENEIAvLRKI-------KHENIVALEDIYESPNHLY 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIF 432
Cdd:cd14168  85 LVMQLVSGGELFDRIVEK----GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL 140
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
289-446 1.17e-08

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: 57.19  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 289 NMKSRYTTefheLEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagSVD--------EQNALREVYAHAVLGQHpHVVR 360
Cdd:cd14134   9 LLTNRYKI----LRLLGEGTFGKVLECWDRKRKRYVAVKIIR-----NVEkyreaakiEIDVLETLAEKDPNGKS-HCVQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 361 YFSAWAEDDHMLIQNEYCnGGSLADAVSEN-YRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI-FISRTSI 438
Cdd:cd14134  79 LRDWFDYRGHMCIVFELL-GPSLYDFLKKNnYGP---FPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENIlLVDSDYV 154

                ....*...
gi 17865613 439 PNAVSEEG 446
Cdd:cd14134 155 KVYNPKKK 162
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
301-506 1.26e-08

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: 56.58  E-value: 1.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagSVDEQNALR-EVyahAVLGQHPHV-VRYFSAWAEDDHMLIQNEYC 378
Cdd:cd14149  17 STRIGSGSFGTVYKGKWHGDVAVKILKVVDP----TPEQFQAFRnEV---AVLRKTRHVnILLFMGYMTKDNLAIVTQWC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVsenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavsEEGdeddwisnkVMF 458
Cdd:cd14149  90 EGSSLYKHL---HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL----------HEG---------LTV 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 459 KIGDLGHVTRIS----SPQVEE--GDSRFLANEV--LQENYSHLPKADIFALALTV 506
Cdd:cd14149 148 KIGDFGLATVKSrwsgSQQVEQptGSILWMAPEVirMQDNNPFSFQSDVYSYGIVL 203
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
301-558 1.47e-08

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: 56.62  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCvkRLD------GCIYAIKrSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYfSAWAEDDH---M 371
Cdd:cd05038   9 IKQLGEGHFGSVELC--RYDplgdntGEQVAVK-SLQPSGEEQHMSDFKREIEILRTL-DHEYIVKY-KGVCESPGrrsL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMSyfteaeLKDLLL---QVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdE 448
Cdd:cd05038  84 RLIMEYLPSGSLRDYLQRHRDQID------LKRLLLfasQICKGMEYLGSQRYIHRDLAARNILV--------------E 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 DDWisnkvMFKIGDLGhVTRISSPQVE------EGDS--RFLANEVLQEN-YSHlpKADIFALALTV-----VCAAGAEP 514
Cdd:cd05038 144 SED-----LVKISDFG-LAKVLPEDKEyyyvkePGESpiFWYAPECLRESrFSS--ASDVWSFGVTLyelftYGDPSQSP 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 515 lPRNGDQWHEIRQG---------------RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05038 216 -PALFLRMIGIAQGqmivtrllellksgeRLPR-PPSCPDEVYDLMKECWEYEPQDRPS 272
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
304-442 1.54e-08

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 56.58  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsvDEQNALREVYAHAVLGQHPHVVR----YFSAWAEDDHMLIQNEYCN 379
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKMLQ-------DCPKARREVELHWRASQCPHIVRivdvYENLYAGRKCLLIVMECLD 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 380 GGSLADAVSEnyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrTSIPNAV 442
Cdd:cd14170  83 GGELFSRIQD--RGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYT-SKRPNAI 142
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
304-433 1.64e-08

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: 56.52  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQN---ALREVYAHAVlgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhimAERNVLLKNL--KHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 381 GSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05603  81 GELFFHLQRERC----FLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL 129
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
304-436 1.69e-08

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: 56.14  E-value: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDG---CIYAIKrSKKPLAGSVDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd05063  13 IGAGEFGEVFRGILKMPGrkeVAVAIK-TLKPGYTEKQRQDFLSEA---SIMGQfsHHNIIRLEGVVTKFKPAMIITEYM 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 379 NGGSLADAVSENYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05063  89 ENGALDKYLRDHD---GEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSN 143
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
298-568 1.99e-08

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: 55.60  E-value: 1.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKrsKKPLAGSvDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAK--IVPYQAE-EKQGVLQEYEILKSL-HHERIMALHEAYITPRYLVLIAEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipNAVseegdeddwisnkvm 457
Cdd:cd14111  81 CSGKELLHSLIDRFR----YSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNL---NAI--------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 fKIGDLGHVTRISSPQVEEGDSR-----FLANEVLQENYSHlPKADIFALA-LTVVCAAGAEPLPRNGDQWHE--IRQGR 529
Cdd:cd14111 139 -KIVDFGSAQSFNPLSLRQLGRRtgtleYMAPEMVKGEPVG-PPADIWSIGvLTYIMLSGRSPFEDQDPQETEakILVAK 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 530 LPRI---PQVlSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14111 217 FDAFklyPNV-SQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
304-565 2.13e-08

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: 55.35  E-value: 2.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKrldgciyaiKRSKKPLAGS-VDEQNALREVYAH--AVLG--QHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd14115   1 IGRGRFSIVKKCLH---------KATRKDVAVKfVSKKMKKKEQAAHeaALLQhlQHPQYITLHDTYESPTSYILVLELM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSENYRVMSYFTEAELKDLLlqvgRGLRYIHSMSLVHMDIKPSNIFISRTsIPNAVSEEGDEDDWISNKVMF 458
Cdd:cd14115  72 DDGRLLDYLMNHDELMEEKVAFYIRDIM----EALQYLHNCRVAHLDIKPENLLIDLR-IPVPRVKLIDLEDAVQISGHR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLghvtrisspqveEGDSRFLANEVLQENYSHLpKADIFALA-LTVVCAAGAEPLPRNGDQWHEIRQGRL-----PR 532
Cdd:cd14115 147 HVHHL------------LGNPEFAAPEVIQGTPVSL-ATDIWSIGvLTYVMLSGVSPFLDESKEETCINVCRVdfsfpDE 213
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd14115 214 YFGDVSQAARDFINVILQEDPRRRPTAATCLQH 246
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
304-436 2.16e-08

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: 56.16  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ---NALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05601   9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsffEEERDIMAKA---NSPWITKLQYAFQDSENLYLVMEYHPG 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 381 GslaDAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05601  86 G---DLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRT 138
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
298-436 2.21e-08

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: 55.76  E-value: 2.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDE---QNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIR---LETEDEgvpSTAIREISLLKEL-NHPNIVRLLDVVHSENKLYLV 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 375 NEYCNGG--SLADAVSENYrvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd07835  77 FEFLDLDlkKYMDSSPLTG-----LDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTE 135
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
298-583 2.22e-08

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: 55.88  E-value: 2.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkpLAGSvDEQNALREVYAHAVLGQHPHVVRYFSAWAE------DDHM 371
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD--VTGD-EEEEIKQEINMLKKYSHHRNIATYYGAFIKknppgmDDQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeDDW 451
Cdd:cd06637  85 WLVMEFCGAGSVTDLIKNTKG--NTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLV------DFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 ISNKVMFKIGDLGhvTRISSPQveegdsrFLANEVL----QENYSHLPKADIFALALTVV-CAAGAEPLPrngdQWHEIR 526
Cdd:cd06637 157 VSAQLDRTVGRRN--TFIGTPY-------WMAPEVIacdeNPDATYDFKSDLWSLGITAIeMAEGAPPLC----DMHPMR 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 527 QGRL-PRIP------QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLlsASRKSAEQLRIEL 583
Cdd:cd06637 224 ALFLiPRNPaprlksKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFI--RDQPNERQVRIQL 285
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
297-475 2.23e-08

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 56.22  E-value: 2.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVyahavlgqhpHVVRYFsawAEDDHMLIQNE 376
Cdd:cd07855   6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLREL----------KILRHF---KHDNIIAIRDI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSEnYRVMSY--------------FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnaV 442
Cdd:cd07855  73 LRPKVPYADFKDV-YVVLDLmesdlhhiihsdqpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL---------V 142
                       170       180       190
                ....*....|....*....|....*....|...
gi 17865613 443 SEEGDeddwisnkvmFKIGDLGHVTRISSPQVE 475
Cdd:cd07855 143 NENCE----------LKIGDFGMARGLCTSPEE 165
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
285-538 2.74e-08

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: 56.16  E-value: 2.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 285 ITESNMKSRyttEFHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQN--ALREVYAHAvlgQHPHVVRY 361
Cdd:cd05621  44 IRELQMKAE---DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKlLSKFEMIKRSDSAFfwEERDIMAFA---NSPWVVQL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 362 FSAWAEDDHMLIQNEYCNGGSLADAVSeNYRVMSYFTEAELKDLLLqvgrGLRYIHSMSLVHMDIKPSNIFISR------ 435
Cdd:cd05621 118 FCAFQDDKYLYMVMEYMPGGDLVNLMS-NYDVPEKWAKFYTAEVVL----ALDAIHSMGLIHRDVKPDNMLLDKyghlkl 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 436 -----------TSIPNAVSEEGDEdDWISNKVMFKIGDLGHVTR--------ISSPQVEEGDSRFLANEVL--------Q 488
Cdd:cd05621 193 adfgtcmkmdeTGMVHCDTAVGTP-DYISPEVLKSQGGDGYYGRecdwwsvgVFLFEMLVGDTPFYADSLVgtyskimdH 271
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 489 ENYSHLPK-ADIFALALTVVCA-----------AGAEPLPRN----GDQWH--EIRQGRLPRIPQVLS 538
Cdd:cd05621 272 KNSLNFPDdVEISKHAKNLICAfltdrevrlgrNGVEEIKQHpffrNDQWNwdNIRETAAPVVPELSS 339
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
302-566 2.74e-08

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: 55.74  E-value: 2.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPL-------------------AGSVDEQNALREVYAH-AVLGQ--HPHV 358
Cdd:cd14199   8 DEIGKGSYGVVKLAYNEDDNTYYAMKvLSKKKLmrqagfprrppprgaraapEGCTQPRGPIERVYQEiAILKKldHPNV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 359 VRYFSAWAE--DDHMLIQNEYCNGGSLADAVSenyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrt 436
Cdd:cd14199  88 VKLVEVLDDpsEDHLYMVFELVKQGPVMEVPT-----LKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL---- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 437 sipnaVSEEGD---EDDWISNKvmFKIGDLGHVTRISSPQveegdsrFLANEVLQE---NYShLPKADIFALALTVVC-A 509
Cdd:cd14199 159 -----VGEDGHikiADFGVSNE--FEGSDALLTNTVGTPA-------FMAPETLSEtrkIFS-GKALDVWAMGVTLYCfV 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 510 AGAEPL--PRNGDQWHEIRQGRL--PRIPQVlSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14199 224 FGQCPFmdERILSLHSKIKTQPLefPDQPDI-SDDLKDLLFRMLDKNPESRISVPEIKLHP 283
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
297-559 2.78e-08

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: 55.83  E-value: 2.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06650   6 DFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQ-IIREL---QVLHEcnSPYIVGFYGAFYSDGEISIC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSM-SLVHMDIKPSNIFI-SRTSIpnavseegdeddwi 452
Cdd:cd06650  82 MEHMDGGSLDQVLKKAGRI----PEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVnSRGEI-------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 snkvmfKIGDLGHVTRISSPQVEE--GDSRFLANEVLQENYSHLpKADIFALALTVVcaagaeplprngdqwhEIRQGRL 530
Cdd:cd06650 144 ------KLCDFGVSGQLIDSMANSfvGTRSYMSPERLQGTHYSV-QSDIWSMGLSLV----------------EMAVGRY 200
                       250       260
                ....*....|....*....|....*....
gi 17865613 531 PrIPQVLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd06650 201 P-IPPPDAKELELMFGCQVEGDAAETPPR 228
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
304-558 2.94e-08

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: 55.50  E-value: 2.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKR--LDGCIYAIKRSKKPL-AGSVDEQNA--LREvyAHaVLGQ--HPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05044   3 LGSGAFGEVFEGTAKdiLGDGSGETKVAVKTLrKGATDQEKAefLKE--AH-LMSNfkHPNILKLLGVCLDNDPQYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVM---SYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVseegdeddwis 453
Cdd:cd05044  80 LMEGGDLLSYLRAARPTAftpPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERV----------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGHVTRISSPQV--EEGDS----RFLANEVLQENYSHLpKADIFALALTV--VCAAGAEPLP--RNGDQWH 523
Cdd:cd05044 149 ----VKIGDFGLARDIYKNDYyrKEGEGllpvRWMAPESLVDGVFTT-QSDVWAFGVLMweILTLGQQPYParNNLEVLH 223
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 524 EIRQ-GRLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05044 224 FVRAgGRLDQ-PDNCPDDLYELMLRCWSTDPEERPS 258
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
296-557 3.06e-08

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 55.80  E-value: 3.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDG-------CIYAIKRSKKPLAgsvdEQNALREVYAHAVLgQHPHVVRYFSAWAED 368
Cdd:cd05108   7 TEFKKIKVLGSGAFGTVYKGLWIPEGekvkipvAIKELREATSPKA----NKEILDEAYVMASV-DNPHVCRLLGICLTS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIqNEYCNGGSLADAVSENY-RVMSYFteaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVseegd 447
Cdd:cd05108  82 TVQLI-TQLMPFGCLLDYVREHKdNIGSQY----LLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKT---PQHV----- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwisnkvmfKIGDLGHVTRISSPQVE---EGDS---RFLANE-VLQENYSHlpKADIFALALTV--VCAAGAEPLprN 518
Cdd:cd05108 149 -----------KITDFGLAKLLGAEEKEyhaEGGKvpiKWMALEsILHRIYTH--QSDVWSYGVTVweLMTFGSKPY--D 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 519 GDQWHEI-----RQGRLPRiPQVLSQELTELLKVMIHPDPERRP 557
Cdd:cd05108 214 GIPASEIssileKGERLPQ-PPICTIDVYMIMVKCWMIDADSRP 256
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
297-565 3.07e-08

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: 55.61  E-value: 3.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDH----ML 372
Cdd:cd07837   2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIYIVRLLDVEHVEENgkplLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNgGSLADAVSENYRVMSYFTEAEL-KDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddw 451
Cdd:cd07837  82 LVFEYLD-TDLKKFIDSYGRGPHNPLPAKTiQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDK---------------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 isNKVMFKIGDLGHVTRISSP----QVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPL-PrnGD------ 520
Cdd:cd07837 145 --QKGLLKIADLGLGRAFTIPiksyTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLfP--GDselqql 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 521 ----------------------QWHEIRQGR---LPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd07837 221 lhifrllgtpneevwpgvsklrDWHEYPQWKpqdLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQH 290
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
295-474 3.81e-08

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: 55.66  E-value: 3.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 295 TTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRY---FSAWAEDDHM 371
Cdd:cd07856   9 TTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHL-RHENIISLsdiFISPLEDIYF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSENYRVMSYFteaelkdlLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnaVSEEGDeddw 451
Cdd:cd07856  88 VTELLGTDLHRLLTSRPLEKQFIQYF--------LYQILRGLKYVHSAGVIHRDLKPSNIL---------VNENCD---- 146
                       170       180
                ....*....|....*....|...
gi 17865613 452 isnkvmFKIGDLGhVTRISSPQV 474
Cdd:cd07856 147 ------LKICDFG-LARIQDPQM 162
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
304-573 4.02e-08

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; 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. Tie1 is a receptor tyr kinase (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. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 55.39  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGC-IYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05089  10 IGEGNFGQVIKAMIKKDGLkMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAIEYAPYGN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LAD------------AVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipNAVSeegdedd 450
Cdd:cd05089  90 LLDflrksrvletdpAFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGE----NLVS------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 wisnkvmfKIGDLGhVTRISSPQVEEG----DSRFLANEVLqeNYS-HLPKADI--FALALTVVCAAGAEPL--PRNGDQ 521
Cdd:cd05089 159 --------KIADFG-LSRGEEVYVKKTmgrlPVRWMAIESL--NYSvYTTKSDVwsFGVLLWEIVSLGGTPYcgMTCAEL 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 522 WHEIRQGRLPRIPQVLSQELTELLKVMIHPDP-ERRPSAMVLVKHSVLLSASR 573
Cdd:cd05089 228 YEKLPQGYRMEKPRNCDDEVYELMRQCWRDRPyERPPFSQISVQLSRMLEARK 280
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
302-558 4.34e-08

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: 54.66  E-value: 4.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCV-KRLDGCIY--AIK--RSKKPLAGSVDEqNALREVYA-HAVlgQHPHVVRYFSAWAEDDHMLIqN 375
Cdd:cd05040   1 EKLGDGSFGVVRRGEwTTPSGKVIqvAVKclKSDVLSQPNAMD-DFLKEVNAmHSL--DHPNLIRLYGVVLSSPLMMV-T 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwiSNK 455
Cdd:cd05040  77 ELAPLGSLLDRLRKD---QGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLAS-----------------KDK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VmfKIGDLGhvtriSSPQVEEGDSRFLANEVLQ-------------ENYSHlpKADIFALALTV--VCAAGAEP-LPRNG 519
Cdd:cd05040 137 V--KIGDFG-----LMRALPQNEDHYVMQEHRKvpfawcapeslktRKFSH--ASDVWMFGVTLweMFTYGEEPwLGLNG 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 520 DQ-WHEI-RQG-RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05040 208 SQiLEKIdKEGeRLER-PDDCPQDIYNVMLQCWAHKPADRPT 248
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
304-573 4.47e-08

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: 54.82  E-value: 4.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRskkpLAGSVDEQNA--LREVYAHAVLGQHPHVVRYFSAWA----EDDHM----LI 373
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALKR----LLSNEEEKNKaiIQEINFMKKLSGHPNIVQFCSAASigkeESDQGqaeyLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGsLADAVSENYRVMSYFTEAELKdLLLQVGRGLRYIHSMS--LVHMDIKPSNIFisrtsipnavseegdeddw 451
Cdd:cd14036  84 LTELCKGQ-LVDFVKKVEAPGPFSPDTVLK-IFYQTCRAVQHMHKQSppIIHRDLKIENLL------------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 452 ISNKVMFKIGDLGHVTRIS-SPQVE-EGDSRFLANEVLQEN-------------YSHLP---KADIFALA--LTVVC--- 508
Cdd:cd14036 143 IGNQGQIKLCDFGSATTEAhYPDYSwSAQKRSLVEDEITRNttpmyrtpemidlYSNYPigeKQDIWALGciLYLLCfrk 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 509 ---AAGAEPLPRNGDqwHEIRQGrlPRIPQVLSQELTELLKVmihpDPERRPSAMVLVKHSVLLSASR 573
Cdd:cd14036 223 hpfEDGAKLRIINAK--YTIPPN--DTQYTVFHDLIRSTLKV----NPEERLSITEIVEQLQELAAAR 282
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
304-431 4.68e-08

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: 55.19  E-value: 4.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSK-----KPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDD--HMLIQNE 376
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNnlsfmRPLDVQMREFEVLKKL-------NHKNIVKLFAIEEELTtrHKVLVME 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 377 YCNGGSLADAVSENYRvmSY-FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd13988  74 LCPCGSLYTVLEEPSN--AYgLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNI 127
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
297-558 4.90e-08

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: 54.65  E-value: 4.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHEL---EKIGSGEFGSVFKCVKRldGCIYAIKRSKK-PLAG-SVDEQNALREVYAHAVLGqHPHVVRYFSAWAEDDHM 371
Cdd:cd14147   1 SFQELrleEVIGIGGFGKVYRGSWR--GELVAVKAARQdPDEDiSVTAESVRQEARLFAMLA-HPNIIALKAVCLEEPNL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 LIQNEYCNGGSLADAVSeNYRVMSYFteaeLKDLLLQVGRGLRYIHSMSLV---HMDIKPSNIfisrtsipnaVSEEGDE 448
Cdd:cd14147  78 CLVMEYAAGGPLSRALA-GRRVPPHV----LVNWAVQIARGMHYLHCEALVpviHRDLKSNNI----------LLLQPIE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 DDWISNKVMfKIGDLG------HVTRISSPqveeGDSRFLANEVLqenyshlpKADIFALAltVVCAAGAEPL------- 515
Cdd:cd14147 143 NDDMEHKTL-KITDFGlarewhKTTQMSAA----GTYAWMAPEVI--------KASTFSKG--SDVWSFGVLLwelltge 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 516 -PRNGDQWHEIRQG------RLPrIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14147 208 vPYRGIDCLAVAYGvavnklTLP-IPSTCPEPFAQLMADCWAQDPHRRPD 256
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
301-562 5.41e-08

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: 54.38  E-value: 5.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVF--KCVKRLDGCIYAIKRskkplaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd05059   9 LKELGSGQFGVVHlgKWRGKIDVAIKMIKE------GSMSEDDFIEEAKVMMKL-SHPKLVQLYGVCTKQRPIFIVTEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 379 NGGSLADAVSENYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmF 458
Cdd:cd05059  82 ANGCLLNYLRERRGK---FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNV-------------------V 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGhVTR--ISSPQVEEGDSRF----LANEVLQEN-YShlPKADI--FALALTVVCAAGAEPLPR--NGDQWHEIRQ 527
Cdd:cd05059 140 KVSDFG-LARyvLDDEYTSSVGTKFpvkwSPPEVFMYSkFS--SKSDVwsFGVLMWEVFSEGKMPYERfsNSEVVEHISQ 216
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 528 G-RLPRiPQVLSQELTELLKVMIHPDPERRPSAMVL 562
Cdd:cd05059 217 GyRLYR-PHLAPTEVYTIMYSCWHEKPEERPTFKIL 251
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
301-564 5.70e-08

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: 54.73  E-value: 5.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFK-----CVKRLDG-CIYAIK-----RSKKPLAGSVDEQNALRevyahaVLGQHPHVVRYFSAWAEDD 369
Cdd:cd05053  17 GKPLGEGAFGQVVKaeavgLDNKPNEvVTVAVKmlkddATEKDLSDLVSEMEMMK------MIGKHKNIINLLGACTQDG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLADAVSENYRVMSYFTEAE---------LKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISrts 437
Cdd:cd05053  91 PLYVVVEYASKGNLREFLRARRPPGEEASPDDprvpeeqltQKDLVsfaYQVARGMEYLASKKCIHRDLAARNVLVT--- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 438 ipnavseegdEDDwisnkVMfKIGDLGHVTRISSPQV--EEGDSR----FLANEVLQEN-YSHlpKADI--FALALTVVC 508
Cdd:cd05053 168 ----------EDN-----VM-KIADFGLARDIHHIDYyrKTTNGRlpvkWMAPEALFDRvYTH--QSDVwsFGVLLWEIF 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 509 AAGAEPLPrnGDQWHE----IRQG-RLPRiPQVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd05053 230 TLGGSPYP--GIPVEElfklLKEGhRMEK-PQNCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
304-433 5.98e-08

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: 54.15  E-value: 5.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDEQNALREVYAH-AVLGQ--HPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKK---RHIVQTRQQEHIFSEkEILEEcnSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 381 GSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05572  78 GELWTILRDR----GLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL 126
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
296-563 6.01e-08

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 54.65  E-value: 6.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGciyaiKRSKKPLAGSVDEQNA--------LREVYAHAVLGQhPHVVRYFSAWAE 367
Cdd:cd05109   7 TELKKVKVLGSGAFGTVYKGIWIPDG-----ENVKIPVAIKVLRENTspkankeiLDEAYVMAGVGS-PYVCRLLGICLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 368 DDHMLIqNEYCNGGSLADAVSENY-RVMSyfteaelKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVs 443
Cdd:cd05109  81 STVQLV-TQLMPYGCLLDYVRENKdRIGS-------QDLLnwcVQIAKGMSYLEEVRLVHRDLAARNVLVKS---PNHV- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 444 eegdeddwisnkvmfKIGDLGHVTRISSPQVE-EGDS-----RFLANE-VLQENYSHlpKADIFALALTV--VCAAGAEP 514
Cdd:cd05109 149 ---------------KITDFGLARLLDIDETEyHADGgkvpiKWMALEsILHRRFTH--QSDVWSYGVTVweLMTFGAKP 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17865613 515 LprNGDQWHEI-----RQGRLPRiPQVLSQELTELLKVMIHPDPERRPSAMVLV 563
Cdd:cd05109 212 Y--DGIPAREIpdlleKGERLPQ-PPICTIDVYMIMVKCWMIDSECRPRFRELV 262
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
296-433 6.09e-08

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: 55.02  E-value: 6.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05602   7 SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKvLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFV 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 375 NEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05602  87 LDYINGGELFYHLQRE----RCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILL 141
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
302-435 6.14e-08

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: 54.30  E-value: 6.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIY---AIKRSKkplAGSVDEQNA--LREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05033  10 KVIGGGEFGEVCSGSLKLPGKKEidvAIKTLK---SGYSDKQRLdfLTEA---SIMGQfdHPNVIRLEGVVTKSRPVMIV 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 375 NEYCNGGSLADAVSENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05033  84 TEYMENGSLDKFLREN---DGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNS 141
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
304-556 6.44e-08

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: 54.71  E-value: 6.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVF---KCVKRLDGCIYAIKRSKKPLAGSVD------EQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05582   3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLKKATLKVRDrvrtkmERDILADV-------NHPFIVKLHYAFQTEGKLYLI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENyrVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsn 454
Cdd:cd05582  76 LDFLRGGDLFTRLSKE--VM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-------------DEDGHI-- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmfKIGDLGhvtrISSPQVEE--------GDSRFLANEVLQENySHLPKADIFALA-LTVVCAAGAepLPRNGDQWHE- 524
Cdd:cd05582 137 ----KLTDFG----LSKESIDHekkaysfcGTVEYMAPEVVNRR-GHTQSADWWSFGvLMFEMLTGS--LPFQGKDRKEt 205
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 525 ---IRQGRLPrIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05582 206 mtmILKAKLG-MPQFLSPEAQSLLRALFKRNPANR 239
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
297-434 6.50e-08

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: 55.05  E-value: 6.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREV--YAHAvlgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd07877  18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELrlLKHM---KHENVIGLLDVFTPARSLEEF 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07877  95 NDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVN 154
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
293-431 6.51e-08

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: 54.91  E-value: 6.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTefheLEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEddhml 372
Cdd:cd07879  16 RYTS----LKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHM-QHENVIGLLDVFTS----- 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 373 iqneycngGSLADAVSENYRVMSY------------FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd07879  86 --------AVSGDEFQDFYLVMPYmqtdlqkimghpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNL 148
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
302-434 6.94e-08

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: 54.11  E-value: 6.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDG---CIYAIKRSKkplAGSVDEQNalREVYAHA-VLGQ--HPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd05065  10 EVIGAGEFGEVCRGRLKLPGkreIFVAIKTLK---SGYTEKQR--RDFLSEAsIMGQfdHPNIIHLEGVVTKSRPVMIIT 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 376 EYCNGGSLADAVSENYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd05065  85 EFMENGALDSFLRQND---GQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVN 140
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
302-558 7.06e-08

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: 54.30  E-value: 7.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDgciYAIKRSKKPLAGSVDEQNALREVyahAVLGQHPHV-VRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14151  14 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEV---GVLRKTRHVnILLFMGYSTKPQLAIVTQWCEG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVsenYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdEDDWIsnkvmfKI 460
Cdd:cd14151  88 SSLYHHL---HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH-------------EDLTV------KI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRIS----SPQVEE--GDSRFLANEV--LQENYSHLPKADIFALALTVV-CAAGAEPLP--RNGDQWHE-IRQG 528
Cdd:cd14151 146 GDFGLATVKSrwsgSHQFEQlsGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYeLMTGQLPYSniNNRDQIIFmVGRG 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 17865613 529 RL-PRIPQVLS---QELTELLKVMIHPDPERRPS 558
Cdd:cd14151 226 YLsPDLSKVRSncpKAMKRLMAECLKKKRDERPL 259
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
301-557 8.04e-08

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: 54.11  E-value: 8.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSkkPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd06619   6 QEILGHGNGGTVYKAYHLLTRRILAVKVI--PLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLadavsENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseegdeddwISNKVMFKI 460
Cdd:cd06619  84 GSL-----DVYRKIP---EHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNML-------------------VNTRGQVKL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRI--SSPQVEEGDSRFLANE-VLQENYSHLpkADIFALALTVVcaagaeplprngdqwhEIRQGRLPrIPQVL 537
Cdd:cd06619 137 CDFGVSTQLvnSIAKTYVGTNAYMAPErISGEQYGIH--SDVWSLGISFM----------------ELALGRFP-YPQIQ 197
                       250       260
                ....*....|....*....|....
gi 17865613 538 SQELT----ELLKVMIHPDPERRP 557
Cdd:cd06619 198 KNQGSlmplQLLQCIVDEDPPVLP 221
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
301-562 8.13e-08

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: 54.48  E-value: 8.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEqnALREVYA-HAVLGQHPHVVRYFSAWAEDDHM-------- 371
Cdd:cd13977   5 IREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVEL--ALREFWAlSSIQRQHPNVIQLEECVLQRDGLaqrmshgs 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 372 --------LIQN--------------------EYCNGGSLadavseNYRVMSYFTEAEL-KDLLLQVGRGLRYIHSMSLV 422
Cdd:cd13977  83 sksdlyllLVETslkgercfdprsacylwfvmEFCDGGDM------NEYLLSRRPDRQTnTSFMLQLSSALAFLHRNQIV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 423 HMDIKPSNIFISRTsipnavseegdeddwiSNKVMFKIGDLG--HVTRISSPQVEE-------------GDSRFLANEVL 487
Cdd:cd13977 157 HRDLKPDNILISHK----------------RGEPILKVADFGlsKVCSGSGLNPEEpanvnkhflssacGSDFYMAPEVW 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 488 QENYShlPKADIFALAltVVCAAGAEPLP-RNGDQWHE-----IRQGR--LP-------------RIPQ----VLSQELT 542
Cdd:cd13977 221 EGHYT--AKADIFALG--IIIWAMVERITfRDGETKKEllgtyIQQGKeiVPlgeallenpklelQIPLkkkkSMNDDMK 296
                       330       340
                ....*....|....*....|
gi 17865613 543 ELLKVMIHPDPERRPSAMVL 562
Cdd:cd13977 297 QLLRDMLAANPQERPDAFQL 316
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
323-559 8.80e-08

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: 53.93  E-value: 8.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 323 IYAIKRSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAV-SENYRVMSYFTEAE 401
Cdd:cd13992  30 IKHITFSRTEKRTILQELNQLKEL-------VHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLlNREIKMDWMFKSSF 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 402 LKDLLlqvgRGLRYIHSMSL-VHMDIKPSNIFIsrtsipnavseegdEDDWisnkvMFKIGDLGhvtrISSPQVEEGDSR 480
Cdd:cd13992 103 IKDIV----KGMNYLHSSSIgYHGRLKSSNCLV--------------DSRW-----VVKLTDFG----LRNLLEEQTNHQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 481 F-----------LANEVLQENYSHL---PKADIFALALT---VVCAAGAEPLPRNGDQWH-EIRQGRLPRIPQVL----- 537
Cdd:cd13992 156 LdedaqhkkllwTAPELLRGSLLEVrgtQKGDVYSFAIIlyeILFRSDPFALEREVAIVEkVISGGNKPFRPELAvllde 235
                       250       260
                ....*....|....*....|...
gi 17865613 538 -SQELTELLKVMIHPDPERRPSA 559
Cdd:cd13992 236 fPPRLVLLVKQCWAENPEKRPSF 258
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
354-563 8.86e-08

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: 54.33  E-value: 8.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVV--RYFSAwAEDDHMLIQNEYCnGGSLADAVSENYRV-MSYFTEAELKDLLLQVGRGLRYIHS-MSLVHMDIKPS 429
Cdd:cd14001  63 NHPNIVgfRAFTK-SEDGSLCLAMEYG-GKSLNDLIEERYEAgLGPFPAATILKVALSIARALEYLHNeKKILHGDIKSG 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 430 NIFISrtsipnavseeGDEDdwisnkvMFKIGDLG-------HVTRISSPQVEE-GDSRFLANEVLQENYSHLPKADIFA 501
Cdd:cd14001 141 NVLIK-----------GDFE-------SVKLCDFGvslplteNLEVDSDPKAQYvGTEPWKAKEALEEGGVITDKADIFA 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 502 LALTV-----VCAAGAEPLPRNGD----------QWHEIRQGRLPRIPQVLS-------QELTELLKVMIHPDPERRPSA 559
Cdd:cd14001 203 YGLVLwemmtLSVPHLNLLDIEDDdedesfdedeEDEEAYYGTLGTRPALNLgelddsyQKVIELFYACTQEDPKDRPSA 282

                ....
gi 17865613 560 MVLV 563
Cdd:cd14001 283 AHIV 286
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
296-566 8.93e-08

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: 53.97  E-value: 8.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLaGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATV-NSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGgSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHS-MSLVHMDIKPSNIFISRtsipnavseEGDeddwisn 454
Cdd:cd06617  80 EVMDT-SLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINR---------NGQ------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDL---GHVTRISSPQVEEGDSRFLANEVL--QENYSHLP-KADIFALALTVV-CAAGAEPLPRNGDQWHEIRQ 527
Cdd:cd06617 143 ---VKLCDFgisGYLVDSVAKTIDAGCKPYMAPERInpELNQKGYDvKSDVWSLGITMIeLATGRFPYDSWKTPFQQLKQ 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 528 ---GRLPRIP-QVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd06617 220 vveEPSPQLPaEKFSPEFQDFVNKCLKKNYKERPNYPELLQHP 262
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
306-558 9.36e-08

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: 53.66  E-value: 9.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 306 SGEFGSVFKCVKRLDGCIYAIKRSKKPLagSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLA- 384
Cdd:cd14027   3 SGGFGKVSLCFHRTQGLVVLKTVYTGPN--CIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMh 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 385 --DAVSENYRVMSYFteaelkdlLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKIGD 462
Cdd:cd14027  81 vlKKVSVPLSVKGRI--------ILEIIEGMAYLHGKGVIHKDLKPENILV-------------DNDFHI------KIAD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVT--RISSPQVEE---------------GDSRFLANEVLQE-NYSHLPKADIFALALTV-VCAAGAEPLP--RNGDQ 521
Cdd:cd14027 134 LGLASfkMWSKLTKEEhneqrevdgtakknaGTLYYMAPEHLNDvNAKPTEKSDVYSFAIVLwAIFANKEPYEnaINEDQ 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 522 -WHEIRQGRLP---RIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14027 214 iIMCIKSGNRPdvdDITEYCPREIIDLMKLCWEANPEARPT 254
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
298-431 9.67e-08

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: 53.62  E-value: 9.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLagsvdEQNAL-REVYAHAVLGQHPHVVR-YFSAWAEDDHMLIQN 375
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDS-----KHPQLeYEAKVYKLLQGGPGIPRlYWFGQEGDYNVMVMD 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 376 EYcnGGSLADAVSENYRVMSYFTEAELKDLLLQvgRgLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14016  77 LL--GPSLEDLFNKCGRKFSLKTVLMLADQMIS--R-LEYLHSKGYIHRDIKPENF 127
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
302-558 1.01e-07

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: 53.44  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRlDGCIYAIKrSKKPlaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd05034   1 KKLGAGQFGEVWMGVWN-GTTKVAVK-TLKP--GTMSPEAFLQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseegdeddwISNKVMFKIG 461
Cdd:cd05034  76 SLLDYLRTGEG--RALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNIL-------------------VGENNVCKVA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGhVTRIsspqVEEG------DSRF----LANEVLqeNYSHLP-KADI--FALALTVVCAAGAEPLP--RNGDQWHEIR 526
Cdd:cd05034 135 DFG-LARL----IEDDeytareGAKFpikwTAPEAA--LYGRFTiKSDVwsFGILLYEIVTYGRVPYPgmTNREVLEQVE 207
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 527 QG-RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05034 208 RGyRMPK-PPGCPDELYDIMLQCWKKEPEERPT 239
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
354-566 1.01e-07

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: 53.96  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAE----DDHMLIQNEYCNGGSLADAVsENYRVMSyftEAELKDLLLQVGRGLRYIHSMS--LVHMDIK 427
Cdd:cd14031  67 QHPNIVRFYDSWESvlkgKKCIVLVTELMTSGTLKTYL-KRFKVMK---PKVLRSWCRQILKGLQFLHTRTppIIHRDLK 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 428 PSNIFIsrTSIPNAVseegdeddwisnkvmfKIGDLGHVT--RISSPQVEEGDSRFLANEVLQENYSHlpKADIFALALT 505
Cdd:cd14031 143 CDNIFI--TGPTGSV----------------KIGDLGLATlmRTSFAKSVIGTPEFMAPEMYEEHYDE--SVDVYAFGMC 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 506 VVCAAGAE-PLP--RNGDQ-WHEIRQGRLP-RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14031 203 MLEMATSEyPYSecQNAAQiYRKVTSGIKPaSFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHA 268
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
354-558 1.01e-07

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 53.64  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAEDDHMLIQnEYCNGGSLadavsENY--RVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd05037  60 SHKHLVKLYGVCVADENIMVQ-EYVRYGPL-----DKYlrRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNI 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 432 FISRtsipnavseegdeDDWISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLP-KADIFALALTV--VC 508
Cdd:cd05037 134 LLAR-------------EGLDGYPPFIKLSDPGVPITVLSREERVDRIPWIAPECLRNLQANLTiAADKWSFGTTLweIC 200
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 509 AAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05037 201 SGGEEPLSALSSQEKLQFYEDQHQLPAPDCAELAELIMQCWTYEPTKRPS 250
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
304-434 1.06e-07

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: 51.29  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsvDEQNALREVYAHAVL------GQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGD-------DVNNEEGEDLESEMDilrrlkGLELNIPKVLVTEDVDGPNILLMEL 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 378 CNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd13968  74 VKGGTLIAYTQE-----EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS 125
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
354-580 1.09e-07

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: 54.22  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENYrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd08216  57 QHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKTHF--PEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILI 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 434 S----------RTSIPnaVSEEGDEddwisNKVMFkigdlghvtriSSPQVEEGDSRFLANEVLQENYS-HLPKADIFAL 502
Cdd:cd08216 135 SgdgkvvlsglRYAYS--MVKHGKR-----QRVVH-----------DFPKSSEKNLPWLSPEVLQQNLLgYNEKSDIYSV 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 503 ALTvVC--AAGAEP--------------------------LPRNGDQWHEIRQGRLPR--------IP--QVLSQELTEL 544
Cdd:cd08216 197 GIT-ACelANGVVPfsdmpatqmllekvrgttpqlldcstYPLEEDSMSQSEDSSTEHpnnrdtrdIPyqRTFSEAFHQF 275
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 545 LKVMIHPDPERRPSAMVLVKHSVLLSASRKSA---EQLR 580
Cdd:cd08216 276 VELCLQRDPELRPSASQLLAHSFFKQCRRSNTsllDLLK 314
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
297-434 1.09e-07

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: 54.11  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplAGSVDeQNALREVYAHA---VLGQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05610   5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKK--ADMIN-KNMVHQVQAERdalALSKSPFIVHLYYSLQSANNVYL 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 374 QNEYCNGGSLADAVSenyrVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd05610  82 VMEYLIGGDVKSLLH----IYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLIS 138
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
302-431 1.10e-07

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: 53.71  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14104   6 EELGRGQFGIVHRCVETSSKKTYMAKFVK---VKGADQVLVKKEISILNIA-RHRNILRLHESFESHEELVMIFEFISGV 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSeNYRVmsYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14104  82 DIFERIT-TARF--ELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENI 128
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
302-431 1.21e-07

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: 53.74  E-value: 1.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSvdEQNALREVyahAVLG--QHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd14169   9 EKLGEGAFSEVVLAQERGSQRLVALKcIPKKALRGK--EAMVENEI---AVLRriNHENIVSLEDIYESPTHLYLAMELV 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 379 NGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14169  84 TGGELFDRIIER----GSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENL 132
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
302-558 1.44e-07

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: 53.22  E-value: 1.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvDEQNALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPD-LKRKFLQEA---RILKQydHPNIVKLIGVCVQKQPIMIVMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYRVMsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFK 459
Cdd:cd05041  77 GGSLLTFLRKKGARL---TVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNV-------------------LK 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGhVTR-------ISSPQVEEGDSRFLANEVLqeNYS-HLPKADI--FALALTVVCAAGAEPLP--RNGDQWHEIRQ 527
Cdd:cd05041 135 ISDFG-MSReeedgeyTVSDGLKQIPIKWTAPEAL--NYGrYTSESDVwsFGILLWEIFSLGATPYPgmSNQQTREQIES 211
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 528 G-RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05041 212 GyRMPA-PELCPEAVYRLMLQCWAYDPENRPS 242
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
284-431 1.44e-07

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: 53.92  E-value: 1.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 284 TITESNMKSRyttEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVD-----EQnalREVYAHAvlgQHPH 357
Cdd:cd05596  17 EITKLRMNAE---DFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLlSKFEMIKRSDsaffwEE---RDIMAHA---NSEW 87
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 358 VVRYFSAWAEDDHMLIQNEYCNGGSLADAVSeNYRV---MSYFTEAELkdlLLqvgrGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd05596  88 IVQLHYAFQDDKYLYMVMDYMPGGDLVNLMS-NYDVpekWARFYTAEV---VL----ALDAIHSMGFVHRDVKPDNM 156
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
299-568 1.57e-07

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: 53.19  E-value: 1.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEK-IGSGEFgSVFKCVKRL-DGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd14074   5 YDLEEtLGRGHF-AVVKLARHVfTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLV-QHPNVVRLYEVIDTQTKLYLILE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwisNKV 456
Cdd:cd14074  83 LGDGGDMYDYIMKHENGLN---EDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFE------------------KQG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISSPQVEE---GDSRFLANEVLQENYSHLPKADIFALAL---TVVCaaGAEPLPRNGDQ--WHEIRQG 528
Cdd:cd14074 142 LVKLTDFGFSNKFQPGEKLEtscGSLAYSAPEILLGDEYDAPAVDIWSLGVilyMLVC--GQPPFQEANDSetLTMIMDC 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 529 RLpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14074 220 KY-TVPAHVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
304-434 1.60e-07

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: 52.95  E-value: 1.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVfkCVKRL------DGCIyAIKRSKkplAGSVDEQNalREVYAHA-VLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05066  12 IGAGEFGEV--CSGRLklpgkrEIPV-AIKTLK---AGYTEKQR--RDFLSEAsIMGQfdHPNIIHLEGVVTRSKPVMIV 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd05066  84 TEYMENGSLDAFLRKH---DGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVN 140
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
298-431 1.71e-07

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: 53.39  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKplagSVDEQNALREVYAHA-VLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd05574   3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKvLDKE----EMIKRNKVKRVLTEReILATldHPFLPTLYASFQTSTHLCF 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 374 QNEYCNGGSLADAVseNYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd05574  79 VMDYCPGGELFRLL--QKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENI 134
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
304-431 1.80e-07

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: 52.92  E-value: 1.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSV---DEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREvceSELNVLRRV-------RHTNIIQLIEVFETKERVYMVMELATG 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 381 GSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14087  82 GELFDRIIAKGS----FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENL 128
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
302-559 1.94e-07

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 52.98  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKcvkrldGCIYA-------IKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05042   1 QEIGNGWFGKVLL------GEIYSgtsvaqvVVKELKASANPKEQDTFLKEGQPYRIL-QHPNILQCLGQCVEAIPYLLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVMSYFTEAE-LKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseegdeddwIS 453
Cdd:cd05042  74 MEFCDLGDLKAYLRSEREHERGDSDTRtLQRMACEVAAGLAHLHKLNFVHSDLALRNCL-------------------LT 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 NKVMFKIGD--LGHvTRISSPQVEEGDS-----RFLANEVLQENYSHLPKAD------IFALALTV--VCAAGAEPLPRN 518
Cdd:cd05042 135 SDLTVKIGDygLAH-SRYKEDYIETDDKlwfplRWTAPELVTEFHDRLLVVDqtkysnIWSLGVTLweLFENGAQPYSNL 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17865613 519 GDQ---WHEIRQGRL----PRIPQVLSQELTELLKVMIHPdPERRPSA 559
Cdd:cd05042 214 SDLdvlAQVVREQDTklpkPQLELPYSDRWYEVLQFCWLS-PEQRPAA 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
286-556 2.06e-07

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: 53.55  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 286 TESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEqnALREVYAHAVLG--QHPHVVRYFS 363
Cdd:cd05593   5 STTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDE--VAHTLTESRVLKntRHPFLTSLKY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 364 AWAEDDHMLIQNEYCNGGSLADAVSENyRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavs 443
Cdd:cd05593  83 SFQTKDRLCFVMEYVNGGELFFHLSRE-RV---FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 444 eegDEDDWIsnkvmfKIGDLG----HVTRISSPQVEEGDSRFLANEVLQENySHLPKADIFALALTVvcaagaeplprng 519
Cdd:cd05593 149 ---DKDGHI------KITDFGlckeGITDAATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVM------------- 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 520 dqwHEIRQGRLP------------------RIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05593 206 ---YEMMCGRLPfynqdheklfelilmediKFPRTLSADAKSLLSGLLIKDPNKR 257
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
301-558 2.27e-07

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: 52.79  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRlDGCIYAIKRSKkplAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05068  13 LRKLGSGQFGEVWEGLWN-NTTPVAVKTLK---PGTMDPEDFLREAQIMKKL-RHPKLIQLYAVCTLEEPIYIITELMKH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFKI 460
Cdd:cd05068  88 GSLLEYLQGKGRSLQL---PQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNI-------------------CKV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQVEEG--DSRF----LANEVLqeNYSHLP-KADI--FALALTVVCAAGAEPLP--RNGDQWHEIRQG- 528
Cdd:cd05068 146 ADFGLARVIKVEDEYEAreGAKFpikwTAPEAA--NYNRFSiKSDVwsFGILLTEIVTYGRIPYPgmTNAEVLQQVERGy 223
                       250       260       270
                ....*....|....*....|....*....|
gi 17865613 529 RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05068 224 RMPC-PPNCPPQLYDIMLECWKADPMERPT 252
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
342-442 2.35e-07

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: 52.71  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 342 ALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQN-EYCNGGSLaDAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMS 420
Cdd:cd13990  51 ALREYEIHKSL-DHPRIVKLYDVFEIDTDSFCTVlEYCDGNDL-DFYLKQHKSIP---EREARSIIMQVVSALKYLNEIK 125
                        90       100
                ....*....|....*....|....
gi 17865613 421 --LVHMDIKPSNIFISRTSIPNAV 442
Cdd:cd13990 126 ppIIHYDLKPGNILLHSGNVSGEI 149
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
303-571 2.52e-07

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: 52.72  E-value: 2.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVfkcvkrldgCIYAIKRSKKPLA-GSVD-EQNALREVYAHAVL----GQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd06657  27 KIGEGSTGIV---------CIATVKSSGKLVAvKKMDlRKQQRRELLFNEVVimrdYQHENVVEMYNSYLVGDELWVVME 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSipnavseegdeddwisnkv 456
Cdd:cd06657  98 FLEGGALTDIVTH-----TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG------------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGDLGHVTRISS--PQVEE--GDSRFLANEVLQEnYSHLPKADIFALALTVVCAAGAEPLPRNG---DQWHEIRQGR 529
Cdd:cd06657 154 RVKLSDFGFCAQVSKevPRRKSlvGTPYWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDNL 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 530 LPRIP--QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLSA 571
Cdd:cd06657 233 PPKLKnlHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKA 276
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
297-556 2.79e-07

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: 52.41  E-value: 2.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SK------KPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDD 369
Cdd:cd14209   2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIlDKqkvvklKQVEHTLNEKRILQAI-------NFPFLVKLEYSFKDNS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 370 HMLIQNEYCNGGSLAdavsENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDED 449
Cdd:cd14209  75 NLYMVMEYVPGGEMF----SHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI-------------DQQ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 DWIsnkvmfKIGDLGHVTRISSPQVEE-GDSRFLANEVLQeNYSHLPKADIFALALTVV-CAAGAEPLprNGDQ----WH 523
Cdd:cd14209 138 GYI------KVTDFGFAKRVKGRTWTLcGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYeMAAGYPPF--FADQpiqiYE 208
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 524 EIRQGRLpRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd14209 209 KIVSGKV-RFPSHFSSDLKDLLRNLLQVDLTKR 240
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
297-580 2.91e-07

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: 53.00  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFkCVKRLDGC----IYAIKRSKKPL----AGSVDEQNALREVYAHavLGQHPHVVRYFSAWAED 368
Cdd:cd05614   1 NFELLKVLGTGAYGKVF-LVRKVSGHdankLYAMKVLRKAAlvqkAKTVEHTRTERNVLEH--VRQSPFLVTLHYAFQTD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDE 448
Cdd:cd05614  78 AKLHLILDYVSGGELFTHLYQR----DHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL-------------DS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 DDWISnkvmfkIGDLGHVTRISSPQVEE-----GDSRFLANEVLQENYSHLPKADIFALALTVV-CAAGAEPLPRNGDQW 522
Cdd:cd05614 141 EGHVV------LTDFGLSKEFLTEEKERtysfcGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFeLLTGASPFTLEGEKN 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 523 HEIRQGRL-----PRIPQVLSQELTELLKVMIHPDPERRpsamvlvkhsvlLSASRKSAEQLR 580
Cdd:cd05614 215 TQSEVSRRilkcdPPFPSFIGPVARDLLQKLLCKDPKKR------------LGAGPQGAQEIK 265
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
301-438 3.49e-07

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: 52.55  E-value: 3.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIK--RSKKPLagsvdEQNALREVyahAVL--------GQHPHVVRYFSAWAEDDH 370
Cdd:cd14210  18 LSVLGKGSFGQVVKCLDHKTGQLVAIKiiRNKKRF-----HQQALVEV---KILkhlndndpDDKHNIVRYKDSFIFRGH 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLI------QNEYcnggSLADavSENYRVMSY-----FTeaelkdllLQVGRGLRYIHSMSLVHMDIKPSNIFI---SRT 436
Cdd:cd14210  90 LCIvfellsINLY----ELLK--SNNFQGLSLslirkFA--------KQILQALQFLHKLNIIHCDLKPENILLkqpSKS 155

                ..
gi 17865613 437 SI 438
Cdd:cd14210 156 SI 157
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
303-435 3.52e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 52.17  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  303 KIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALrEVYAHAVLGQHPHVVR-YFSAWAEDDHMLIQnEYCNGG 381
Cdd:PHA03390  23 KLIDGKFGKVSVLKHKPTQKLFVQKIIKA------KNFNAI-EPMVHQLMKDNPNFIKlYYSVTTLKGHVLIM-DYIKDG 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17865613  382 SLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:PHA03390  95 DLFDLLKKEGK----LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR 144
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
304-495 3.84e-07

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: 52.14  E-value: 3.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRldGCIYAIKRSKK--PLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14159   1 IGEGGFGCVYQAVMR--NTEYAVKRLKEdsELDWSVVKNSFLTEVEKLSRF-RHPNIVDLAGYSAQQGNYCLIYVYLPNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENYRVMSYFTEAELkDLLLQVGRGLRYIH--SMSLVHMDIKPSNIFISRTSIPnavseegdeddwisnkvmfK 459
Cdd:cd14159  78 SLEDRLHCQVSCPCLSWSQRL-HVLLGTARAIQYLHsdSPSLIHGDVKSSNILLDAALNP-------------------K 137
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17865613 460 IGDLGhVTRISSPQVEEGDSRFLA-NEVLQENYSHLP 495
Cdd:cd14159 138 LGDFG-LARFSRRPKQPGMSSTLArTQTVRGTLAYLP 173
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
304-559 4.96e-07

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 51.49  E-value: 4.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRldGCIYAIKRSKKPLAGSVDEQNALreVYAHAvlgQHPHVVrYFSAWAEDDHMLIQnEYCNGGSL 383
Cdd:cd14068   2 LGDGGFGSVYRAVYR--GEDVAVKIFNKHTSFRLLRQELV--VLSHL---HHPSLV-ALLAAGTAPRMLVM-ELAPKGSL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 384 aDAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrTSIPNAvseegdeddwisnKVMFKIGDL 463
Cdd:cd14068  73 -DALLQQDN--ASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLF-TLYPNC-------------AIIAKIADY 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 464 G---HVTRISSpQVEEGDSRFLANEVLQENYSHLPKADIFALAL----TVVCAAGAEPLPRNGDQWHEIR-QGRLPRIPQ 535
Cdd:cd14068 136 GiaqYCCRMGI-KTSEGTPGFRAPEVARGNVIYNQQADVYSFGLllydILTCGERIVEGLKFPNEFDELAiQGKLPDPVK 214
                       250       260
                ....*....|....*....|....*...
gi 17865613 536 VLS----QELTELLKVMIHPDPERRPSA 559
Cdd:cd14068 215 EYGcapwPGVEALIKDCLKENPQCRPTS 242
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
302-502 4.99e-07

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: 51.65  E-value: 4.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvdEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14090   8 ELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHS--RSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSEnyRVmsYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVSEegdeddwisnkvmFKIG 461
Cdd:cd14090  86 PLLSHIEK--RV--HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCES---MDKVSP-------------VKIC 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 462 DL----------GHVTRISSPQVEE--GDSRFLANEVLQ----ENYSHLPKADIFAL 502
Cdd:cd14090 146 DFdlgsgiklssTSMTPVTTPELLTpvGSAEYMAPEVVDafvgEALSYDKRCDLWSL 202
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
297-436 7.06e-07

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: 51.77  E-value: 7.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ---NALREVYAHAvlgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05629   2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLahvKAERDVLAES---DSPWVVSLYYSFQDAQYLYL 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 374 QNEYCNGGSLADAVSeNYRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05629  79 IMEFLPGGDLMTMLI-KYDT---FSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRG 137
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
301-558 7.17e-07

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: 51.22  E-value: 7.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVkrLDGCIYAIKRSKKPlaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDhMLIQNEYCNG 380
Cdd:cd05070  14 IKRLGNGQFGEVWMGT--WNGNTKVAIKTLKP--GTMSPESFLEEAQIMKKL-KHDKLVQLYAVVSEEP-IYIVTEYMSK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENY-RVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwisNKVMFK 459
Cdd:cd05070  88 GSLLDFLKDGEgRALKL---PNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVG-------------------NGLICK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISSPQ-VEEGDSRFLANEVLQEN--YSHLP-KADI--FALALTVVCAAGAEPLP--RNGDQWHEIRQG-RL 530
Cdd:cd05070 146 IADFGLARLIEDNEyTARQGAKFPIKWTAPEAalYGRFTiKSDVwsFGILLTELVTKGRVPYPgmNNREVLEQVERGyRM 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 531 PrIPQVLSQELTELlkvMIH---PDPERRPS 558
Cdd:cd05070 226 P-CPQDCPISLHEL---MIHcwkKDPEERPT 252
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
301-558 7.75e-07

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: 51.17  E-value: 7.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCvkRLD------GCIYAIKRskkpLAGSVDE--QNALREVYAHAVLgQHPHVVRY----FSAWAED 368
Cdd:cd14205   9 LQQLGKGNFGSVEMC--RYDplqdntGEVVAVKK----LQHSTEEhlRDFEREIEILKSL-QHDNIVKYkgvcYSAGRRN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIqnEYCNGGSLADAVSENYRVMSYfteaelKDLLL---QVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavsee 445
Cdd:cd14205  82 LRLIM--EYLPYGSLRDYLQKHKERIDH------IKLLQytsQICKGMEYLGTKRYIHRDLATRNIL------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 446 gdeddwISNKVMFKIGDLGhVTRIsSPQVEE-------GDSRFL--ANEVLQENYSHLpKADIFALALTVV--------- 507
Cdd:cd14205 141 ------VENENRVKIGDFG-LTKV-LPQDKEyykvkepGESPIFwyAPESLTESKFSV-ASDVWSFGVVLYelftyieks 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 508 CAAGAEPLPRNGDQ-------WHEI----RQGRLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14205 212 KSPPAEFMRMIGNDkqgqmivFHLIellkNNGRLPR-PDGCPDEIYMIMTECWNNNVNQRPS 272
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
302-435 8.00e-07

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: 50.73  E-value: 8.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14079   8 KTLGVGSFGKVKLAEHELTGHKVAVKiLNRQKIKSLDMEEKIRREIQILKLF-RHPHIIRLYEVIETPTDIFMVMEYVSG 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 381 GSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd14079  87 GELFDYIVQKGRL----SEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDS 137
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
302-434 8.04e-07

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: 50.88  E-value: 8.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCV---KRLDGCIYAIKRSKKPLAGSVDEqNALREVYAHAVLgQHPHVVRYFSAwAEDDHMLIQNEYC 378
Cdd:cd05056  12 RCIGEGQFGDVYQGVymsPENEKIAVAVKTCKNCTSPSVRE-KFLQEAYIMRQF-DHPHIVKLIGV-ITENPVWIVMELA 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 379 NGGSLADAVSENYrvmsyfTEAELKDLLL---QVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd05056  89 PLGELRSYLQVNK------YSLDLASLILyayQLSTALAYLESKRFVHRDIAARNVLVS 141
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
301-558 8.22e-07

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: 50.81  E-value: 8.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKcvKRLDGCIyAIKRSKkpLAGSVDEQ-NALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd14063   5 KEVIGKGRFGRVHR--GRWHGDV-AIKLLN--IDYLNEEQlEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENYrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKVMfk 459
Cdd:cd14063  80 GRTLYSLIHERK---EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE------------------NGRVV-- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLG--HVTRISSPQVEEGDSR-------FLANEVL------QENYSHLP---KADIFALaltvvcaagaeplprnGDQ 521
Cdd:cd14063 137 ITDFGlfSLSGLLQPGRREDTLVipngwlcYLAPEIIralspdLDFEESLPftkASDVYAF----------------GTV 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 522 WHEIRQGRLP--------RIPQV------------LSQELTELLKVMIHPDPERRPS 558
Cdd:cd14063 201 WYELLAGRWPfkeqpaesIIWQVgcgkkqslsqldIGREVKDILMQCWAYDPEKRPT 257
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
298-434 8.59e-07

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: 51.59  E-value: 8.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd07878  17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHM-KHENVIGLLDVFTPATSIENFNEV 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 378 CNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07878  96 YLVTNLMGADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVN 152
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
293-538 1.00e-06

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: 51.54  E-value: 1.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEFHELEK-IGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQN--ALREVYAHAvlgQHPHVVRYFSAWAED 368
Cdd:cd05622  69 RMKAEDYEVVKvIGRGAFGEVQLVRHKSTRKVYAMKLlSKFEMIKRSDSAFfwEERDIMAFA---NSPWVVQLFYAFQDD 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHMLIQNEYCNGGSLADAVSeNYRVMSYFTEAELKDLLLqvgrGLRYIHSMSLVHMDIKPSNIFISRT--------SIPN 440
Cdd:cd05622 146 RYLYMVMEYMPGGDLVNLMS-NYDVPEKWARFYTAEVVL----ALDAIHSMGFIHRDVKPDNMLLDKSghlkladfGTCM 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 441 AVSEEG--------DEDDWISNKVMFKIGDLGHVTR--------ISSPQVEEGDSRFLANEVL--------QENYSHLPK 496
Cdd:cd05622 221 KMNKEGmvrcdtavGTPDYISPEVLKSQGGDGYYGRecdwwsvgVFLYEMLVGDTPFYADSLVgtyskimnHKNSLTFPD 300
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 497 -ADIFALALTVVCA-----------AGAEPLPRNG----DQ--WHEIRQGRLPRIPQVLS 538
Cdd:cd05622 301 dNDISKEAKNLICAfltdrevrlgrNGVEEIKRHLffknDQwaWETLRDTVAPVVPDLSS 360
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
298-556 1.05e-06

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: 50.79  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIK-------RSKKPLAGSVDEQNALREVYAHavlgqhpHVVRYFSAWAEDDH 370
Cdd:cd05630   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKklekkriKKRKGEAMALNEKQILEKVNSR-------FVVSLAYAYETKDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSL-------ADAVSENYRVMSYFTEaelkdlllqVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavs 443
Cdd:cd05630  75 LCLVLTLMNGGDLkfhiyhmGQAGFPEARAVFYAAE---------ICCGLEDLHRERIVYRDLKPENILL---------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 444 eegDEDDWIsnkvmfKIGDLG---HVTRISSPQVEEGDSRFLANEVLQ-ENYSHLPkaDIFALA-LTVVCAAGAEPLPRN 518
Cdd:cd05630 136 ---DDHGHI------RISDLGlavHVPEGQTIKGRVGTVGYMAPEVVKnERYTFSP--DWWALGcLLYEMIAGQSPFQQR 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17865613 519 GDQwheIRQGRLPRIPQVLSQELTE--------LLKVMIHPDPERR 556
Cdd:cd05630 205 KKK---IKREEVERLVKEVPEEYSEkfspqarsLCSMLLCKDPAER 247
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
301-436 1.37e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 51.33  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgsvDEQNAL----REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:NF033483  12 GERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDLA---RDPEFVarfrREAQSAASL-SHPNIVSVYDVGEDGGIPYIVME 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  377 YCNGGSLADAVSENYRvMSYfTEAElkDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:NF033483  88 YVDGRTLKDYIREHGP-LSP-EEAV--EIMIQILSALEHAHRNGIVHRDIKPQNILITKD 143
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
382-564 1.48e-06

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: 50.77  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENYRVMSYFTEA-ELKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvm 457
Cdd:cd14207 158 SLSDVEEEEEDSGDFYKRPlTMEDLIsysFQVARGMEFLSSRKCIHRDLAARNILLSENNV------------------- 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRI-SSPQ-VEEGDSR----FLANE-VLQENYShlPKADI--FALALTVVCAAGAEPLPR---NGDQWHEI 525
Cdd:cd14207 219 VKICDFGLARDIyKNPDyVRKGDARlplkWMAPEsIFDKIYS--TKSDVwsYGVLLWEIFSLGASPYPGvqiDEDFCSKL 296
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17865613 526 RQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd14207 297 KEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVE 335
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
303-558 1.50e-06

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: 49.91  E-value: 1.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVkrLDGCIYAIKRSKKPlaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDhMLIQNEYCNGGS 382
Cdd:cd14203   2 KLGQGCFGEVWMGT--WNGTTKVAIKTLKP--GTMSPEAFLEEAQIMKKL-RHDKLVQLYAVVSEEP-IYIVTEFMSKGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseegdeddwISNKVMFKIGD 462
Cdd:cd14203  76 LLDFLKDGEG--KYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANIL-------------------VGDNLVCKIAD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSpqveegdsrflaNEVLQENYSHLP----------------KADI--FALALTVVCAAGAEPLP--RNGDQW 522
Cdd:cd14203 135 FGLARLIED------------NEYTARQGAKFPikwtapeaalygrftiKSDVwsFGILLTELVTKGRVPYPgmNNREVL 202
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 523 HEIRQG-RLPrIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14203 203 EQVERGyRMP-CPPGCPESLHELMCQCWRKDPEERPT 238
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
304-556 1.70e-06

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: 50.46  E-value: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDvECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddwisnkvmFKIGD 462
Cdd:cd05592  83 LMFHIQQSGR----FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDR---------EGH----------IKIAD 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LG----HVTRISSPQVEEGDSRFLANEVLQ-ENYSHlpKADIFALA-LTVVCAAGAEPLprNGDQ----WHEIRQGRlPR 532
Cdd:cd05592 140 FGmckeNIYGENKASTFCGTPDYIAPEILKgQKYNQ--SVDWWSFGvLLYEMLIGQSPF--HGEDedelFWSICNDT-PH 214
                       250       260
                ....*....|....*....|....
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05592 215 YPRWLTKEAASCLSLLLERNPEKR 238
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
304-555 1.71e-06

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: 49.99  E-value: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL-REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14162   8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLpREIEVIKGL-KHPNLICFYEAIETTSRVYIIMELAENGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDwisnkvMFKIGD 462
Cdd:cd14162  87 LLDYIRKN----GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL-------------DKNN------NLKITD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQveegDSRFLANEVLQENYSHLPK------------ADIFALAL---TVVCAAgaepLPRNGDQWH---- 523
Cdd:cd14162 144 FGFARGVMKTK----DGKPKLSETYCGSYAYASPeilrgipydpflSDIWSMGVvlyTMVYGR----LPFDDSNLKvllk 215
                       250       260       270
                ....*....|....*....|....*....|...
gi 17865613 524 EIRQG-RLPRIPQVlSQELTELLKVMIHPDPER 555
Cdd:cd14162 216 QVQRRvVFPKNPTV-SEECKDLILRMLSPVKKR 247
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
304-558 1.74e-06

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: 49.95  E-value: 1.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsVDEQNA---LREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIR-----FDEETQrtfLKEVKVMRCL-EHPNVLKFIGVLYKDKRLNFITEYIKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSEnyrVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsRTSIPNAVSEEGdeddwISNKVMFKI 460
Cdd:cd14221  75 GTLRGIIKS---MDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLV-RENKSVVVADFG-----LARLMVDEK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGHVTRISSPQVEE-----GDSRFLANEVLQeNYSHLPKADIFALALtVVCA----AGAEP--LPRNGDQWHEIRqGR 529
Cdd:cd14221 146 TQPEGLRSLKKPDRKKrytvvGNPYWMAPEMIN-GRSYDEKVDVFSFGI-VLCEiigrVNADPdyLPRTMDFGLNVR-GF 222
                       250       260       270
                ....*....|....*....|....*....|
gi 17865613 530 LPR-IPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14221 223 LDRyCPPNCPPSFFPIAVLCCDLDPEKRPS 252
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
302-558 1.74e-06

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: 50.02  E-value: 1.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCV--KRLDGCIYAIKRSKKPLAGSVDEQNALREVyahavlgQHPHVVRyFSAWAEDDHMLIQNEYCN 379
Cdd:cd05073  17 KKLGAGQFGEVWMATynKHTKVAVKTMKPGSMSVEAFLAEANVMKTL-------QHDKLVK-LHAVVTKEPIYIITEFMA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVS--ENYRVMSyfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavseegdeddwisnkVM 457
Cdd:cd05073  89 KGSLLDFLKsdEGSKQPL----PKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSAS-------------------LV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 458 FKIGDLGHVTRISSPQ--VEEGDS---RFLANEVLqeNY-SHLPKADI--FALALTVVCAAGAEPLP--RNGDQWHEIRQ 527
Cdd:cd05073 146 CKIADFGLARVIEDNEytAREGAKfpiKWTAPEAI--NFgSFTIKSDVwsFGILLMEIVTYGRIPYPgmSNPEVIRALER 223
                       250       260       270
                ....*....|....*....|....*....|..
gi 17865613 528 G-RLPRIpQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05073 224 GyRMPRP-ENCPEELYNIMMRCWKNRPEERPT 254
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
297-557 1.84e-06

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: 50.43  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd06649   6 DFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQ-IIREL---QVLHEcnSPYIVGFYGAFYSDGEISIC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSM-SLVHMDIKPSNIFI-SRTSIpnavseegdeddwi 452
Cdd:cd06649  82 MEHMDGGSLDQVLKEAKRI----PEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVnSRGEI-------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 snkvmfKIGDLGHVTRISSPQVEE--GDSRFLANEVLQENYSHLpKADIFALALTVV-CAAGAEPLPRNGDQWHEIRQGR 529
Cdd:cd06649 144 ------KLCDFGVSGQLIDSMANSfvGTRSYMSPERLQGTHYSV-QSDIWSMGLSLVeLAIGRYPIPPPDAKELEAIFGR 216
                       250       260
                ....*....|....*....|....*...
gi 17865613 530 lpripQVLSQELTELLKVMIHPDPERRP 557
Cdd:cd06649 217 -----PVVDGEEGEPHSISPRPRPPGRP 239
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
297-433 1.97e-06

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: 50.11  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplAGSVDE---QNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIR---LESEEEgvpSTAIREISLLKEL-QHPNIVCLEDVLMQENRLYL 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 374 QNEY--CNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07861  77 VFEFlsMDLKKYLDSLPKG----KYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLI 134
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
301-433 2.07e-06

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: 49.85  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDD---HMLIQnEY 377
Cdd:cd14132  23 IRKIGRGKYSEVFEGINIGNNEKVVIKVLKP-----VKKKKIKREIKILQNLRGGPNIVKLLDVVKDPQsktPSLIF-EY 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 378 CNggsladavSENYRVM-SYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14132  97 VN--------NTDFKTLyPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI 145
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
304-565 2.36e-06

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: 49.70  E-value: 2.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSK-KPLAGSVDEQNALREVYAHAVLG-QHPHVVRYFSAWAE--DDHMLIQNEYCN 379
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGRELAAKQVQfDPESPETSKEVSALECEIQLLKNlQHERIVQYYGCLRDraEKTLTIFMEYMP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVsenyRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisRTSIPNAvseegdeddwisnkvmfK 459
Cdd:cd06651  95 GGSVKDQL----KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNV-----------------K 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTRISSPQVE-------EGDSRFLANEVLQ-ENYSHlpKADIFALALTVVCAAGAEPlprngdQWHEIR----- 526
Cdd:cd06651 152 LGDFGASKRLQTICMSgtgirsvTGTPYWMSPEVISgEGYGR--KADVWSLGCTVVEMLTEKP------PWAEYEamaai 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 527 -----QGRLPRIPQVLSQELTELLKvMIHPDPERRPSAMVLVKH 565
Cdd:cd06651 224 fkiatQPTNPQLPSHISEHARDFLG-CIFVEARHRPSAEELLRH 266
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
301-433 3.07e-06

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: 49.28  E-value: 3.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAED-DHMLIQ 374
Cdd:cd14040  11 LHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKEL-DHPRIVKLYDYFSLDtDTFCTV 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 375 NEYCNGGSLaDAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMS--LVHMDIKPSNIFI 433
Cdd:cd14040  90 LEYCEGNDL-DFYLKQHKLMS---EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL 146
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
303-501 3.15e-06

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: 49.42  E-value: 3.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKcvKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHaVLG--QHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd14158  22 KLGEGGFGVVFK--GYINDKNVAVKKLAAMVDISTEDLTKQFEQEIQ-VMAkcQHENLVELLGYSCDGPQLCLVYTYMPN 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLAD--AVSENYRVMSYFTEAelkDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegdeddwisnkvmf 458
Cdd:cd14158  99 GSLLDrlACLNDTPPLSWHMRC---KIAQGTANGINYLHENNHIHRDIKSANILLDETFVP------------------- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 459 KIGDLGhVTRiSSPQVEE--------GDSRFLANEVLQENYShlPKADIFA 501
Cdd:cd14158 157 KISDFG-LAR-ASEKFSQtimterivGTTAYMAPEALRGEIT--PKSDIFS 203
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
290-570 3.32e-06

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: 49.29  E-value: 3.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 290 MKSRYTT---EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDEQNA--LREVyaHAVLGQH--PHVVRYF 362
Cdd:cd06618   6 DGKKYKAdlnDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRR---SGNKEENKriLMDL--DVVLKSHdcPYIVKCY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 363 SAWAEDDHMLIQNEYCngGSLADAVSEnyRVMSYFTEAELKDLLLQVGRGLRYI-HSMSLVHMDIKPSNIFIsrtsipna 441
Cdd:cd06618  81 GYFITDSDVFICMELM--STCLDKLLK--RIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILL-------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 442 vseegdedDWISNkvmFKIGDLGhvtrISSPQVEE-------GDSRFLANEVL--QENYSHLPKADIFALALTVV-CAAG 511
Cdd:cd06618 149 --------DESGN---VKLCDFG----ISGRLVDSkaktrsaGCAAYMAPERIdpPDNPKYDIRADVWSLGISLVeLATG 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 512 AEPLPRNGDQWH---EIRQGRLPRIP--QVLSQELTELLKVMIHPDPERRPSAMVLVKHSVLLS 570
Cdd:cd06618 214 QFPYRNCKTEFEvltKILNEEPPSLPpnEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRR 277
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
296-563 3.64e-06

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: 48.79  E-value: 3.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKCVKRLDGCIyAIKRSKKplaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIRE---GAMSEEDFIEEAEVMMKL-SHPKLVQLYGVCLEQAPICLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnk 455
Cdd:cd05112  79 EFMEHGCLSDYLRTQ---RGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQV----------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 vmFKIGDLGhVTRI------SSPQVEEGDSRFLANEVLQ-ENYShlPKADI--FALALTVVCAAGAEPLPR--NGDQWHE 524
Cdd:cd05112 139 --VKVSDFG-MTRFvlddqyTSSTGTKFPVKWSSPEVFSfSRYS--SKSDVwsFGVLMWEVFSEGKIPYENrsNSEVVED 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 525 IRQG-RLPRiPQVLSQELTELLKVMIHPDPERRPSAMVLV 563
Cdd:cd05112 214 INAGfRLYK-PRLASTHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
304-556 3.65e-06

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: 49.52  E-value: 3.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNA-LREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECtMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseEGDeddwisnkvmFKIGD 462
Cdd:cd05590  83 LMFHIQKSRR----FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDH---------EGH----------CKLAD 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGhvtrISSPQVEEGDSR--------FLANEVLQENYsHLPKADIFALA-LTVVCAAGAEPL-PRNGDQWHEIRQGRLPR 532
Cdd:cd05590 140 FG----MCKEGIFNGKTTstfcgtpdYIAPEILQEML-YGPSVDWWAMGvLLYEMLCGHAPFeAENEDDLFEAILNDEVV 214
                       250       260
                ....*....|....*....|....
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05590 215 YPTWLSQDAVDILKAFMTKNPTMR 238
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
298-435 3.70e-06

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: 49.66  E-value: 3.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKP---LAGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDILAEA---DNEWVVRLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 375 NEYCNGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05625  80 MDYIPGGDMMSLLIR----MGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR 136
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
260-556 3.80e-06

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: 49.64  E-value: 3.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 260 NDSSEDMEASdyefedETRPAKRITITEsnmksrytteFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE 339
Cdd:cd05594   5 NSGAEEMEVS------LTKPKHKVTMND----------FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 340 -QNALREvyaHAVL--GQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENyRVmsyFTEAELKDLLLQVGRGLRYI 416
Cdd:cd05594  69 vAHTLTE---NRVLqnSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRE-RV---FSEDRARFYGAEIVSALDYL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 417 HS-MSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKIGDLG----HVTRISSPQVEEGDSRFLANEVLQENy 491
Cdd:cd05594 142 HSeKNVVYRDLKLENLML-------------DKDGHI------KITDFGlckeGIKDGATMKTFCGTPEYLAPEVLEDN- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 492 SHLPKADIFALALTVvcaagaeplprngdqwHEIRQGRLP------------------RIPQVLSQELTELLKVMIHPDP 553
Cdd:cd05594 202 DYGRAVDWWGLGVVM----------------YEMMCGRLPfynqdheklfelilmeeiRFPRTLSPEAKSLLSGLLKKDP 265

                ...
gi 17865613 554 ERR 556
Cdd:cd05594 266 KQR 268
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
297-434 4.00e-06

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: 48.88  E-value: 4.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIY-AIKRSKKPLAGSVDEQNALREVyahAVLGQ-----HPHVVRYF-----SAW 365
Cdd:cd07862   2 QYECVAEIGEGAYGKVFKARDLKNGGRFvALKRVRVQTGEEGMPLSTIREV---AVLRHletfeHPNVVRLFdvctvSRT 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQNEYCNggslADAVSENYRVMSYFTEAE-LKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07862  79 DRETKLTLVFEHVD----QDLTTYLDKVPEPGVPTEtIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVT 144
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
297-435 4.54e-06

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 49.05  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEM-QHGNIVRLQDVVHSEKRLYLVFE 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613  377 YCN------GGSLADaVSENYRVmsyfteaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:PLN00009  82 YLDldlkkhMDSSPD-FAKNPRL--------IKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDR 137
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
297-434 4.54e-06

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 48.81  E-value: 4.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQ--HPHVVRYFSAWAEddhmLIQ 374
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEAfdHPNIVRLMDVCAT----SRT 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 375 NEYCNGGSLADAVSENYRvmSYFTEA--------ELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07863  77 DRETKVTLVFEHVDQDLR--TYLDKVpppglpaeTIKDLMRQFLRGLDFLHANCIVHRDLKPENILVT 142
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
298-433 4.79e-06

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: 49.24  E-value: 4.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIK--RSKKPL-AGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05626   3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKtlRKKDVLnRNQVAHVKAERDILAEA---DNEWVVKLYYSFQDKDNLYFV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 375 NEYCNGGslaDAVSENYRvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05626  80 MDYIPGG---DMMSLLIR-MEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI 134
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
321-562 5.22e-06

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. 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 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-A/B 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: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 48.75  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 321 GCIYAIK---RSKKPLAGSV-DEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAV-SENYRVMS 395
Cdd:cd14042  30 GNLVAIKkvnKKRIDLTREVlKELKHMRDL-------QHDNLTRFIGACVDPPNICILTEYCPKGSLQDILeNEDIKLDW 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 396 YFTEAELKDLLlqvgRGLRYIHSMSLV-HMDIKPSNIFI-SRtsipnavseegdeddWisnkvMFKIGDLGHVTRISSPQ 473
Cdd:cd14042 103 MFRYSLIHDIV----KGMHYLHDSEIKsHGNLKSSNCVVdSR---------------F-----VLKITDFGLHSFRSGQE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 474 VEEGDSRFLAN------EVLQENYSHLP---KADIFALALTVvcaagAEPLPRNGdQWH---------EIRQGRLPRI-- 533
Cdd:cd14042 159 PPDDSHAYYAKllwtapELLRDPNPPPPgtqKGDVYSFGIIL-----QEIATRQG-PFYeegpdlspkEIIKKKVRNGek 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 534 --------PQVLSQELTELLKVMIHPDPERRPSAMVL 562
Cdd:cd14042 233 ppfrpsldELECPDEVLSLMQRCWAEDPEERPDFSTL 269
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
302-566 5.32e-06

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: 48.43  E-value: 5.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ------NALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd14181  16 EVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQleevrsSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdeDDwisnK 455
Cdd:cd14181  96 DLMRRGELFDYLTEKVTL----SEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---------------DD----Q 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLGHVTRIS-SPQVEE--GDSRFLANEVLQ----ENYSHLPK-ADIFALALTV-VCAAGAEPLprngdqWHE-- 524
Cdd:cd14181 153 LHIKLSDFGFSCHLEpGEKLRElcGTPGYLAPEILKcsmdETHPGYGKeVDLWACGVILfTLLAGSPPF------WHRrq 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 525 ------IRQGRLpripQVLSQE-------LTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14181 227 mlmlrmIMEGRY----QFSSPEwddrsstVKDLISRLLVVDPEIRLTAEQALQHP 277
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
297-562 5.74e-06

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: 48.20  E-value: 5.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCV--KRLDGCIYAIKRSKKPLAGS-VDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05148   7 EFTLERKLGSGYFGEVWEGLwkNRVRVAIKILKSDDLLKQQDfQKEVQALKRL-------RHKHLISLFAVCSVGEPVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGS----LADAVSENYRVmsyfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseeGDEd 449
Cdd:cd05148  80 ITELMEKGSllafLRSPEGQVLPV------ASLIDMACQVAEGMAYLEEQNSIHRDLAARNILV------------GED- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 dwisnkVMFKIGDLGHVTRISSPQVEEGDS----RFLANEVLqeNYSHLP-KADI--FALALTVVCAAGAEPLP--RNGD 520
Cdd:cd05148 141 ------LVCKVADFGLARLIKEDVYLSSDKkipyKWTAPEAA--SHGTFStKSDVwsFGILLYEMFTYGQVPYPgmNNHE 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 521 QWHEIRQG-RLPRiPQVLSQELTELLKVMIHPDPERRPSAMVL 562
Cdd:cd05148 213 VYDQITAGyRMPC-PAKCPQEIYKIMLECWAAEPEDRPSFKAL 254
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
302-558 5.80e-06

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: 48.33  E-value: 5.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKcvkrldGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDhMLIQNEYCNGG 381
Cdd:cd05083  12 EIIGEGEFGAVLQ------GEYMGQKVAVKNIKCDVTAQAFLEETAVMTKL-QHKNLVRLLGVILHNG-LYIVMELMSKG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENYRVMsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnaVSEEGDEddwisnkvmfKIG 461
Cdd:cd05083  84 NLVNFLRSRGRAL--VPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNIL---------VSEDGVA----------KIS 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 462 DLGhvtrISSPQVEEGDSRFL-----ANEVLQeNYSHLPKADI--FALALTVVCAAGAEPLPRNG--DQWHEIRQGRLPR 532
Cdd:cd05083 143 DFG----LAKVGSMGVDNSRLpvkwtAPEALK-NKKFSSKSDVwsYGVLLWEVFSYGRAPYPKMSvkEVKEAVEKGYRME 217
                       250       260
                ....*....|....*....|....*.
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05083 218 PPEGCPPDVYSIMTSCWEAEPGKRPS 243
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
304-556 5.97e-06

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: 48.51  E-value: 5.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEqnalrevYAHA-----VLGQ--HPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05571   3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDE-------VAHTltenrVLQNtrHPFLTSLKYSFQTNDRLCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENyRVmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkv 456
Cdd:cd05571  76 YVNGGELFFHLSRE-RV---FSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL-------------DKDGHI---- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfKIGDLG----HVTRISSPQVEEGDSRFLANEVLQEN-YShlpkadifalaltvvcaagaeplpRNGDQW------HEI 525
Cdd:cd05571 135 --KITDFGlckeEISYGATTKTFCGTPEYLAPEVLEDNdYG------------------------RAVDWWglgvvmYEM 188
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17865613 526 RQGRLP------------------RIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05571 189 MCGRLPfynrdhevlfelilmeevRFPSTLSPEAKSLLAGLLKKDPKKR 237
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
407-557 6.25e-06

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: 48.26  E-value: 6.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 407 LQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwISNKVmfKIGDLGHV---TRISSPQVeeGDSRFLA 483
Cdd:cd13975 109 LDVVEGIRFLHSQGLVHRDIKLKNVLLD-----------------KKNRA--KITDLGFCkpeAMMSGSIV--GTPIHMA 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 484 NEVLQENYSHlpKADIFALALTV--VCaAGAEPLP-------RNGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPE 554
Cdd:cd13975 168 PELFSGKYDN--SVDVYAFGILFwyLC-AGHVKLPeafeqcaSKDHLWNNVRKGVRPERLPVFDEECWNLMEACWSGDPS 244

                ...
gi 17865613 555 RRP 557
Cdd:cd13975 245 QRP 247
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
303-558 6.50e-06

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: 48.14  E-value: 6.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFkcVKRLDGCIYAIKRSKKPlaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDhMLIQNEYCNGGS 382
Cdd:cd05069  19 KLGQGCFGEVW--MGTWNGTTKVAIKTLKP--GTMMPEAFLQEAQIMKKL-RHDKLVPLYAVVSEEP-IYIVTEFMGKGS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipNAVSEEGDeddwisnkvmFKIGD 462
Cdd:cd05069  93 LLDFLKEGDG--KYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD----NLVCKIAD----------FGLAR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQVEEGDSRFLANEVLQenYSHLP-KADI--FALALTVVCAAGAEPLPR--NGDQWHEIRQG-RLPrIPQV 536
Cdd:cd05069 157 LIEDNEYTARQGAKFPIKWTAPEAAL--YGRFTiKSDVwsFGILLTELVTKGRVPYPGmvNREVLEQVERGyRMP-CPQG 233
                       250       260
                ....*....|....*....|..
gi 17865613 537 LSQELTELLKVMIHPDPERRPS 558
Cdd:cd05069 234 CPESLHELMKLCWKKDPDERPT 255
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
354-566 6.70e-06

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: 48.15  E-value: 6.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAEDDH----MLIQNEYCNGGSLADAVsENYRVMSyftEAELKDLLLQVGRGLRYIHSMS--LVHMDIK 427
Cdd:cd14032  58 QHPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYL-KRFKVMK---PKVLRSWCRQILKGLLFLHTRTppIIHRDLK 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 428 PSNIFIsrTSIPNAVseegdeddwisnkvmfKIGDLGHVT--RISSPQVEEGDSRFLANEVLQENYSHlpKADIFALALT 505
Cdd:cd14032 134 CDNIFI--TGPTGSV----------------KIGDLGLATlkRASFAKSVIGTPEFMAPEMYEEHYDE--SVDVYAFGMC 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 506 VVCAAGAE-PLP--RNGDQ-WHEIRQGRLP-RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14032 194 MLEMATSEyPYSecQNAAQiYRKVTCGIKPaSFEKVTDPEIKEIIGECICKNKEERYEIKDLLSHA 259
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
303-535 6.80e-06

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 48.51  E-value: 6.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKcVKRLDgciyaIKRSKKPLAGSVDEQNALREVY----AHAVLGQHPHV---VRYFSAWAEDDHMLIQN 375
Cdd:cd13981   7 ELGEGGYASVYL-AKDDD-----EQSDGSLVALKVEKPPSIWEFYicdqLHSRLKNSRLResiSGAHSAHLFQDESILVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSEnyrvMSYFTEAELKDLL-----LQVGRGLRYIHSMSLVHMDIKPSNIFISRTsiPNAVSEEGDEDD 450
Cdd:cd13981  81 DYSSQGTLLDVVNK----MKNKTGGGMDEPLamfftIELLKVVEALHEVGIIHGDIKPDNFLLRLE--ICADWPGEGENG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 WiSNKVMfKIGDLGHVTRIS------SPQVEEGDSRFLANEvLQENYSHLPKADIFALALTVVCA-AG--AEPLPRNGDQ 521
Cdd:cd13981 155 W-LSKGL-KLIDFGRSIDMSlfpknqSFKADWHTDSFDCIE-MREGRPWTYQIDYFGIAATIHVMlFGkyMELTQESGRW 231
                       250
                ....*....|....
gi 17865613 522 whEIRQgRLPRIPQ 535
Cdd:cd13981 232 --KINQ-NLKRYWQ 242
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
303-434 8.13e-06

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: 47.89  E-value: 8.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIKrsKKPLagsvdEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd13991  13 RIGRGSFGEVHRMEDKQTGFQCAVK--KVRL-----EVFRAEELMACAGL-TSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17865613 383 LADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd13991  85 LGQLIKE----QGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLS 132
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
303-433 8.27e-06

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: 47.62  E-value: 8.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIK-------RSKKPLAGSVDeqnALREVYAH--AVLGQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd14005   7 LLGKGGFGTVYSGVRIRDGLPVAVKfvpksrvTEWAMINGPVP---VPLEIALLlkASKPGVPGVIRLLDWYERPDGFLL 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 374 QNEY---CNggSLADAVSEnYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14005  84 IMERpepCQ--DLFDFITE-RGALS---ENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI 140
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
304-559 8.56e-06

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: 48.34  E-value: 8.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKR-------SKKPLAGSVDEQNALrevyAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVlskkvivAKKEVAHTIGERNIL----VRTALDESPFIVGLKFSFQTPTDLYLVTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWISnkv 456
Cdd:cd05586  77 YMSGGELFWHLQKEGR----FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL-------------DANGHIA--- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 mfkIGDLGhvtrISSPQVEE--------GDSRFLANEVLQENYSHLPKADIFALALTV--VCaAGAEPL--PRNGDQWHE 524
Cdd:cd05586 137 ---LCDFG----LSKADLTDnkttntfcGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVfeMC-CGWSPFyaEDTQQMYRN 208
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17865613 525 IRQGRLpRIPQ-VLSQELTELLKVMIHPDPERRPSA 559
Cdd:cd05586 209 IAFGKV-RFPKdVLSDEGRSFVKGLLNRNPKHRLGA 243
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
297-438 9.08e-06

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: 47.79  E-value: 9.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKP---LAGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQnliLRNQIQQVFVERDILTFA---ENPFVVSMYCSFETKRHLCM 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 374 QNEYCNGGSLAD------AVSENYRVMsYFTEAELkdlllqvgrGLRYIHSMSLVHMDIKPSNIFIsrTSI 438
Cdd:cd05609  78 VMEYVEGGDCATllknigPLPVDMARM-YFAETVL---------ALEYLHSYGIVHRDLKPDNLLI--TSM 136
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
298-435 9.20e-06

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: 48.08  E-value: 9.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplaGSVDEQN------ALREVYAHAvlgQHPHVVRYFSAWAEDDHM 371
Cdd:cd05598   3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRK---KDVLKRNqvahvkAERDILAEA---DNEWVVKLYYSFQDKENL 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 372 LIQNEYCNGGSLadavsenyrvMS------YFTE-------AELKdlllqvgRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05598  77 YFVMDYIPGGDL----------MSllikkgIFEEdlarfyiAELV-------CAIESVHKMGFIHRDIKPDNILIDR 136
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
305-558 9.33e-06

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: 47.64  E-value: 9.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 305 GSGEFGSVFKCVKRLDGCIYAIKRSKKplagsVDEQNALREVYAHAvlgqhpHVVRYFSAWAEDDHMLIQNEYCNGGSLA 384
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK-----IEKEAEILSVLSHR------NIIQFYGAILEAPNYGIVTEYASYGSLF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 385 DAVSENY-------RVMSYFTEaelkdlllqVGRGLRYIHS---MSLVHMDIKPSNIFISRTSIpnavseegdeddwisn 454
Cdd:cd14060  71 DYLNSNEseemdmdQIMTWATD---------IAKGMHYLHMeapVKVIHRDLKSRNVVIAADGV---------------- 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmFKIGDLG------HVTRISSpqveEGDSRFLANEVLQEnyshLPKA---DIFALALtVVCAAGAEPLPRNGDQ---- 521
Cdd:cd14060 126 ---LKICDFGasrfhsHTTHMSL----VGTFPWMAPEVIQS----LPVSetcDTYSYGV-VLWEMLTREVPFKGLEglqv 193
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 522 -WHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd14060 194 aWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKERPS 231
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
304-436 1.03e-05

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: 47.49  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRlDGCIYAIKRSKKPLAGSVDEQNAlREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14664   1 IGRGGAGTVYKGVMP-NGTLVAVKRLKGEGTQGGDHGFQ-AEIQTLGMI-RHRNIVRLRGYCSNPTTNLLVYEYMPNGSL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 384 ADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIH---SMSLVHMDIKPSNIFISRT 436
Cdd:cd14664  78 GELLHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEE 133
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
302-488 1.18e-05

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: 47.71  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvdEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14173   8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHS--RSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsiPNAVSEEGDEDDWISNKVMFKig 461
Cdd:cd14173  86 SILSHIHRR----RHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEH---PNQVSPVKICDFDLGSGIKLN-- 156
                       170       180
                ....*....|....*....|....*....
gi 17865613 462 dlGHVTRISSPQVEE--GDSRFLANEVLQ 488
Cdd:cd14173 157 --SDCSPISTPELLTpcGSAEYMAPEVVE 183
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
303-433 1.46e-05

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: 46.88  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVkrldgciYAIKRSKKPLAGSV----DEQNALR-EVYAHAVLGQ---HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05116   2 ELGSGNFGTVKKGY-------YQMKKVVKTVAVKIlkneANDPALKdELLREANVMQqldNPYIVRMIGICEAESWMLVM 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 375 nEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05116  75 -EMAELGPLNKFLQKNRHV----TEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLL 128
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
302-435 1.68e-05

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 47.28  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCvkRLDGC----------------IYAIKRSKkPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAW 365
Cdd:cd05097  11 EKLGEGQFGEVHLC--EAEGLaeflgegapefdgqpvLVAVKMLR-ADVTKTARNDFLKEIKIMSRL-KNPNIIRLLGVC 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 366 AEDDHMLIQNEYCNGGSLADAVSENyRVMSYFTEA------ELKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05097  87 VSDDPLCMITEYMENGDLNQFLSQR-EIESTFTHAnnipsvSIANLLymaVQIASGMKYLASLNFVHRDLATRNCLVGN 164
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
297-433 1.75e-05

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: 47.33  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL---REVYAHAvlgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05600  12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVlteRDILTTT---NSPWLVKLLYAFQDPENVYL 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 374 QNEYCNGGSLADAVSeNYRVMS------YFTEaelkdLLLQVGRglryIHSMSLVHMDIKPSNIFI 433
Cdd:cd05600  89 AMEYVPGGDFRTLLN-NSGILSeeharfYIAE-----MFAAISS----LHQLGYIHRDLKPENFLI 144
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
289-558 1.82e-05

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: 46.90  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 289 NMKsryttEFHELEKIGSGEFGSVfkcvkrLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAED 368
Cdd:cd05082   4 NMK-----ELKLLQTIGKGEFGDV------MLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQL-RHSNLVQLLGVIVEE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 369 DHML-IQNEYCNGGSLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPnavseegd 447
Cdd:cd05082  72 KGGLyIVTEYMAKGSLVDYLRSRGR--SVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVA-------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 448 eddwisnkvmfKIGDLGHVTRISSPQ-VEEGDSRFLANEVLQEN-YShlPKADI--FALALTVVCAAGAEPLPRNG--DQ 521
Cdd:cd05082 142 -----------KVSDFGLTKEASSTQdTGKLPVKWTAPEALREKkFS--TKSDVwsFGILLWEIYSFGRVPYPRIPlkDV 208
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 522 WHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05082 209 VPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPS 245
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
301-563 1.94e-05

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: 46.80  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGsVFKCVKRLDGCIYAIKRSKKplaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05113   9 LKELGTGQFG-VVKYGKWRGQYDVAIKMIKE---GSMSEDEFIEEAKVMMNL-SHEKLVQLYGVCTKQRPIFIITEYMAN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRvmsYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNaVSEEGDE----DDWISNKV 456
Cdd:cd05113  84 GCLLNYLREMRK---RFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVK-VSDFGLSryvlDDEYTSSV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 457 MFKIGdlghvTRISSPQVeegdsrflaneVLQENYShlPKADIFALALTV--VCAAGAEPLPR--NGDQWHEIRQGRLPR 532
Cdd:cd05113 160 GSKFP-----VRWSPPEV-----------LMYSKFS--SKSDVWAFGVLMweVYSLGKMPYERftNSETVEHVSQGLRLY 221
                       250       260       270
                ....*....|....*....|....*....|.
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERRPSAMVLV 563
Cdd:cd05113 222 RPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
304-558 2.03e-05

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 47.33  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVfkcvkrLDGCIYAIKRSK----------KPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05105  45 LGSGAFGKV------VEGTAYGLSRSQpvmkvavkmlKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSL------------------------------ADAVSENYRVMSY--------------------------- 396
Cdd:cd05105 119 ITEYCFYGDLvnylhknrdnflsrhpekpkkdldifginpADESTRSYVILSFenkgdymdmkqadttqyvpmleikeas 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 397 ------------------FTEAELKDLL-----------------LQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpna 441
Cdd:cd05105 199 kysdiqrsnydrpasykgSNDSEVKNLLsddgseglttldllsftYQVARGMEFLASKNCVHRDLAARNVLLAQGKI--- 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 442 vseegdeddwisnkvmFKIGDLGHVTRI--SSPQVEEGDS----RFLANEVLQEN-YSHLPKADIFALALTVVCAAGAEP 514
Cdd:cd05105 276 ----------------VKICDFGLARDImhDSNYVSKGSTflpvKWMAPESIFDNlYTTLSDVWSYGILLWEIFSLGGTP 339
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 17865613 515 LPR---NGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05105 340 YPGmivDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPS 386
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
301-433 2.32e-05

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: 46.98  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIK-----RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAED-DHMLIQ 374
Cdd:cd14041  11 LHLLGRGGFSEVYKAFDLTEQRYVAVKihqlnKNWRDEKKENYHKHACREYRIHKEL-DHPRIVKLYDYFSLDtDSFCTV 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 375 NEYCNGGSLaDAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMS--LVHMDIKPSNIFI 433
Cdd:cd14041  90 LEYCEGNDL-DFYLKQHKLMS---EKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILL 146
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
304-556 2.41e-05

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: 46.86  E-value: 2.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDvECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRVMSY---FTEAELKdlllqvgRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfK 459
Cdd:cd05620  83 LMFHIQDKGRFDLYratFYAAEIV-------CGLQFLHSKGIIYRDLKLDNVML-------------DRDGHI------K 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLG----HVTRISSPQVEEGDSRFLANEVLQ-ENYSHlpKADIFALALTVV-CAAGAEPLprNGDQWHE----IRQGR 529
Cdd:cd05620 137 IADFGmckeNVFGDNRASTFCGTPDYIAPEILQgLKYTF--SVDWWSFGVLLYeMLIGQSPF--HGDDEDElfesIRVDT 212
                       250       260
                ....*....|....*....|....*..
gi 17865613 530 lPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05620 213 -PHYPRWITKESKDILEKLFERDPTRR 238
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
301-433 3.01e-05

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: 46.67  E-value: 3.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNalrEVYAHAVLGQHP----HVVRYFSAWAEDDH------ 370
Cdd:cd14211   4 LEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI---EVSILSRLSQENadefNFVRAYECFQHKNHtclvfe 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 371 MLIQNEYcnggslaDAVSENYrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14211  81 MLEQNLY-------DFLKQNK--FSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIML 134
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
304-574 3.13e-05

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: 46.01  E-value: 3.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd14117  14 LGKGKFGNVYLAREKQSKFIVALKvLFKSQIEKEGVEHQLRREIEIQSHL-RHPNILRLYNYFHDRKRIYLILEYAPRGE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwisnKVMFKIGD 462
Cdd:cd14117  93 LYKELQKHGR----FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGY-------------------KGELKIAD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHvtRISSPQVEE----GDSRFLANEVLqENYSHLPKADIFALA-LTVVCAAGAEPL--PRNGDQWHEIRQGRLpRIPQ 535
Cdd:cd14117 150 FGW--SVHAPSLRRrtmcGTLDYLPPEMI-EGRTHDEKVDLWCIGvLCYELLVGMPPFesASHTETYRRIVKVDL-KFPP 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17865613 536 VLSQELTELL-KVMIHPDPERRPSAMVLvKHSVLLSASRK 574
Cdd:cd14117 226 FLSDGSRDLIsKLLRYHPSERLPLKGVM-EHPWVKANSRR 264
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
297-433 3.19e-05

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: 46.53  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQN 375
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDvECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 376 EYCNGGSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05616  81 EYVNGGDLMYHIQQVGR----FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML 134
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
289-436 3.40e-05

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: 46.53  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 289 NMKSRYTTefheLEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkPLAGSVDEQNALREVyahAVLGQHPH--------VVR 360
Cdd:cd07849   2 DVGPRYQN----LSYIGEGAYGMVCSAVHKPTGQKVAIKKIS-PFEHQTYCLRTLREI---KILLRFKHeniigildIQR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 361 YFSAWAEDDHMLIQnEYCNggsladavSENYRVMS----------YFteaelkdlLLQVGRGLRYIHSMSLVHMDIKPSN 430
Cdd:cd07849  74 PPTFESFKDVYIVQ-ELME--------TDLYKLIKtqhlsndhiqYF--------LYQILRGLKYIHSANVLHRDLKPSN 136

                ....*.
gi 17865613 431 IFISRT 436
Cdd:cd07849 137 LLLNTN 142
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
303-556 3.75e-05

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: 46.10  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPL----------------AGSVDEQNA---LREVYAH-AVLGQ--HPHVV 359
Cdd:cd14200   7 EIGKGSYGVVKLAYNESDDKYYAMKvLSKKKLlkqygfprrppprgskAAQGEQAKPlapLERVYQEiAILKKldHVNIV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 360 RYFSAW---AEDD-HMLIqnEYCNGGSLADAVSEnyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsr 435
Cdd:cd14200  87 KLIEVLddpAEDNlYMVF--DLLRKGPVMEVPSD-----KPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLL-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 436 tsipnavseeGDEDDwisnkvmFKIGDLGhvtriSSPQVEEGDSR---------FLANEVLQEN-YSHLPKA-DIFALAL 504
Cdd:cd14200 158 ----------GDDGH-------VKIADFG-----VSNQFEGNDALlsstagtpaFMAPETLSDSgQSFSGKAlDVWAMGV 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 505 TVVC-AAGAEPLPrngDQW-----HEIRQG--RLPRIPQVlSQELTELLKVMIHPDPERR 556
Cdd:cd14200 216 TLYCfVYGKCPFI---DEFilalhNKIKNKpvEFPEEPEI-SEELKDLILKMLDKNPETR 271
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
304-433 3.78e-05

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: 46.14  E-value: 3.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIY--AIKRSKKpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd05088  15 IGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 382 SLAD------------AVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05088  94 NLLDflrksrvletdpAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 157
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
354-566 3.85e-05

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: 45.81  E-value: 3.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAEDDH----MLIQNEYCNGGSLADAVsENYRVMSYFTeaeLKDLLLQVGRGLRYIHSMS--LVHMDIK 427
Cdd:cd14030  82 QHPNIVRFYDSWESTVKgkkcIVLVTELMTSGTLKTYL-KRFKVMKIKV---LRSWCRQILKGLQFLHTRTppIIHRDLK 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 428 PSNIFIsrTSIPNAVseegdeddwisnkvmfKIGDLGHVT--RISSPQVEEGDSRFLANEVLQENYSHlpKADIFALALT 505
Cdd:cd14030 158 CDNIFI--TGPTGSV----------------KIGDLGLATlkRASFAKSVIGTPEFMAPEMYEEKYDE--SVDVYAFGMC 217
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 506 VVCAAGAE-PLP--RNGDQ-WHEIRQGRLP-RIPQVLSQELTELLKVMIHPDPERRPSAMVLVKHS 566
Cdd:cd14030 218 MLEMATSEyPYSecQNAAQiYRRVTSGVKPaSFDKVAIPEVKEIIEGCIRQNKDERYAIKDLLNHA 283
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
301-430 4.07e-05

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 45.67  E-value: 4.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKcVKRLDGCIYAIKR------SKKPLAGSVDEQNALREvyahavLGQHPHVVRYFSA--WAEDDHML 372
Cdd:cd14131   6 LKQLGKGGSSKVYK-VLNPKKKIYALKRvdlegaDEQTLQSYKNEIELLKK------LKGSDRIIQLYDYevTDEDDYLY 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 373 IQNEyCNGGSLA-------DAVSENYRVMSYFTEaelkdLLLQVgrglRYIHSMSLVHMDIKPSN 430
Cdd:cd14131  79 MVME-CGEIDLAtilkkkrPKPIDPNFIRYYWKQ-----MLEAV----HTIHEEGIVHSDLKPAN 133
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
352-579 4.12e-05

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: 46.09  E-value: 4.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 352 LGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENYrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd08227  55 LFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHF--MDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHI 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 432 FIsrtSIPNAVSEEGDEddwiSNKVMFKIGDLGHVTRiSSPQVEEGDSRFLANEVLQEN----------YS--------- 492
Cdd:cd08227 133 LI---SVDGKVYLSGLR----SNLSMINHGQRLRVVH-DFPKYSVKVLPWLSPEVLQQNlqgydaksdiYSvgitacela 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 493 --HLPKADIFA-------LALTVVCAAGAEPLPRN-------------------GDQWHEIRQGRLPRIP--QVLSQELT 542
Cdd:cd08227 205 ngHVPFKDMPAtqmllekLNGTVPCLLDTTTIPAEeltmkpsrsgansglgestTVSTPRPSNGESSSHPynRTFSPHFH 284
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 543 ELLKVMIHPDPERRPSAMVLVKHSVLLSASRKSAEQL 579
Cdd:cd08227 285 HFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEAL 321
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
298-435 4.19e-05

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: 45.93  E-value: 4.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsVDEQ-----NALREVYAHAVLgQHPHVVRYFSAWAEDDHML 372
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH------LDAEegtpsTAIREISLMKEL-KHENIVRLHDVIHTENKLM 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 373 IQNEYCNgGSLADAVsENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd07836  75 LVFEYMD-KDLKKYM-DTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINK 135
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
304-565 4.29e-05

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. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR 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: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 45.94  E-value: 4.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKC----VKRLDGC-IYAIKRSKKplAGSVDEQNAL-REVYAHAVLGQHPHVVRYFSA--WAEDDHMLIQn 375
Cdd:cd05054  15 LGRGAFGKVIQAsafgIDKSATCrTVAVKMLKE--GATASEHKALmTELKILIHIGHHLNVVNLLGActKPGGPLMVIV- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSEN------YRVMSYFTEAE-------------LKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05054  92 EFCKFGNLSNYLRSKreefvpYRDKGARDVEEeedddelykepltLEDLIcysFQVARGMEFLASRKCIHRDLAARNILL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 434 SRTSIpnavseegdeddwisnkvmFKIGDLGHVTRI-SSPQ-VEEGDSR----FLANE-VLQENYSHlpKADI--FALAL 504
Cdd:cd05054 172 SENNV-------------------VKICDFGLARDIyKDPDyVRKGDARlplkWMAPEsIFDKVYTT--QSDVwsFGVLL 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 505 TVVCAAGAEPLP---RNGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLVKH 565
Cdd:cd05054 231 WEIFSLGASPYPgvqMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEK 294
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
298-556 4.38e-05

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: 45.64  E-value: 4.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLA------GSVDEQNALREVYAHavlgqhpHVVRYFSAWAEDDH 370
Cdd:cd05608   3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKlNKKRLKkrkgyeGAMVEKRILAKVHSR-------FIVSLAYAFQTKTD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 371 MLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDD 450
Cdd:cd05608  76 LCLVMTIMNGGDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL-------------DDDG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 451 WIsnkvmfKIGDLGHVTRISSPQVE----EGDSRFLANEVLQ-ENYSHlpKADIFALALTV---VCAAGaePLPRNGDQW 522
Cdd:cd05608 143 NV------RISDLGLAVELKDGQTKtkgyAGTPGFMAPELLLgEEYDY--SVDYFTLGVTLyemIAARG--PFRARGEKV 212
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 523 H--EIRQGRLPR---IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05608 213 EnkELKQRILNDsvtYSEKFSPASKSICEALLAKDPEKR 251
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
301-433 4.75e-05

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: 45.79  E-value: 4.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplAGSVDEQNALrEVYAHAVLGQHP----HVVRYFSAWAEDDH------ 370
Cdd:cd14229   5 LDFLGRGTFGQVVKCWKRGTNEIVAVKILKN--HPSYARQGQI-EVGILARLSNENadefNFVRAYECFQHRNHtclvfe 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 371 MLIQNEYcnggslaDAVSENYrvmsyFTEAELK---DLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14229  82 MLEQNLY-------DFLKQNK-----FSPLPLKvirPILQQVATALKKLKSLGLIHADLKPENIML 135
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
303-558 4.92e-05

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: 45.45  E-value: 4.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCVkrLDGCIYAIKRSKKPlaGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDhMLIQNEYCNGGS 382
Cdd:cd05071  16 KLGQGCFGEVWMGT--WNGTTRVAIKTLKP--GTMSPEAFLQEAQVMKKL-RHEKLVQLYAVVSEEP-IYIVTEYMSKGS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipNAVSEEGDeddwisnkvmFKIGD 462
Cdd:cd05071  90 LLDFLKGEMG--KYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE----NLVCKVAD----------FGLAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTRISSPQVEEGDSRFLANEVLQENYSHLpKADI--FALALTVVCAAGAEPLPR--NGDQWHEIRQG-RLPrIPQVL 537
Cdd:cd05071 154 LIEDNEYTARQGAKFPIKWTAPEAALYGRFTI-KSDVwsFGILLTELTTKGRVPYPGmvNREVLDQVERGyRMP-CPPEC 231
                       250       260
                ....*....|....*....|.
gi 17865613 538 SQELTELLKVMIHPDPERRPS 558
Cdd:cd05071 232 PESLHDLMCQCWRKEPEERPT 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
302-558 4.98e-05

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: 45.31  E-value: 4.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVyahAVLGQ--HPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAK-FLQEA---RILKQysHPNIVRLIGVCTQKQPIYIVMELVQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGS-LADAVSENYRVMSyfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmF 458
Cdd:cd05084  78 GGDfLTFLRTEGPRLKV----KELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNV-------------------L 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 459 KIGDLGhVTRisspqvEEGDSRFLANEVLQE-----------NYS-HLPKADI--FALALTVVCAAGAEPLPRNGDQW-- 522
Cdd:cd05084 135 KISDFG-MSR------EEEDGVYAATGGMKQipvkwtapealNYGrYSSESDVwsFGILLWETFSLGAVPYANLSNQQtr 207
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17865613 523 HEIRQG-RLPrIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05084 208 EAVEQGvRLP-CPENCPDEVYRLMEQCWEYDPRKRPS 243
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
304-556 5.04e-05

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: 45.68  E-value: 5.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05619  13 LGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDvECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVMEYLNGGD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRV---MSYFTEAElkdlllqVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfK 459
Cdd:cd05619  93 LMFHIQSCHKFdlpRATFYAAE-------IICGLQFLHSKGIVYRDLKLDNILL-------------DKDGHI------K 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 460 IGDLGHVTR--ISSPQVEE--GDSRFLANEV-LQENYSHLPKADIFALALTVVCaAGAEPLPRNGDQ--WHEIRQGRlPR 532
Cdd:cd05619 147 IADFGMCKEnmLGDAKTSTfcGTPDYIAPEIlLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEelFQSIRMDN-PF 224
                       250       260
                ....*....|....*....|....
gi 17865613 533 IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05619 225 YPRWLEKEAKDILVKLFVREPERR 248
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
301-433 5.25e-05

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: 45.86  E-value: 5.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKcVKRLDGC----IYAIK--------RSKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAED 368
Cdd:cd05584   1 LKVLGKGGYGKVFQ-VRKTTGSdkgkIFAMKvlkkasivRNQKDTAHTKAERNILEAV-------KHPFIVDLHYAFQTG 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 369 DHMLIQNEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05584  73 GKLYLILEYLSGGELFMHLERE----GIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL 133
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
288-556 5.79e-05

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: 45.76  E-value: 5.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 288 SNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLGQHPHVVRYFSAWA 366
Cdd:cd05615   2 NNLDRVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDvECTMVEKRVLALQDKPPFLTQLHSCFQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 367 EDDHMLIQNEYCNGGSLADAVSEnyrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEG 446
Cdd:cd05615  82 TVDRLYFVMEYVNGGDLMYHIQQ----VGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML---------DSEG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 447 DeddwisnkvmFKIGDLG----HVTRISSPQVEEGDSRFLANEVLQenYSHLPKA-DIFALALTVVCAAGAEPlPRNGDQ 521
Cdd:cd05615 149 H----------IKIADFGmckeHMVEGVTTRTFCGTPDYIAPEIIA--YQPYGRSvDWWAYGVLLYEMLAGQP-PFDGED 215
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17865613 522 WHEIRQGRLPR---IPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05615 216 EDELFQSIMEHnvsYPKSLSKEAVSICKGLMTKHPAKR 253
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
284-556 5.99e-05

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 45.58  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  284 TITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvdeQNALR-----EVYAHAVLGQ---H 355
Cdd:PTZ00263   6 MFTKPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKK--------REILKmkqvqHVAQEKSILMelsH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  356 PHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENYRV---MSYFTEAELkdlLLqvgrGLRYIHSMSLVHMDIKPSNIF 432
Cdd:PTZ00263  78 PFIVNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFpndVAKFYHAEL---VL----AFEYLHSKDIIYRDLKPENLL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  433 isrtsipnavseegdeddwISNKVMFKIGDLGHVTRISSPQVEE-GDSRFLANEVLQENySHLPKADIFALA-LTVVCAA 510
Cdd:PTZ00263 151 -------------------LDNKGHVKVTDFGFAKKVPDRTFTLcGTPEYLAPEVIQSK-GHGKAVDWWTMGvLLYEFIA 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 17865613  511 GAEPLPRNG--DQWHEIRQGRLpRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:PTZ00263 211 GYPPFFDDTpfRIYEKILAGRL-KFPNWFDGRARDLVKGLLQTDHTKR 257
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
402-572 5.99e-05

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: 45.74  E-value: 5.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 402 LKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFKIGDLGHVTRI-SSPQ-VEE 476
Cdd:cd05103 178 LEDLIcysFQVAKGMEFLASRKCIHRDLAARNILLSENNV-------------------VKICDFGLARDIyKDPDyVRK 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 477 GDSR----FLANEVLQENYsHLPKADI--FALALTVVCAAGAEPLPrnGDQWHE-----IRQGRLPRIPQVLSQELTELL 545
Cdd:cd05103 239 GDARlplkWMAPETIFDRV-YTIQSDVwsFGVLLWEIFSLGASPYP--GVKIDEefcrrLKEGTRMRAPDYTTPEMYQTM 315
                       170       180
                ....*....|....*....|....*...
gi 17865613 546 KVMIHPDPERRPSAMVLVKH-SVLLSAS 572
Cdd:cd05103 316 LDCWHGEPSQRPTFSELVEHlGNLLQAN 343
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
303-556 6.73e-05

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: 45.34  E-value: 6.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVF--KCVKRL---DGCIYAIKRSKKplAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd05092  12 ELGEGAFGKVFlaECHNLLpeqDKMLVAVKALKE--ATESARQDFQREAELLTVL-QHQHIVRFYGVCTEGEPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSL--------ADA-VSENYRVMSY--FTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnavseeg 446
Cdd:cd05092  89 MRHGDLnrflrshgPDAkILDGGEGQAPgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCL-------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 447 deddwISNKVMFKIGDLGHVTRISSPQVEEGDSRFL-------ANEVLQENYShlPKADI--FALALTVVCAAGAEPLPR 517
Cdd:cd05092 155 -----VGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMlpirwmpPESILYRKFT--TESDIwsFGVVLWEIFTYGKQPWYQ 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 518 --NGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05092 228 lsNTEAIECITQGRELERPRTCPPEVYAIMQGCWQREPQQR 268
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
302-488 6.96e-05

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 45.02  E-value: 6.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvdEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGG 381
Cdd:cd14174   8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHS--RSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrTSIPNAVSEEGDEDDWISNKVMFKig 461
Cdd:cd14174  86 SILAHIQKR----KHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL---CESPDKVSPVKICDFDLGSGVKLN-- 156
                       170       180
                ....*....|....*....|....*....
gi 17865613 462 dlGHVTRISSPQVEE--GDSRFLANEVLQ 488
Cdd:cd14174 157 --SACTPITTPELTTpcGSAEYMAPEVVE 183
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
296-558 7.17e-05

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: 45.15  E-value: 7.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 296 TEFHELEKIGSGEFGSVFKC-VKRLDgciyaIKRSKKPLA----GSVDEQNAL----REVYAHAVLgQHPHVVRYFSAWA 366
Cdd:cd05046   5 SNLQEITTLGRGEFGEVFLAkAKGIE-----EEGGETLVLvkalQKTKDENLQsefrRELDMFRKL-SHKNVVRLLGLCR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 367 EDDHMLIQNEYCNGGSL-----ADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNa 441
Cdd:cd05046  79 EAEPHYMILEYTDLGDLkqflrATKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVK- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 442 VSEEGDEDDWISNkvmfkigDLGHVTRISSPqveegdSRFLANEVLQEN-YShlPKADIFALALTV--VCAAGAEPLPRN 518
Cdd:cd05046 158 VSLLSLSKDVYNS-------EYYKLRNALIP------LRWLAPEAVQEDdFS--TKSDVWSFGVLMweVFTQGELPFYGL 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17865613 519 GDQ--WHEIRQGRLP-RIPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05046 223 SDEevLNRLQAGKLElPVPEGCPSRLYKLMTRCWAVNPKDRPS 265
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
304-458 7.62e-05

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: 44.79  E-value: 7.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFkcVKRLDGCIYAIKRSKKPlagSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSL 383
Cdd:cd14059   1 LGSGAQGAVF--LGKFRGEEVAVKKVRDE---KETDIKHLRKL-------NHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 384 ADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNaVSEEGDEDDW--ISNKVMF 458
Cdd:cd14059  69 YEVLRAGREI----TPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLK-ISDFGTSKELseKSTKMSF 140
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
301-559 9.58e-05

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 44.47  E-value: 9.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVfkcvkrLDGCIY-------AIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05086   2 IQEIGNGWFGKV------LLGEIYtgtsvarVVVKELKASANPKEQDDFLQQGEPYYIL-QHPNILQCVGQCVEAIPYLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAV-SENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseeGDeddwi 452
Cdd:cd05086  75 VFEFCDLGDLKTYLaNQQEKLRGDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLT-----------SD----- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 snkVMFKIGDLG-HVTRISSPQVEEGDS-----RFLANEVLQENYSHLPKAD------IFALALTV--VCAAGAEPLPRN 518
Cdd:cd05086 139 ---LTVKVGDYGiGFSRYKEDYIETDDKkyaplRWTAPELVTSFQDGLLAAEqtkysnIWSLGVTLweLFENAAQPYSDL 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17865613 519 GDQ---WHEIRQGRL----PRIPQVLSQELTELLKVMIHPdPERRPSA 559
Cdd:cd05086 216 SDRevlNHVIKERQVklfkPHLEQPYSDRWYEVLQFCWLS-PEKRPTA 262
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
301-568 1.06e-04

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: 44.47  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKpLAGSVD--------EQNALREVyahavlgQHPHVVRYFSAWAEDDHML 372
Cdd:cd14164   5 GTTIGEGSFSKVKLATSQKYCCKVAIKIVDR-RRASPDfvqkflprELSILRRV-------NHPNIVQMFECIEVANGRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQNEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwi 452
Cdd:cd14164  77 YIVMEAAATDLLQKIQEVHHI----PKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLS------------------ 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 SNKVMFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQeNYSHLPKA-DIFALALtVVCAAGAEPLPRNGDQWHEIR- 526
Cdd:cd14164 135 ADDRKIKIADFGFARFVEDYPELSttfcGSRAYTPPEVIL-GTPYDPKKyDVWSLGV-VLYVMVTGTMPFDETNVRRLRl 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17865613 527 QGRLPRIPQ--VLSQELTELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14164 213 QQRGVLYPSgvALEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
298-433 1.22e-04

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 44.63  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCV-NHKNIISLLNVFTPQKSLEEFQDV 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 378 CNGGSLADA-------VSENYRVMSYfteaelkdLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07876 102 YLVMELMDAnlcqvihMELDHERMSY--------LLYQMLCGIKHLHSAGIIHRDLKPSNIVV 156
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
304-556 1.29e-04

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: 44.31  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRL---DGCIYAIKRSKKplAGSVDEQNAL------REVYAHavLGQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05583   2 LGTGAYGKVFLVRKVGghdAGKLYAMKVLKK--ATIVQKAKTAehtmteRQVLEA--VRQSPFLVTLHYAFQTDAKLHLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsn 454
Cdd:cd05583  78 LDYVNGGELFTHLYQR----EHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL-------------DSEGHV-- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 455 kvmfKIGDLGhVTRISSPQVEE------GDSRFLANEVLQENYS-HLPKADIFALA-LTVVCAAGAEPLPRNGDQ--WHE 524
Cdd:cd05583 139 ----VLTDFG-LSKEFLPGENDraysfcGTIEYMAPEVVRGGSDgHDKAVDWWSLGvLTYELLTGASPFTVDGERnsQSE 213
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 525 IRQGRL---PRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05583 214 ISKRILkshPPIPKTFSAEAKDFILKLLEKDPKKR 248
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
298-433 1.32e-04

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: 44.70  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSV--FKCVKRLDGCIYAIKR-----SKKPLAgsvdeQNALREVYAHAVLGQHPHVVryfsaWAEDDH 370
Cdd:cd07857   2 YELIKELGQGAYGIVcsARNAETSEEETVAIKKitnvfSKKILA-----KRALRELKLLRHFRGHKNIT-----CLYDMD 71
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 371 MLIQNEYcNGGSL------ADaVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07857  72 IVFPGNF-NELYLyeelmeAD-LHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLV 138
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
304-556 1.40e-04

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: 44.51  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL---REVYAHAvlGQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTmteKRVLALA--NRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 381 GSLADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDEDDWIsnkvmfKI 460
Cdd:cd05570  81 GDLMFHIQRARR----FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL-------------DAEGHI------KI 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 461 GDLGhvtrISSPQVEEGDS--------RFLANEVLQE-NYShlPKADIFALA-LTVVCAAGAEPLPRNGDQ--WHEIrQG 528
Cdd:cd05570 138 ADFG----MCKEGIWGGNTtstfcgtpDYIAPEILREqDYG--FSVDWWALGvLLYEMLAGQSPFEGDDEDelFEAI-LN 210
                       250       260
                ....*....|....*....|....*...
gi 17865613 529 RLPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05570 211 DEVLYPRWLSREAVSILKGLLTKDPARR 238
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
339-568 1.41e-04

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: 44.06  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 339 EQNALREVYAHAVLGQHPHVVRYFSAW----AEDDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLR 414
Cdd:cd13984  38 QEEKIRAVFDNLIQLDHPNIVKFHRYWtdvqEEKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKSWKRWCTQILSALS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 415 YIHSMS--LVHMDIKPSNIFISRTSipnavseegdeddwisnkvMFKIGDLGHVT---RISSPQVEEGDSRFLANEvlqe 489
Cdd:cd13984 118 YLHSCDppIIHGNLTCDTIFIQHNG-------------------LIKIGSVAPDAihnHVKTCREEHRNLHFFAPE---- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 490 nYSHL----PKADIFALALTVVCAAGAEPLPRNGDQwhEIRQGRLPRIPQVLSQELT-ELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd13984 175 -YGYLedvtTAVDIYSFGMCALEMAALEIQSNGEKV--SANEEAIIRAIFSLEDPLQkDFIRKCLSVAPQDRPSARDLLF 251

                ....
gi 17865613 565 HSVL 568
Cdd:cd13984 252 HPVL 255
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
302-435 1.45e-04

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 44.21  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKC----VKRLDGCIYAIKRSK-KPLAGSVD------EQNA----LREVYAHAVLgQHPHVVRYFSAWA 366
Cdd:cd05095  11 EKLGEGQFGEVHLCeaegMEKFMDKDFALEVSEnQPVLVAVKmlradaNKNArndfLKEIKIMSRL-KDPNIIRLLAVCI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 367 EDDHMLIQNEYCNGGSLAD-----------AVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd05095  90 TDDPLCMITEYMENGDLNQflsrqqpegqlALPSNALTVSY---SDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK 166
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
344-504 1.46e-04

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: 44.29  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 344 REVYAHAVLgQHPHVVRYFSAWAE----DDHMLIQNEYCNGGSLADavsenYRVMSYFTEAELKDLLLQVGRGLRYIHS- 418
Cdd:cd14055  44 KDIFTDASL-KHENILQFLTAEERgvglDRQYWLITAYHENGSLQD-----YLTRHILSWEDLCKMAGSLARGLAHLHSd 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 419 --------MSLVHMDIKPSNIFisrtsipnaVSEEGDeddwisnkvmFKIGDLGHVTRI----------SSPQVeeGDSR 480
Cdd:cd14055 118 rtpcgrpkIPIAHRDLKSSNIL---------VKNDGT----------CVLADFGLALRLdpslsvdelaNSGQV--GTAR 176
                       170       180
                ....*....|....*....|....*....
gi 17865613 481 FLANEVLQ-----ENYSHLPKADIFALAL 504
Cdd:cd14055 177 YMAPEALEsrvnlEDLESFKQIDVYSMAL 205
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
301-440 1.51e-04

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: 44.16  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvdeQNALREVYAHAVLGQ------HPHVVRYFsawaedDHMLIQ 374
Cdd:cd14212   4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYF---RQAMLEIAILTLLNTkydpedKHHIVRLL------DHFMHH 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 375 NEYCN-----GGSLADAVSEN-YRVMSYFTeaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPN 440
Cdd:cd14212  75 GHLCIvfellGVNLYELLKQNqFRGLSLQL---IRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPE 143
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
302-504 1.53e-04

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: 44.27  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKcvKRLDGCIYAIKRSkkpLAGSVDEQNALREVYAhAVLGQHPHVVRYFSA------WAEDDHMLIQn 375
Cdd:cd14054   1 QLIGQGRYGTVWK--GSLDERPVAVKVF---PARHRQNFQNEKDIYE-LPLMEHSNILRFIGAderptaDGRMEYLLVL- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 376 EYCNGGSLADAVSENYrvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPsnifisrtsipnAVSEEgdedDWISNK 455
Cdd:cd14054  74 EYAPKGSLCSYLRENT-----LDWMSSCRMALSLTRGLAYLHTDLRRGDQYKP------------AIAHR----DLNSRN 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 456 VMFK------IGDLGHVTRISS-------PQVEEGDS-------RFLANEV------LQENYSHLPKADIFALAL 504
Cdd:cd14054 133 VLVKadgscvICDFGLAMVLRGsslvrgrPGAAENASisevgtlRYMAPEVlegavnLRDCESALKQVDVYALGL 207
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
300-434 1.70e-04

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: 43.84  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 300 ELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagSVDEQ---NALREVYAHAVLgQHPHVVRYfsawaeddHMLIQNE 376
Cdd:cd07871   9 KLDKLGEGTYATVFKGRSKLTENLVALKEIRL----EHEEGapcTAIREVSLLKNL-KHANIVTL--------HDIIHTE 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 377 YCN-------GGSLADAVSENYRVMSYFTeaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07871  76 RCLtlvfeylDSDLKQYLDNCGNLMSMHN---VKIFMFQLLRGLSYCHKRKILHRDLKPQNLLIN 137
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
297-436 1.72e-04

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: 44.26  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVfkCVKRL--DGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05597   2 DFEILKVIGRGAFGEV--AVVKLksTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLV 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 375 NEYCNGGSL-------ADAVSENyrvMSYFTEAELkdlLLqvgrGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05597  80 MDYYCGGDLltllskfEDRLPEE---MARFYLAEM---VL----AIDSIHQLGYVHRDIKPDNVLLDRN 138
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
304-433 1.89e-04

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: 43.68  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIK---RSK----KPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSaWAE--DDHMLIQ 374
Cdd:cd14101   8 LGKGGFGTVYAGHRISDGLQVAIKqisRNRvqqwSKLPGVNPVPNEVALLQSVGGGPGHRGVIRLLD-WFEipEGFLLVL 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 375 NEYCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14101  87 ERPQHCQDLFDYITER----GALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV 141
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
293-558 1.96e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 43.73  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 293 RYTTEFHELekiGSGEFGSVfkCVKRLD------GCIYAIKRSKKPL-----AGSVDEQNALREVYahavlgqHPHVVRY 361
Cdd:cd05080   4 RYLKKIRDL---GEGHFGKV--SLYCYDptndgtGEMVAVKALKADCgpqhrSGWKQEIDILKTLY-------HENIVKY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 362 FSAWAE--DDHMLIQNEYCNGGSLADAVSENyrvmsyftEAELKDLLL---QVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05080  72 KGCCSEqgGKSLQLIMEYVPLGSLRDYLPKH--------SIGLAQLLLfaqQICEGMAYLHSQHYIHRDLAARNVLLDND 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 437 SIpnavseegdeddwisnkvmFKIGDLGHVTRISSPQV-----EEGDSR--FLANEVLQENYSHLpKADIFALALTVV-- 507
Cdd:cd05080 144 RL-------------------VKIGDFGLAKAVPEGHEyyrvrEDGDSPvfWYAPECLKEYKFYY-ASDVWSFGVTLYel 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 508 ---CAAGAEPlPRNGDQWHEIRQG---------------RLPRiPQVLSQELTELLKVMIHPDPERRPS 558
Cdd:cd05080 204 lthCDSSQSP-PTKFLEMIGIAQGqmtvvrliellergeRLPC-PDKCPQEVYHLMKNCWETEASFRPT 270
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
299-433 2.22e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 42.29  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 299 HELEKIGSGEFGSVFKCVkrlDGCIYAIKrskkpLAGSVDEQNALREVYAHAVLGQHP--HVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05120   1 ISVKLIKEGGDNKVYLLG---DPREYVLK-----IGPPRLKKDLEKEAAMLQLLAGKLslPVPKVYGFGESDGWEYLLME 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLADavsenyrVMSYFTEAELKDLLLQVGRGLRYIHSM---SLVHMDIKPSNIFI 433
Cdd:cd05120  73 RIEGETLSE-------VWPRLSEEEKEKIADQLAEILAALHRIdssVLTHGDLHPGNILV 125
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
302-434 2.26e-04

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: 43.27  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAgsvdeqnaLREVYAHAVLgQHPHVVRYFSAWaeDDHMLIQNEYCNG 380
Cdd:cd14109  10 EDEKRAAQGAPFHVTERSTGRNFLAQlRYGDPFL--------MREVDIHNSL-DHPNIVQMHDAY--DDEKLAVTVIDNL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 381 GSLADAVSEN-YRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd14109  79 ASTIELVRDNlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ 133
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
298-433 2.26e-04

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: 43.74  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREvyaHAVLGQ--HPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05607   4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKlDKKRLKKKSGEKMALLE---KEILEKvnSPFIVSLAYAFETKTHLCLV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865613 375 NEYCNGGSLadavseNYRVMSYFTEA-ELKDLLL---QVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05607  81 MSLMNGGDL------KYHIYNVGERGiEMERVIFysaQITCGILHLHSLKIVYRDMKPENVLL 137
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
300-434 2.59e-04

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: 43.44  E-value: 2.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 300 ELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVdEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEYCN 379
Cdd:cd07872  10 KLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGA-PCTAIREVSLLKDL-KHANIVTLHDIVHTDKSLTLVFEYLD 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17865613 380 GgSLADAVSENYRVMSYFTeaeLKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd07872  88 K-DLKQYMDDCGNIMSMHN---VKIFLYQILRGLAYCHRRKVLHRDLKPQNLLIN 138
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
298-436 2.61e-04

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: 43.53  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsVDEQ-----NALREVYAHAVLgQHPHVVRYFSAWAEDDHML 372
Cdd:cd07869   7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR------LQEEegtpfTAIREASLLKGL-KHANIVLLHDIIHTKETLT 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 373 IQNEYCNggslADAVSENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd07869  80 LVFEYVH----TDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDT 139
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
298-556 2.73e-04

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: 43.42  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREVYAHAVLGQHpHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05632   4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRlEKKRIKKRKGESMALNEKQILEKVNSQ-FVVNLAYAYETKDALCLVLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSL-------ADAVSENYRVMSYFTEaelkdlllqVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegDED 449
Cdd:cd05632  83 IMNGGDLkfhiynmGNPGFEEERALFYAAE---------ILCGLEDLHRENTVYRDLKPENILL-------------DDY 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 450 DWIsnkvmfKIGDLGHVTRIssPQVEE-----GDSRFLANEVLQ-ENYSHLPkaDIFALA-LTVVCAAGAEPL-PRNGDQ 521
Cdd:cd05632 141 GHI------RISDLGLAVKI--PEGESirgrvGTVGYMAPEVLNnQRYTLSP--DYWGLGcLIYEMIEGQSPFrGRKEKV 210
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 522 WHEIRQGRLPRIPQVLSQELTE----LLKVMIHPDPERR 556
Cdd:cd05632 211 KREEVDRRVLETEEVYSAKFSEeaksICKMLLTKDPKQR 249
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
304-431 2.88e-04

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: 43.46  E-value: 2.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQ---NALREVYAHAVlgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVkhiMAERNVLLKNV--KHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17865613 381 GSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd05575  81 GELFFHLQRE----RHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENI 127
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
297-433 2.96e-04

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: 43.51  E-value: 2.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05627   3 DFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIME 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 377 YCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05627  83 FLPGGDMMTLLMKK----DTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLL 135
pknD PRK13184
serine/threonine-protein kinase PknD;
303-504 2.98e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 43.99  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  303 KIGSGEFGSVF-----KCVKRLdgciyAIKRSKKPLAGSVDEQNA-LREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:PRK13184   9 LIGKGGMGEVYlaydpVCSRRV-----ALKKIREDLSENPLLKKRfLREAKIAADL-IHPGIVPVYSICSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613  377 YCNGGSLADAVSENYRVMSYFTEAELKD-------LLLQVGRGLRYIHSMSLVHMDIKPSNIFI---SRTSIPN---AVS 443
Cdd:PRK13184  83 YIEGYTLKSLLKSVWQKESLSKELAEKTsvgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLglfGEVVILDwgaAIF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613  444 EEGDEDDWISNKVMFKiGDLGHvtRISSPQVEEGDSRFLANEVLQENYSHLpKADIFALAL 504
Cdd:PRK13184 163 KKLEEEDLLDIDVDER-NICYS--SMTIPGKIVGTPDYMAPERLLGVPASE-STDIYALGV 219
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
339-569 3.89e-04

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 42.81  E-value: 3.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 339 EQNALREVYAHAVLGQHPHVVRYFSAWAE----DDHMLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLR 414
Cdd:cd14034  53 QEEKVKAVFDNLIQLEHLNIVKFHKYWADvkenRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALS 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 415 YIHSMS--LVHMDIKPSNIFISRTSipnavseegdeddwisnkvMFKIGDLGHVT---RISSPQVEEGDSRFLANEvLQE 489
Cdd:cd14034 133 YLHSCDppIIHGNLTCDTIFIQHNG-------------------LIKIGSVAPDTinnHVKTCREEQKNLHFFAPE-YGE 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 490 NYSHLPKADIFALALTVVCAAGAEpLPRNGDQWHeIRQGRLPRIPQVLSQELT-ELLKVMIHPDPERRPSAMVLVKHSVL 568
Cdd:cd14034 193 VANVTTAVDIYSFGMCALEMAVLE-IQGNGESSY-VPQEAINSAIQLLEDPLQrEFIQKCLEVDPSKRPTARELLFHQAL 270

                .
gi 17865613 569 L 569
Cdd:cd14034 271 F 271
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
297-433 4.01e-04

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: 43.10  E-value: 4.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05628   2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 377 YCNGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05628  82 FLPGGDMMTLLMKK----DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLL 134
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
295-433 4.46e-04

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: 42.77  E-value: 4.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 295 TTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplAGSVDEQNALrEVYAHAVLGQHP----HVVRYFSAWAEDDH 370
Cdd:cd14227  14 TNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKN--HPSYARQGQI-EVSILARLSTESaddyNFVRAYECFQHKNH 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 371 ------MLIQNEYcnggslaDAVSENYrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14227  91 tclvfeMLEQNLY-------DFLKQNK--FSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIML 150
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
297-556 4.69e-04

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: 43.10  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGS---VDEQNALREVYAHAvlGQHPHVVRYFSAWAEDDHMLI 373
Cdd:cd05618  21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDdedIDWVQTEKHVFEQA--SNHPFLVGLHSCFQTESRLFF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 QNEYCNGGSLADAVSENYRVmsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavSEEGDeddwis 453
Cdd:cd05618  99 VIEYVNGGDLMFHMQRQRKL----PEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLL---------DSEGH------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 454 nkvmFKIGDLGHVTRISSPQVEE----GDSRFLANEVLQ-ENYSHlpKADIFALA-LTVVCAAGAEPL-----PRNGDQW 522
Cdd:cd05618 160 ----IKLTDYGMCKEGLRPGDTTstfcGTPNYIAPEILRgEDYGF--SVDWWALGvLMFEMMAGRSPFdivgsSDNPDQN 233
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17865613 523 HE-----IRQGRLPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05618 234 TEdylfqVILEKQIRIPRSLSVKAASVLKSFLNKDPKER 272
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
405-433 4.72e-04

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: 42.74  E-value: 4.72e-04
                        10        20
                ....*....|....*....|....*....
gi 17865613 405 LLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd07858 113 FLYQLLRGLKYIHSANVLHRDLKPSNLLL 141
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
297-438 5.33e-04

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: 42.29  E-value: 5.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 297 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHpHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd07848   2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQE-NIVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 377 YCNGGSLaDAVSEnyrVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSI 438
Cdd:cd07848  81 YVEKNML-ELLEE---MPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV 138
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
304-431 5.36e-04

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: 42.32  E-value: 5.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKR-----SKKPLAGSVDEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYC 378
Cdd:cd14088   9 IKTEEFCEIFRAKDKTTGKLYTCKKflkrdGRKVRKAAKNEINILKMV-------KHPNILQLVDVFETRKEYFIFLELA 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17865613 379 NGGSLADAVSENyrvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNI 431
Cdd:cd14088  82 TGREVFDWILDQ----GYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENL 130
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
331-564 5.47e-04

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: 42.31  E-value: 5.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 331 KPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAV-SENYRVMSY--------FTEAE 401
Cdd:cd05098  54 KSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLqARRPPGMEYcynpshnpEEQLS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 402 LKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdEDDwisnkvMFKIGDLG------HVTRISSP 472
Cdd:cd05098 134 SKDLVscaYQVARGMEYLASKKCIHRDLAARNVLVT-------------EDN------VMKIADFGlardihHIDYYKKT 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 473 QVEEGDSRFLANEVLQEN-YSHLPKADIFALALTVVCAAGAEPLPrnGDQWHE----IRQGRLPRIPQVLSQELTELLKV 547
Cdd:cd05098 195 TNGRLPVKWMAPEALFDRiYTHQSDVWSFGVLLWEIFTLGGSPYP--GVPVEElfklLKEGHRMDKPSNCTNELYMMMRD 272
                       250
                ....*....|....*..
gi 17865613 548 MIHPDPERRPSAMVLVK 564
Cdd:cd05098 273 CWHAVPSQRPTFKQLVE 289
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
280-433 5.53e-04

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: 42.69  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 280 AKRITITESNMKsRYTTEFHELEKIGSGEFGSV----FKCVKRldgcIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQH 355
Cdd:cd05624  57 AKPFTQLVKEMQ-LHRDDFEIIKVIGRGAFGEVavvkMKNTER----IYAMKILNKWEMLKRAETACFREERNVLVNGDC 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 356 PHVVRYFSAWAEDDHMLIQNEYCNGGSL-------ADAVSENyrvMSYFTEAELKdlllqvgRGLRYIHSMSLVHMDIKP 428
Cdd:cd05624 132 QWITTLHYAFQDENYLYLVMDYYVGGDLltllskfEDKLPED---MARFYIGEMV-------LAIHSIHQLHYVHRDIKP 201

                ....*
gi 17865613 429 SNIFI 433
Cdd:cd05624 202 DNVLL 206
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
298-564 6.37e-04

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 41.86  E-value: 6.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 298 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVY--AHAVLGQ--HPH-VVRYFSAWAEDDHML 372
Cdd:cd05078   1 LIFNESLGQGTFTKIFKGIRREVGDYGQLHETEVLLKVLDKAHRNYSESFfeAASMMSQlsHKHlVLNYGVCVCGDENIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 373 IQnEYCNGGSLADAVSENYRVMSYFTEAELKDlllQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegDEDDWI 452
Cdd:cd05078  81 VQ-EYVKFGSLDTYLKKNKNCINILWKLEVAK---QLAWAMHFLEEKTLVHGNVCAKNILLIR-----------EEDRKT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 453 SNKVMFKIGDLGHVTRIsspqveegdsrfLANEVLQENYSHLPKADI--------------FALALTVVCAAGAEPL--- 515
Cdd:cd05078 146 GNPPFIKLSDPGISITV------------LPKDILLERIPWVPPECIenpknlslatdkwsFGTTLWEICSGGDKPLsal 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17865613 516 -PRNGDQWHEIRQgrlpRIPQVLSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd05078 214 dSQRKLQFYEDRH----QLPAPKWTELANLINNCMDYEPDHRPSFRAIIR 259
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
304-467 6.49e-04

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 42.31  E-value: 6.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDG----CIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHpHVVRYFSAWAEDDHMLIQNEYCn 379
Cdd:cd14215  20 LGEGTFGRVVQCIDHRRGgarvALKIIKNVEKYKEAARLEINVLEKINEKDPENKN-LCVQMFDWFDYHGHMCISFELL- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 380 GGSLADAVSENyrvmSYFTEA--ELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEEGDEDDWISNKVM 457
Cdd:cd14215  98 GLSTFDFLKEN----NYLPYPihQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTA 173
                       170
                ....*....|
gi 17865613 458 FKIGDLGHVT 467
Cdd:cd14215 174 IRVVDFGSAT 183
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
304-556 7.62e-04

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: 42.09  E-value: 7.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDE-QNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGS 382
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDvDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 383 LADAVSENYRvmsyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseEGDEDDWISNKVMFKIGD 462
Cdd:cd05591  83 LMFQIQRARK----FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL-----------DAEGHCKLADFGMCKEGI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 463 LGHVTrissPQVEEGDSRFLANEVLQEnYSHLPKADIFALALTVVCAAGAEPlPRNGDQWHEIRQGRLPR---IPQVLSQ 539
Cdd:cd05591 148 LNGKT----TTTFCGTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQP-PFEADNEDDLFESILHDdvlYPVWLSK 221
                       250
                ....*....|....*..
gi 17865613 540 ELTELLKVMIHPDPERR 556
Cdd:cd05591 222 EAVSILKAFMTKNPAKR 238
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
402-491 7.76e-04

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: 42.04  E-value: 7.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 402 LKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdeddwiSNKVMfKIGDLGHVtrisspQVEEGD-SR 480
Cdd:cd07853 105 VKVFLYQILRGLKYLHSAGILHRDIKPGNLLVN------------------SNCVL-KICDFGLA------RVEEPDeSK 159
                        90
                ....*....|.
gi 17865613 481 FLANEVLQENY 491
Cdd:cd07853 160 HMTQEVVTQYY 170
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
329-564 1.01e-03

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: 41.54  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 329 SKKPLAGSVDEQNALRevyahaVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLAD--------AVSENYRVMSYFTEA 400
Cdd:cd05101  69 TEKDLSDLVSEMEMMK------MIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREylrarrppGMEYSYDINRVPEEQ 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 401 -ELKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRtsipnavseegdeddwisNKVMfKIGDLGHVTRISSPQVEE 476
Cdd:cd05101 143 mTFKDLVsctYQLARGMEYLASQKCIHRDLAARNVLVTE------------------NNVM-KIADFGLARDINNIDYYK 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 477 GDS------RFLANEVLQEN-YSHLPKADIFALALTVVCAAGAEPLPrnGDQWHE----IRQGRLPRIPQVLSQELTELL 545
Cdd:cd05101 204 KTTngrlpvKWMAPEALFDRvYTHQSDVWSFGVLMWEIFTLGGSPYP--GIPVEElfklLKEGHRMDKPANCTNELYMMM 281
                       250
                ....*....|....*....
gi 17865613 546 KVMIHPDPERRPSAMVLVK 564
Cdd:cd05101 282 RDCWHAVPSQRPTFKQLVE 300
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
354-434 1.05e-03

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: 41.78  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAEDDHMLIQNEYCNGGSladavsENYRVMSYFTE----AELKDLLLQVGRGLRYIHSMSLVHMDIKPS 429
Cdd:cd08226  57 RHPNIMTHWTVFTEGSWLWVISPFMAYGS------ARGLLKTYFPEgmneALIGNILYGAIKALNYLHQNGCIHRSVKAS 130

                ....*
gi 17865613 430 NIFIS 434
Cdd:cd08226 131 HILIS 135
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
302-556 1.07e-03

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: 41.30  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVF--KCVKRL---DGCIYAIKRSKKPlAGSVDEQNALREVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNE 376
Cdd:cd05049  11 RELGEGAFGKVFlgECYNLEpeqDKMLVAVKTLKDA-SSPDARKDFEREAELLTNL-QHENIVKFYGVCTEGDPLLMVFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 377 YCNGGSLA--------DAVS--ENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseeG 446
Cdd:cd05049  89 YMEHGDLNkflrshgpDAAFlaSEDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLV------------G 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 447 DeddwisnKVMFKIGDLGHVTRI-SSPQVEEGDSRFL------ANEVLQENYShlPKADIFALALTV--VCAAGAEPLPR 517
Cdd:cd05049 157 T-------NLVVKIGDFGMSRDIySTDYYRVGGHTMLpirwmpPESILYRKFT--TESDVWSFGVVLweIFTYGKQPWFQ 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17865613 518 --NGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERR 556
Cdd:cd05049 228 lsNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQR 268
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
295-433 1.11e-03

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: 41.61  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 295 TTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKK----PLAGSVDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDH 370
Cdd:cd14228  14 TNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNhpsyARQGQIEVSILSRLSSENA---DEYNFVRSYECFQHKNH 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 371 ------MLIQNEYcnggslaDAVSENYrvMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd14228  91 tclvfeMLEQNLY-------DFLKQNK--FSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIML 150
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
302-564 1.17e-03

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: 41.15  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsvDEQNAL----REVYAHAVLgQHPHVVRYFSAWAEDDHMLIQNEY 377
Cdd:cd14153   6 ELIGKGRFGQVYHGRWHGEVAIRLIDIER-------DNEEQLkafkREVMAYRQT-RHENVVLFMGACMSPPHLAIITSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 378 CNGGSLADAVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIP---------NAVSEEGDE 448
Cdd:cd14153  78 CKGRTLYSVVRDAKVVLDV---NKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVitdfglftiSGVLQAGRR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 449 DDwisnKVMFKIGDLGHVtrisSPQVeegdSRFLANEVLQENYSHLPKADIFALAlTVVCAAGAEPLPRNGDQ-----Wh 523
Cdd:cd14153 155 ED----KLRIQSGWLCHL----APEI----IRQLSPETEEDKLPFSKHSDVFAFG-TIWYELHAREWPFKTQPaeaiiW- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17865613 524 EIRQGRLPRIPQV-LSQELTELLKVMIHPDPERRPSAMVLVK 564
Cdd:cd14153 221 QVGSGMKPNLSQIgMGKEISDILLFCWAYEQEERPTFSKLME 262
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
406-559 1.78e-03

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 41.23  E-value: 1.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 406 LLQVGRGL----RYIHSMSLVHMDIKPSNIFISRTSIPNAVseegDEDDwisnkvmFKIGDLGHVtrissPQVEEGDSRF 481
Cdd:COG4248 123 LLRTARNLaaavAALHAAGYVHGDVNPSNILVSDTALVTLI----DTDS-------FQVRDPGKV-----YRCVVGTPEF 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 482 LANEVLQENYSHL---PKADIFALALTV--VCAAGAEPL------PRNGDQWHE-IRQGRLPRIPQ-------------- 535
Cdd:COG4248 187 TPPELQGKSFARVdrtEEHDRFGLAVLIfqLLMEGRHPFsgvyqgDGDDPTLEErIAMGHFVYHPNrrvlirpppraipy 266
                       170       180
                ....*....|....*....|....*...
gi 17865613 536 -VLSQELTEL-LKVMI--HPDPERRPSA 559
Cdd:COG4248 267 eILHPYLQELfERAFIdgHHNPQLRPSA 294
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
402-522 1.92e-03

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 40.78  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 402 LKDLLLQVGRGLRYIHSM-SLVHMDIKPSNIFISRTSI-PNAVSEEGDE----------DDWISNKVMFKIGDLGHVTRI 469
Cdd:cd14216 121 VKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSVNEQyIRRLAAEATEwqrnflvnplEPKNAEKLKVKIADLGNACWV 200
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 470 SSPQVEEGDSR-FLANEVLQENYSHLPkADIFALALTVVCAAGAEPL--PRNGDQW 522
Cdd:cd14216 201 HKHFTEDIQTRqYRSLEVLIGSGYNTP-ADIWSTACMAFELATGDYLfePHSGEDY 255
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
295-438 2.01e-03

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 40.71  E-value: 2.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 295 TTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQnALREVYAHAV-LGQ--HPHVVRYFSAWAEDDHM 371
Cdd:cd05111   6 ETELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQ-SFQAVTDHMLaIGSldHAYIVRLLGICPGASLQ 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865613 372 LIqNEYCNGGSLADAVSENYRVMSyftEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSI 438
Cdd:cd05111  85 LV-TQLLPLGSLLDHVRQHRGSLG---PQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQ 147
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
304-434 2.09e-03

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: 40.29  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKcvkrldGCIYAIKRSKKPLA------GSVDEQNA--LREVyahAVLGQ--HPHVVRYFSAWAEDDHMLI 373
Cdd:cd05064  13 LGTGRFGELCR------GCLKLPSKRELPVAihtlraGCSDKQRRgfLAEA---LTLGQfdHSNIVRLEGVITRGNTMMI 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 374 QNEYCNGGSLaDAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFIS 434
Cdd:cd05064  84 VTEYMSNGAL-DSFLRKHE--GQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVN 141
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
301-435 2.68e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 40.04  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKCVKRL--DGCIYAIKRSKKPlagsvdEQNALREVYAHAVLGQHPHVVRYFSAWAED--DHMLIQne 376
Cdd:cd14129   5 LRKIGGGGFGEIYDALDLLtrENVALKVESAQQP------KQVLKMEVAVLKKLQGKDHVCRFIGCGRNDrfNYVVMQ-- 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17865613 377 yCNGGSLADAVSENYRvmSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISR 435
Cdd:cd14129  77 -LQGRNLADLRRSQSR--GTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGR 132
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
301-426 3.04e-03

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 40.01  E-value: 3.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 301 LEKIGSGEFGSVFKC---------------VKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAW 365
Cdd:cd05051  10 VEKLGEGQFGEVHLCeanglsdltsddfigNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQL-KDPNIVRLLGVC 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865613 366 AEDDHMLIQNEYCNGGSL-----------ADAVSENYRVMSYFTeaeLKDLLLQVGRGLRYIHSMSLVHMDI 426
Cdd:cd05051  89 TRDEPLCMIVEYMENGDLnqflqkheaetQGASATNSKTLSYGT---LLYMATQIASGMKYLESLNFVHRDL 157
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
303-575 3.28e-03

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: 40.02  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVF--KCVK---RLDGCIYAIKRSKKPlagsvdEQNALREVYAHAVLG---QHPHVVRYFSAWAEDDHMLIQ 374
Cdd:cd05093  12 ELGEGAFGKVFlaECYNlcpEQDKILVAVKTLKDA------SDNARKDFHREAELLtnlQHEHIVKFYGVCVEGDPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 375 NEYCNGGSL--------ADAV-SENYRVMSYFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTsipnavsee 445
Cdd:cd05093  86 FEYMKHGDLnkflrahgPDAVlMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN--------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 446 gdeddwisnkVMFKIGDLGHVTRISSPQVEE--GDS----RFLANE-VLQENYShlPKADIFALALTV--VCAAGAEPLP 516
Cdd:cd05093 157 ----------LLVKIGDFGMSRDVYSTDYYRvgGHTmlpiRWMPPEsIMYRKFT--TESDVWSLGVVLweIFTYGKQPWY 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865613 517 R--NGDQWHEIRQGRLPRIPQVLSQELTELLKVMIHPDPERRPSAMVLvkHSVLLSASRKS 575
Cdd:cd05093 225 QlsNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEI--HSLLQNLAKAS 283
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
302-441 3.52e-03

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 39.78  E-value: 3.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIK----RSKKPlagsvdeqnALREVY-AHAVLGQHPHV--VRYFSAwaEDDHMLIQ 374
Cdd:cd14127   6 KKIGEGSFGVIFEGTNLLNGQQVAIKfeprKSDAP---------QLRDEYrTYKLLAGCPGIpnVYYFGQ--EGLHNILV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865613 375 NEYCnGGSLADAVSENYRVMSYFTEAEL-KDLLLQVgrglRYIHSMSLVHMDIKPSNIFISRTSIPNA 441
Cdd:cd14127  75 IDLL-GPSLEDLFDLCGRKFSVKTVVMVaKQMLTRV----QTIHEKNLIYRDIKPDNFLIGRPGTKNA 137
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
354-562 3.68e-03

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: 39.95  E-value: 3.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 354 QHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAVSENYRVMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFi 433
Cdd:cd14152  54 RHENVVLFMGACMHPPHLAIITSFCKGRTLYSFVRDPKTSLDI---NKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 434 srtsipnavseegdeddWISNKVMfkIGDLGHVTriSSPQVEEGDSR-----------FLANEVLQE-----NYSHLP-- 495
Cdd:cd14152 130 -----------------YDNGKVV--ITDFGLFG--ISGVVQEGRREnelklphdwlcYLAPEIVREmtpgkDEDCLPfs 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865613 496 -KADIFALA-LTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLS-----QELTELLKVMIHPDPERRPSAMVL 562
Cdd:cd14152 189 kAADVYAFGtIWYELQARDWPLKNQPAEALIWQIGSGEGMKQVLTtislgKEVTEILSACWAFDLEERPSFTLL 262
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
303-472 4.11e-03

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: 39.67  E-value: 4.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKcVKRLDGCI---YAIKRskkpLAGSVDEQNALREVYAHAVLgQHPHVV---RYFSAWAEDDHMLI--- 373
Cdd:cd07867   9 KVGRGTYGHVYK-AKRKDGKDekeYALKQ----IEGTGISMSACREIALLREL-KHPNVIalqKVFLSHSDRKVWLLfdy 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 374 -QNEYCNGGSLADAVSENYRVMSyFTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFisrtsipnaVSEEGDEDDWI 452
Cdd:cd07867  83 aEHDLWHIIKFHRASKANKKPMQ-LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANIL---------VMGEGPERGRV 152
                       170       180
                ....*....|....*....|
gi 17865613 453 snkvmfKIGDLGHVTRISSP 472
Cdd:cd07867 153 ------KIADMGFARLFNSP 166
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
402-564 4.57e-03

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 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. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 39.58  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 402 LKDLL---LQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIpnavseegdeddwisnkvmFKIGDLGHVTRI-SSPQ-VEE 476
Cdd:cd05102 171 MEDLIcysFQVARGMEFLASRKCIHRDLAARNILLSENNV-------------------VKICDFGLARDIyKDPDyVRK 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 477 GDSR----FLANE-VLQENYSHLPKADIFALALTVVCAAGAEPLPR---NGDQWHEIRQGRLPRIPQVLSQELTELLKVM 548
Cdd:cd05102 232 GSARlplkWMAPEsIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGvqiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSC 311
                       170
                ....*....|....*.
gi 17865613 549 IHPDPERRPSAMVLVK 564
Cdd:cd05102 312 WHGDPKERPTFSDLVE 327
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
304-436 5.15e-03

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: 39.48  E-value: 5.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 304 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGS---VDEQNALREVYAHAvlgQHPHVVRYFSAWAEDDHMLIQNEYCNG 380
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSrseVTHTLAERTVLAQV---DCPFIVPLKFSFQSPEKLYLVLAFING 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 381 GSLADAVSENYRVMSYFTEAELKDLLLqvgrGLRYIHSMSLVHMDIKPSNIFISRT 436
Cdd:cd05585  79 GELFHHLQREGRFDLSRARFYTAELLC----ALECLHKFNVIYRDLKPENILLDYT 130
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
303-433 5.70e-03

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 39.16  E-value: 5.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 303 KIGSGEFGSVFKCV-----KRLDgciYAIKRSKKPLAGSVDEQNALREVYAHAVlgQHPHVVRYFSAWAEDDHMLIQnEY 377
Cdd:cd05115  11 ELGSGNFGCVKKGVykmrkKQID---VAIKVLKQGNEKAVRDEMMREAQIMHQL--DNPYIVRMIGVCEAEALMLVM-EM 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17865613 378 CNGGSLADAVSENYRVMsyfTEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:cd05115  85 ASGGPLNKFLSGKKDEI---TVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL 137
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
408-433 6.04e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 39.47  E-value: 6.04e-03
                         10        20
                 ....*....|....*....|....*.
gi 17865613  408 QVGRGLRYIHSMSLVHMDIKPSNIFI 433
Cdd:PHA03209 165 QILEGLRYLHAQRIIHRDVKTENIFI 190
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
302-433 7.31e-03

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 38.76  E-value: 7.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKC----------------VKRLDGCIYAIKrSKKPLAGSVDEQNALREVYAHAVLgQHPHVVRYFSAW 365
Cdd:cd05096  11 EKLGEGQFGEVHLCevvnpqdlptlqfpfnVRKGRPLLVAVK-ILRPDANKNARNDFLKEVKILSRL-KDPNIIRLLGVC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 366 AEDDHMLIQNEYCNGGSL----------------ADAVSENYR--VMSYfteAELKDLLLQVGRGLRYIHSMSLVHMDIK 427
Cdd:cd05096  89 VDEDPLCMITEYMENGDLnqflsshhlddkeengNDAVPPAHClpAISY---SSLLHVALQIASGMKYLSSLNFVHRDLA 165

                ....*.
gi 17865613 428 PSNIFI 433
Cdd:cd05096 166 TRNCLV 171
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
340-569 7.78e-03

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 38.75  E-value: 7.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 340 QNALREVYAHAVLGQHPHVVRYFSAW--AEDDH--MLIQNEYCNGGSLADAVSENYRVMSYFTEAELKDLLLQVGRGLRY 415
Cdd:cd14035  39 EDKIKTMFENLTLVDHPNIVKFHKYWldVKDNHarVVFITEYVSSGSLKQFLKKTKKNHKTMNARAWKRWCTQILSALSY 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 416 IHSMS--LVHMDIKPSNIFISRTSipnavseegdeddwisnkvMFKIGDLGHvtRISSPQVEEGDSRFLANEVLQE--NY 491
Cdd:cd14035 119 LHSCEppIIHGNLTSDTIFIQHNG-------------------LIKIGSVWH--RLFVNVLPEGGVRGPLRQEREElrNL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 492 SHLP----------KADIFALALTVVCAAGAEpLPRNGDQwhEIRQGRLPRIPQVLSQ-ELTELLKVMIHPDPERRPSAM 560
Cdd:cd14035 178 HFFPpeygscedgtAVDIFSFGMCALEMAVLE-IQANGDT--RVSEEAIARARHSLEDpNMREFILSCLRHNPCKRPTAH 254

                ....*....
gi 17865613 561 VLVKHSVLL 569
Cdd:cd14035 255 DLLFHRVLF 263
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
313-543 7.98e-03

Pseudokinase domain of the unknown subfamily 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: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 38.69  E-value: 7.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 313 FKCVKRLDGCIYAIKRSKK---PLAGSV-DEQNALREVyahavlgQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADA-V 387
Cdd:cd14045  22 FTQTGIYDGRTVAIKKIAKksfTLSKRIrKEVKQVREL-------DHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVlL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 388 SENYRVMSYFTEAELKDlllqVGRGLRYIHSMSLVHMDIKPSNIFIsrtsipnavseegdEDDWISnkvmfKIGDLGhvt 467
Cdd:cd14045  95 NEDIPLNWGFRFSFATD----IARGMAYLHQHKIYHGRLKSSNCVI--------------DDRWVC-----KIADYG--- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 468 rISSPQVEEGDSRF-----------LANEVLQENYSHLPKA-DIFALALTVV-CAAGAEPLPrngDQWHEIRQGRLPRIP 534
Cdd:cd14045 149 -LTTYRKEDGSENAsgyqqrlmqvyLPPENHSNTDTEPTQAtDVYSYAIILLeIATRNDPVP---EDDYSLDEAWCPPLP 224

                ....*....
gi 17865613 535 QVLSQELTE 543
Cdd:cd14045 225 ELISGKTEN 233
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
338-564 8.67e-03

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: 38.85  E-value: 8.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 338 DEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAV-SENYRVMSYFTEA--------ELKDLL-- 406
Cdd:cd05100  60 DLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLrARRPPGMDYSFDTcklpeeqlTFKDLVsc 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 407 -LQVGRGLRYIHSMSLVHMDIKPSNIFISrtsipnavseegdEDDwisnkvMFKIGDLGHVTRISSPQVEEGDS------ 479
Cdd:cd05100 140 aYQVARGMEYLASQKCIHRDLAARNVLVT-------------EDN------VMKIADFGLARDVHNIDYYKKTTngrlpv 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 480 RFLANEVLQEN-YSHLPKADIFALALTVVCAAGAEPLPrnGDQWHE----IRQGRLPRIPQVLSQELTELLKVMIHPDPE 554
Cdd:cd05100 201 KWMAPEALFDRvYTHQSDVWSFGVLLWEIFTLGGSPYP--GIPVEElfklLKEGHRMDKPANCTHELYMIMRECWHAVPS 278
                       250
                ....*....|
gi 17865613 555 RRPSAMVLVK 564
Cdd:cd05100 279 QRPTFKQLVE 288
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
302-558 9.08e-03

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 38.63  E-value: 9.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 302 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKpLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIqnEYCNGG 381
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPS-LHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGLVM--EYMETG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 382 SLADAVSenyrvmsyfTEAELKDLLLQV----GRGLRYIHSMS--LVHMDIKPSNIFIsrtsipnavseEGDEDDWISNK 455
Cdd:cd14025  79 SLEKLLA---------SEPLPWELRFRIihetAVGMNFLHCMKppLLHLDLKPANILL-----------DAHYHVKISDF 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865613 456 VMFKIGDLGHVTRISSPQVeEGDSRFLANE-VLQENYSHLPKADIFALALtVVCAAGAEPLPRNGDQWH-----EIRQGR 529
Cdd:cd14025 139 GLAKWNGLSHSHDLSRDGL-RGTIAYLPPErFKEKNRCPDTKHDVYSFAI-VIWGILTQKKPFAGENNIlhimvKVVKGH 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17865613 530 ---LPRIPQVLSQELTELLKVMIH---PDPERRPS 558
Cdd:cd14025 217 rpsLSPIPRQRPSECQQMICLMKRcwdQDPRKRPT 251
 
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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