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Conserved domains on  [gi|1907200402|ref|XP_036011189|]
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serine/threonine-protein kinase ULK3 isoform X1 [Mus musculus]

Protein Classification

serine/threonine-protein kinase ULK3( domain architecture ID 10197517)

serine/threonine-protein kinase ULK3 (unc-51 like kinase 3) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
18-269 0e+00

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: 533.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSP 177
Cdd:cd14121    81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLRGSP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14121   161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPIEIPTRPELSADCRDLLLRLLQRDPDR 240
                         250
                  ....*....|..
gi 1907200402 258 RISFKDFFAHPW 269
Cdd:cd14121   241 RISFEEFFAHPF 252
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
279-353 6.68e-35

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


:

Pssm-ID: 239147  Cd Length: 75  Bit Score: 124.54  E-value: 6.68e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 279 ESLAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQ 353
Cdd:cd02684     1 ESLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALIASDTQ 75
MIT super family cl00299
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
374-425 4.67e-05

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


The actual alignment was detected with superfamily member cd02656:

Pssm-ID: 469712  Cd Length: 75  Bit Score: 41.53  E-value: 4.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 374 PRLLAALEVASAALaKEEEAGKEQDALDLYQHSLGELLVLLAGKAPALVRAL 425
Cdd:cd02656     1 ELLQQAKELIKQAV-KEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKL 51
 
Name Accession Description Interval E-value
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
18-269 0e+00

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: 533.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSP 177
Cdd:cd14121    81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLRGSP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14121   161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPIEIPTRPELSADCRDLLLRLLQRDPDR 240
                         250
                  ....*....|..
gi 1907200402 258 RISFKDFFAHPW 269
Cdd:cd14121   241 RISFEEFFAHPF 252
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-270 1.07e-100

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 301.37  E-value: 1.07e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLAR-DKKTGKLVAIKVI-KKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGHVKLADFGLARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS-FSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 1907200402  253 RDPARRISFKDFFAHPWV 270
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
14-270 1.95e-65

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 209.41  E-value: 1.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAK-HRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASAlqflhernishldlkpqnillssLEKPHlkladfgfaqhmspwdEKHVL 173
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEG-----------------------LESGS----------------SLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLER 253
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKK 200
                         250
                  ....*....|....*..
gi 1907200402 254 DPARRISFKDFFAHPWV 270
Cdd:pfam00069 201 DPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
9-446 2.09e-65

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 217.96  E-value: 2.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDGFILTERLGSGTYATVYKAYAKkDTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:COG0515     4 LLLGRYRILRLLGRGGMGVVYLARDL-RLGRPVALKVLRPELAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPW 167
Cdd:COG0515    83 YLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT--PDGRVKLIDFGIARALGGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 D--EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELP-LRPQLSLDCR 244
Cdd:COG0515   161 TltQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSeLRPDLPPALD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 245 DLLQRLLERDPARRI-SFKDFFAhpwvDLEHMPSGESLAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVD 323
Cdd:COG0515   241 AIVLRALAKDPEERYqSAAELAA----ALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 324 AQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTTVQELLREMARDKPRLLAALEVASAALAKEEEAGKEQDALDLY 403
Cdd:COG0515   317 AAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAA 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 404 QHSLGELLVLLAGKAPALVRALPLVTLSSPSPLSLQQRPQAEG 446
Cdd:COG0515   397 AAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAA 439
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
5-259 2.11e-46

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 163.45  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWglpRLDGFILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQ-LKDFQw 82
Cdd:PTZ00263   14 SW---KLSDFEMGETLGTGSFGRVRIAK-HKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNmMCSFQ- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  83 DNDNIYLIMEFCAGGDLsrFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF 160
Cdd:PTZ00263   89 DENRVYFLLEFVVGGEL--FTHLRKAgrFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDN--KGHVKVTDFGF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSpwDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLS 240
Cdd:PTZ00263  165 AKKVP--DRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL-KFP--NWFD 239
                         250
                  ....*....|....*....
gi 1907200402 241 LDCRDLLQRLLERDPARRI 259
Cdd:PTZ00263  240 GRARDLVKGLLQTDHTKRL 258
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
279-353 6.68e-35

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


Pssm-ID: 239147  Cd Length: 75  Bit Score: 124.54  E-value: 6.68e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 279 ESLAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQ 353
Cdd:cd02684     1 ESLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALIASDTQ 75
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
16-213 1.08e-32

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 130.30  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAyakKDTR--EVVAIKcVAKKSLnkASVENLlteieILKGIR---------HPHIVQLKDFQWDN 84
Cdd:NF033483   11 IGERIGRGGMAEVYLA---KDTRldRDVAVK-VLRPDL--ARDPEF-----VARFRReaqsaaslsHPNIVSVYDVGEDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTR-RILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:NF033483   80 GIPYIVMEYVDGRTLKDYIREHgPLSPEEAVEI-MIQILSALEHAHRNGIVHRDIKPQNILIT--KDGRVKVTDFGIARA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 164 MSpwdE------KHVLrGSPLYMAPE-----MVcrrqyDARVDLWSVGVILYEALFGQPPF 213
Cdd:NF033483  157 LS---SttmtqtNSVL-GTVHYLSPEqarggTV-----DARSDIYSLGIVLYEMLTGRPPF 208
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
281-346 7.90e-17

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


Pssm-ID: 461228  Cd Length: 66  Bit Score: 74.50  E-value: 7.90e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200402 281 LAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKA 346
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
374-425 4.67e-05

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


Pssm-ID: 239121  Cd Length: 75  Bit Score: 41.53  E-value: 4.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 374 PRLLAALEVASAALaKEEEAGKEQDALDLYQHSLGELLVLLAGKAPALVRAL 425
Cdd:cd02656     1 ELLQQAKELIKQAV-KEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKL 51
 
Name Accession Description Interval E-value
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
18-269 0e+00

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: 533.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSP 177
Cdd:cd14121    81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLRGSP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14121   161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPIEIPTRPELSADCRDLLLRLLQRDPDR 240
                         250
                  ....*....|..
gi 1907200402 258 RISFKDFFAHPW 269
Cdd:cd14121   241 RISFEEFFAHPF 252
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
20-269 1.16e-148

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: 423.17  E-value: 1.16e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14009     1 IGRGSFATVWKGRHKQ-TGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLS-SLEKPHLKLADFGFAQHMSPWDEKHVLRGSPL 178
Cdd:cd14009    80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLStSGDDPVLKIADFGFARSLQPASMAETLCGSPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14009   160 YMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIeRSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                         250
                  ....*....|..
gi 1907200402 258 RISFKDFFAHPW 269
Cdd:cd14009   240 RISFEEFFAHPF 251
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-270 1.07e-100

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 301.37  E-value: 1.07e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLAR-DKKTGKLVAIKVI-KKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGHVKLADFGLARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS-FSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 1907200402  253 RDPARRISFKDFFAHPWV 270
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
14-269 6.96e-97

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: 291.69  E-value: 6.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKK-TGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSS-LEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd05117    81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkDPDSPIKIIDFGLAKIFEEGEKLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLRPQ--LSLDCRDLLQRL 250
Cdd:cd05117   161 VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGK-YSFDSPEWknVSEEAKDLIKRL 239
                         250
                  ....*....|....*....
gi 1907200402 251 LERDPARRISFKDFFAHPW 269
Cdd:cd05117   240 LVVDPKKRLTAAEALNHPW 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
14-270 1.00e-89

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: 273.20  E-value: 1.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVE-NLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKK-SGFIVALKVISKSQLQKSGLEhQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHmSPWDEKHV 172
Cdd:cd14007    81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG--SNGELKLADFGWSVH-APSNRRKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPlrPQLSLDCRDLLQRLLE 252
Cdd:cd14007   158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVD-IKFP--SSVSPEAKDLISKLLQ 234
                         250
                  ....*....|....*...
gi 1907200402 253 RDPARRISFKDFFAHPWV 270
Cdd:cd14007   235 KDPSKRLSLEQVLNHPWI 252
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
14-269 2.35e-88

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: 269.39  E-value: 2.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKL-TGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:cd14003    81 ASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD--KNGNLKIIDFGLSNEFRGGSLLKTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIELPlrPQLSLDCRDLLQRLLE 252
Cdd:cd14003   159 CGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKIL-KGKYPIP--SHLSPDARDLIRRMLV 235
                         250
                  ....*....|....*..
gi 1907200402 253 RDPARRISFKDFFAHPW 269
Cdd:cd14003   236 VDPSKRITIEEILNHPW 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
20-268 1.17e-84

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: 260.38  E-value: 1.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKAsvENLLT-EIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKPDLPVAIKCITKKNLSKS--QNLLGkEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPH-------LKLADFGFAQHMSPWDEKH 171
Cdd:cd14120    79 LADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKpspndirLKIADFGFARFLQDGMMAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLL 251
Cdd:cd14120   159 TLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIPSGTSPALKDLLLGLL 238
                         250
                  ....*....|....*..
gi 1907200402 252 ERDPARRISFKDFFAHP 268
Cdd:cd14120   239 KRNPKDRIDFEDFFSHP 255
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-269 1.58e-74

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: 233.95  E-value: 1.58e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAGG 97
Cdd:cd05123     1 LGKGSFGKVLLV-RKKDTGKLYAMKVLRKKEIIKRKeVEHTLNERNILERVNHPFIVKLHyAFQ-TEEKLYLVLDYVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEK-HVLRGS 176
Cdd:cd05123    79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLD--SDGHIKLTDFGLAKELSSDGDRtYTFCGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd05123   157 PEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKS---PLKFPEYVSPEAKSLISGLLQKDPT 233
                         250
                  ....*....|....*.
gi 1907200402 257 RRI---SFKDFFAHPW 269
Cdd:cd05123   234 KRLgsgGAEEIKAHPF 249
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
16-270 4.22e-74

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: 232.91  E-value: 4.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD-FQWDNDnIYLIMEFc 94
Cdd:cd14002     5 VLELIGEGSFGKVYKG-RRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDsFETKKE-FVVVTEY- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSpwDEKHVLR 174
Cdd:cd14002    82 AQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGK--GGVVKLCDFGFARAMS--CNTLVLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 ---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLSLDCRDLLQRLL 251
Cdd:cd14002   158 sikGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPV-KWP--SNMSPEFKSFLQGLL 234
                         250
                  ....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWV 270
Cdd:cd14002   235 NKDPSKRLSWPDLLEHPFV 253
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
20-271 5.96e-73

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: 230.67  E-value: 5.96e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKAsvENLL-TEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKHDLEVAVKCINKKNLAKS--QTLLgKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSS----LEKPH---LKLADFGFAQHMSPWDEKH 171
Cdd:cd14202    88 LADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYsggrKSNPNnirIKIADFGFARYLQNNMMAA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLL 251
Cdd:cd14202   168 TLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGLL 247
                         250       260
                  ....*....|....*....|
gi 1907200402 252 ERDPARRISFKDFFAHPWVD 271
Cdd:cd14202   248 QRNQKDRMDFDEFFHHPFLD 267
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
20-269 5.32e-71

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: 225.13  E-value: 5.32e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKA-SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14099     9 LGKGGFAKCYEV-TDMSTGKVYAGKVVPKSSLTKPkQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHV-LRGSP 177
Cdd:cd14099    88 LMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD--ENMNVKIGDFGLAARLEYDGERKKtLCGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQ-YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd14099   166 NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNE-YSFPSHLSISDEAKDLIRSMLQPDPT 244
                         250
                  ....*....|...
gi 1907200402 257 RRISFKDFFAHPW 269
Cdd:cd14099   245 KRPSLDEILSHPF 257
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
20-270 1.51e-70

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: 224.35  E-value: 1.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASV------------ENLLTEIEILKGIRHPHIVQLKDFQWD--ND 85
Cdd:cd14008     1 LGRGSFGKVKLAL-DTETGQLYAIKIFNKSRLRKRREgkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIDDpeSD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:cd14008    80 KLYLVLEYCEGGPVMELDsgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLT--ADGTVKISDFGVSEM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSpwDEKHVLR---GSPLYMAPEMvCR---RQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLR 236
Cdd:cd14008   158 FE--DGNDTLQktaGTPAFLAPEL-CDgdsKTYSGKaADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQN-DEFPIP 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 237 PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14008   234 PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
13-270 2.81e-70

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: 223.60  E-value: 2.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKA-YAKKDTREVVAIKCVAKKslnKAS---VENLLT-EIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd14080     1 GYRLGKTIGEGSYSKVKLAeYTKSGLKEKVACKIIDKK---KAPkdfLEKFLPrELEILRKLRHPNIIQVYSIFERGSKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPw 167
Cdd:cd14080    78 FIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDS--NNNVKLSDFGFARLCPD- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLR----GSPLYMAPEMVCRRQYDARV-DLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIELPLRPQ-LSL 241
Cdd:cd14080   155 DDGDVLSktfcGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQ-NRKVRFPSSVKkLSP 233
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 242 DCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14080   234 ECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
14-270 3.00e-70

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: 223.17  E-value: 3.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd06606     2 WKKGELLGKGSFGSVYLAL-NLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMS---PWDEK 170
Cdd:cd06606    81 VPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDS--DGVVKLADFGCAKRLAeiaTGEGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFA--SRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQ 248
Cdd:cd06606   159 KSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSelGNPVAALFKIGSSGEPPPIP--EHLSEEAKDFLR 236
                         250       260
                  ....*....|....*....|..
gi 1907200402 249 RLLERDPARRISFKDFFAHPWV 270
Cdd:cd06606   237 KCLQRDPKKRPTADELLQHPFL 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
13-258 3.51e-67

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: 215.53  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTReVVAIKCV-AKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGR-PVAIKVLrPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM--SPWDE 169
Cdd:cd14014    80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLT--EDGRVKLTDFGIARALgdSGLTQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELP-LRPQLSLDCRDLLQ 248
Cdd:cd14014   158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSpLNPDVPPALDAIIL 237
                         250
                  ....*....|
gi 1907200402 249 RLLERDPARR 258
Cdd:cd14014   238 RALAKDPEER 247
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
20-268 7.51e-67

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: 212.90  E-value: 7.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd00180     1 LGKGSFGKVYKAR-DKETGKKVAVKVI-PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRR-ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHM-SPWDEKHVLRGS- 176
Cdd:cd00180    79 KDLLKENKgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS--DGTVKLADFGLAKDLdSDDSLLKTTGGTt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 -PLYMAPEMVCRRQYDARVDLWSVGVILYealfgqppfasrsfsELEEkirsnrvielplrpqlsldCRDLLQRLLERDP 255
Cdd:cd00180   157 pPYYAPPELLGGRYYGPKVDIWSLGVILY---------------ELEE-------------------LKDLIRRMLQYDP 202
                         250
                  ....*....|...
gi 1907200402 256 ARRISFKDFFAHP 268
Cdd:cd00180   203 KKRPSAKELLEHL 215
Pkinase pfam00069
Protein kinase domain;
14-270 1.95e-65

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 209.41  E-value: 1.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAK-HRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASAlqflhernishldlkpqnillssLEKPHlkladfgfaqhmspwdEKHVL 173
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEG-----------------------LESGS----------------SLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLER 253
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKK 200
                         250
                  ....*....|....*..
gi 1907200402 254 DPARRISFKDFFAHPWV 270
Cdd:pfam00069 201 DPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
9-446 2.09e-65

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 217.96  E-value: 2.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDGFILTERLGSGTYATVYKAYAKkDTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:COG0515     4 LLLGRYRILRLLGRGGMGVVYLARDL-RLGRPVALKVLRPELAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPW 167
Cdd:COG0515    83 YLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT--PDGRVKLIDFGIARALGGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 D--EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELP-LRPQLSLDCR 244
Cdd:COG0515   161 TltQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSeLRPDLPPALD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 245 DLLQRLLERDPARRI-SFKDFFAhpwvDLEHMPSGESLAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVD 323
Cdd:COG0515   241 AIVLRALAKDPEERYqSAAELAA----ALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 324 AQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTTVQELLREMARDKPRLLAALEVASAALAKEEEAGKEQDALDLY 403
Cdd:COG0515   317 AAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAA 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 404 QHSLGELLVLLAGKAPALVRALPLVTLSSPSPLSLQQRPQAEG 446
Cdd:COG0515   397 AAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAA 439
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
20-271 3.45e-65

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: 210.64  E-value: 3.45e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVEnLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14201    14 VGHGAFAVVFKGRHRKKTDWEVAIKSINKKNLSKSQIL-LGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLS-------SLEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14201    93 ADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkksSVSGIRIKIADFGFARYLQSNMMAAT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:cd14201   173 LCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRETSPYLADLLLGLLQ 252
                         250
                  ....*....|....*....
gi 1907200402 253 RDPARRISFKDFFAHPWVD 271
Cdd:cd14201   253 RNQKDRMDFEAFFSHPFLE 271
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
18-268 9.04e-65

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: 209.24  E-value: 9.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKaYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd08215     6 RVIGKGSFGSAYL-VRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI----HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEK-HV 172
Cdd:cd08215    85 DLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTK--DGVVKLGDFGISKVLESTTDLaKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMvCRRQ-YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQRLL 251
Cdd:cd08215   163 VVGTPYYLSPEL-CENKpYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIP--SQYSSELRDLVNSML 239
                         250
                  ....*....|....*..
gi 1907200402 252 ERDPARRISFKDFFAHP 268
Cdd:cd08215   240 QKDPEKRPSANEILSSP 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
14-270 1.84e-63

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: 205.57  E-value: 1.84e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLL-TEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCV-TGQKVAIKIVNKEKLSKESVLMKVeREIAIMKLIEHPNVLKLYDVYENKKYLYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQhMSPwdEKHV 172
Cdd:cd14081    82 YVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLD--EKNNIKIADFGMAS-LQP--EGSL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LR---GSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIELPlrPQLSLDCRDLLQ 248
Cdd:cd14081   157 LEtscGSPHYACPEVIKGEKYDGRkADIWSCGVILYALLVGALPFDDDNLRQLLEKVK-RGVFHIP--HFISPDAQDLLR 233
                         250       260
                  ....*....|....*....|..
gi 1907200402 249 RLLERDPARRISFKDFFAHPWV 270
Cdd:cd14081   234 RMLEVNPEKRITIEEIKKHPWF 255
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
22-269 2.05e-63

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: 205.91  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  22 SGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIMEFCAGGDL 99
Cdd:cd05579     3 RGAYGRVYLA-KKKSTGDLYAIKVIKKRDMiRKNQVDSVLAERNILSQAQNPFVVKLyYSFQ-GKKNLYLVMEYLPGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF--------------AQHMS 165
Cdd:cd05579    81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDA--NGHLKLTDFGLskvglvrrqiklsiQKKSN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLR--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIELPLRPQLSLDC 243
Cdd:cd05579   159 GAPEKEDRRivGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNIL-NGKIEWPEDPEVSDEA 237
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 244 RDLLQRLLERDPARRI---SFKDFFAHPW 269
Cdd:cd05579   238 KDLISKLLTPDPEKRLgakGIEEIKNHPF 266
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
20-269 2.83e-63

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 204.81  E-value: 2.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAiKCVAKKSLNKASVENlltEIEILKGIRHPHIVQLKDfQWDNDNIY-LIMEFCAGGD 98
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAA-KFIPKRDKKKEAVLR---EISILNQLQHPRIIQLHE-AYESPTELvLILELCSGGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPL 178
Cdd:cd14006    76 LLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEELKEIFGTPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEMVcrrQYDARV---DLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14006   156 FVAPEIV---NGEPVSlatDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVdFSEEYFSSVSQEAKDFIRKLLVKE 232
                         250
                  ....*....|....*
gi 1907200402 255 PARRISFKDFFAHPW 269
Cdd:cd14006   233 PRKRPTAQEALQHPW 247
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
14-269 5.90e-62

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: 202.14  E-value: 5.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKasvenLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKG-RRKGTIEFVAIKCVDKSKRPE-----VLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFA------------ 161
Cdd:cd14010    76 CTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD--GNGTLKLSDFGLArregeilkelfg 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 -----QHMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLR 236
Cdd:cd14010   154 qfsdeGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPK 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907200402 237 --PQLSLDCRDLLQRLLERDPARRISFKDFFAHP-W 269
Cdd:cd14010   234 vsSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
18-270 8.68e-62

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: 201.28  E-value: 8.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSlnKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05122     6 EKIGKGGFGVVYKARHKK-TGQIVAIKKINLES--KEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI-HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05122    83 SLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLT--SDGEVKLIDFGLSAQLSDGKTRNTFVGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd05122   161 PYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFKDFLKKCLQKDPE 240
                         250
                  ....*....|....
gi 1907200402 257 RRISFKDFFAHPWV 270
Cdd:cd05122   241 KRPTAEQLLKHPFI 254
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
13-269 1.70e-61

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: 200.56  E-value: 1.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAK-KSLNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLI 90
Cdd:cd05578     1 HFQILRVIGKGSFGKVCIV-QKKDTKKMFAMKYMNKqKCIEKDSVRNVLNELEILQELEHPFLVNLWySFQ-DEEDMYMV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd05578    79 VDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLD--EQGHVHITDFNIATKLTDGTLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRL 250
Cdd:cd05578   157 TSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGWSEEAIDLINKL 236
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRIS-FKDFFAHPW 269
Cdd:cd05578   237 LERDPQKRLGdLSDLKNHPY 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
14-269 1.85e-61

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: 200.78  E-value: 1.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKkDTREVVAIKCVAKKS--LNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEV-ETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFA--QHMSPWDE 169
Cdd:cd14098    81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAkvIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVlrGSPLYMAPEMVCRRQ------YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRP-QLSLD 242
Cdd:cd14098   161 TFC--GTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDfNISEE 238
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 243 CRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14098   239 AIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
14-269 2.47e-61

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: 201.27  E-value: 2.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAK-KSLNKASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIM 91
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLV-KHKDSGKYYALKILKKaKIIKLKQVEHVLNEKRILSEVRHPFIVNLlGSFQ-DDRNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLsrFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSpwDE 169
Cdd:cd05580    81 EYVPGGEL--FSLLRRSgrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDS--DGHIKITDFGFAKRVK--DR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPlrPQLSLDCRDLLQR 249
Cdd:cd05580   155 TYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGK-IRFP--SFFDPDAKDLIKR 231
                         250       260
                  ....*....|....*....|....*
gi 1907200402 250 LLERDPARRI-SFK----DFFAHPW 269
Cdd:cd05580   232 LLVVDLTKRLgNLKngveDIKNHPW 256
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-268 2.21e-59

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: 195.45  E-value: 2.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDtREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDN--IYLIMEFCA 95
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSD-GKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVMEYCE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFI----HTRRILPEKVARVFMQQLASALQFLHERN-----ISHLDLKPQNILLSslEKPHLKLADFGFA---QH 163
Cdd:cd08217    85 GGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLD--SDNNVKLGDFGLArvlSH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVlrGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRpqLSLDC 243
Cdd:cd08217   163 DSSFAKTYV--GTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRIPSR--YSSEL 238
                         250       260
                  ....*....|....*....|....*
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd08217   239 NEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
20-269 1.99e-58

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: 192.62  E-value: 1.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14663     8 LGEGTFAKVKFARNTK-TGESVAIKIIDKEQVAREGmVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF---AQHMSPWDEKHVLRG 175
Cdd:cd14663    87 LFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLD--EDGNLKISDFGLsalSEQFRQDGLLHTTCG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYD-ARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSnrvIELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14663   165 TPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMK---GEFEYPRWFSPGAKSLIKRILDPN 241
                         250
                  ....*....|....*
gi 1907200402 255 PARRISFKDFFAHPW 269
Cdd:cd14663   242 PSTRITVEQIMASPW 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
14-270 3.39e-58

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: 192.05  E-value: 3.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKG-LNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWD-EKHV 172
Cdd:cd06627    81 VENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG--LVKLADFGVATKLNEVEkDENS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR-SFSELeEKIRSNRviELPLRPQLSLDCRDLLQRLL 251
Cdd:cd06627   159 VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLqPMAAL-FRIVQDD--HPPLPENISPELRDFLLQCF 235
                         250
                  ....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWV 270
Cdd:cd06627   236 QKDPTLRPSAKELLKHPWL 254
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
12-274 3.60e-58

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: 194.81  E-value: 3.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYaKKDTREVVAIKcVAKKS--LNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIY 88
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVR-DKDTGQVYAMK-ILRKSdmLKREQIAHVRAERDILADADSPWIVRLHyAFQ-DEDHLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHM---- 164
Cdd:cd05573    78 LVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDA--DGHIKLADFGLCTKMnksg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 ----------------------SPWDEKHVLR----GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF 218
Cdd:cd05573   156 dresylndsvntlfqdnvlarrRPHKQRRVRAysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSL 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 219 SELEEKIRSNRV-IELPLRPQLSLDCRDLLQRLLeRDPARRI-SFKDFFAHPW---VDLEH 274
Cdd:cd05573   236 VETYSKIMNWKEsLVFPDDPDVSPEAIDLIRRLL-CDPEDRLgSAEEIKAHPFfkgIDWEN 295
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
20-274 3.96e-58

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: 193.97  E-value: 3.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKcVAKKS--LNKASVENLLTEIEIL-KGIRHPHIVQLKD-FQwDNDNIYLIMEFCA 95
Cdd:cd05570     3 LGKGSFGKVMLAERKK-TDELYAIK-VLKKEviIEDDDVECTMTEKRVLaLANRHPFLTGLHAcFQ-TEDRLYFVMEYVN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDEKHVLR 174
Cdd:cd05570    80 GGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDA--EGHIKIADFGMCkEGIWGGNTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLSLDCRDLLQRLLERD 254
Cdd:cd05570   158 GTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEV-LYP--RWLSREAVSILKGLLTKD 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 255 PARRISF-----KDFFAHP------WVDLEH 274
Cdd:cd05570   235 PARRLGCgpkgeADIKAHPffrnidWDKLEK 265
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
20-263 9.06e-58

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: 190.44  E-value: 9.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKkdtREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd13999     1 IGSGSFGEVYKGKWR---GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKH-VLRGSP 177
Cdd:cd13999    78 YDLLHKKKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLD--ENFTVKIADFGLSRIKNSTTEKMtGVVGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfsELEEKIRSNRVIELPLRPQLSLDC----RDLLQRLLER 253
Cdd:cd13999   156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFK-----ELSPIQIAAAVVQKGLRPPIPPDCppelSKLIKRCWNE 230
                         250
                  ....*....|
gi 1907200402 254 DPARRISFKD 263
Cdd:cd13999   231 DPEKRPSFSE 240
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
14-270 1.58e-57

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: 190.29  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLN-KASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14073     3 YELLETLGKGTYGKVKLAI-ERATGREVAIKSIKKDKIEdEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHmspWDEKHV 172
Cdd:cd14073    82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLD--QNGNAKIADFGLSNL---YSKDKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LR---GSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIElPLRPQlslDCRDLLQ 248
Cdd:cd14073   157 LQtfcGSPLYASPEIVNGTPYQGpEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYRE-PTQPS---DASGLIR 232
                         250       260
                  ....*....|....*....|..
gi 1907200402 249 RLLERDPARRISFKDFFAHPWV 270
Cdd:cd14073   233 WMLTVNPKRRATIEDIANHWWV 254
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
12-270 4.16e-57

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: 189.91  E-value: 4.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKAS------VENLLTEIEILKGIRHPHIVQLKDFQWDND 85
Cdd:cd14084     6 KKYIMSRTLGSGACGEVKLAY-DKSTCKKVAIKIINKRKFTIGSrreinkPRNIETEIEILKKLSHPCIIKIEDFFDAED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDL-SRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSL-EKPHLKLADFGFAQH 163
Cdd:cd14084    85 DYYIVLELMEGGELfDRVVSNKR-LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQeEECLIKITDFGLSKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MspwDEKHVLR---GSPLYMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPPFA-SRSFSELEEKIRSNRVIELPLR 236
Cdd:cd14084   164 L---GETSLMKtlcGTPTYLAPEVLrsfGTEGYTRAVDCWSLGVILFICLSGYPPFSeEYTQMSLKEQILSGKYTFIPKA 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 237 PQ-LSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14084   241 WKnVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
14-269 2.90e-56

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: 187.81  E-value: 2.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNK-ASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIM 91
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLA-KEKETGKEYAIKVLDKRHIIKeKKVKYVTIEKEVLSRLAHPGIVKLyYTFQ-DESKLYFVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSP----- 166
Cdd:cd05581    81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD--EDMHIKITDFGTAKVLGPdsspe 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 ---WDEKHVLR----------GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFasRSFSELE--EKIRSnrvI 231
Cdd:cd05581   159 stkGDADSQIAynqaraasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPF--RGSNEYLtfQKIVK---L 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907200402 232 ELPLRPQLSLDCRDLLQRLLERDPARRISFKDFF------AHPW 269
Cdd:cd05581   234 EYEFPENFPPDAKDLIQKLLVLDPSKRLGVNENGgydelkAHPF 277
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
14-269 5.02e-56

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: 187.30  E-value: 5.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAK-DKKTGEIVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGgDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAqhmspwdekhv 172
Cdd:cd07829    80 CDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINR--DGVLKLADFGLA----------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 lR--GSPL-----------YMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFASRS--------------------- 217
Cdd:cd07829   146 -RafGIPLrtythevvtlwYRAPEILLGsKHYSTAVDIWSVGCIFAELITGKPLFPGDSeidqlfkifqilgtpteeswp 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 218 -FSELE---------EKIRSNRVIelplrPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07829   225 gVTKLPdykptfpkwPKNDLEKVL-----PRLDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
14-271 1.12e-55

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: 186.35  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASveNLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRS-TGKLYALKCIKKSPLSRDS--SLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNIL-LSSLEKPHLKLADFGfaqhMSPWDEKHV 172
Cdd:cd14166    82 VSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKIMITDFG----LSKMEQNGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LR---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDCRDLLQ 248
Cdd:cd14166   158 MStacGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYeFESPFWDDISESAKDFIR 237
                         250       260
                  ....*....|....*....|...
gi 1907200402 249 RLLERDPARRISFKDFFAHPWVD 271
Cdd:cd14166   238 HLLEKNPSKRYTCEKALSHPWII 260
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
13-270 1.75e-55

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: 186.10  E-value: 1.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLN-----KASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd14096     2 NYRLINKIGEGAFSNVYKAVPLRNTGKPVAIKVVRKADLSsdnlkGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLE-------KPHL------- 153
Cdd:cd14096    82 YIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIPfipsivkLRKAdddetkv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 154 -----------------KLADFGFAQHMSPWDEKHVLrGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR 216
Cdd:cd14096   162 degefipgvggggigivKLADFGLSKQVWDSNTKTPC-GTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 217 SFSELEEKI-RSNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14096   241 SIETLTEKIsRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
13-269 1.88e-55

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 184.78  E-value: 1.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLT-EIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14079     3 NYILGKTLGVGSFGKVKLAEHEL-TGHKVAVKILNRQKIKSLDMEEKIRrEIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSpwdEKH 171
Cdd:cd14079    82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDS--NMNVKIADFGLSNIMR---DGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLR---GSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrVIELPlrPQLSLDCRDLL 247
Cdd:cd14079   157 FLKtscGSPNYAAPEVISGKLYAGpEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSG-IYTIP--SHLSPGARDLI 233
                         250       260
                  ....*....|....*....|..
gi 1907200402 248 QRLLERDPARRISFKDFFAHPW 269
Cdd:cd14079   234 KRMLVVDPLKRITIPEIRQHPW 255
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-269 1.95e-55

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: 184.88  E-value: 1.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLN--KASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKA-TGKLVAIKCIDKKALKgkEDSLEN---EIAVLRKIKHPNIVQLLDIYESKSHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNIL-LSSLEKPHLKLADFGfaqhMSPWD 168
Cdd:cd14083    79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyYSPDEDSKIMISDFG----LSKME 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLR---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCR 244
Cdd:cd14083   155 DSGVMStacGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQIlKAEYEFDSPYWDDISDSAK 234
                         250       260
                  ....*....|....*....|....*
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14083   235 DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
11-270 2.22e-55

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: 184.78  E-value: 2.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLT-EIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd14116     4 LEDFEIGRPLGKGKFGNVYLA-REKQSKFILALKVLFKAQLEKAGVEHQLRrEVEIQSHLRHPNILRLYGYFHDATRVYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHmSPWDE 169
Cdd:cd14116    83 ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS--AGELKIADFGWSVH-APSSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSnrvIELPLRPQLSLDCRDLLQR 249
Cdd:cd14116   160 RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISR---VEFTFPDFVTEGARDLISR 236
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd14116   237 LLKHNPSQRPMLREVLEHPWI 257
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
13-269 5.48e-55

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 183.83  E-value: 5.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLT-EIEILKGIRHPHIVQLKD-FQWDNDNIYLI 90
Cdd:cd14165     2 GYILGINLGEGSYAKVKSAYSERLKCNV-AIKIIDKKKAPDDFVEKFLPrELEILARLNHKSIIKTYEiFETSDGKVYIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSpWDE- 169
Cdd:cd14165    81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLD--KDFNIKLTDFGFSKRCL-RDEn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 -KHVLR----GSPLYMAPEMVCRRQYDARV-DLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPLRPQLSLDC 243
Cdd:cd14165   158 gRIVLSktfcGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRV-RFPRSKNLTSEC 236
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14165   237 KDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
14-269 7.06e-55

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: 183.30  E-value: 7.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAK-KSLNKAS-VENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKA-TDKEYALKIIDKaKCKGKEHmIEN---EVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMspwde 169
Cdd:cd14095    78 ELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveHEDGSKSLKLADFGLATEV----- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLR---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAS--RSFSELEEKIRSNRVIEL-PLRPQLSLDC 243
Cdd:cd14095   153 KEPLFtvcGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpdRDQEELFDLILAGEFEFLsPYWDNISDSA 232
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14095   233 KDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
16-270 5.04e-54

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: 181.07  E-value: 5.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14074     7 LEETLGRGHFAVV-KLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFI--HTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHL-KLADFGFAQHMSPWDEKHV 172
Cdd:cd14074    86 GGDMYDYImkHENG-LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFF--EKQGLvKLTDFGFSNKFQPGEKLET 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIelpLRPQLSLDCRDLLQRLL 251
Cdd:cd14074   163 SCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYT---VPAHVSPECKDLIRRML 239
                         250
                  ....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWV 270
Cdd:cd14074   240 IRDPKKRASLEEIENHPWL 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-270 8.91e-54

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: 180.61  E-value: 8.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSL--NKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKR-TQKLVAIKCIAKKALegKETSIEN---EIAVLHKIKHPNIVALDDIYESGGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSL-EKPHLKLADFGFAQHMSPWD 168
Cdd:cd14167    79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLdEDSKIMISDFGLSKIEGSGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCRDLL 247
Cdd:cd14167   159 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQIlKAEYEFDSPYWDDISDSAKDFI 238
                         250       260
                  ....*....|....*....|...
gi 1907200402 248 QRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14167   239 QHLMEKDPEKRFTCEQALQHPWI 261
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
16-270 9.15e-54

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: 180.27  E-value: 9.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNkASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14078     7 LHETIGSGGFAKV-KLATHILTGEKVAIKIMDKKALG-DDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLR- 174
Cdd:cd14078    85 GGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLD--EDQNLKLIDFGLCAKPKGGMDHHLETc 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 -GSPLYMAPEMVCRRQY-DARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLSLDCRDLLQRLLE 252
Cdd:cd14078   163 cGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKY-EEP--EWLSPSSKLLLDQMLQ 239
                         250
                  ....*....|....*...
gi 1907200402 253 RDPARRISFKDFFAHPWV 270
Cdd:cd14078   240 VDPKKRITVKELLNHPWV 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
13-270 5.10e-53

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: 178.64  E-value: 5.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKslnKASvENLLT-----EIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd14162     1 GYIVGKTLGHGSYAVVKKAYSTKHKCKV-AIKIVSKK---KAP-EDYLQkflprEIEVIKGLKHPNLICFYEAIETTSRV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH-MSP 166
Cdd:cd14162    76 YIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD--KNNNLKITDFGFARGvMKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLR----GSPLYMAPEMVCRRQYDARV-DLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIeLPLRPQLSL 241
Cdd:cd14162   154 KDGKPKLSetycGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQ-RRVV-FPKNPTVSE 231
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 242 DCRDLLQRLLERDPaRRISFKDFFAHPWV 270
Cdd:cd14162   232 ECKDLILRMLSPVK-KRITIEEIKRDPWF 259
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
20-269 6.36e-53

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: 178.57  E-value: 6.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIMEFCAGG 97
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGR-TFALKCVKKRHIVQTRqQEHIFSEKEILEECNSPFIVKLyRTFK-DKKYLYMLMEYCLGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRGSP 177
Cdd:cd05572    79 ELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDS--NGYVKLVDFGFAKKLGSGRKTWTFCGTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELE---EKIRSNRVIELPlrPQLSLDCRDLLQRLLERD 254
Cdd:cd05572   157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMKiynIILKGIDKIEFP--KYIDKNAKNLIKQLLRRN 234
                         250       260
                  ....*....|....*....|
gi 1907200402 255 PARRI-----SFKDFFAHPW 269
Cdd:cd05572   235 PEERLgylkgGIRDIKKHKW 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
20-270 9.84e-53

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: 177.98  E-value: 9.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKkDTREVVAIKCVA---KKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd06632     8 LGSGSFGSVYEGFNG-DTGDFFAVKEVSlvdDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd06632    87 GSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDT--NGVVKLADFGMAKHVEAFSFAKSFKGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEmVCRRQ---YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRviELPLRPQ-LSLDCRDLLQRLLE 252
Cdd:cd06632   165 PYWMAPE-VIMQKnsgYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSG--ELPPIPDhLSPDAKDFIRLCLQ 241
                         250
                  ....*....|....*...
gi 1907200402 253 RDPARRISFKDFFAHPWV 270
Cdd:cd06632   242 RDPEDRPTASQLLEHPFV 259
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
13-270 1.98e-52

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: 177.14  E-value: 1.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14069     2 DWDLVQTLGEGAFGEVFLAVNRN-TEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14069    81 YASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD--ENDNLKISDFGLATVFRYKGKERL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 L---RGSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELE-EKIRSNRVIELPLRPQLSLDCRDLL 247
Cdd:cd14069   159 LnkmCGTLPYVAPELLAKKKYRAePVDVWSCGIVLFAMLAGELPWDQPSDSCQEySDWKENKKTYLTPWKKIDTAALSLL 238
                         250       260
                  ....*....|....*....|...
gi 1907200402 248 QRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14069   239 RKILTENPNKRITIEDIKKHPWY 261
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
16-270 3.08e-52

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: 176.17  E-value: 3.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14072     4 LLKTIGKGNFAKVKLARHVLTGREV-AIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYAS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRG 175
Cdd:cd14072    83 GGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDA--DMNIKIADFGFSNEFTPGNKLDTFCG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPLrpQLSLDCRDLLQRLLERD 254
Cdd:cd14072   161 SPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPF--YMSTDCENLLKKFLVLN 237
                         250
                  ....*....|....*.
gi 1907200402 255 PARRISFKDFFAHPWV 270
Cdd:cd14072   238 PSKRGTLEQIMKDRWM 253
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
11-270 1.24e-51

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: 175.44  E-value: 1.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLT-EIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd14117     5 IDDFDIGRPLGKGKFGNVYLAREKQ-SKFIVALKVLFKSQIEKEGVEHQLRrEIEIQSHLRHPNILRLYNYFHDRKRIYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHmSPWDE 169
Cdd:cd14117    84 ILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGY--KGELKIADFGWSVH-APSLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSnrvIELPLRPQLSLDCRDLLQR 249
Cdd:cd14117   161 RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVK---VDLKFPPFLSDGSRDLISK 237
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd14117   238 LLRYHPSERLPLKGVMEHPWV 258
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
13-268 1.69e-51

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: 174.50  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTrEVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDN-QVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFI----HTRRILPEK-VARVFMQqLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSpw 167
Cdd:cd08530    80 YAPFGDLSKLIskrkKKRRLFPEDdIWRIFIQ-MLRGLKALHDQKILHRDLKSANILLSAGDL--VKIGDLGISKVLK-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 deKHVLR---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCR 244
Cdd:cd08530   155 --KNLAKtqiGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIP--PVYSQDLQ 230
                         250       260
                  ....*....|....*....|....
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd08530   231 QIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
18-268 3.77e-51

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: 173.55  E-value: 3.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVvAIKcvaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06614     6 EKIGEGASGEVYKATDRATGKEV-AIK---KMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI-HTRRILPE-KVARVfMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF-AQHMSPWDEKHVLR 174
Cdd:cd06614    82 SLTDIItQNPVRMNEsQIAYV-CREVLQGLEYLHSQNVIHRDIKSDNILLSK--DGSVKLADFGFaAQLTKEKSKRNSVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd06614   159 GTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFLNKCLVKD 238
                         250
                  ....*....|....
gi 1907200402 255 PARRISFKDFFAHP 268
Cdd:cd06614   239 PEKRPSAEELLQHP 252
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
20-270 9.54e-51

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: 172.88  E-value: 9.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVyKAYAKKDTRE--VVAIKCVAKK---SLNKASVENLLTEIEILKGIRHPHIVQLKD-FQWDNDNIYLIMEF 93
Cdd:cd13994     1 IGKGATSVV-RIVTKKNPRSgvLYAVKEYRRRddeSKRKDYVKRLTSEYIISSKLHHPNIVKVLDlCQDLHGKWCLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM-SPWD-EKH 171
Cdd:cd13994    80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLD--EDGVLKLTDFGTAEVFgMPAEkESP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 V---LRGSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIE-----LPLRPQLSLD 242
Cdd:cd13994   158 MsagLCGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFtngpyEPIENLLPSE 237
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 243 CRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd13994   238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
14-269 9.87e-51

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: 172.03  E-value: 9.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKcvaKKSLNKASVENLLTEIEILK----GIRHPHIVQLKDFQWDN--DNI 87
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKV-TGEKVAIK---KIKNDFRHPKAALREIKLLKhlndVEGHPNIVKLLDVFEHRggNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCaGGDLSRFI-HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLsSLEKPHLKLADFGFAQHMSP 166
Cdd:cd05118    77 CLVFELM-GMNLYELIkDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI-NLELGQLKLADFGLARSFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 wdEKHVLRGSPL-YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRsnRVIELPLrpqlsldCR 244
Cdd:cd05118   155 --PPYTPYVATRwYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV--RLLGTPE-------AL 223
                         250       260
                  ....*....|....*....|....*
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd05118   224 DLLSKMLKYDPAKRITASQALAHPY 248
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
12-270 1.58e-50

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: 172.29  E-value: 1.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKA----SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd14105     5 DFYDIGEELGSGQFAVVKKC-REKSTGLEYAAKFIKKRRSKASrrgvSREDIEREVSILRQVLHPNIITLHDVFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMS 165
Cdd:cd14105    84 VLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldKNVPIPRIKLIDFGLAHKIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIRSNRVIELPLRPQLSLDCR 244
Cdd:cd14105   164 DGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQEtLANITAVNYDFDDEYFSNTSELAK 243
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14105   244 DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
20-269 1.75e-50

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: 171.64  E-value: 1.75e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVA--IKCvaKKSLNKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAkfIKC--RKAKDREDVRN---EIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd14103    76 ELfERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDPDKKLKVLFGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVcrrQYDA---RVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:cd14103   156 PEFVAPEVV---NYEPisyATDMWSVGVICYVLLSGLSPFMGDNDAEtLANVTRAKWDFDDEAFDDISDEAKDFISKLLV 232
                         250
                  ....*....|....*..
gi 1907200402 253 RDPARRISFKDFFAHPW 269
Cdd:cd14103   233 KDPRKRMSAAQCLQHPW 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
19-270 2.78e-50

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: 171.72  E-value: 2.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd06626     7 KIGEGTFGKVYTAV-NLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA------QHMSPWDEKHV 172
Cdd:cd06626    86 LEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDS--NGLIKLGDFGSAvklknnTTTMAPGEVNS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDAR---VDLWSVGVILYEALFGQPPfasrsFSELEE------KIRSNRVIELPLRPQLSLDC 243
Cdd:cd06626   164 LVGTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMATGKRP-----WSELDNewaimyHVGMGHKPPIPDSLQLSPEG 238
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06626   239 KDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
18-269 5.99e-50

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: 170.27  E-value: 5.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ER-LGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd14071     5 ERtIGKGNFAVV-KLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd14071    84 GEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDA--NMNIKIADFGFSNFFKPGELLKTWCGS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLRpqLSLDCRDLLQRLLERDP 255
Cdd:cd14071   162 PPYAAPEVFEGKEYEGpQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGR-FRIPFF--MSTDCEHLIRRMLVLDP 238
                         250
                  ....*....|....
gi 1907200402 256 ARRISFKDFFAHPW 269
Cdd:cd14071   239 SKRLTIEQIKKHKW 252
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
20-274 1.23e-49

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: 171.68  E-value: 1.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTReVVAIKCVAKKS-LNKASVENLLTEIEIL-KGIRHPHIVQLK-DFQwDNDNIYLIMEFCAG 96
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGK-YYAVKVLQKKViLNRKEQKHIMAERNVLlKNVKHPFLVGLHySFQ-TTDKLYFVLDFVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPWDEKHVLRG 175
Cdd:cd05604    82 GELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDS--QGHIVLTDFGLCKEgISNSDTTTTFCG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDP 255
Cdd:cd05604   160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHK---PLVLRPGISLTAWSILEELLEKDR 236
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 256 ARRISFKDFFA----HP------WVDLEH 274
Cdd:cd05604   237 QLRLGAKEDFLeiknHPffesinWTDLVQ 265
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
19-270 1.87e-49

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 169.65  E-value: 1.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14097     8 KLGQGSFGVVIEATHKE-TQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSL-----EKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:cd14097    87 LKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnnDKLNIKVTDFGLSVQKYGLGEDMLQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 R--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDCRDLLQRL 250
Cdd:cd14097   167 EtcGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLtFTQSVWQSVSDAAKNVLQQL 246
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd14097   247 LKVDPAHRMTASELLDNPWI 266
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
34-274 3.62e-49

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: 170.49  E-value: 3.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  34 KKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAGGDLSRFIHTRRILPE 111
Cdd:cd05599    22 KKDTGHVYAMKKLRKSEmLEKEQVAHVRAERDILAEADNPWVVKLYySFQ-DEENLYLIMEFLPGGDMMTLLMKKDTLTE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 112 KVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAqhmSPWDEKHVLR---GSPLYMAPEMVCRR 188
Cdd:cd05599   101 EETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDA--RGHIKLSDFGLC---TGLKKSHLAYstvGTPDYIAPEVFLQK 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 189 QYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPLRPQLSLDCRDLLQRLLErDPARRISFK---DF 264
Cdd:cd05599   176 GYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWReTLVFPPEVPISPEAKDLIERLLC-DAEHRLGANgveEI 254
                         250
                  ....*....|...
gi 1907200402 265 FAHPW---VDLEH 274
Cdd:cd05599   255 KSHPFfkgVDWDH 267
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
12-269 6.37e-49

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: 168.74  E-value: 6.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNK-ASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14209     1 DDFDRIKTLGTGSFGRV-MLVRHKETGNYYAMKILDKQKVVKlKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLsrFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSpwD 168
Cdd:cd14209    80 MEYVPGGEM--FSHLRRIgrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQ--QGYIKVTDFGFAKRVK--G 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLSLDCRDLLQ 248
Cdd:cd14209   154 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFP--SHFSSDLKDLLR 230
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 249 RLLERDPARRI-----SFKDFFAHPW 269
Cdd:cd14209   231 NLLQVDLTKRFgnlknGVNDIKNHKW 256
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
20-270 7.26e-49

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: 167.73  E-value: 7.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14186     9 LGKGSFACVYRARSLHTGLEV-AIKMIDKKAMQKAGmVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFI-HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKH-VLRGS 176
Cdd:cd14186    88 MSRYLkNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR--NMNIKIADFGLATQLKMPHEKHfTMCGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFseleeKIRSNRVI--ELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14186   166 PNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTV-----KNTLNKVVlaDYEMPAFLSREAQDLIHQLLRKN 240
                         250
                  ....*....|....*.
gi 1907200402 255 PARRISFKDFFAHPWV 270
Cdd:cd14186   241 PADRLSLSSVLDHPFM 256
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
18-269 8.31e-49

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: 167.92  E-value: 8.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYaKKDTREVVAIKCV----AKKSLNKAS--VENLLTEIEILKGI-RHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14093     9 EILGRGVSSTVRRCI-EKETGQEFAVKIIditgEKSSENEAEelREATRREIEILRQVsGHPNIIELHDVFESPTFIFLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14093    88 FELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLD--DNLNVKISDFGFATRLDEGEKL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDA------RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDC 243
Cdd:cd14093   166 RELCGTPGYLAPEVLKCSMYDNapgygkEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYeFGSPEWDDISDTA 245
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14093   246 KDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
20-274 9.37e-49

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: 169.42  E-value: 9.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEIL-KGIRHPHIVQLK-DFQwDNDNIYLIMEFCAG 96
Cdd:cd05575     3 IGKGSFGKVLLA-RHKAEGKLYAVKVLQKKAiLKRNEVKHIMAERNVLlKNVKHPFLVGLHySFQ-TKDKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLsrFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPWDEKHVL 173
Cdd:cd05575    81 GEL--FFHLQreRHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDS--QGHVVLTDFGLCKEgIEPSDTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLER 253
Cdd:cd05575   157 CGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHK---PLRLRTNVSPSARDLLEGLLQK 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 254 DPARRI----SFKDFFAHP------WVDLEH 274
Cdd:cd05575   234 DRTKRLgsgnDFLEIKNHSffrpinWDDLEA 264
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
18-270 4.31e-48

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 165.96  E-value: 4.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAI---KCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd14194    11 EELGSGQFAVVKKCREKSTGLQYAAKfikKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14194    91 AGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldRNVPKPRIKIIDFGLAHKIDFGNEFKN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDCRDLLQRLL 251
Cdd:cd14194   171 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAvNYEFEDEYFSNTSALAKDFIRRLL 250
                         250
                  ....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWV 270
Cdd:cd14194   251 VKDPKKRMTIQDSLQHPWI 269
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-259 1.23e-47

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: 165.30  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVA-KKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLV-RDRISEHYYALKVMAiPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSpwDEK 170
Cdd:cd05612    80 MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDK--EGHIKLTDFGFAKKLR--DRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPlrPQLSLDCRDLLQRL 250
Cdd:cd05612   156 WTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGK-LEFP--RHLDLYAKDLIKKL 232

                  ....*....
gi 1907200402 251 LERDPARRI 259
Cdd:cd05612   233 LVVDRTRRL 241
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
15-269 1.58e-47

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: 167.90  E-value: 1.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTErLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIME 92
Cdd:cd05600    15 ILTQ-VGQGGYGSVFLA-RKKDTGEICALKIMKKKVLFKLNeVNHVLTERDILTTTNSPWLVKLlYAFQ-DPENVYLAME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA------QHMSP 166
Cdd:cd05600    92 YVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDS--SGHIKLTDFGLAsgtlspKKIES 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEK--------------------------------HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFA 214
Cdd:cd05600   170 MKIRleevkntafleltakerrniyramrkedqnyaNSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFS 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 215 SRSFSELEEKIRSNR-VIELP------LRPQLSLDCRDLLQRLLErDPARRI-SFKDFFAHPW 269
Cdd:cd05600   250 GSTPNETWANLYHWKkTLQRPvytdpdLEFNLSDEAWDLITKLIT-DPQDRLqSPEQIKNHPF 311
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
14-270 1.64e-47

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: 163.98  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVakksLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd06612     5 FDILEKLGEGSYGSVYKA-IHKETGQVVAIKVV----PVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIH-TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS-PWDEKH 171
Cdd:cd06612    80 CGAGSVSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLN--EEGQAKLADFGVSGQLTdTMAKRN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASrsfseleekIRSNRVI-ELPLRP--------QLSLD 242
Cdd:cd06612   158 TVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSD---------IHPMRAIfMIPNKPpptlsdpeKWSPE 228
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 243 CRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06612   229 FNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
13-293 2.54e-47

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: 164.73  E-value: 2.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKkslNKASVENlltEIEILkgIR---HPHIVQLKDFQWDNDNIYL 89
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCI-HKATGKEYAVKIIDK---SKRDPSE---EIEIL--LRygqHPNIITLRDVYDDGNSVYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK--PHLKLADFGFAQHMSpw 167
Cdd:cd14091    72 VTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpESLRICDFGFAKQLR-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLRgSPLY----MAPEmVCRRQ-YDARVDLWSVGVILYEALFGQPPFASR---SFSELEEKIRSNRV-IELPLRPQ 238
Cdd:cd14091   150 AENGLLM-TPCYtanfVAPE-VLKKQgYDAACDIWSLGVLLYTMLAGYTPFASGpndTPEVILARIGSGKIdLSGGNWDH 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFKDFFAHPWV-DLEHMPSGE-SLAQARALVVEAVK 293
Cdd:cd14091   228 VSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIrNRDSLPQRQlTDPQDAALVKGAVA 284
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
12-276 2.94e-47

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: 165.57  E-value: 2.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYL 89
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLV-RKKDTNALYAMKTLRKKDvLKRNQVAHVKAERDILAEADNEWVVKLyYSFQ-DKENLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-----QHM 164
Cdd:cd05598    79 VMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDR--DGHIKLTDFGLCtgfrwTHD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 SPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPLRPQLSLDC 243
Cdd:cd05598   157 SKYYLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRtTLKIPHEANLSPEA 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907200402 244 RDLLQRLLeRDPARRISFKD--------FFAH-PWVDLEHMP 276
Cdd:cd05598   237 KDLILRLC-CDAEDRLGRNGadeikahpFFAGiDWEKLRKQK 277
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-270 4.11e-47

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: 164.13  E-value: 4.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRC-VQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK-PHLKLADFGFAQHMSpwDEK 170
Cdd:cd14086    80 DLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgAAVKLADFGLAIEVQ--GDQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 ---HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlRPQLSL---DCR 244
Cdd:cd14086   158 qawFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAY-DYP-SPEWDTvtpEAK 235
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14086   236 DLINQMLTVNPAKRITAAEALKHPWI 261
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
20-269 7.36e-47

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: 162.87  E-value: 7.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVA-IKCVAK--KSLNKAS-VENLLTEIEILKGIRHPHIVQLKD-FQWDNDNIYLIMEFC 94
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACkIHQLNKdwSEEKKQNyIKHALREYEIHKSLDHPRIVKLYDvFEIDTDSFCTVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILL-SSLEKPHLKLADFGFAQHMspwDEKH 171
Cdd:cd13990    88 DGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLhSGNVSGEIKITDFGLSKIM---DDES 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLR----------GSPLYMAPEMVCR----RQYDARVDLWSVGVILYEALFGQPPFASRSFSE--LEEK-IRSNRVIELP 234
Cdd:cd13990   165 YNSdgmeltsqgaGTYWYLPPECFVVgktpPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEaiLEENtILKATEVEFP 244
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 235 LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd13990   245 SKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
18-270 1.21e-46

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: 162.58  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASveNLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd14090     8 ELLGEGAYASV-QTCINLYTGKEYAVKIIEKHPGHSRS--RVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK--PhLKLADFGFA-------QHMSPW 167
Cdd:cd14090    85 GPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvsP-VKICDFDLGsgiklssTSMTPV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLR--GSPLYMAPEMV-----CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE---------------LEEKI 225
Cdd:cd14090   164 TTPELLTpvGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqdcqelLFHSI 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907200402 226 RSNRvIELPLR--PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14090   244 QEGE-YEFPEKewSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
16-269 1.24e-46

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: 162.50  E-value: 1.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIMEFc 94
Cdd:cd07832     4 ILGRIGEGAHGIVFKAKDRE-TGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEY- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFI-HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWDEK--- 170
Cdd:cd07832    82 MLSSLSEVLrDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG--VLKIADFGLARLFSEEDPRlys 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLrGSPLYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRS----------------------FSELEE--KI 225
Cdd:cd07832   160 HQV-ATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNGSPLFPGENdieqlaivlrtlgtpnektwpeLTSLPDynKI 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907200402 226 RSNRVIELPLR---PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07832   239 TFPESKGIRLEeifPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
15-263 1.52e-46

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: 161.56  E-value: 1.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   15 ILTERLGSGTYATVYKAYAK---KDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKgkgDGKEVEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   92 EFCAGGDLSRFIHTRRI----LPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPW 167
Cdd:smart00221  81 EYMPGGDLLDYLRKNRPkelsLSDLLS--FALQIARGMEYLESKNFIHRDLAARNCLVG--ENLVVKISDFGLSRDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  168 DEKHVLRG-SPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCR 244
Cdd:smart00221 157 DYYKVKGGkLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKKGYRLPKP--PNCPPELY 234
                          250
                   ....*....|....*....
gi 1907200402  245 DLLQRLLERDPARRISFKD 263
Cdd:smart00221 235 KLMLQCWAEDPEDRPTFSE 253
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
20-270 1.76e-46

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: 161.35  E-value: 1.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14075    10 LGSGNFSQV-KLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRGSPLY 179
Cdd:cd14075    89 YTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYAS--NNCVKVGDFGFSTHAKRGETLNTFCGSPPY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 180 MAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIeLPlrPQLSLDCRDLLQRLLERDPARR 258
Cdd:cd14075   167 AAPELFKDEHYIGIyVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYT-IP--SYVSEPCQELIRGILQPVPSDR 243
                         250
                  ....*....|..
gi 1907200402 259 ISFKDFFAHPWV 270
Cdd:cd14075   244 YSIDEIKNSEWL 255
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
5-259 2.11e-46

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 163.45  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWglpRLDGFILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQ-LKDFQw 82
Cdd:PTZ00263   14 SW---KLSDFEMGETLGTGSFGRVRIAK-HKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNmMCSFQ- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  83 DNDNIYLIMEFCAGGDLsrFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF 160
Cdd:PTZ00263   89 DENRVYFLLEFVVGGEL--FTHLRKAgrFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDN--KGHVKVTDFGF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSpwDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLS 240
Cdd:PTZ00263  165 AKKVP--DRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL-KFP--NWFD 239
                         250
                  ....*....|....*....
gi 1907200402 241 LDCRDLLQRLLERDPARRI 259
Cdd:PTZ00263  240 GRARDLVKGLLQTDHTKRL 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
16-270 3.76e-46

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: 161.21  E-value: 3.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSL--NKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14169     7 LKEKLGEGAFSEVVLA-QERGSQRLVALKCIPKKALrgKEAMVEN---EIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSS-LEKPHLKLADFGfaqhMSPWDEKHV 172
Cdd:cd14169    83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpFEDSKIMISDFG----LSKIEAQGM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LR---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCRDLLQ 248
Cdd:cd14169   159 LStacGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQIlKAEYEFDSPYWDDISESAKDFIR 238
                         250       260
                  ....*....|....*....|..
gi 1907200402 249 RLLERDPARRISFKDFFAHPWV 270
Cdd:cd14169   239 HLLERDPEKRFTCEQALQHPWI 260
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
9-270 4.00e-46

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: 160.59  E-value: 4.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDGFILTER-LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILK-GIRHPHIVQLKDFQWDNDN 86
Cdd:cd14106     4 NINEVYTVESTpLGRGKFAVVRKC-IHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLElCKDCPRVVNLHEVYETRSE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPH--LKLADFGFAQHM 164
Cdd:cd14106    83 LILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTS-EFPLgdIKLCDFGISRVI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 SPWDEKHVLRGSPLYMAPEMVcrrQYDA---RVDLWSVGVILYEALFGQPPFASRSFSELEEKIrSNRVIELP--LRPQL 239
Cdd:cd14106   162 GEGEEIREILGTPDYVAPEIL---SYEPislATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNI-SQCNLDFPeeLFKDV 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 240 SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14106   238 SPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
14-263 5.39e-46

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: 159.97  E-value: 5.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAK---KDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKgegENTKIKVAVKTL-KEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRI---LPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPW 167
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRkltLKDLLS--MALQIAKGMEYLESKNFVHRDLAARNCLVS--ENLVVKISDFGLSRDIYDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDC 243
Cdd:pfam07714 156 DYYRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDGYRLPQP--ENCPDEL 233
                         250       260
                  ....*....|....*....|
gi 1907200402 244 RDLLQRLLERDPARRISFKD 263
Cdd:pfam07714 234 YDLMKQCWAYDPEDRPTFSE 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
16-263 5.81e-46

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 160.00  E-value: 5.81e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   16 LTERLGSGTYATVYKAYAK---KDTREVVAIKCvAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKgkgGKKKVEVAVKT-LKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   93 FCAGGDLSRFIHTRRI---LPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDE 169
Cdd:smart00219  82 YMEGGDLLSYLRKNRPklsLSDLLS--FALQIARGMEYLESKNFIHRDLAARNCLVG--ENLVVKISDFGLSRDLYD-DD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  170 KHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRD 245
Cdd:smart00219 157 YYRKRGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKNGYRLPQP--PNCPPELYD 234
                          250
                   ....*....|....*...
gi 1907200402  246 LLQRLLERDPARRISFKD 263
Cdd:smart00219 235 LMLQCWAEDPEDRPTFSE 252
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
17-270 1.06e-45

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: 160.93  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  17 TERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSlnkasveNLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14092    11 EEALGDGSFSVCRKCVHKKTGQEF-AVKIVSRRL-------DTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL-SSLEKPHLKLADFGFAQhMSPwdEKHVLR 174
Cdd:cd14092    83 GGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtDEDDDAEIKIVDFGFAR-LKP--ENQPLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 gSPL----YMAPEMVCRRQ----YDARVDLWSVGVILYEALFGQPPFASRSF----SELEEKIRSNRV-IELPLRPQLSL 241
Cdd:cd14092   160 -TPCftlpYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRnesaAEIMKRIKSGDFsFDGEEWKNVSS 238
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 242 DCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14092   239 EAKSLIQGLLTVDPSKRLTMSELRNHPWL 267
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
12-270 1.48e-45

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: 159.35  E-value: 1.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVVAiKCVAKKSLNKA----SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAA-KFIKKRQSRASrrgvSREEIEREVSILRQVLHPNIITLHDVYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMS 165
Cdd:cd14196    84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldKNIPIPHIKLIDFGLAHEIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDCR 244
Cdd:cd14196   164 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvSYDFDEEFFSHTSELAK 243
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14196   244 DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
14-270 2.28e-45

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: 158.44  E-value: 2.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKAS--VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGL-HAVTGEKVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF---AQHMSPWD 168
Cdd:cd14070    83 ELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLD--ENDNIKLIDFGLsncAGILGYSD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFS--ELEEKIRSNRVIELPlrPQLSLDCRDL 246
Cdd:cd14070   161 PFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSlrALHQKMVDKEMNPLP--TDLSPGAISF 238
                         250       260
                  ....*....|....*....|....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14070   239 LRSLLEPDPLKRPNIKQALANRWL 262
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
16-263 2.98e-45

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: 158.28  E-value: 2.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENL-----LTEIEILKGI-RHPHIVQLKDFQWDNDNIYL 89
Cdd:cd13993     4 LISPIGEGAYGVVYLAVDLRTGRKY-AIKCLYKSGPNSKDGNDFqklpqLREIDLHRRVsRHPNIITLHDVFETEVAIYI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEK--VARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKpHLKLADFGFA--QHMS 165
Cdd:cd13993    83 VLEYCPNGDLFEAITENRIYVGKteLIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG-TVKLCDFGLAttEKIS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PwdekHVLRGSPLYMAPEmvCRRQYD--------ARVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIRSNRVIELPLR 236
Cdd:cd13993   162 M----DFGVGSEFYMAPE--CFDEVGrslkgypcAAGDIWSLGIILLNLTFGRNPWKIASESDpIFYDYYLNSPNLFDVI 235
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 237 PQLSLDCRDLLQRLLERDPARRISFKD 263
Cdd:cd13993   236 LPMSDDFYNLLRQIFTVNPNNRILLPE 262
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
20-269 3.36e-45

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: 158.01  E-value: 3.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYAtVYKAYAKKDTREVVAIKCVAKkslNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14662     8 IGSGNFG-VARLMRNKETKELVAVKYIER---GLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQ----HMSPwdeKHVLrG 175
Cdd:cd14662    84 FERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKssvlHSQP---KSTV-G 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARV-DLWSVGVILYEALFGQPPFAS----RSFSELEEKIRSNRViELPLRPQLSLDCRDLLQRL 250
Cdd:cd14662   160 TPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSVQY-KIPDYVRVSQDCRHLLSRI 238
                         250
                  ....*....|....*....
gi 1907200402 251 LERDPARRISFKDFFAHPW 269
Cdd:cd14662   239 FVANPAKRITIPEIKNHPW 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-263 4.29e-45

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: 157.70  E-value: 4.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAK--KDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKggDGKTVDVAVKTL-KEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRR---------ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSP 166
Cdd:cd00192    80 GGDLLDFLRKSRpvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVG--EDLVVKISDFGLSRDIYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrpqlsLD 242
Cdd:cd00192   158 DDYYRKKTGGKLpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEVLEYLRKGYRLPKP------EN 231
                         250       260
                  ....*....|....*....|....*
gi 1907200402 243 CRDLLQRLLER----DPARRISFKD 263
Cdd:cd00192   232 CPDELYELMLScwqlDPEDRPTFSE 256
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
16-294 4.76e-45

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: 158.86  E-value: 4.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTRE-VVAIKCVAK-KSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14094     7 LCEVIGKGPFSVVRRCIHRETGQQfAVKIVDVAKfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRR----ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPH-LKLADFGFAQHMSPWD 168
Cdd:cd14094    87 MDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLGESG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 -EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFaSRSFSELEEKIRSNRV-IELPLRPQLSLDCRDL 246
Cdd:cd14094   167 lVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYkMNPRQWSHISESAKDL 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWV-DLEHMPSGESLAQaralVVEAVKK 294
Cdd:cd14094   246 VRRMLMLDPAERITVYEALNHPWIkERDRYAYRIHLPE----TVEQLRK 290
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
20-270 6.51e-45

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: 157.03  E-value: 6.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNK--ASVENLLTEIEILKGIRHPHIVQLKDFQWDNDN--IYLIMEFCA 95
Cdd:cd14119     1 LGEGSYGKV-KEVLDTETLCRRAVKILKKRKLRRipNGEANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GG-----DLSRFIHtrriLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDEK 170
Cdd:cd14119    80 GGlqemlDSAPDKR----LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT--LKISDFGVAEALDLFAED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLR---GSPLYMAPEMV--CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIrSNRVIELPlrPQLSLDCRD 245
Cdd:cd14119   154 DTCTtsqGSPAFQPPEIAngQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENI-GKGEYTIP--DDVDPDLQD 230
                         250       260
                  ....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14119   231 LLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
20-270 7.25e-45

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: 157.52  E-value: 7.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNK---------------------ASVENLLTEIEILKGIRHPHIVQLK 78
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLY-AMKILSKKKLLKqagffrrppprrkpgalgkplDPLDRVYREIAILKKLDHPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  79 DFQWD--NDNIYLIMEFCAGGDLSRfIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLA 156
Cdd:cd14118    81 EVLDDpnEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG--DDGHVKIA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 157 DFGFAQHMSPWD---EKHVlrGSPLYMAPEMVC--RRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRV 230
Cdd:cd14118   158 DFGVSNEFEGDDallSSTA--GTPAFMAPEALSesRKKFSGKaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIK-TDP 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907200402 231 IELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14118   235 VVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
20-269 8.42e-45

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: 157.03  E-value: 8.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVyKAYAKKDTREVVAIKCVAKKSLnKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14185     8 IGDGNFAVV-KECRHWNENQEYAMKIIDKSKL-KGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLE--KPHLKLADFGFAQHMSpwDEKHVLRGSP 177
Cdd:cd14185    86 FDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkSTTLKLADFGLAKYVT--GPIFTVCGTP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAS--RSFSELEEKIRSNRVIEL-PLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14185   164 TYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpeRDQEELFQIIQLGHYEFLpPYWDNISEAAKDLISRLLVVD 243
                         250
                  ....*....|....*
gi 1907200402 255 PARRISFKDFFAHPW 269
Cdd:cd14185   244 PEKRYTAKQVLQHPW 258
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
20-274 1.31e-44

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: 158.21  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTReVVAIKCVAKKS-LNKASVENLLTEIEIL-KGIRHPHIVQLK-DFQwDNDNIYLIMEFCAG 96
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGK-FYAVKVLQKKTiLKKKEQNHIMAERNVLlKNLKHPFLVGLHySFQ-TSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPWDEKHVLRG 175
Cdd:cd05603    81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDC--QGHVVLTDFGLCKEgMEPEETTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDP 255
Cdd:cd05603   159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHK---PLHLPGGKTVAACDLLQGLLHKDQ 235
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 256 ARRISFK-DF-------FAHP--WVDLEH 274
Cdd:cd05603   236 RRRLGAKaDFleiknhvFFSPinWDDLYH 264
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
14-265 1.71e-44

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: 158.64  E-value: 1.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTReVVAIKCVAKKS-LNKASVENLLTEIEIL-KGIRHPHIVQLK-DFQwDNDNIYLI 90
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEK-FYAVKVLQKKAiLKKKEEKHIMSERNVLlKNVKHPFLVGLHfSFQ-TTDKLYFV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDE 169
Cdd:cd05602    87 LDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDS--QGHIVLTDFGLCkENIEPNGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQR 249
Cdd:cd05602   165 TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNK---PLQLKPNITNSARHLLEG 241
                         250
                  ....*....|....*.
gi 1907200402 250 LLERDPARRISFKDFF 265
Cdd:cd05602   242 LLQKDRTKRLGAKDDF 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
14-269 1.73e-44

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: 156.93  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKcVAKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLA-RNKETGELVAIK-KMKKKFYSWEECMNLREVKSLRKLnEHPNIVKLKEVFRENDELYFVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGgDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAqhmspwdeK 170
Cdd:cd07830    79 YMEG-NLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV--VKIADFGLA--------R 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPL--------YMAPEMVCRRQ-YDARVDLWSVGVILYEALFGQPPFASRsfSELEE--KI-------------- 225
Cdd:cd07830   148 EIRSRPPYtdyvstrwYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGS--SEIDQlyKIcsvlgtptkqdwpe 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 226 ----------RSNRVIELPLR---PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07830   226 gyklasklgfRFPQFAPTSLHqliPNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
23-269 1.75e-44

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: 156.10  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  23 GTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRH-PHIVQL-KDFQwDNDNIYLIMEFCAGGDL 99
Cdd:cd05611     7 GAFGSVYLA-KKRSTGDYFAIKVLKKSDMiAKNQVTNVKAERAIMMIQGEsPYVAKLyYSFQ-SKDYLYLVMEYLNGGDC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGSPLY 179
Cdd:cd05611    85 ASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLID--QTGHLKLTDFGLSRNGLEKRHNKKFVGTPDY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 180 MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLRPQ--LSLDCRDLLQRLLERDPAR 257
Cdd:cd05611   163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRR-INWPEEVKefCSPEAVDLINRLLCMDPAK 241
                         250
                  ....*....|....*
gi 1907200402 258 RIS---FKDFFAHPW 269
Cdd:cd05611   242 RLGangYQEIKSHPF 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
18-269 2.41e-44

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: 155.65  E-value: 2.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGg 97
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDV-AIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHG- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK-PHLKLADFGFAQHMSpwdEKHVLR 174
Cdd:cd14082    87 DMLEMIlsSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfPQVKLCDFGFARIIG---EKSFRR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 ---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRsNRVIELPLRP--QLSLDCRDLLQR 249
Cdd:cd14082   164 svvGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDINDQIQ-NAAFMYPPNPwkEISPDAIDLINN 240
                         250       260
                  ....*....|....*....|
gi 1907200402 250 LLERDPARRISFKDFFAHPW 269
Cdd:cd14082   241 LLQVKMRKRYSVDKSLSHPW 260
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
12-270 2.69e-44

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: 155.93  E-value: 2.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVVAiKCVAKKSLNKA----SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd14195     5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAA-KFIKKRRLSSSrrgvSREEIEREVNILREIQHPNIITLHDIFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMS 165
Cdd:cd14195    84 VLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldKNVPNPRIKLIDFGIAHKIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDCR 244
Cdd:cd14195   164 AGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAvNYDFDEEYFSNTSELAK 243
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14195   244 DFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
14-270 3.22e-44

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: 155.68  E-value: 3.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKS---LNKASVENLLTEI--------EILKG--IRHPHIVQLKDF 80
Cdd:cd14077     3 WEFVKTIGAGSMGKV-KLAKHIRTGEKCAIKIIPRASnagLKKEREKRLEKEIsrdirtirEAALSslLNHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF 160
Cdd:cd14077    82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS--KSGNIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSPWDEKHVLRGSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQL 239
Cdd:cd14077   160 SNLYDPRRLLRTFCGSLYFAAPELLQAQPYTGpEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKV-EYP--SYL 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 240 SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14077   237 SSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
16-270 4.06e-44

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: 155.67  E-value: 4.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSlnKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd06611     9 IIGELGDGAFGKVYKAQ-HKETGLFAAAKIIQIES--EEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF-AQHMSPWDEKHVL 173
Cdd:cd06611    86 GGALdSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTL--DGDVKLADFGVsAKNKSTLQKRDTF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPE-MVCR----RQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELpLRPQL-SLDCRDLL 247
Cdd:cd06611   164 IGTPYWMAPEvVACEtfkdNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTL-DQPSKwSSSFNDFL 242
                         250       260
                  ....*....|....*....|...
gi 1907200402 248 QRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06611   243 KSCLVKDPDDRPTAAELLKHPFV 265
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
16-269 4.35e-44

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: 155.14  E-value: 4.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYAtVYKAYAKKDTREVVAIKCVAKkslNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14665     4 LVKDIGSGNFG-VARLMRDKQTKELVAVKYIER---GEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRG 175
Cdd:cd14665    80 GGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARV-DLWSVGVILYEALFGQPPFAS----RSFSELEEKIRSNRViELPLRPQLSLDCRDLLQRL 250
Cdd:cd14665   160 TPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQY-SIPDYVHISPECRHLISRI 238
                         250
                  ....*....|....*....
gi 1907200402 251 LERDPARRISFKDFFAHPW 269
Cdd:cd14665   239 FVADPATRITIPEIRNHEW 257
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
14-270 5.48e-44

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: 155.98  E-value: 5.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLN--KASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLA-EERATGKLFAVKCIPKKALKgkESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNIL-LSSLEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14168    88 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyFSQDEESKIMISDFGLSKMEGKGDVM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCRDLLQR 249
Cdd:cd14168   168 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIlKADYEFDSPYWDDISDSAKDFIRN 247
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd14168   248 LMEKDPNKRYTCEQALRHPWI 268
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
20-272 5.60e-44

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: 156.80  E-value: 5.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAK--KDTREVVAIKCVAKKSL--NKASVENLLTEIEILKGIRHPHIVQLK-DFQWDNdNIYLIMEFC 94
Cdd:cd05584     4 LGKGGYGKVFQVRKTtgSDKGKIFAMKVLKKASIvrNQKDTAHTKAERNILEAVKHPFIVDLHyAFQTGG-KLYLILEYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLsrFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEK-H 171
Cdd:cd05584    83 SGGEL--FMHLERegIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDA--QGHVKLTDFGLCKESIHDGTVtH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIeLPlrPQLSLDCRDLLQRLL 251
Cdd:cd05584   159 TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLN-LP--PYLTNEARDLLKKLL 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907200402 252 ERDPARR----------ISFKDFFAH-PWVDL 272
Cdd:cd05584   236 KRNVSSRlgsgpgdaeeIKAHPFFRHiNWDDL 267
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
14-268 6.13e-44

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: 155.74  E-value: 6.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKkDTREVVAIKCVA--KKSLNKasvenlltEIEILKGIRHPHIVQLKDF----QWDNDNI 87
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLL-ETGEVVAIKKVLqdKRYKNR--------ELQIMRRLKHPNIVKLKYFfyssGEKKDEV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YL--IMEFCAGgDLSRFIHT----RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFA 161
Cdd:cd14137    77 YLnlVMEYMPE-TLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDP-ETGVLKLCDFGSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 QHMSPwDEKHV-LRGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIR------------ 226
Cdd:cd14137   155 KRLVP-GEPNVsYICSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDqLVEIIKvlgtptreqika 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 227 SNRVIELPLRPQL-------------SLDCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14137   234 MNPNYTEFKFPQIkphpwekvfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
14-270 1.37e-43

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: 154.32  E-value: 1.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVakkSLNKAS--VENLLTEIEILKGIRHPHIVQ-----LKDFqwdndN 86
Cdd:cd06609     3 FTLLERIGKGSFGEVYKGIDKR-TNQVVAIKVI---DLEEAEdeIEDIQQEIQFLSQCDSPYITKyygsfLKGS-----K 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS- 165
Cdd:cd06609    74 LWIIMEYCGGGSVLDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS--EEGDVKLADFGVSGQLTs 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASrsfseleekIRSNRVIEL-PLR--PQL--- 239
Cdd:cd06609   151 TMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSD---------LHPMRVLFLiPKNnpPSLegn 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 240 --SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06609   222 kfSKPFKDFVELCLNKDPKERPSAKELLKHKFI 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
14-269 1.94e-43

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: 155.09  E-value: 1.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQL-KDFQWDnDNIYLIM 91
Cdd:cd05574     3 FKKIKLLGKGDVGRVYLV-RLKGTGKLFAMKVLDKEEMIKRNkVKRVLTEREILATLDHPFLPTLyASFQTS-THLCFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH------ 163
Cdd:cd05574    81 DYCPGGELFRLLQKQpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLH--ESGHIMLTDFDLSKQssvtpp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 ------MSPWDEKHVLRGSPL------------------YMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFS 219
Cdd:cd05574   159 pvrkslRKGSRRSSVKSIEKEtfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 220 ELEEKIRSNRVIeLPLRPQLSLDCRDLLQRLLERDPARRISFK----DFFAHPW 269
Cdd:cd05574   239 ETFSNILKKELT-FPESPPVSSEAKDLIRKLLVKDPSKRLGSKrgasEIKRHPF 291
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
20-283 2.60e-43

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: 154.99  E-value: 2.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDN-----IYLIMEFc 94
Cdd:cd07834     8 IGSGAYGVVCSAY-DKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPeefndVYIVTEL- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWDEKHVL- 173
Cdd:cd07834    86 METDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC--DLKICDFGLARGVDPDEDKGFLt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 -----RgspLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELEEKIRSNRVIE 232
Cdd:cd07834   164 eyvvtR---WYRAPElLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYidqlnlivevlgtpsEEDLKFISSEKARN 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 233 ----LPLRPQLSL---------DCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQ 283
Cdd:cd07834   241 ylksLPKKPKKPLsevfpgaspEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPEDEPVAK 304
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
18-270 3.30e-43

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: 152.80  E-value: 3.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTreVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd14161     9 ETLGKGTYGRVKKARDSSGR--LVAIKSIRKDRIkDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd14161    87 GDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLD--ANGNIKIADFGLSNLYNQDKFLQTYCGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIElPLRPQlslDCRDLLQRLLERDP 255
Cdd:cd14161   165 PLYASPEIVNGRPYIGpEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYRE-PTKPS---DACGLIRWLLMVNP 240
                         250
                  ....*....|....*
gi 1907200402 256 ARRISFKDFFAHPWV 270
Cdd:cd14161   241 ERRATLEDVASHWWV 255
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
18-268 4.91e-43

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: 152.75  E-value: 4.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdtREVVAIKCVAKKSLNKASVENLLTEIEILKGIRH-PHIVQLKDFQW--DNDNIYLIMEfC 94
Cdd:cd14131     7 KQLGKGGSSKVYKVLNPK--KKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYEVtdEDDYLYMVME-C 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSsleKPHLKLADFGFAQHMSPwDEKHV 172
Cdd:cd14131    84 GEIDLATILKKKRpkPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV---KGRLKLIDFGIAKAIQN-DTTSI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LR----GSPLYMAPEMVCRRQYDARV----------DLWSVGVILYEALFGQPPFAsrSFSELEEKIRS----NRVIELP 234
Cdd:cd14131   160 VRdsqvGTLNYMSPEAIKDTSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPFQ--HITNPIAKLQAiidpNHEIEFP 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 235 LRPQLSLdcRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14131   238 DIPNPDL--IDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-270 8.84e-43

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: 151.62  E-value: 8.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKS-LNKASVEN---LLTEIEILK---GIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14005     8 LGKGGFGTVYSGVRIRDGLPV-AVKFVPKSRvTEWAMINGpvpVPLEIALLLkasKPGVPGVIRLLDWYERPDGFLLIME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 F---CAggDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSsLEKPHLKLADFGFAQ--HMSPW 167
Cdd:cd14005    87 RpepCQ--DLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLIN-LRTGEVKLIDFGCGAllKDSVY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEkhvLRGSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFasrsfsELEEKIRSNRVIelpLRPQLSLDCRDL 246
Cdd:cd14005   164 TD---FDGTRVYSPPEWIRHGRYHGRpATVWSLGILLYDMLCGDIPF------ENDEQILRGNVL---FRPRLSKECCDL 231
                         250       260
                  ....*....|....*....|....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14005   232 ISRCLQFDPSKRPSLEQILSHPWF 255
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
14-258 1.01e-42

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: 151.41  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGR-VYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTR--RILPEK-VARVFMQQLAsALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSP-WDE 169
Cdd:cd08529    81 AENGDLHSLIKSQrgRPLPEDqIWKFFIQTLL-GLSHLHSKKILHRDIKSMNIFLDKGDN--VKIGDLGVAKILSDtTNF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVieLPLRPQLSLDCRDLLQR 249
Cdd:cd08529   158 AQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKY--PPISASYSQDLSQLIDS 235

                  ....*....
gi 1907200402 250 LLERDPARR 258
Cdd:cd08529   236 CLTKDYRQR 244
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
18-270 2.46e-42

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: 150.46  E-value: 2.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKAsvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06647    13 EKIGQGASGTVYTAIDVATGQEV-AIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIhTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKH-VLRGS 176
Cdd:cd06647    90 SLTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM--DGSVKLTDFGFCAQITPEQSKRsTMVGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd06647   167 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVE 246
                         250
                  ....*....|....
gi 1907200402 257 RRISFKDFFAHPWV 270
Cdd:cd06647   247 KRGSAKELLQHPFL 260
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
13-270 4.98e-42

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: 149.62  E-value: 4.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVEN-LLTEIEILKGIRHPHIVQLKD-FQWDNDNIYLI 90
Cdd:cd14164     1 GYTLGTTIGEGSFSKVKLATSQKYCCKV-AIKIVDRRRASPDFVQKfLPRELSILRRVNHPNIVQMFEcIEVANGRLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEfCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKpHLKLADFGFAQHMSPWDE- 169
Cdd:cd14164    80 ME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR-KIKIADFGFARFVEDYPEl 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFASRSFSELEekiRSNRVIELPLRPQLSLDCRDLLQ 248
Cdd:cd14164   158 STTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDETNVRRLR---LQQRGVLYPSGVALEEPCRALIR 234
                         250       260
                  ....*....|....*....|..
gi 1907200402 249 RLLERDPARRISFKDFFAHPWV 270
Cdd:cd14164   235 TLLQFNPSTRPSIQQVAGNSWL 256
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
20-269 5.01e-42

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: 151.35  E-value: 5.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKcVAKKS--LNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAG 96
Cdd:cd05571     3 LGKGTFGKVILC-REKATGELYAIK-ILKKEviIAKDEVAHTLTENRVLQNTRHPFLTSLKySFQ-TNDRLCFVMEYVNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLsrFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDEKHVL 173
Cdd:cd05571    80 GEL--FFHLSreRVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDK--DGHIKITDFGLCkEEISYGATTKTF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLER 253
Cdd:cd05571   156 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILME---EVRFPSTLSPEAKSLLAGLLKK 232
                         250       260
                  ....*....|....*....|.
gi 1907200402 254 DPARRI-----SFKDFFAHPW 269
Cdd:cd05571   233 DPKKRLgggprDAKEIMEHPF 253
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
14-270 6.33e-42

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: 149.07  E-value: 6.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVVaIKCVAK-KSLNKASVEN-----LLTEIEI---LKGIRHPHIVQLKDFQWDN 84
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVV-IKFIFKeRILVDTWVRDrklgtVPLEIHIldtLNKRSHPNIVKLLDFFEDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIME-FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH 163
Cdd:cd14004    81 EFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDG--NGTIKLIDFGSAAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MS--PWDekhVLRGSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPfasrsFSELEEkirsnrVIELPLRP--Q 238
Cdd:cd14004   159 IKsgPFD---TFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENP-----FYNIEE------ILEADLRIpyA 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14004   225 VSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
11-270 9.65e-42

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: 149.73  E-value: 9.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKDTrEVVAIKCVAKKSL------------------------NKASVENLLTEIEIL 66
Cdd:cd14199     1 LNQYKLKDEIGKGSYGVVKLAYNEDDN-TYYAMKVLSKKKLmrqagfprrppprgaraapegctqPRGPIERVYQEIAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  67 KGIRHPHIVQLKDFQWD--NDNIYLIMEFCAGGDLSRfIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNIL 144
Cdd:cd14199    80 KKLDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 145 LSslEKPHLKLADFGFAQHMSPWDEkhVLR---GSPLYMAPEMVC--RRQYDAR-VDLWSVGVILYEALFGQPPFASRSF 218
Cdd:cd14199   159 VG--EDGHIKIADFGVSNEFEGSDA--LLTntvGTPAFMAPETLSetRKIFSGKaLDVWAMGVTLYCFVFGQCPFMDERI 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 219 SELEEKIRsNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14199   235 LSLHSKIK-TQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
13-270 1.23e-41

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 148.60  E-value: 1.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLT-EIEILKGIRHPHIVQLKDFQWDND-NIYLI 90
Cdd:cd14163     1 GYQLGKTIGEGTYSKVKEAFSKKHQRKV-AIKIIDKSGGPEEFIQRFLPrELQIVERLDHKNIIHVYEMLESADgKIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkphLKLADFGFAQHMsPWDEK 170
Cdd:cd14163    80 MELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT---LKLTDFGFAKQL-PKGGR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLR---GSPLYMAPEMVCRRQYDARV-DLWSVGVILYEALFGQPPFASRSFSELeeKIRSNRVIELPLRPQLSLDCRDL 246
Cdd:cd14163   156 ELSQtfcGSTAYAAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPFDDTDIPKM--LCQQQKGVSLPGHLGVSRTCQDL 233
                         250       260
                  ....*....|....*....|....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14163   234 LKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
20-265 1.80e-41

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: 148.54  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKaYAKKDTREVVAIKCVAKKSLNKA-SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14187    15 LGKGGFAKCYE-ITDADTKEVFAGKIVPKSLLLKPhQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS-PWDEKHVLRGSP 177
Cdd:cd14187    94 LLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLN--DDMEVKIGDFGLATKVEyDGERKKTLCGTP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14187   172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKN---EYSIPKHINPVAASLIQKMLQTDPTA 248

                  ....*...
gi 1907200402 258 RISFKDFF 265
Cdd:cd14187   249 RPTINELL 256
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
20-286 1.87e-41

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: 149.02  E-value: 1.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSlnKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd06643    13 LGDGAFGKVYKA-QNKETGILAAAKVIDTKS--EEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 -SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF-AQHMSPWDEKHVLRGSP 177
Cdd:cd06643    90 dAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTL--DGDIKLADFGVsAKNTRTLQRRDSFIGTP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMV-CR----RQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:cd06643   168 YWMAPEVVmCEtskdRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSPEFKDFLRKCLE 247
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907200402 253 RDPARRISFKDFFAHPWVDL--EHMPSGESLAQARA 286
Cdd:cd06643   248 KNVDARWTTSQLLQHPFVSVlvSNKPLRELIAEAKA 283
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
18-268 2.50e-41

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: 147.53  E-value: 2.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd13997     6 EQIGSGSFSEVFKVRSKVDGC-LYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELCEN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHT---RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSP-WDekhV 172
Cdd:cd13997    85 GSLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISN--KGTCKIGDFGLATRLETsGD---V 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRsfsELEEKIRSNRVIeLPLRPQLSLDCRDLLQRLL 251
Cdd:cd13997   160 EEGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLPRNG---QQWQQLRQGKLP-LPPGLVLSQELTRLLKVML 235
                         250
                  ....*....|....*..
gi 1907200402 252 ERDPARRISFKDFFAHP 268
Cdd:cd13997   236 DPDPTRRPTADQLLAHD 252
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
13-258 2.56e-41

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: 147.80  E-value: 2.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNKA-SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGR-LVALKKVQIFEMMDAkARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHT----RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPW 167
Cdd:cd08224    80 ELADAGDLSRLIKHfkkqKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITA--NGVVKLGDLGLGRFFSSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 D-EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF--ASRSFSELEEKIRSNRVIELPlRPQLSLDCR 244
Cdd:cd08224   158 TtAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFygEKMNLYSLCKKIEKCEYPPLP-ADLYSQELR 236
                         250
                  ....*....|....
gi 1907200402 245 DLLQRLLERDPARR 258
Cdd:cd08224   237 DLVAACIQPDPEKR 250
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
20-259 5.17e-41

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: 148.69  E-value: 5.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILK-GIRHPHIVQL-KDFQwDNDNIYLIMEFCAG 96
Cdd:cd05592     3 LGKGSFGKVMLA-ELKGTNQYFAIKALKKDVvLEDDDVECTMIERRVLAlASQHPFLTHLfCTFQ-TESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDEKHVLRG 175
Cdd:cd05592    81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDR--EGHIKIADFGMCkENIYGENKASTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvielPLRPQ-LSLDCRDLLQRLLERD 254
Cdd:cd05592   159 TPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDT----PHYPRwLTKEAASCLSLLLERN 234

                  ....*
gi 1907200402 255 PARRI 259
Cdd:cd05592   235 PEKRL 239
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
20-267 6.52e-41

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: 146.61  E-value: 6.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKA-SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14189     9 LGKGGFARCYEM-TDLATNKTYAVKVIPHSRVAKPhQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDE-KHVLRGSP 177
Cdd:cd14189    88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN--ENMELKVGDFGLAARLEPPEQrKKTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASrsfSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14189   166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFET---LDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGD 242
                         250
                  ....*....|
gi 1907200402 258 RISFKDFFAH 267
Cdd:cd14189   243 RLTLDQILEH 252
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
11-270 7.92e-41

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: 146.57  E-value: 7.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRK---EIQIMNQLHHPKLINLHDAFEDDNEMVLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDE 169
Cdd:cd14114    78 LEFLSGGELfERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHLDPKES 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDCRDLLQ 248
Cdd:cd14114   158 VKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKScDWNFDDSAFSGISEEAKDFIR 237
                         250       260
                  ....*....|....*....|..
gi 1907200402 249 RLLERDPARRISFKDFFAHPWV 270
Cdd:cd14114   238 KLLLADPNKRMTIHQALEHPWL 259
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
14-269 9.37e-41

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: 146.86  E-value: 9.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd07836     2 FKQLEKLGEGTYATVYKG-RNRTTGEIVALKEIHLDA-EEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGgDLSRFIHT---RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMspwdek 170
Cdd:cd07836    80 MDK-DLKKYMDThgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINK--RGELKLADFGLARAF------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 hvlrGSPL-----------YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASR---------------------- 216
Cdd:cd07836   151 ----GIPVntfsnevvtlwYRAPDvLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTnnedqllkifrimgtptestwp 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 217 SFSELEE-KIRSNRVIELPLR---PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07836   227 GISQLPEyKPTFPRYPPQDLQqlfPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-270 1.07e-40

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: 146.04  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKDTREVVaikcVAKKSLNKASV-ENLLTEIE--ILKGIRHPHIVQLKD-FQWDNDNIY 88
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYV----IKKLNLKNASKrERKAAEQEakLLSKLKHPNIVSYKEsFEGEDGFLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHM-S 165
Cdd:cd08223    77 IVMGFCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNI--IKVGDLGIARVLeS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRD 245
Cdd:cd08223   155 SSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMP--KQYSPELGE 232
                         250       260
                  ....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd08223   233 LIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
20-270 1.70e-40

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: 145.58  E-value: 1.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKAS---VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd06625     8 LGQGAFGQVYLCY-DADTGRELAVKQVEIDPINTEAskeVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA---QHMSPWDEKHVL 173
Cdd:cd06625    87 GSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDS--NGNVKLGDFGASkrlQTICSSTGMKSV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfsELEE-----KIRSNRVI-ELPlrPQLSLDCRDLL 247
Cdd:cd06625   165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWA-----EFEPmaaifKIATQPTNpQLP--PHVSEDARDFL 237
                         250       260
                  ....*....|....*....|...
gi 1907200402 248 QRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06625   238 SLIFVRNKKQRPSAEELLSHSFV 260
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
14-270 1.72e-40

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: 145.53  E-value: 1.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVakKSLNKASVENLLTEIEILKGIRHPHIVQ-LKDFQWdNDNIYLIME 92
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIA-TGELAAVKVI--KLEPGDDFEIIQQEISMLKECRHPNIVAyFGSYLR-RDKLWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEK-VARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQHMSPWDEK 170
Cdd:cd06613    78 YCGGGSLQDIYQVTGPLSELqIAYVCRETL-KGLAYLHSTGKIHRDIKGANILLT--EDGDVKLADFGVsAQLTATIAKR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPP-----------FASRSFSE---LEEKIRsnrviel 233
Cdd:cd06613   155 KSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPmfdlhpmralfLIPKSNFDppkLKDKEK------- 227
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 234 plrpqLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06613   228 -----WSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
20-288 1.78e-40

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: 146.33  E-value: 1.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKslNKASVENLLTEIEILKGIRHPHIVQLKD-FQWDNdNIYLIMEFCAGGD 98
Cdd:cd06644    20 LGDGAFGKVYKA-KNKETGALAAAKVIETK--SEEELEDYMVEIEILATCNHPYIVKLLGaFYWDG-KLWIMIEFCPGGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 L-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQHMSPWDEKHVLRGS 176
Cdd:cd06644    96 VdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLT--LDGDIKLADFGVsAKNVKTLQRRDSFIGT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMV-CRRQ----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLL 251
Cdd:cd06644   174 PYWMAPEVVmCETMkdtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPSKWSMEFRDFLKTAL 253
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWVD--LEHMPSGESLAQARALV 288
Cdd:cd06644   254 DKHPETRPSAAQLLEHPFVSsvTSNRPLRELVAEAKAEV 292
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
7-270 3.59e-40

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: 144.89  E-value: 3.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   7 GLPR--LDGFIlteRLGSGTYATVYKAYAKKDTREVvAIKcvaKKSLNKASVENLL-TEIEILKGIRHPHIVQLKDFQWD 83
Cdd:cd06648     3 GDPRsdLDNFV---KIGEGSTGIVCIATDKSTGRQV-AVK---KMDLRKQQRRELLfNEVVIMRDYQHPNIVEMYSSYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  84 NDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF-AQ 162
Cdd:cd06648    76 GDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRAVL-KALSFLHSQGVIHRDIKSDSILLTS--DGRVKLSDFGFcAQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLD 242
Cdd:cd06648   153 VSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPR 232
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 243 CRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06648   233 LRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
18-269 4.49e-40

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: 144.26  E-value: 4.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVenlLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14107     8 EEIGRGTFGFV-KRVTHKGNGECCAAKFIPLRSSTRARA---FQERDILARLSHRRLTCLLDQFETRKTLILILELCSSE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSP 177
Cdd:cd14107    84 ELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSKYGSP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVI-ELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd14107   164 EFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSwDTPEITHLSEDAKDFIKRVLQPDPE 243
                         250
                  ....*....|...
gi 1907200402 257 RRISFKDFFAHPW 269
Cdd:cd14107   244 KRPSASECLSHEW 256
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
14-270 5.10e-40

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: 144.55  E-value: 5.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATV----YKAYAKKDTREVVAIKCVAKKSLNKASVE-NLLTEIEILKGIRHPHIVQLKDFQWDNDNIY 88
Cdd:cd14076     3 YILGRTLGEGEFGKVklgwPLPKANHRSGVQVAIKLIRRDTQQENCQTsKIMREINILKGLTHPNIVRLLDVLKTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPwD 168
Cdd:cd14076    83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNR--NLVITDFGFANTFDH-F 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLR---GSPLYMAPEMV-CRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVI---ELPLRPQL 239
Cdd:cd14076   160 NGDLMStscGSPCYAAPELVvSDSMYAGRkADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVpRLYRYIcntPLIFPEYV 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 240 SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14076   240 TPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
20-269 5.58e-40

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: 145.41  E-value: 5.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKcvaKKSLNKASVEN------LLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd07841     8 LGEGTYAVVYKARDKE-TGRIVAIK---KIKLGERKEAKdginftALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGgDLSRFIHTRRIL--PEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDE- 169
Cdd:cd07841    84 MET-DLEKVIKDKSIVltPADI-KSYMLMTLRGLEYLHSNWILHRDLKPNNLLIAS--DGVLKLADFGLArSFGSPNRKm 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 --KHVLRgspLYMAPEMV--CrRQYDARVDLWSVGVILYEALFGQPPFASRS----------------------FSELEE 223
Cdd:cd07841   160 thQVVTR---WYRAPELLfgA-RHYGVGVDMWSVGCIFAELLLRVPFLPGDSdidqlgkifealgtpteenwpgVTSLPD 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200402 224 KIRSNRVIELPLR---PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07841   236 YVEFKPFPPTPLKqifPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
18-269 8.46e-40

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: 144.36  E-value: 8.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCaGG 97
Cdd:cd07835     5 EKIGEGTYGVVYKA-RDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFL-DL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMspwdekhvlrG 175
Cdd:cd07835    83 DLKKYMdsSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDT--EGALKLADFGLARAF----------G 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPL-----------YMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRVIELP--------- 234
Cdd:cd07835   151 VPVrtythevvtlwYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGD--SEIDQLFRIFRTLGTPdedvwpgvt 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 235 -------------------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07835   229 slpdykptfpkwarqdlskVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-311 1.00e-39

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: 144.58  E-value: 1.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVvAIKcVAKKSLNKASVEnllTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14085     3 DFFEIESELGRGATSVVYRCRQKGTQKPY-AVK-KLKKTVDKKIVR---TEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSL-EKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14085    78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPaPDAPLKIADFGLSKIVDQQVTM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFasrsFSELEEKIRSNRVIEL------PLRPQLSLDCR 244
Cdd:cd14085   158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPF----YDERGDQYMFKRILNCdydfvsPWWDDVSLNAK 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWVdlehmpSGEslAQARALVVEAVKKDQEGDAAAALSLYCKAL 311
Cdd:cd14085   234 DLVKKLIVLDPKKRLTTQQALQHPWV------TGK--AANFAHMDTAQKKLQEFNARRKLKAAVKAV 292
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
15-269 2.13e-39

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: 142.81  E-value: 2.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKAYAKKdTREVVAIKcVAKKSLnKASvenllTEIEI-LKGIRHPHIVQLKDFQwdnDNIY----- 88
Cdd:cd14089     4 ISKQVLGLGINGKVLECFHKK-TGEKFALK-VLRDNP-KAR-----REVELhWRASGCPHIVRIIDVY---ENTYqgrkc 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 --LIMEFCAGGDLSRFIHTRRILP--EKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkPH--LKLADFGFAQ 162
Cdd:cd14089    73 llVVMECMEGGELFSRIQERADSAftEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKG-PNaiLKLTDFGFAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMspwDEKHVLRG---SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSEL----EEKIRsNRVIELPl 235
Cdd:cd14089   152 ET---TTKKSLQTpcyTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgmKKRIR-NGQYEFP- 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 236 RP---QLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14089   227 NPewsNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
18-269 2.80e-39

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: 143.09  E-value: 2.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQL------KDFQWDNDNIYLIM 91
Cdd:cd07840     5 AQIGEGTYGQVYKA-RNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLkeivtsKGSAKYKGSIYMVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGgDLSRFIHTR--RILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSP--- 166
Cdd:cd07840    84 EYMDH-DLTGLLDNPevKFTESQIKCY-MKQLLEGLQYLHSNGILHRDIKGSNILINN--DGVLKLADFGLARPYTKenn 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 ----------WdekhvlrgsplYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-------- 227
Cdd:cd07840   160 adytnrvitlW-----------YRPPELLLgATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFElcgsptee 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 228 --NRVIELP----LRPQ--------------LSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07840   229 nwPGVSDLPwfenLKPKkpykrrlrevfknvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
12-270 7.90e-39

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: 141.29  E-value: 7.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVakKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKK-TKKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14191    79 EMVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLENAGSL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDCRDLLQR 249
Cdd:cd14191   159 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWdFDDEAFDEISDDAKDFISN 238
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd14191   239 LLKKDMKARLTCTQCLQHPWL 259
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
20-267 9.10e-39

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: 140.99  E-value: 9.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVY--KAYAKKDTREVVAIKCVAKKSL--NKASVENLLTEIEILKGIRH-PHIVQLK-DFQWDNdNIYLIMEF 93
Cdd:cd05583     2 LGTGAYGKVFlvRKVGGHDAGKLYAMKVLKKATIvqKAKTAEHTMTERQVLEAVRQsPFLVTLHyAFQTDA-KLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEK--H 171
Cdd:cd05583    81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDS--EGHVVLTDFGLSKEFLPGENDraY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMV--CRRQYDARVDLWSVGVILYEALFGQPPFA----SRSFSELEEKIRSNRVielPLRPQLSLDCRD 245
Cdd:cd05583   159 SFCGTIEYMAPEVVrgGSDGHDKAVDWWSLGVLTYELLTGASPFTvdgeRNSQSEISKRILKSHP---PIPKTFSAEAKD 235
                         250       260
                  ....*....|....*....|..
gi 1907200402 246 LLQRLLERDPARRISFKDFFAH 267
Cdd:cd05583   236 FILKLLEKDPKKRLGAGPRGAH 257
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
20-263 1.09e-38

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: 141.13  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05577     1 LGRGGFGEVC-ACQVKATGKMYACKKLDKKRIKKKKGETMaLNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05577    80 LKYHIynVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLD--DHGHVRISDLGLAVEFKGGKKIKGRVGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIELPLRPQ--LSLDCRDLLQRLLER 253
Cdd:cd05577   158 HGYMAPEVLQKeVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELK-RRTLEMAVEYPdsFSPEARSLCEGLLQK 236
                         250
                  ....*....|
gi 1907200402 254 DPARRISFKD 263
Cdd:cd05577   237 DPERRLGCRG 246
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
18-270 1.31e-38

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: 141.32  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASveNLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEY-AVKIIEKRPGHSRS--RVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILlssLEKPH----LKLADFGFAQHM------SP 166
Cdd:cd14173    85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENIL---CEHPNqvspVKICDFDLGSGIklnsdcSP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLR--GSPLYMAPEMVCRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSE---------------LEEK 224
Cdd:cd14173   162 ISTPELLTpcGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDcgwdrgeacpacqnmLFES 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 225 IRSNRViELPLR--PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14173   242 IQEGKY-EFPEKdwAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
18-270 1.69e-38

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: 140.87  E-value: 1.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTReVVAIKCVaKKSLNKASV-ENLLTEIEILKGIR---HPHIVQLKDF--QWDNDN---IY 88
Cdd:cd07838     5 AEIGEGAYGTVYKARDLQDGR-FVALKKV-RVPLSEEGIpLSTIREIALLKQLEsfeHPNVVRLLDVchGPRTDRelkLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCaGGDLSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ---- 162
Cdd:cd07838    83 LVFEHV-DQDLATYLdkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTS--DGQVKLADFGLARiysf 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMS-------PWdekhvlrgsplYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFasRSFSELEEKIRSNRVIELP- 234
Cdd:cd07838   160 EMAltsvvvtLW-----------YRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLF--RGSSEADQLGKIFDVIGLPs 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 235 -------------------------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd07838   227 eeewprnsalprssfpsytprpfksFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
18-269 1.85e-38

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: 140.88  E-value: 1.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTRE-VVAIKCVAKKSLNKASVENL----LTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14181    16 EVIGRGVSSVVRRCVHRHTGQEfAVKIIEVTAERLSPEQLEEVrsstLKEIHILRQVSgHPSIITLIDSYESSTFIFLVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKH 171
Cdd:cd14181    96 DLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLD--DQLHIKLSDFGFSCHLEPGEKLR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMV-CRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDCR 244
Cdd:cd14181   174 ELCGTPGYLAPEILkCSMDethpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYqFSSPEWDDRSSTVK 253
                         250       260
                  ....*....|....*....|....*
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14181   254 DLISRLLVVDPEIRLTAEQALQHPF 278
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
19-277 3.01e-38

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: 140.97  E-value: 3.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKdTREVVAIKCV----AKKSLNKASvenlLTEIEILKGIRHPHIVQLKDFQWDN--DNIYLIME 92
Cdd:cd07845    14 RIGEGTYGIVYRARDTT-SGEIVALKKVrmdnERDGIPISS----LREITLLLNLRHPNIVELKEVVVGKhlDSIFLVME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGgDLSRFI-HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFA-------QHM 164
Cdd:cd07845    89 YCEQ-DLASLLdNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLT--DKGCLKIADFGLArtyglpaKPM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 SP-----WdekhvlrgsplYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-----RSNRVI-- 231
Cdd:cd07845   166 TPkvvtlW-----------YRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIiqllgTPNESIwp 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 232 ---ELPLR-----------------PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW-------VDLEHMPS 277
Cdd:cd07845   235 gfsDLPLVgkftlpkqpynnlkhkfPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYfkekplpCEPEMMPT 307
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
20-267 4.07e-38

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: 138.99  E-value: 4.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKA-SVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14188     9 LGKGGFAKCYEM-TDLTTNKVYAAKIIPHSRVSKPhQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKH-VLRGSP 177
Cdd:cd14188    88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN--ENMELKVGDFGLAARLEPLEHRRrTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvieLPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14188   166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREAR---YSLPSSLLAPAKHLIASMLSKNPED 242
                         250
                  ....*....|
gi 1907200402 258 RISFKDFFAH 267
Cdd:cd14188   243 RPSLDEIIRH 252
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
14-270 4.17e-38

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: 139.10  E-value: 4.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKK--DTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKatADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDL----SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLsslEKPHLKLADFGFAQ-HMSP 166
Cdd:cd08222    82 EYCEGGDLddkiSEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL---KNNVIKVGDFGISRiLMGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLdcRDL 246
Cdd:cd08222   159 SDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSLPDKYSKEL--NAI 236
                         250       260
                  ....*....|....*....|....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd08222   237 YSRMLNKDPALRPSAAEILKIPFI 260
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
20-270 5.31e-38

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: 138.88  E-value: 5.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd06623     9 LGQGSSGVVYKVRHKP-TGKIYALKKIHVDG-DEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLH-ERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKH---VlrG 175
Cdd:cd06623    87 ADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINS--KGEVKIADFGISKVLENTLDQCntfV--G 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR---SFSELEEKIRSNRVIELPLRpQLSLDCRDLLQRLLE 252
Cdd:cd06623   163 TVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPgqpSFFELMQAICDGPPPSLPAE-EFSPEFRDFISACLQ 241
                         250
                  ....*....|....*...
gi 1907200402 253 RDPARRISFKDFFAHPWV 270
Cdd:cd06623   242 KDPKKRPSAAELLQHPFI 259
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
14-270 6.01e-38

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: 138.55  E-value: 6.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVVaIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCV-IKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPhLKLADFGFAQHMSPWDE-K 170
Cdd:cd08225    81 CDGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMV-AKLGDFGIARQLNDSMElA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVieLPLRPQLSLDCRDLLQRL 250
Cdd:cd08225   160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYF--APISPNFSRDLRSLISQL 237
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd08225   238 FKVSPRDRPSITSILKRPFL 257
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
20-270 6.25e-38

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: 138.82  E-value: 6.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14087     9 IGRGSFSRVVRV-EHRVTRQPYAIKMIETKCRGREVCES---ELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLS-SLEKPHLKLADFGFAQHMSPWDEKHVLR--GS 176
Cdd:cd14087    85 FDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYhPGPDSKIMITDFGLASTRKKGPNCLMKTtcGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCRDLLQRLLERDP 255
Cdd:cd14087   165 PEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQIlRAKYSYSGEPWPSVSNLAKDFIDRLLTVNP 244
                         250
                  ....*....|....*
gi 1907200402 256 ARRISFKDFFAHPWV 270
Cdd:cd14087   245 GERLSATQALKHPWI 259
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
11-273 7.49e-38

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: 140.44  E-value: 7.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKS-LNKASVENLLTEIEILK-GIRHPHIVQLK-DFQwDNDNI 87
Cdd:cd05619     4 IEDFVLHKMLGKGSFGKVFLAELKG-TNQFFAIKALKKDVvLMDDDVECTMVEKRVLSlAWEHPFLTHLFcTFQ-TKENL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPW 167
Cdd:cd05619    82 FFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDK--DGHIKIADFGMCKENMLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEK-HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvielPLRPQ-LSLDCRD 245
Cdd:cd05619   160 DAKtSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDN----PFYPRwLEKEAKD 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFK-DFFAHP------WVDLE 273
Cdd:cd05619   236 ILVKLFVREPERRLGVRgDIRQHPffreinWEALE 270
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
12-270 7.90e-38

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: 138.97  E-value: 7.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKasvENLLTEIEILKGI-RHPHIVQ------LKDFQWDN 84
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKK-TGQLAAIKIMDIIEDEE---EEIKLEINILRKFsNHPNIATfygafiKKDPPGGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGG---DLSRFIHTR-RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF 160
Cdd:cd06608    82 DQLWLVMEYCGGGsvtDLVKGLRKKgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT--EEAEVKLVDFGV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 -AQHMSPWDEKHVLRGSPLYMAPEMV-CRRQ----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELp 234
Cdd:cd06608   160 sAQLDSTLGRRNTFIGTPYWMAPEVIaCDQQpdasYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTL- 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 235 LRPQL-SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06608   239 KSPEKwSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
18-269 9.70e-38

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 138.51  E-value: 9.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTRE--VVAIKCVAKKSLNKASVENL----LTEIEILKGIR-HPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14182     9 EILGRGVSSVVRRCIHKPTRQEyaVKIIDITGGGSFSPEEVQELreatLKEIDILRKVSgHPNIIQLKDTYETNTFFFLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14182    89 FDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLD--DDMNIKLTDFGFSCQLDPGEKL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMV-CRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDC 243
Cdd:cd14182   167 REVCGTPGYLAPEIIeCSMDdnhpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSgNYQFGSPEWDDRSDTV 246
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14182   247 KDLISRFLVVQPQKRYTAEEALAHPF 272
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
20-271 1.09e-37

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: 139.63  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAGG 97
Cdd:cd05585     2 IGKGSFGKVMQV-RKKDTSRIYALKTIRKAHIvSRSEVTHTLAERTVLAQVDCPFIVPLKfSFQ-SPEKLYLVLAFINGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLsrFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ-HMSPWDEKHVLR 174
Cdd:cd05585    80 EL--FHHLQRegRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDY--TGHIALCDFGLCKlNMKDDDKTNTFC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIrsnrvIELPLR--PQLSLDCRDLLQRLLE 252
Cdd:cd05585   156 GTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKI-----LQEPLRfpDGFDRDAKDLLIGLLN 230
                         250       260
                  ....*....|....*....|..
gi 1907200402 253 RDPARRISF---KDFFAHPWVD 271
Cdd:cd05585   231 RDPTKRLGYngaQEIKNHPFFD 252
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
12-270 1.31e-37

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 138.62  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYaTVYKAYAKKDTREVVAIKCVAKKSLNKASvenlltEIEILKGI-RHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14175     1 DGYVVKETIGVGSY-SVCKRCVHKATNMEYAVKVIDKSKRDPSE------EIEILLRYgQHPNIITLKDVYDDGKHVYLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMSPwd 168
Cdd:cd14175    74 TELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdESGNPESLRICDFGFAKQLRA-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 eKHVLRGSPLY----MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFA---SRSFSELEEKIRSNRvieLPLR----P 237
Cdd:cd14175   152 -ENGLLMTPCYtanfVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGK---FTLSggnwN 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 238 QLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14175   228 TVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
35-268 1.74e-37

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: 139.37  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  35 KDTREVVAIKCVAKK-SLNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAGGDL----SRFihtRRI 108
Cdd:cd05601    23 KATGDIYAMKVLKKSeTLAQEEVSFFEEERDIMAKANSPWITKLQyAFQ-DSENLYLVMEYHPGGDLlsllSRY---DDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 109 LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPwdEKHVLR----GSPLYMAPEM 184
Cdd:cd05601    99 FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDR--TGHIKLADFGSAAKLSS--DKTVTSkmpvGTPDYIAPEV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 185 ------VCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDCRDLLQRLLErDPAR 257
Cdd:cd05601   175 ltsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNfKKFLKFPEDPKVSESAVDLIKGLLT-DAKE 253
                         250
                  ....*....|.
gi 1907200402 258 RISFKDFFAHP 268
Cdd:cd05601   254 RLGYEGLCCHP 264
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
16-270 1.91e-37

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: 138.16  E-value: 1.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNK------------------------ASVENLLTEIEILKGIRH 71
Cdd:cd14200     4 LQSEIGKGSYGVVKLAYNESDDKYY-AMKVLSKKKLLKqygfprrppprgskaaqgeqakplAPLERVYQEIAILKKLDH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  72 PHIVQLKDFQWD--NDNIYLIMEFCAGGDLSRfIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslE 149
Cdd:cd14200    83 VNIVKLIEVLDDpaEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG--D 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 150 KPHLKLADFGFAQHMSPWDEK-HVLRGSPLYMAPEMVC--RRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKI 225
Cdd:cd14200   160 DGHVKIADFGVSNQFEGNDALlSSTAGTPAFMAPETLSdsGQSFSGKaLDVWAMGVTLYCFVYGKCPFIDEFILALHNKI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907200402 226 RsNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14200   240 K-NKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
12-270 2.58e-37

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: 137.85  E-value: 2.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILT-ERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASveNLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYL 89
Cdd:cd14174     1 DLYRLTdELLGEGAYAKVQGCVSLQNGKEY-AVKIIEKNAGHSRS--RVFREVETLYQCQgNKNILELIEFFEDDTRFYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK-PHLKLADFGFAQHM---- 164
Cdd:cd14174    78 VFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvSPVKICDFDLGSGVklns 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 --SPWDEKHVLR--GSPLYMAPEMV-----CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE--------------- 220
Cdd:cd14174   158 acTPITTPELTTpcGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDcgwdrgevcrvcqnk 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 221 LEEKIRSNRViELPLR--PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14174   238 LFESIQEGKY-EFPDKdwSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
18-269 2.64e-37

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: 137.83  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD-FQWDNdNIYLIMEFCAG 96
Cdd:cd07833     7 GVVGEGAYGVVLKC-RNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEaFRRKG-RLYLVFEYVER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHM-----SPWDEKH 171
Cdd:cd07833    85 TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGV--LKLCDFGFARALtarpaSPLTDYV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRgspLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQP-------------------PFASRSFSELEEKIRSNRVI 231
Cdd:cd07833   163 ATR---WYRAPElLVGDTNYGKPVDVWAIGCIMAELLDGEPlfpgdsdidqlyliqkclgPLPPSHQELFSSNPRFAGVA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 232 ELPLRPQLSLDCR----------DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07833   240 FPEPSQPESLERRypgkvsspalDFLKACLRMDPKERLTCDELLQHPY 287
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
18-279 3.10e-37

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: 138.84  E-value: 3.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR-HPHIVQLKD-FQWDNDN-IYLIMEFc 94
Cdd:cd07852    13 KKLGKGAYGIVWKAIDKK-TGEVVALKKIFDAFRNATDAQRTFREIMFLQELNdHPNIIKLLNvIRAENDKdIYLVFEY- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHtRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHvlr 174
Cdd:cd07852    91 METDLHAVIR-ANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNS--DCRVKLADFGLARSLSQLEEDD--- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPL---------YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRS-FSELE--------------EKIRSN- 228
Cdd:cd07852   165 ENPVltdyvatrwYRAPEiLLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTStLNQLEkiievigrpsaediESIQSPf 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 229 --RVIE-LPLRPQLSL---------DCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGE 279
Cdd:cd07852   245 aaTMLEsLPPSRPKSLdelfpkaspDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPADE 307
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
18-270 4.38e-37

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: 136.59  E-value: 4.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKslNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14190    10 EVLGGGKFGKVHTC-TEKRTGLKLAAKVINKQ--NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd14190    87 ELfERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREKLKVNFGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDP 255
Cdd:cd14190   167 PEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTEtLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKER 246
                         250
                  ....*....|....*
gi 1907200402 256 ARRISFKDFFAHPWV 270
Cdd:cd14190   247 SARMSATQCLKHPWL 261
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
17-270 4.67e-37

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: 137.21  E-value: 4.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  17 TERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSlnKASVENLLTeieiLKGIRHPHIVQLKDFqWDND----------- 85
Cdd:cd14171    11 TQKLGTGISGPV-RVCVKKSTGERFALKILLDRP--KARTEVRLH----MMCSGHPNIVQIYDV-YANSvqfpgesspra 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPhLKLADFGFAQH 163
Cdd:cd14171    83 RLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdNSEDAP-IKLCDFGFAKV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 -----MSPwdekhvlRGSPLYMAPEMV--CRRQ---------------YDARVDLWSVGVILYEALFGQPPFASRSFS-- 219
Cdd:cd14171   162 dqgdlMTP-------QFTPYYVAPQVLeaQRRHrkersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSrt 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200402 220 ---ELEEKIRSNRvIELPLR--PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14171   235 itkDMKRKIMTGS-YEFPEEewSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
20-310 5.53e-37

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: 137.48  E-value: 5.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSlnKASVENLLTEIEILKGirHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEY-AVKIVSKRM--EANTQREIAALKLCEG--HPNIVKLHEVYHDQLHTFLVMELLKGGEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLS-SLEKPHLKLADFGFAQhMSPWDEKhvLRGSPL 178
Cdd:cd14179    90 LERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTdESDNSEIKIIDFGFAR-LKPPDNQ--PLKTPC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 ----YMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR-------SFSELEEKIRSNRV-IELPLRPQLSLDCRDL 246
Cdd:cd14179   167 ftlhYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQGDFsFEGEAWKNVSQEAKDL 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLaqaralvveaVKKDQEGDAAAALSLYCKA 310
Cdd:cd14179   247 IQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSNPL----------MTPDILGSSGASVHTCVKA 300
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
14-270 6.39e-37

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: 135.86  E-value: 6.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVakKSlNKASVENLLTEIEILKGIR------HPHIVQLKDFQWDNDNI 87
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCY-DLLTGEEVALKII--KN-NKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFcAGGDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMS 165
Cdd:cd14133    77 CIVFEL-LSQNLYEFLKQNKFqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 pwDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELeekirSNRVIELPLRPQLSL---- 241
Cdd:cd14133   156 --QRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQ-----LARIIGTIGIPPAHMldqg 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 242 -----DCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14133   229 kaddeLFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
18-272 6.71e-37

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: 137.16  E-value: 6.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKasvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06655    25 EKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKK---ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIhTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKH-VLRGS 176
Cdd:cd06655   102 SLTDVV-TETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGM--DGSVKLTDFGFCAQITPEQSKRsTMVGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd06655   179 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVE 258
                         250
                  ....*....|....*.
gi 1907200402 257 RRISFKDFFAHPWVDL 272
Cdd:cd06655   259 KRGSAKELLQHPFLKL 274
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
16-258 6.77e-37

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: 135.97  E-value: 6.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTrevVAIKCVAKKSLNKASVENLLTEIEILKgIRHPHIVQ-LKDFQ-WDNDNIYLI-ME 92
Cdd:cd13979     7 LQEPLGSGGFGSVYKATYKGET---VAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRvLAAETgTDFASLGLIiME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRR-ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPhlKLADFGFAQHMSPWDEK- 170
Cdd:cd13979    83 YCGNGTLQQLIYEGSePLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVC--KLCDFGCSVKLGEGNEVg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 ---HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASrsfseLEEKIRSNrVIELPLRPQLS------- 240
Cdd:cd13979   161 tprSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG-----LRQHVLYA-VVAKDLRPDLSgledsef 234
                         250
                  ....*....|....*....
gi 1907200402 241 -LDCRDLLQRLLERDPARR 258
Cdd:cd13979   235 gQRLRSLISRCWSAQPAER 253
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
12-270 1.01e-36

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: 135.89  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTER-LGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVEnllTEIEILKGirhPHIVQLKDFQwdnDNIY-- 88
Cdd:cd14172     3 DDYKLSKQvLGLGVNGKVLECF-HRRTGQKCALKLLYDSPKARREVE---HHWRASGG---PHIVHILDVY---ENMHhg 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 -----LIMEFCAGGDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK-PHLKLADFGF 160
Cdd:cd14172    73 krcllIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKdAVLKLTDFGF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE----LEEKIRSNRV-IELPL 235
Cdd:cd14172   153 AKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAispgMKRRIRMGQYgFPNPE 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 236 RPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14172   233 WAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
9-276 1.01e-36

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: 137.70  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDGFILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:cd05610     1 PSIEEFVIVKPISRGAFGKVYLGR-KKNNSKLYAVKVVKKADMiNKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ----- 162
Cdd:cd05610    80 YLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISN--EGHIKLTDFGLSKvtlnr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 --------------------------------HMS------------------PWDEKHVLrGSPLYMAPEMVCRRQYDA 192
Cdd:cd05610   158 elnmmdilttpsmakpkndysrtpgqvlslisSLGfntptpyrtpksvrrgaaRVEGERIL-GTPDYLAPELLLGKPHGP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 193 RVDLWSVGVILYEALFGQPPFASRSFSELEEKIRsNRVIELPL-RPQLSLDCRDLLQRLLERDPARRISFKDFFAHP--- 268
Cdd:cd05610   237 AVDWWALGVCLFEFLTGIPPFNDETPQQVFQNIL-NRDIPWPEgEEELSVNAQNAIEILLTMDPTKRAGLKELKQHPlfh 315
                         330
                  ....*....|.
gi 1907200402 269 ---WVDLEHMP 276
Cdd:cd05610   316 gvdWENLQNQT 326
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
23-259 1.30e-36

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 135.61  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  23 GTYATVYKAyAKKDTREVVAIKCVAKKSLN-KASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAGGDLS 100
Cdd:cd05609    11 GAYGAVYLV-RHRETRQRFAMKKINKQNLIlRNQIQQVFVERDILTFAENPFVVSMYcSFE-TKRHLCMVMEYVEGGDCA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 101 RFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQH--MS------------- 165
Cdd:cd05609    89 TLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMG--HIKLTDFGLSKIglMSlttnlyeghiekd 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 --PWDEKHVLrGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDC 243
Cdd:cd05609   167 trEFLDKQVC-GTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDDALPDDA 245
                         250
                  ....*....|....*.
gi 1907200402 244 RDLLQRLLERDPARRI 259
Cdd:cd05609   246 QDLITRLLQQNPLERL 261
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
18-272 1.66e-36

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: 136.00  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKAsvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06656    25 EKIGQGASGTVYTAIDIATGQEV-AIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIhTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKH-VLRGS 176
Cdd:cd06656   102 SLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM--DGSVKLTDFGFCAQITPEQSKRsTMVGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd06656   179 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVD 258
                         250
                  ....*....|....*.
gi 1907200402 257 RRISFKDFFAHPWVDL 272
Cdd:cd06656   259 RRGSAKELLQHPFLKL 274
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
14-270 2.67e-36

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: 134.99  E-value: 2.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14104     2 YMIAEELGRGQFGIVHRC-VETSSKKTYMAKFVKVKGADQVLVKK---EISILNIARHRNILRLHESFESHEELVMIFEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14104    78 ISGVDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKPGDKFRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPLRPQLSLDCRDLLQRLL 251
Cdd:cd14104   158 QYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEyAFDDEAFKNISIEALDFVDRLL 237
                         250
                  ....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWV 270
Cdd:cd14104   238 VKERKSRMTAQEALNHPWL 256
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
20-259 4.62e-36

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: 135.42  E-value: 4.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTReVVAIKCVAKKS-LNKASVENLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05590     3 LGKGSFGKVMLARLKESGR-LYAVKVLKKDViLQDDDVECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH-MSPWDEKHVLRGS 176
Cdd:cd05590    82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLD--HEGHCKLADFGMCKEgIFNGKTTSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIelpLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd05590   160 PDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVV---YPTWLSQDAVDILKAFMTKNPT 236

                  ...
gi 1907200402 257 RRI 259
Cdd:cd05590   237 MRL 239
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
18-260 6.07e-36

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: 133.40  E-value: 6.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVaIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd08218     6 KKIGEGSFGKALLVKSKEDGKQYV-IKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDE-KHVLR 174
Cdd:cd08218    85 DLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT--KDGIIKLGDFGIARVLNSTVElARTCI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEK-IRSNRVielPLRPQLSLDCRDLLQRLLER 253
Cdd:cd08218   163 GTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKiIRGSYP---PVPSRYSYDLRSLVSQLFKR 239

                  ....*..
gi 1907200402 254 DPARRIS 260
Cdd:cd08218   240 NPRDRPS 246
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
20-270 6.79e-36

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: 133.18  E-value: 6.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14113    15 LGRGRFSVVKKC-DQRGTKRAVATKFVNKKLMKRDQVTH---ELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL-SSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPL 178
Cdd:cd14113    91 LDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdQSLSKPTIKLADFGDAVQLNTTYYIHQLLGSPE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI-RSNRVIELPLRPQLSLDCRDLLQRLLERDPAR 257
Cdd:cd14113   171 FAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNIcRLDFSFPDDYFKGVSQKAKDFVCFLLQMDPAK 250
                         250
                  ....*....|...
gi 1907200402 258 RISFKDFFAHPWV 270
Cdd:cd14113   251 RPSAALCLQEQWL 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
20-269 7.19e-36

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: 133.23  E-value: 7.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTRE-----VVAIKCVAKKSLnkasVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd14184     9 IGDGNFAVVKECVERSTGKEfalkiIDKAKCCGKEHL----IEN---EVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPH----LKLADFGFAQHMSpwDEK 170
Cdd:cd14184    82 KGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVC--EYPDgtksLKLGDFGLATVVE--GPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFasRSFSELEEKIRSNRVI-----ELPLRPQLSLDCRD 245
Cdd:cd14184   158 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF--RSENNLQEDLFDQILLgklefPSPYWDNITDSAKE 235
                         250       260
                  ....*....|....*....|....
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14184   236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
19-269 7.48e-36

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: 133.89  E-value: 7.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKdTREVVAIKCVakkslnKASVENL------LTEIEILKGIRHPHIVQLKD--FQWDNDNIYLI 90
Cdd:cd07843    12 RIEEGTYGVVYRARDKK-TGEIVALKKL------KMEKEKEgfpitsLREINILLKLQHPNIVTVKEvvVGSNLDKIYMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGgDLSRFI--HTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMspwd 168
Cdd:cd07843    85 MEYVEH-DLKSLMetMKQPFLQSEV-KCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNN--RGILKICDFGLAREY---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 ekhvlrGSPL-----------YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRS------------------- 217
Cdd:cd07843   157 ------GSPLkpytqlvvtlwYRAPElLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSeidqlnkifkllgtpteki 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 218 ---FSELeEKIRSNRVIELP---LR---PQLSLDCR--DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07843   231 wpgFSEL-PGAKKKTFTKYPynqLRkkfPALSLSDNgfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
16-279 1.10e-35

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 134.80  E-value: 1.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQW------DNDNIYL 89
Cdd:cd07855     9 PIETIGSGAYGVVCSAIDTK-SGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRpkvpyaDFKDVYV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGgDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDE 169
Cdd:cd07855    88 VLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVN--ENCELKIGDFGMARGLCTSPE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLR-----GSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELEEKIRSN 228
Cdd:cd07855   165 EHKYFmteyvATRWYRAPElMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYvhqlqliltvlgtpsQAVINAIGAD 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 229 RV---IE-LP---------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGE 279
Cdd:cd07855   245 RVrryIQnLPnkqpvpwetLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDE 308
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
14-268 1.84e-35

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: 132.55  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR---HPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHT----RRILPEKVARVFMQqLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMsP 166
Cdd:cd14052    82 TELCENGSLDVFLSElgllGRLDEFRVWKILVE-LSLGLRFIHDHHFVHLDLKPANVLIT--FEGTLKIGDFGMATVW-P 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALF-------GQPPFASRS--FSEL----------EEKIRS 227
Cdd:cd14052   158 LIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAAnvvlpdnGDAWQKLRSgdLSDAprlsstdlhsASSPSS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907200402 228 NRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14052   238 NPPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
12-292 1.89e-35

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: 132.83  E-value: 1.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYAtVYKAYAKKDTREVVAIKCVAKKSLNKASvenlltEIEIL-KGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14178     3 DGYEIKEDIGIGSYS-VCKRCVHKATSTEYAVKIIDKSKRDPSE------EIEILlRYGQHPNIITLKDVYDDGKFVYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMSPwd 168
Cdd:cd14178    76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmdESGNPESIRICDFGFAKQLRA-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 eKHVLRGSPLY----MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEE---KIRSNR-VIELPLRPQLS 240
Cdd:cd14178   154 -ENGLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEilaRIGSGKyALSGGNWDSIS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 241 LDCRDLLQRLLERDPARRISFKDFFAHPW-VDLEHMPSGESLAQARALVVEAV 292
Cdd:cd14178   233 DAAKDIVSKMLHVDPHQRLTAPQVLRHPWiVNREYLSQNQLSRQDVHLVKGAM 285
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
20-260 2.59e-35

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: 132.01  E-value: 2.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTreVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14066     1 IGSGGFGTVYKGVLENGT--VVAVKRLNEMN-CAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPE-------KVArvfmQQLASALQFLHE---RNISHLDLKPQNILLSSLEKPhlKLADFGFAQHMSPWD- 168
Cdd:cd14066    78 EDRLHCHKGSPPlpwpqrlKIA----KGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEP--KLTDFGLARLIPPSEs 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 --EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPfasrsFSELEEKIRSNRVIELpLRPQLSLDCRDL 246
Cdd:cd14066   152 vsKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPA-----VDENRENASRKDLVEW-VESKGKEELEDI 225
                         250
                  ....*....|....
gi 1907200402 247 LQRLLERDPARRIS 260
Cdd:cd14066   226 LDKRLVDDDGVEEE 239
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
11-258 3.91e-35

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: 131.30  E-value: 3.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd08228     1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFI----HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSP 166
Cdd:cd08228    81 LELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA--TGVVKLGDLGLGRFFSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 -WDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFS--ELEEKIRSNRVIELPlRPQLSLDC 243
Cdd:cd08228   159 kTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYPPLP-TEHYSEKL 237
                         250
                  ....*....|....*
gi 1907200402 244 RDLLQRLLERDPARR 258
Cdd:cd08228   238 RELVSMCIYPDPDQR 252
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
20-259 4.18e-35

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: 132.62  E-value: 4.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILK-GIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05591     3 LGKGSFGKVMLA-ERKGTDEVYAIKVLKKDViLQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPWDEKHVLRGS 176
Cdd:cd05591    82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDA--EGHCKLADFGMCKEgILNGKTTTTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVielpLRP-QLSLDCRDLLQRLLERDP 255
Cdd:cd05591   160 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV----LYPvWLSKEAVSILKAFMTKNP 235

                  ....
gi 1907200402 256 ARRI 259
Cdd:cd05591   236 AKRL 239
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
18-270 5.14e-35

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: 130.96  E-value: 5.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYaKKDTREVVAIKCVA--------KKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd06629     7 ELIGKGTYGRVYLAM-NATTGEMLAVKQVElpktssdrADSRQKTVVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLssLEKPHLKLADFGF---AQHMSP 166
Cdd:cd06629    86 FLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILV--DLEGICKISDFGIskkSDDIYG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPLYMAPEMV--CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPLRPQLSLDC 243
Cdd:cd06629   164 NNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRsAPPVPEDVNLSPEA 243
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06629   244 LDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
17-270 5.59e-35

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: 130.80  E-value: 5.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  17 TERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENlltEIEILKGIRHPHIVQLKD-FQWDNDnIYLIMEFCA 95
Cdd:cd14193     9 EEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKN---EIEVMNQLNHANLIQLYDaFESRND-IVLVMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLR 174
Cdd:cd14193    85 GGELfDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPREKLRVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIRSNRVIELPLRPQLSLDCRDLLQRLLER 253
Cdd:cd14193   165 GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNEtLNNILACQWDFEDEEFADISEEAKDFISKLLIK 244
                         250
                  ....*....|....*..
gi 1907200402 254 DPARRISFKDFFAHPWV 270
Cdd:cd14193   245 EKSWRMSASEALKHPWL 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
16-268 6.40e-35

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: 130.94  E-value: 6.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKkDTREVVAIKCVakkSLNK--ASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd06610     5 LIEVIGSGATAVVYAAYCL-PKKEKVAIKRI---DLEKcqTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGG---DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQHMSPWDE 169
Cdd:cd06610    81 LSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLG--EDGSVKIADFGVsASLATGGDR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLR----GSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfseleeKIRSNRVIELPLR---PQLSL 241
Cdd:cd06610   159 TRKVRktfvGTPCWMAPEvMEQVRGYDFKADIWSFGITAIELATGAAPYS---------KYPPMKVLMLTLQndpPSLET 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907200402 242 DC---------RDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd06610   230 GAdykkysksfRKMISLCLQKDPSKRPTAEELLKHK 265
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
279-353 6.68e-35

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


Pssm-ID: 239147  Cd Length: 75  Bit Score: 124.54  E-value: 6.68e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 279 ESLAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQ 353
Cdd:cd02684     1 ESLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALIASDTQ 75
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
18-295 9.80e-35

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: 131.00  E-value: 9.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKasvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06654    26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIhTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKH-VLRGS 176
Cdd:cd06654   103 SLTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM--DGSVKLTDFGFCAQITPEQSKRsTMVGT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd06654   180 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVE 259
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907200402 257 RRISFKDFFAHPWVDLEHMPSgeSLAQARALVVEAVKKD 295
Cdd:cd06654   260 KRGSAKELLQHQFLKIAKPLS--SLTPLIAAAKEATKNN 296
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
7-270 1.05e-34

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: 131.26  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   7 GLPR--LDGFIlteRLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKAsvENLLTEIEILKGIRHPHIVQLKDFQWDN 84
Cdd:cd06659    17 GDPRqlLENYV---KIGEGSTGVVCIAREKHSGRQV-AVKMMDLRKQQRR--ELLFNEVVIMRDYQHPNVVEMYKSYLVG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTRRILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGF-AQH 163
Cdd:cd06659    91 EELWVLMEYLQGGALTDIVSQTRLNEEQIATV-CEAVLQALAYLHSQGVIHRDIKSDSILLTLDGR--VKLSDFGFcAQI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDC 243
Cdd:cd06659   168 SKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVL 247
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06659   248 RDFLERMLVRDPQERATAQELLDHPFL 274
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
18-270 1.39e-34

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: 129.70  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd14192    10 EVLGGGRFGQVHKC-TELSTGLTLAAKIIKVKGAkEREEVKN---EINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRG 175
Cdd:cd14192    86 GELfDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPREKLKVNFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE-LEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14192   166 TPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAEtMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKE 245
                         250
                  ....*....|....*.
gi 1907200402 255 PARRISFKDFFAHPWV 270
Cdd:cd14192   246 KSCRMSATQCLKHEWL 261
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
14-266 1.72e-34

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: 132.44  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIM 91
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLA-CKVDTHALYAMKTLRKKDvLNRNQVAHVKAERDILAEADNEWVVKLYySFQ-DKDNLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA---------- 161
Cdd:cd05626    81 DYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDL--DGHIKLTDFGLCtgfrwthnsk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 ----------QHMSP---WDE-------------------------KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVIL 203
Cdd:cd05626   159 yyqkgshirqDSMEPsdlWDDvsncrcgdrlktleqratkqhqrclAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVIL 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 204 YEALFGQPPFASRSFSELEEK-IRSNRVIELPLRPQLSLDCRDLLQRL-------LERDPARRISFKDFFA 266
Cdd:cd05626   239 FEMLVGQPPFLAPTPTETQLKvINWENTLHIPPQVKLSPEAVDLITKLccsaeerLGRNGADDIKAHPFFS 309
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
20-259 1.83e-34

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: 131.28  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIYLIMEFCAGG 97
Cdd:cd05595     3 LGKGTFGKVILV-REKATGRYYAMKILRKEVIiAKDEVAHTVTESRVLQNTRHPFLTALKyAFQ-THDRLCFVMEYANGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH-MSPWDEKHVLRGS 176
Cdd:cd05595    81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLD--KDGHIKITDFGLCKEgITDGATMKTFCGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd05595   159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILME---EIRFPRTLSPEAKSLLAGLLKKDPK 235

                  ...
gi 1907200402 257 RRI 259
Cdd:cd05595   236 QRL 238
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
14-268 2.36e-34

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: 128.88  E-value: 2.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAK------KDTREVVAIKCVAKKSlnkaSVENLLTEIEILKGIR-HPHIVQLKDFQWDNDN 86
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKlhdlydRNKGRLVALKHIYPTS----SPSRILNELECLERLGgSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTrriLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSP 166
Cdd:cd14019    79 VVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNR-ETGKGVLVDFGLAQREED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLR-GSPLYMAPE--MVCRRQYDArVDLWSVGVILYEALFGQ-PPF-ASRSFSELEE--KIRSNRvielplrpql 239
Cdd:cd14019   155 RPEQRAPRaGTRGFRAPEvlFKCPHQTTA-IDIWSAGVILLSILSGRfPFFfSSDDIDALAEiaTIFGSD---------- 223
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 240 slDCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14019   224 --EAYDLLDKLLELDPSKRITAEEALKHP 250
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
18-269 2.51e-34

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: 129.86  E-value: 2.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCaGG 97
Cdd:cd07839     6 EKIGEGTYGTVFKA-KNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC-DQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEK-VARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMspwdekhvlrGS 176
Cdd:cd07839    84 DLKKYFDSCNGDIDPeIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN--KNGELKLADFGLARAF----------GI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PL-----------YMAPEMVC-RRQYDARVDLWSVGVILYE-ALFGQPPFAS--------RSFSELEEKIRSN--RVIEL 233
Cdd:cd07839   152 PVrcysaevvtlwYRPPDVLFgAKLYSTSIDMWSAGCIFAElANAGRPLFPGndvddqlkRIFRLLGTPTEESwpGVSKL 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 234 P----------------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07839   232 PdykpypmypattslvnVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
20-259 2.59e-34

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 130.88  E-value: 2.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKS-LNKASVENLLTE---IEILKGIRHPHIVQLKD-FQwDNDNIYLIMEFC 94
Cdd:cd05589     7 LGRGHFGKVLLAEYKP-TGELFAIKALKKGDiIARDEVESLMCEkriFETVNSARHPFLVNLFAcFQ-TPEHVCFVMEYA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRrILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPWDEKHVL 173
Cdd:cd05589    85 AGGDLMMHIHED-VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDT--EGYVKIADFGLCKEgMGFGDRTSTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVielplR-PQ-LSLDCRDLLQRLL 251
Cdd:cd05589   162 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEV-----RyPRfLSTEAISIMRRLL 236

                  ....*...
gi 1907200402 252 ERDPARRI 259
Cdd:cd05589   237 RKNPERRL 244
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
12-270 3.15e-34

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: 130.91  E-value: 3.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYaTVYKAYAKKDTREVVAIKCVAKKSLNKASvenlltEIEIL-KGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14176    19 DGYEVKEDIGVGSY-SVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEILlRYGQHPNIITLKDVYDDGKYVYVV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMSPwd 168
Cdd:cd14176    92 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNPESIRICDFGFAKQLRA-- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 eKHVLRGSPLY----MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEE---KIRSNRV-IELPLRPQLS 240
Cdd:cd14176   170 -ENGLLMTPCYtanfVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEilaRIGSGKFsLSGGYWNSVS 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907200402 241 LDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14176   249 DTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
15-270 3.33e-34

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: 128.40  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKAYAKKDTREVVAIKcvakkslnKASVENLLTEIEILKGIRHPHIVQLKDFQWDND-NIYLIMEF 93
Cdd:cd14109     7 IGEEDEKRAAQGAPFHVTERSTGRNFLAQL--------RYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVIDNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSR--FIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlekPHLKLADFGFAQHMSPWDEKH 171
Cdd:cd14109    79 ASTIELVRdnLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD---DKLKLADFGQSRRLLRGKLTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR--VIELPLRPqLSLDCRDLLQR 249
Cdd:cd14109   156 LIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKwsFDSSPLGN-ISDDARDFIKK 234
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd14109   235 LLVYIPESRLTVDEALNHPWF 255
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
20-270 4.86e-34

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: 128.42  E-value: 4.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCVAKKSLN-------KASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd06628     8 IGSGSFGSVYLGM-NASSGELMAVKQVELPSVSaenkdrkKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-------MS 165
Cdd:cd06628    87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDN--KGGIKISDFGISKKleanslsTK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrSFSELEE--KIRSNRVIELPlrPQLSLDC 243
Cdd:cd06628   165 NNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP--DCTQMQAifKIGENASPTIP--SNISSEA 240
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06628   241 RDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
14-270 5.20e-34

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: 128.50  E-value: 5.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTER-LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14198     9 YILTSKeLGRGKFAVVRQCISKS-TGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLsrFIHT----RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK-PHLKLADFGFAQHMSP 166
Cdd:cd14198    88 EYAAGGEI--FNLCvpdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlGDIKIVDFGMSRKIGH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLRPQLSLDCRD 245
Cdd:cd14198   166 ACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVdYSEETFSSVSQLATD 245
                         250       260
                  ....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14198   246 FIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
20-259 5.74e-34

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: 129.68  E-value: 5.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILK-GIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05620     3 LGKGSFGKVLLA-ELKGKGEYFAVKALKKDVvLIDDDVECTMVEKRVLAlAWENPFLTHLYCTFQTKEHLFFVMEFLNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEK-HVLRGS 176
Cdd:cd05620    82 DLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLD--RDGHIKIADFGMCKENVFGDNRaSTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRsnrvIELPLRPQ-LSLDCRDLLQRLLERDP 255
Cdd:cd05620   160 PDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIR----VDTPHYPRwITKESKDILEKLFERDP 235

                  ....
gi 1907200402 256 ARRI 259
Cdd:cd05620   236 TRRL 239
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
20-259 8.70e-34

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 129.05  E-value: 8.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKcVAKKS--LNKASVENLLTEIEILKGIRHPH-IVQLKD-FQwDNDNIYLIMEFCA 95
Cdd:cd05587     4 LGKGSFGKVMLA-ERKGTDELYAIK-ILKKDviIQDDDVECTMVEKRVLALSGKPPfLTQLHScFQ-TMDRLYFVMEYVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDEKHVLR 174
Cdd:cd05587    81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDA--EGHIKIADFGMCkEGIFGGKTTRTFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLSLDCRDLLQRLLERD 254
Cdd:cd05587   159 GTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNV-SYP--KSLSKEAVSICKGLLTKH 235

                  ....*
gi 1907200402 255 PARRI 259
Cdd:cd05587   236 PAKRL 240
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
19-269 1.20e-33

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: 127.77  E-value: 1.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKDTREVvAIKCVaKKSLNKASVENLLTEIEILKGIR-HPHIVQLKDFQWDNDN--IYLIMEFcA 95
Cdd:cd07831     6 KIGEGTFSEVLKAQSRKTGKYY-AIKCM-KKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLFDRKTgrLALVFEL-M 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRR-ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILlssLEKPHLKLADFGFAQHMS---PWDEKH 171
Cdd:cd07831    83 DMNLYELIKGRKrPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENIL---IKDDILKLADFGSCRGIYskpPYTEYI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRgspLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRS---------------FSELEEKIRSNRVIEL-- 233
Cdd:cd07831   160 STR---WYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNeldqiakihdvlgtpDAEVLKKFRKSRHMNYnf 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907200402 234 ---------PLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07831   237 pskkgtglrKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
20-270 1.26e-33

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: 127.08  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd06605     9 LGEGNGGVVSKVRHRP-SGQIMAVKVI-RLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKV-ARVFMQQLaSALQFLHE-RNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPwDEKHVLRGSP 177
Cdd:cd06605    87 DKILKEVGRIPERIlGKIAVAVV-KGLIYLHEkHKIIHRDVKPSNILVNS--RGQVKLCDFGVSGQLVD-SLAKTFVGTR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASrsfselEEKIRSNRVIEL---------PLRPQ--LSLDCRDL 246
Cdd:cd06605   163 SYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPP------PNAKPSMMIFELlsyivdeppPLLPSgkFSPDFQDF 236
                         250       260
                  ....*....|....*....|....
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06605   237 VSQCLQKDPTERPSYKELMEHPFI 260
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
18-269 1.56e-33

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 127.62  E-value: 1.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGg 97
Cdd:cd07860     6 EKIGEGTYGVVYKARNKL-TGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQ- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMspwdekhvlrG 175
Cdd:cd07860    84 DLKKFMDASALtgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLIN--TEGAIKLADFGLARAF----------G 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPL-----------YMAPEMV--CrRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNR------------V 230
Cdd:cd07860   152 VPVrtythevvtlwYRAPEILlgC-KYYSTAVDIWSLGCIFAEMVTRRALFPGD--SEIDQLFRIFRtlgtpdevvwpgV 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 231 IELP----------------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07860   229 TSMPdykpsfpkwarqdfskVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
20-271 1.71e-33

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: 127.03  E-value: 1.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14183    14 IGDGNFAVVKECVERSTGREY-ALKII-NKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLE--KPHLKLADFGFAQHMSpwDEKHVLRGSP 177
Cdd:cd14183    92 FDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgSKSLKLGDFGLATVVD--GPLYTVCGTP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE--LEEKIRSNRV-IELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14183   170 TYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQevLFDQILMGQVdFPSPYWDNVSDSAKELITMMLQVD 249
                         250
                  ....*....|....*..
gi 1907200402 255 PARRISFKDFFAHPWVD 271
Cdd:cd14183   250 VDQRYSALQVLEHPWVN 266
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
12-270 2.97e-33

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: 126.77  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKkDTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDN--DNIYL 89
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLR-NTKTIFALKTITTDP-NPDVQKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFI-----HTRRIlPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFA-QH 163
Cdd:cd06621    79 AMEYCEGGSLDSIYkkvkkKGGRI-GEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLT--RKGQVKLCDFGVSgEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVlrGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFS-----ELEEKIRSNRVIELPLRPQ 238
Cdd:cd06621   156 VNSLAGTFT--GTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVNMPNPELKDEPE 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907200402 239 L----SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06621   234 NgikwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWI 269
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
14-284 3.38e-33

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: 127.69  E-value: 3.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTER------LGSGTYATVYKAyakKD--TREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD-FQWDN 84
Cdd:cd07856     6 FEITTRysdlqpVGMGAFGLVCSA---RDqlTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDiFISPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFcAGGDLSRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM 164
Cdd:cd07856    83 EDIYFVTEL-LGTDLHRLLTSRP-LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVN--ENCDLKICDFGLARIQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 SPWDEKHVlrGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRS----FS-----------ELEEKIRS- 227
Cdd:cd07856   159 DPQMTGYV--STRYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDhvnqFSiitellgtppdDVINTICSe 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 228 ---NRVIELPLR---------PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQA 284
Cdd:cd07856   237 ntlRFVQSLPKRervpfsekfKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDPTDEPVADE 305
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
14-258 5.36e-33

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: 125.69  E-value: 5.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLN--------KASVENLLTEIEILK-GIRHPHIVQLKDFQWDN 84
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGQTLLALKEINMTNPAfgrteqerDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHT-----RRILPEKVARVFMQqLASALQFLH-ERNISHLDLKPQNILLSSLEKphLKLADF 158
Cdd:cd08528    82 DRLYIVMELIEGAPLGEHFSSlkeknEHFTEDRIWNIFVQ-MVLALRYLHkEKQIVHRDLKPNNIMLGEDDK--VTITDF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 159 GFAQHMSpWDEKHVLR--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlR 236
Cdd:cd08528   159 GLAKQKG-PESSKMTSvvGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLP-E 236
                         250       260
                  ....*....|....*....|..
gi 1907200402 237 PQLSLDCRDLLQRLLERDPARR 258
Cdd:cd08528   237 GMYSDDITFVIRSCLTPDPEAR 258
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
17-270 7.65e-33

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: 125.28  E-value: 7.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  17 TERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRH---PHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd06917     6 LELVGRGSYGAVYRGYHVK-TGRVVALKVLNLDT-DDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRIlPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlekPH-LKLADFGFA-QHMSPWDEKH 171
Cdd:cd06917    84 CEGGSIRTLMRAGPI-AERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTN---TGnVKLCDFGVAaSLNQNSSKRS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRpQLSLDCRDLLQRL 250
Cdd:cd06917   160 TFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEGN-GYSPLLKEFVAAC 238
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd06917   239 LDEEPKDRLSADELLKSKWI 258
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
18-270 7.68e-33

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: 125.24  E-value: 7.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAkkDTREVVAIKCVAKKSLNKASVE----NLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd06631     7 NVLGKGAYGTVYCGLT--STGQLIAVKQVELDTSDKEKAEkeyeKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLssLEKPHLKLADFGFAQHMSpWDEKHV- 172
Cdd:cd06631    85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIML--MPNGVIKLIDFGCAKRLC-INLSSGs 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 -------LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRD 245
Cdd:cd06631   162 qsqllksMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLPDKFSPEARD 241
                         250       260
                  ....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06631   242 FVHACLTRDQDERPSAEQLLKHPFI 266
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-268 8.15e-33

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: 127.11  E-value: 8.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDGFILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKAS-VENLLTEIEILKGIRHPHIVQLK-DFQwDNDN 86
Cdd:cd05596    23 MNAEDFDVIKVIGRGAFGEV-QLVRHKSTKKVYAMKLLSKFEMIKRSdSAFFWEERDIMAHANSEWIVQLHyAFQ-DDKY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRRIlPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMsp 166
Cdd:cd05596   101 LYMVMDYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA--SGHLKLADFGTCMKM-- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 wDEKHVLR-----GSPLYMAPEmVCRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPL 235
Cdd:cd05596   176 -DKDGLVRsdtavGTPDYISPE-VLKSQggdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKnSLQFPD 253
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 236 RPQLSLDCRDLLQRLLERDPAR--RISFKDFFAHP 268
Cdd:cd05596   254 DVEISKDAKSLICAFLTDREVRlgRNGIEEIKAHP 288
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-268 1.03e-32

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: 124.46  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd08220     8 VGRGAYGTVYLC-RRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRR---ILPEKVARVFMQQLAsALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd08220    87 FEYIQQRKgslLSEEEILHFFVQILL-ALHHVHSKQILHRDLKTQNILLNK-KRTVVKIGDFGISKILSSKSKAYTVVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIelPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd08220   165 PCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFA--PISDRYSEELRHLILSMLHLDPN 242
                         250
                  ....*....|..
gi 1907200402 257 RRISFKDFFAHP 268
Cdd:cd08220   243 KRPTLSEIMAQP 254
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
16-213 1.08e-32

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 130.30  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAyakKDTR--EVVAIKcVAKKSLnkASVENLlteieILKGIR---------HPHIVQLKDFQWDN 84
Cdd:NF033483   11 IGERIGRGGMAEVYLA---KDTRldRDVAVK-VLRPDL--ARDPEF-----VARFRReaqsaaslsHPNIVSVYDVGEDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTR-RILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:NF033483   80 GIPYIVMEYVDGRTLKDYIREHgPLSPEEAVEI-MIQILSALEHAHRNGIVHRDIKPQNILIT--KDGRVKVTDFGIARA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 164 MSpwdE------KHVLrGSPLYMAPE-----MVcrrqyDARVDLWSVGVILYEALFGQPPF 213
Cdd:NF033483  157 LS---SttmtqtNSVL-GTVHYLSPEqarggTV-----DARSDIYSLGIVLYEMLTGRPPF 208
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
14-269 1.49e-32

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: 124.84  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKK-TGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGgDLSRFIHT---RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMspwdek 170
Cdd:cd07861    81 LSM-DLKKYLDSlpkGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDN--KGVIKLADFGLARAF------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 hvlrGSPL-----------YMAPEMVCRRQ-YDARVDLWSVGVILYEALFGQPPFASRSfsELEEKIRSNRVIELP---- 234
Cdd:cd07861   152 ----GIPVrvythevvtlwYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDS--EIDQLFRIFRILGTPtedi 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 235 ------------------------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07861   226 wpgvtslpdykntfpkwkkgslrtAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-270 1.67e-32

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 125.15  E-value: 1.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKAYAKKdTREVVAIKCVakKSLNKASvenllTEIEI-LKGIRHPHIVQLKDFQwdnDNIY----- 88
Cdd:cd14170     5 VTSQVLGLGINGKVLQIFNKR-TQEKFALKML--QDCPKAR-----REVELhWRASQCPHIVRIVDVY---ENLYagrkc 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 --LIMEFCAGGDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPH--LKLADFGFAQ 162
Cdd:cd14170    74 llIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTS-KRPNaiLKLTDFGFAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR---SFSE-LEEKIRSNRViELPlRP- 237
Cdd:cd14170   153 ETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglAISPgMKTRIRMGQY-EFP-NPe 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 238 --QLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14170   231 wsEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 265
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
20-259 1.84e-32

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: 125.59  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVY--KAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLK-DFQWDNdNIYLIMEFCAG 96
Cdd:cd05582     3 LGQGSFGKVFlvRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHyAFQTEG-KLYLILDFLRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHmSPWDEKHVLR-- 174
Cdd:cd05582    82 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EDGHIKLTDFGLSKE-SIDHEKKAYSfc 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvieLPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd05582   159 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAK---LGMPQFLSPEAQSLLRALFKRN 235

                  ....*
gi 1907200402 255 PARRI 259
Cdd:cd05582   236 PANRL 240
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
13-283 2.18e-32

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: 125.59  E-value: 2.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKA-YAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR-HPHIVQLKD----FQWDNDN 86
Cdd:cd07857     1 RYELIKELGQGAYGIVCSArNAETSEEETVAIKKITNVFSKKILAKRALRELKLLRHFRgHKNITCLYDmdivFPGNFNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGgDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSP 166
Cdd:cd07857    81 LYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA--DCELKICDFGLARGFSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEK-------HVlrGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELEE 223
Cdd:cd07857   158 NPGEnagfmteYV--ATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYvdqlnqilqvlgtpdEETLS 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 224 KIRSNRVIE----LPLRPQLSL---------DCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQ 283
Cdd:cd07857   236 RIGSPKAQNyirsLPNIPKKPFesifpnanpLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPDDEPVCQ 308
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
6-283 4.54e-32

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 125.10  E-value: 4.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPrlDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQL-------- 77
Cdd:cd07851    11 WEVP--DRYQNLSPVGSGAYGQVCSAFDTK-TGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLldvftpas 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  78 --KDFQwdndNIYLIMEFcAGGDLSRFIHTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKL 155
Cdd:cd07851    88 slEDFQ----DVYLVTHL-MGADLNNIVKCQKLSDDHI-QFLVYQILRGLKYIHSAGIIHRDLKPSNLAVN--EDCELKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 156 ADFGFAQHMSPWDEKHVlrGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------S 219
Cdd:cd07851   160 LDFGLARHTDDEMTGYV--ATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHidqlkrimnlvgtpdE 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 220 ELEEKIRSNR---VIE-LPLRPQ---------LSLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQ 283
Cdd:cd07851   238 ELLKKISSESarnYIQsLPQMPKkdfkevfsgANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPEDEPVAP 314
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
14-258 4.69e-32

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 123.17  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASvENLLTEIEILKGIRHPHIVQLKDfQWDNDN-IYLIME 92
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVDGVTY-AIKKIRLTEKSSAS-EKVLREVKALAKLNHPNIVRYYT-AWVEEPpLYIQME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILP---EKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKpHLKLADFGFAQHMSPWDE 169
Cdd:cd13996    85 LCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDL-QVKIGDFGLATSIGNQKR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLR---------------GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALfgQPPfasRSFSELEEKIRSNRVIELP 234
Cdd:cd13996   164 ELNNLnnnnngntsnnsvgiGTPLYASPEQLDGENYNEKADIYSLGIILFEML--HPF---KTAMERSTILTDLRNGILP 238
                         250       260
                  ....*....|....*....|....*
gi 1907200402 235 LRPQLSLDC-RDLLQRLLERDPARR 258
Cdd:cd13996   239 ESFKAKHPKeADLIQSLLSKNPEER 263
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
20-270 5.07e-32

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: 122.56  E-value: 5.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKcvaKKSLN-KASVE---NLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd06607     9 IGHGSFGAVYYARNKR-TSEVVAIK---KMSYSgKQSTEkwqDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 G--GDLSRfIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwdeKHVL 173
Cdd:cd06607    85 GsaSDIVE-VHKKPLQEVEIAAICHGAL-QGLAYLHSHNRIHRDVKAGNILLT--EPGTVKLADFGSASLVCP---ANSF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVC---RRQYDARVDLWSVGVILYEALFGQPP-FASRSFSELEEkIRSNRVIELPLRPqLSLDCRDLLQR 249
Cdd:cd06607   158 VGTPYWMAPEVILamdEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALYH-IAQNDSPTLSSGE-WSDDFRNFVDS 235
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd06607   236 CLQKIPQDRPSAEDLLKHPFV 256
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
7-277 5.41e-32

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: 123.61  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   7 GLPR--LDGFIlteRLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKasvENLLTEIEILKGIRHPHIVQLKDFQWDN 84
Cdd:cd06658    18 GDPReyLDSFI---KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRR---ELLFNEVVIMRDYHHENVVDMYNSYLVG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF-AQH 163
Cdd:cd06658    92 DELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVL-RALSYLHNQGVIHRDIKSDSILLTS--DGRIKLSDFGFcAQV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDC 243
Cdd:cd06658   169 SKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVL 248
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPWVDLEHMPS 277
Cdd:cd06658   249 RGFLDLMLVREPSQRATAQELLQHPFLKLAGPPS 282
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
20-270 6.07e-32

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: 123.83  E-value: 6.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSlnKASVENLLTEIEILKGirHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEY-AVKIISRRM--EANTQREVAALRLCQS--HPNIVALHEVLHDQYHTYLVMELLRGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSS-LEKPHLKLADFGFAQHMSPWDEK-HVLRGSP 177
Cdd:cd14180    89 LDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADeSDGAVLKVIDFGFARLRPQGSRPlQTPCFTL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS-------FSELEEKIRSNRV-IELPLRPQLSLDCRDLLQR 249
Cdd:cd14180   169 QYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfhnhAADIMHKIKEGDFsLEGEAWKGVSEEAKDLVRG 248
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARRISFKDFFAHPWV 270
Cdd:cd14180   249 LLTVDPAKRLKLSELRESDWL 269
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
10-269 7.81e-32

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 124.32  E-value: 7.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAK-KSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIY 88
Cdd:PTZ00426   28 KYEDFNFIRTLGTGSFGRVILATYKNEDFPPVAIKRFEKsKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSpwD 168
Cdd:PTZ00426  108 LVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLD--KDGFIKMTDFGFAKVVD--T 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrVIELPlrPQLSLDCRDLLQ 248
Cdd:PTZ00426  184 RTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEG-IIYFP--KFLDNNCKHLMK 260
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 249 RLLERDPARRI-----SFKDFFAHPW 269
Cdd:PTZ00426  261 KLLSHDLTKRYgnlkkGAQNVKEHPW 286
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
20-259 9.73e-32

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 123.83  E-value: 9.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILK---GIRHPHIVQLK-DFQWDNDnIYLIMEFC 94
Cdd:cd05586     1 IGKGTFGQVYQV-RKKDTRRIYAMKVLSKKVIvAKKEVAHTIGERNILVrtaLDESPFIVGLKfSFQTPTD-LYLVTDYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ-HMSPWDEKHVL 173
Cdd:cd05586    79 SGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDA--NGHIALCDFGLSKaDLTDNKTTNTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQ-YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlRPQLSLDCRDLLQRLLE 252
Cdd:cd05586   157 CGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKV-RFP-KDVLSDEGRSFVKGLLN 234

                  ....*..
gi 1907200402 253 RDPARRI 259
Cdd:cd05586   235 RNPKHRL 241
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
60-270 1.17e-31

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: 121.85  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  60 LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLK 139
Cdd:cd14111    47 LQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 140 PQNILLSSLEKphLKLADFGFAQHMSPWDEKHVLR--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS 217
Cdd:cd14111   127 PDNIMVTNLNA--IKIVDFGSAQSFNPLSLRQLGRrtGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQD 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 218 FSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14111   205 PQETEAKILVAKFDAFKLYPNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
20-275 1.40e-31

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 123.30  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLN-KASVENLLTEIEILK-GIRHPHIVQLKD-FQwDNDNIYLIMEFCAG 96
Cdd:cd05588     3 IGRGSYAKVLMVELKK-TKRIYAMKVIKKELVNdDEDIDWVQTEKHVFEtASNHPFLVGLHScFQ-TESRLFFVIEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPWDEKHVLRG 175
Cdd:cd05588    81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDS--EGHIKLTDYGMCKEgLRPGDTTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF----ASRSFSELEEKIRSNRVIELPLR-PQ-LSLDCRDLLQR 249
Cdd:cd05588   159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNPDQNTEDYLFQVILEKPIRiPRsLSVKAASVLKG 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 250 LLERDPARRI------SFKDFFAHPW---VDLEHM 275
Cdd:cd05588   239 FLNKNPAERLgchpqtGFADIQSHPFfrtIDWEQL 273
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
12-263 1.43e-31

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 122.30  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNK-ASVENLLTEIEILKGIRHPHIVQLK-DFQWDNDnIYL 89
Cdd:cd05608     1 DWFLDFRVLGKGGFGEVS-ACQMRATGKLYACKKLNKKRLKKrKGYEGAMVEKRILAKVHSRFIVSLAyAFQTKTD-LCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHT----RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS 165
Cdd:cd05608    79 VMTIMNGGDLRYHIYNvdeeNPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLD--DDGNVRISDLGLAVELK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEK-HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSfSELEEKIRSNRVIELPLR--PQLSLD 242
Cdd:cd05608   157 DGQTKtKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARG-EKVENKELKQRILNDSVTysEKFSPA 235
                         250       260
                  ....*....|....*....|.
gi 1907200402 243 CRDLLQRLLERDPARRISFKD 263
Cdd:cd05608   236 SKSICEALLAKDPEKRLGFRD 256
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
20-284 2.43e-31

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 122.86  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDF----QWDNDN-IYLIMEFc 94
Cdd:cd07858    13 IGRGAYGIVCSA-KNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDImpppHREAFNdVYIVYEL- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-------QHMSpw 167
Cdd:cd07858    91 MDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNA--NCDLKICDFGLArttsekgDFMT-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 dEKHVLRgspLYMAPEMV-CRRQYDARVDLWSVGVILYEALFGQPPF----------------ASRSFSELEEkIRSNR- 229
Cdd:cd07858   167 -EYVVTR---WYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFpgkdyvhqlklitellGSPSEEDLGF-IRNEKa 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 230 ---VIELPLRPQLSLDCR---------DLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQA 284
Cdd:cd07858   242 rryIRSLPYTPRQSFARLfphanplaiDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQT 308
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
7-277 3.77e-31

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: 121.28  E-value: 3.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   7 GLPR--LDGFIlteRLGSGTYATVYKAYAKKdTREVVAIKcvaKKSLNKASVENLL-TEIEILKGIRHPHIVQLKDFQWD 83
Cdd:cd06657    16 GDPRtyLDNFI---KIGEGSTGIVCIATVKS-SGKLVAVK---KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  84 NDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQ 162
Cdd:cd06657    89 GDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVL-KALSVLHAQGVIHRDIKSDSILLT--HDGRVKLSDFGFcAQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLD 242
Cdd:cd06657   166 VSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPS 245
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 243 CRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPS 277
Cdd:cd06657   246 LKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPS 280
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
19-213 5.47e-31

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: 120.84  E-value: 5.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKaYAKKDTREVVAIK-CvaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWD------NDNIYLIM 91
Cdd:cd14038     1 RLGTGGFGNVLR-WINQETGEQVAIKqC--RQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGlqklapNDLPLLAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRI---LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHL-KLADFGFAQHMSPW 167
Cdd:cd14038    78 EYCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKIIDLGYAKELDQG 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 168 DEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14038   158 SLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
20-269 6.10e-31

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: 119.74  E-value: 6.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSlnkASVENLLTEIEI-LKGIRHPHIVQLKDFQWDNDNIYLI-MEFCAGG 97
Cdd:cd13987     1 LGEGTYGKVLLAVHKG-SGTKMALKFVPKPS---TKLKDFLREYNIsLELSVHPHIIKTYDVAFETEDYYVFaQEYAPYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHM-SPwdEKHVLRGS 176
Cdd:cd13987    77 DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVgST--VKRVSGTI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PlYMAPEmVC------RRQYDARVDLWSVGVILYEALFGQPPF--ASRSFSELEE--KIRSNRVIELP--LRPqLSLDCR 244
Cdd:cd13987   155 P-YTAPE-VCeakkneGFVVDPSIDVWAFGVLLFCCLTGNFPWekADSDDQFYEEfvRWQKRKNTAVPsqWRR-FTPKAL 231
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 245 DLLQRLLERDPARRISFKD---FFAHPW 269
Cdd:cd13987   232 RMFKKLLAPEPERRCSIKEvfkYLGDRW 259
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
18-214 6.99e-31

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 119.64  E-value: 6.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYakkDTREVVAIK-CVAK-KSLNKASVENLLTEIEILKGIRHPHIVQLKDFqW---DNDNIYLIME 92
Cdd:cd13983     7 EVLGRGSFKTVYRAF---DTEEGIEVAwNEIKlRKLPKAERQRFKQEIEILKSLKHPNIIKFYDS-WeskSKKEVIFITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILLSSLEKpHLKLADFGFAQHMSPWDEK 170
Cdd:cd13983    83 LMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTG-EVKIGDLGLATLLRQSFAK 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907200402 171 HVLrGSPLYMAPEMVcRRQYDARVDLWSVGVILYEALFGQPPFA 214
Cdd:cd13983   162 SVI-GTPEFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPYS 203
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
20-268 7.73e-31

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 119.84  E-value: 7.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIK----CVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd06630     8 LGTGAFSSCYQARDVK-TGTLMAVKqvsfCRNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKpHLKLADFGFAQHMSP----WDE-K 170
Cdd:cd06630    87 GGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQ-RLRIADFGAAARLASkgtgAGEfQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE---LEEKIRSnrVIELPLRPQ-LSLDCRDL 246
Cdd:cd06630   166 GQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNhlaLIFKIAS--ATTPPPIPEhLSPGLRDV 243
                         250       260
                  ....*....|....*....|..
gi 1907200402 247 LQRLLERDPARRISFKDFFAHP 268
Cdd:cd06630   244 TLRCLELQPEDRPPARELLKHP 265
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
10-269 1.31e-30

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: 119.73  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVeNLLTEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd07871     3 KLETYVKLDKLGEGTYATVFKGRSKL-TENLVALKEIRLEHEEGAPC-TAIREVSLLKNLKHANIVTLHDIIHTERCLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCaGGDLSRFI-HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWD 168
Cdd:cd07871    81 VFEYL-DSDLKQYLdNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLIN--EKGELKLADFGLARAKSVPT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPE--MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE------------LEEK---IRSNRVI 231
Cdd:cd07871   158 KTYSNEVVTLWYRPPdvLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEelhlifrllgtpTEETwpgVTSNEEF 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907200402 232 EL---------PLR---PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07871   238 RSylfpqyraqPLInhaPRLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
6-270 1.46e-30

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 119.91  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRLDGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLK------- 78
Cdd:cd07864     1 WGKRCVDKFDIIGIIGEGTYGQVYKA-KDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKeivtdkq 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  79 ---DFQWDNDNIYLIMEFcAGGDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLK 154
Cdd:cd07864    80 dalDFKKDKGAFYLVFEY-MDHDLMGLLESGLVhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNN--KGQIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 155 LADFGFAQHMS-----PWDEKHVlrgSPLYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPF-ASRSFSELE--EKI 225
Cdd:cd07864   157 LADFGLARLYNseesrPYTNKVI---TLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIFqANQELAQLEliSRL 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 226 RSN-------RVIELP--------------LRPQLSL---DCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd07864   234 CGSpcpavwpDVIKLPyfntmkpkkqyrrrLREEFSFiptPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
11-259 1.81e-30

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 120.57  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd05593    14 MNDFDYLKLLGKGTFGKVILV-REKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH-MSPWD 168
Cdd:cd05593    93 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD--KDGHIKITDFGLCKEgITDAA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPlrPQLSLDCRDLLQ 248
Cdd:cd05593   171 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED-IKFP--RTLSADAKSLLS 247
                         250
                  ....*....|.
gi 1907200402 249 RLLERDPARRI 259
Cdd:cd05593   248 GLLIKDPNKRL 258
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-259 2.05e-30

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: 120.02  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVY--KAYAKKDTREVVAIKCVAKKSLNK--ASVENLLTEIEILKGIRH-PHIVQLK-DFQWDNdNI 87
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvRKVSGHDANKLYAMKVLRKAALVQkaKTVEHTRTERNVLEHVRQsPFLVTLHyAFQTDA-KL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPW 167
Cdd:cd05614    81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDS--EGHVVLTDFGLSKEFLTE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLR--GSPLYMAPEMV-CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIrSNRVIEL--PLRPQLSLD 242
Cdd:cd05614   159 EKERTYSfcGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEV-SRRILKCdpPFPSFIGPV 237
                         250
                  ....*....|....*..
gi 1907200402 243 CRDLLQRLLERDPARRI 259
Cdd:cd05614   238 ARDLLQKLLCKDPKKRL 254
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
10-259 2.44e-30

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: 120.10  E-value: 2.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGI-RHPHIVQLKDFQWDNDNI 87
Cdd:cd05615     8 RLTDFNFLMVLGKGSFGKVMLA-ERKGSDELYAIKILKKDVvIQDDDVECTMVEKRVLALQdKPPFLTQLHSCFQTVDRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSP 166
Cdd:cd05615    87 YFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDS--EGHIKIADFGMCkEHMVE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVielPLRPQLSLDCRDL 246
Cdd:cd05615   165 GVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNV---SYPKSLSKEAVSI 241
                         250
                  ....*....|...
gi 1907200402 247 LQRLLERDPARRI 259
Cdd:cd05615   242 CKGLMTKHPAKRL 254
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
12-279 2.54e-30

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: 119.76  E-value: 2.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVykAYAK-KDTREVVAIKCVAK-KSLNKASVENLLTEIEIL-KGIRhPHIVQLK-DFQwDNDNI 87
Cdd:cd05597     1 DDFEILKVIGRGAFGEV--AVVKlKSTEKVYAMKILNKwEMLKRAETACFREERDVLvNGDR-RWITKLHyAFQ-DENYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGD----LSRFihtRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH 163
Cdd:cd05597    77 YLVMDYYCGGDlltlLSKF---EDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDR--NGHIRLADFGSCLK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPwDEK---HVLRGSPLYMAPEMV-----CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELP 234
Cdd:cd05597   152 LRE-DGTvqsSVAVGTPDYISPEILqamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKeHFSFP 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 235 LR-PQLSLDCRDLLQRLLErDPARRI---SFKDFFAHPW---VDLEHMPSGE 279
Cdd:cd05597   231 DDeDDVSEEAKDLIRRLIC-SRERRLgqnGIDDFKKHPFfegIDWDNIRDST 281
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
13-269 2.68e-30

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: 119.98  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTER------LGSGTYATVYKAYAKKdTREVVAIKCVakKSLNKASvENLLTEIEILKGIRH------PHIVQLKD- 79
Cdd:cd14134     7 GDLLTNRykilrlLGEGTFGKVLECWDRK-RKRYVAVKII--RNVEKYR-EAAKIEIDVLETLAEkdpngkSHCVQLRDw 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  80 FQWDNdNIYLIMEFCaGGDLSRFIHTRRILP---EKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSS--------- 147
Cdd:cd14134    83 FDYRG-HMCIVFELL-GPSLYDFLKKNNYGPfplEHV-QHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynp 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 148 --------LEKPHLKLADFGFAqhmSPWDEKHvlrgSPL-----YMAPEMVCRRQYDARVDLWSVGVILYE-----ALF- 208
Cdd:cd14134   160 kkkrqirvPKSTDIKLIDFGSA---TFDDEYH----SSIvstrhYRAPEVILGLGWSYPCDVWSIGCILVElytgeLLFq 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 209 ---------------GQPP--FASRS---------------FSELEEKIRSNRVIELPLRPQLSLDCR------DLLQRL 250
Cdd:cd14134   233 thdnlehlammerilGPLPkrMIRRAkkgakyfyfyhgrldWPEGSSSGRSIKRVCKPLKRLMLLVDPehrllfDLIRKM 312
                         330
                  ....*....|....*....
gi 1907200402 251 LERDPARRISFKDFFAHPW 269
Cdd:cd14134   313 LEYDPSKRITAKEALKHPF 331
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
14-269 3.09e-30

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: 120.92  E-value: 3.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLA-RKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF------------ 160
Cdd:cd05625    82 YIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILID--RDGHIKLTDFGLctgfrwthdsky 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 --------------------------AQHMSPWDEK----------HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILY 204
Cdd:cd05625   160 yqsgdhlrqdsmdfsnewgdpencrcGDRLKPLERRaarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 205 EALFGQPPFASRSFSELEEK-IRSNRVIELPLRPQLSLDCRDLLQRLLeRDPARRI---SFKDFFAHPW 269
Cdd:cd05625   240 EMLVGQPPFLAQTPLETQMKvINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLgknGADEIKAHPF 307
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
11-269 3.86e-30

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: 120.14  E-value: 3.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNK-ASVENLLTEIEIL-KGIRHPHIVQLKDFQWDNDNIY 88
Cdd:cd05618    19 LQDFDLLRVIGRGSYAKVLLVRLKK-TERIYAMKVVKKELVNDdEDIDWVQTEKHVFeQASNHPFLVGLHSCFQTESRLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSPW 167
Cdd:cd05618    98 FVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDS--EGHIKLTDYGMCKEgLRPG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQ------LSL 241
Cdd:cd05618   176 DTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQiriprsLSV 255
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 242 DCRDLLQRLLERDPARRI------SFKDFFAHPW 269
Cdd:cd05618   256 KAASVLKSFLNKDPKERLgchpqtGFADIQGHPF 289
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
20-224 4.50e-30

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: 118.32  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKaYAKKDTREVVAIK-CVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDF------QWDNDNIYLIME 92
Cdd:cd13989     1 LGSGGFGYVTL-WKHQDTGEYVAIKkCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVppelekLSPNDLPLLAME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIHTRRI---LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLE-KPHLKLADFGFAQHMSPWD 168
Cdd:cd13989    80 YCSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgRVIYKLIDLGYAKELDQGS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS-----FSELEEK 224
Cdd:cd13989   160 LCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWqpvqwHGKVKQK 220
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
20-269 4.82e-30

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 117.84  E-value: 4.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05605     8 LGKGGFGEVC-ACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHT--RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05605    87 LKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLD--DHGHVRISDLGLAVEIPEGETIRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR----SFSELEEKIRSNRVielPLRPQLSLDCRDLLQRLLE 252
Cdd:cd05605   165 VGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKEDQE---EYSEKFSEEAKSICSQLLQ 241
                         250       260
                  ....*....|....*....|..
gi 1907200402 253 RDPARRI-----SFKDFFAHPW 269
Cdd:cd05605   242 KDPKTRLgcrgeGAEDVKSHPF 263
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
18-269 4.90e-30

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 118.14  E-value: 4.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTrEVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGg 97
Cdd:cd07870     6 EKLGEGSYATVYKGISRING-QLVALKVISMKT-EEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI--HTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDEKHVLRG 175
Cdd:cd07870    83 DLAQYMiqHPGGLHPYNV-RLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE--LKLADFGLARAKSIPSQTYSSEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPE--MVCRRQYDARVDLWSVGVILYEALFGQPPFA--SRSFSELeEKI-------------------RSNRVIE 232
Cdd:cd07870   160 VTLWYRPPdvLLGATDYSSALDIWGAGCIFIEMLQGQPAFPgvSDVFEQL-EKIwtvlgvptedtwpgvsklpNYKPEWF 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907200402 233 LPLRPQLSLD----------CRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07870   239 LPCKPQQLRVvwkrlsrppkAEDLASQMLMMFPKDRISAQDALLHPY 285
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
20-269 6.38e-30

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 118.71  E-value: 6.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVEN------------LLTEIEILKGIRHPHIVQLKDFQWDNDNI 87
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIV-AIKKVKIIEISNDVTKDrqlvgmcgihftTLRELKIMNEIKHENIMGLVDVYVEGDFI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGgDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA------ 161
Cdd:PTZ00024   96 NLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINS--KGICKIADFGLArrygyp 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 ---------QHMSPwDEKHVLRGSPL-YMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFA--------SRSFSELE 222
Cdd:PTZ00024  173 pysdtlskdETMQR-REEMTSKVVTLwYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPgeneidqlGRIFELLG 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 223 EKIRSN--RVIELPLR---------------PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:PTZ00024  252 TPNEDNwpQAKKLPLYteftprkpkdlktifPNASDDAIDLLQSLLKLNPLERISAKEALKHEY 315
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-269 7.39e-30

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 117.48  E-value: 7.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIK-----------CVAkkslnkasvenlLTEIEILKGIRHPHIVQLKDFQWDNDN 86
Cdd:cd07844     6 DKLGEGSYATVYKGRSKL-TGQLVALKeirleheegapFTA------------IREASLLKDLKHANIVTLHDIIHTKKT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGgDLSRFI--HTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM 164
Cdd:cd07844    73 LTLVFEYLDT-DLKQYMddCGGGLSMHNV-RLFLFQLLRGLAYCHQRRVLHRDLKPQNLLIS--ERGELKLADFGLARAK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 S----------------PWDekhVLRGSplymapemvcrRQYDARVDLWSVGVILYEALFGQPPFASRSFSELE-EKI-- 225
Cdd:cd07844   149 SvpsktysnevvtlwyrPPD---VLLGS-----------TEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQlHKIfr 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 226 ----------------------RSNRVIELPLR---PQLSL--DCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07844   215 vlgtpteetwpgvssnpefkpySFPFYPPRPLInhaPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
12-270 7.41e-30

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 117.81  E-value: 7.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYaTVYKAYAKKDTREVVAIKCVAKKSLNKASvenlltEIEIL-KGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd14177     4 DVYELKEDIGVGSY-SVCKRCIHRATNMEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDVYDDGRYVYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHmspwd 168
Cdd:cd14177    77 TELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmdDSANADSIRICDFGFAKQ----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 ekhvLRG------SPLY----MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLR-- 236
Cdd:cd14177   152 ----LRGenglllTPCYtanfVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSgg 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907200402 237 --PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14177   228 nwDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
20-270 9.75e-30

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: 116.96  E-value: 9.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14197    17 LGRGKFAVVRKC-VEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 L-SRFIHTR-RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKP--HLKLADFGFAQHMSPWDEKHVLR 174
Cdd:cd14197    96 IfNQCVADReEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTS-ESPlgDIKIVDFGLSRILKNSEELREIM 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF----ASRSFSELEEKIRSNRVIELPLrpqLSLDCRDLLQRL 250
Cdd:cd14197   175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFlgddKQETFLNISQMNVSYSEEEFEH---LSESAIDFIKTL 251
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd14197   252 LIKKPENRATAEDCLKHPWL 271
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
5-270 1.02e-29

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: 116.66  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWGLPRLdgfilterLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKAS--VENLLTEIEILKGIRHPHIVQ----LK 78
Cdd:cd06653     3 NWRLGKL--------LGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSkeVNALECEIQLLKNLRHDRIVQyygcLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  79 DFQWDNDNIYLimEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADF 158
Cdd:cd06653    75 DPEEKKLSIFV--EYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDS--AGNVKLGDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 159 GFAQH-----MSPWDEKHVlRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfsELEEKIRSNRVIEL 233
Cdd:cd06653   151 GASKRiqticMSGTGIKSV-TGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA-----EYEAMAAIFKIATQ 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907200402 234 PLRPQL----SLDCRDLLQRLLERDpARRISFKDFFAHPWV 270
Cdd:cd06653   225 PTKPQLpdgvSDACRDFLRQIFVEE-KRRPTAEFLLRHPFV 264
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-259 1.38e-29

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: 117.02  E-value: 1.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVY--KAYAKKDTREVVAIKCVAKKSL-NKA-SVENLLTEIEILKGIRH-PHIVQLK-DFQWDNdNI 87
Cdd:cd05613     2 FELLKVLGTGAYGKVFlvRKVSGHDAGKLYAMKVLKKATIvQKAkTAEHTRTERQVLEHIRQsPFLVTLHyAFQTDT-KL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-MSP 166
Cdd:cd05613    81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS--SGHVVLTDFGLSKEfLLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEK-HVLRGSPLYMAPEMV--CRRQYDARVDLWSVGVILYEALFGQPPFA----SRSFSELEEKIRSNrviELPLRPQL 239
Cdd:cd05613   159 ENERaYSFCGTIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKS---EPPYPQEM 235
                         250       260
                  ....*....|....*....|
gi 1907200402 240 SLDCRDLLQRLLERDPARRI 259
Cdd:cd05613   236 SALAKDIIQRLLMKDPKKRL 255
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-270 1.40e-29

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: 116.10  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDtREVVAIKCVAK-KSLNKASVENLLT---EIEILK----GIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14101     8 LGKGGFGTVYAGHRISD-GLQVAIKQISRnRVQQWSKLPGVNPvpnEVALLQsvggGPGHRGVIRLLDWFEIPEGFLLVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 E---FCAggDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLsSLEKPHLKLADFGFAQ--HMSP 166
Cdd:cd14101    87 ErpqHCQ--DLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV-DLRTGDIKLIDFGSGAtlKDSM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEkhvLRGSPLYMAPEMVCRRQYDA-RVDLWSVGVILYEALFGQPPFasrsfsELEEKIRSnrvIELPLRPQLSLDCRD 245
Cdd:cd14101   164 YTD---FDGTRVYSPPEWILYHQYHAlPATVWSLGILLYDMVCGDIPF------ERDTDILK---AKPSFNKRVSNDCRS 231
                         250       260
                  ....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14101   232 LIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
20-269 1.79e-29

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: 115.44  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKasvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14115     1 IGRGRFSIVKKC-LHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLS-SLEKPHLKLADFGFAQHMSPWDEKHVLRGSPL 178
Cdd:cd14115    77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRViELPLRPQ----LSLDCRDLLQRLLERD 254
Cdd:cd14115   157 FAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDE--SKEETCINVCRV-DFSFPDEyfgdVSQAARDFINVILQED 233
                         250
                  ....*....|....*
gi 1907200402 255 PARRISFKDFFAHPW 269
Cdd:cd14115   234 PRRRPTAATCLQHPW 248
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
20-259 1.86e-29

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 118.21  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05594    33 LGKGTFGKVILV-KEKATGRYYAMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLH-ERNISHLDLKPQNILLSslEKPHLKLADFGFAQH-MSPWDEKHVLRGS 176
Cdd:cd05594   112 LFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD--KDGHIKITDFGLCKEgIKDGATMKTFCGT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDPA 256
Cdd:cd05594   190 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---EIRFPRTLSPEAKSLLSGLLKKDPK 266

                  ...
gi 1907200402 257 RRI 259
Cdd:cd05594   267 QRL 269
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
7-269 2.09e-29

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: 117.03  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   7 GLPRLDGFILTERLGSGTYATVYKAyAKKDTREVVAIKcvakKSLNKASVENL----LTEIEILKGIRHPHIVQLKDFQW 82
Cdd:cd07866     3 GCSKLRDYEILGKLGEGTFGEVYKA-RQIKTGRVVALK----KILMHNEKDGFpitaLREIKILKKLKHPNVVPLIDMAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  83 DNDN--------IYLIMEFCAGgDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHL 153
Cdd:cd07866    78 ERPDkskrkrgsVYMVTPYMDH-DLSGLLENPSVkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDN--QGIL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 154 KLADFGFAQhmsPWDEKHVLRGSPL---------------YMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRS 217
Cdd:cd07866   155 KIADFGLAR---PYDGPPPNPKGGGgggtrkytnlvvtrwYRPPELLLgERRYTTAVDIWGIGCVFAEMFTRRPILQGKS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 218 FSELEEKI----------------------------RSNRVIELPLRPQLSlDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07866   232 DIDQLHLIfklcgtpteetwpgwrslpgcegvhsftNYPRTLEERFGKLGP-EGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
18-271 2.43e-29

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: 116.47  E-value: 2.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRH-PHIVQLKDFQWDNDN----IYLIME 92
Cdd:cd07837     7 EKIGEGTYGKVYKA-RDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLDVEHVEENgkplLYLVFE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGgDLSRFIHTRR-----ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSPW 167
Cdd:cd07837    86 YLDT-DLKKFIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDK-QKGLLKIADLGLGRAFTIP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLRGSPL-YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSfsELEEKIRSNRVIELP----------L 235
Cdd:cd07837   164 IKSYTHEIVTLwYRAPEvLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDS--ELQQLLHIFRLLGTPneevwpgvskL 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 236 R-----------------PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVD 271
Cdd:cd07837   242 RdwheypqwkpqdlsravPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYFD 294
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
14-267 2.55e-29

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: 115.67  E-value: 2.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTReVVAIKCVakkslnKASVENLLTEIEILKGIRHPHIVQL----KDFQWDNDN--- 86
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGK-TYAIKRV------KLNNEKAEREVKALAKLDHPNIVRYngcwDGFDYDPETsss 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 ---------IYLIMEFCAGGDLSRFIHTRRILP-EKV-ARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKL 155
Cdd:cd14047    81 nssrsktkcLFIQMEFCEKGTLESWIEKRNGEKlDKVlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK--VKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 156 ADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALfgqppFASRSFSELEEKIRSNRVIELPL 235
Cdd:cd14047   159 GDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL-----HVCDSAFEKSKFWTDLRNGILPD 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 236 R--PQLSLDcRDLLQRLLERDPARRISFKDFFAH 267
Cdd:cd14047   234 IfdKRYKIE-KTIIKKMLSKKPEDRPNASEILRT 266
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
20-263 3.14e-29

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: 115.18  E-value: 3.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdtrEVVAIKCVAKKSLNKASV--ENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14061     2 IGVGGFGKVYRGIWRG---EEVAVKAARQDPDEDISVtlENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEkVARVFMQQLASALQFLHERN---ISHLDLKPQNILLS------SLEKPHLKLADFGFAQHMSpwd 168
Cdd:cd14061    79 ALNRVLAGRKIPPH-VLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILeaieneDLENKTLKITDFGLAREWH--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 ekHVLR----GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLRPQLSLDCR 244
Cdd:cd14061   155 --KTTRmsaaGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNK-LTLPIPSTCPEPFA 231
                         250
                  ....*....|....*....
gi 1907200402 245 DLLQRLLERDPARRISFKD 263
Cdd:cd14061   232 QLMKDCWQPDPHDRPSFAD 250
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
16-266 3.30e-29

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: 115.21  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKA-YAKKDTREV-VAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDnIYLIMEF 93
Cdd:cd05056    10 LGRCIGEGQFGDVYQGvYMSPENEKIaVAVK-TCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWIVMEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlekPH-LKLADFGFAQHMSPWDEKH 171
Cdd:cd05056    88 APLGELRSYLQVNKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS---PDcVKLGDFGLSRYMEDESYYK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGS-PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKI-RSNRvieLPLRPQLSLDCRDLL 247
Cdd:cd05056   165 ASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILmLGVKPFQGVKNNDVIGRIeNGER---LPMPPNCPPTLYSLM 241
                         250
                  ....*....|....*....
gi 1907200402 248 QRLLERDPARRISFKDFFA 266
Cdd:cd05056   242 TKCWAYDPSKRPRFTELKA 260
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
20-259 3.62e-29

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 116.64  E-value: 3.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILK-GIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05616     8 LGKGSFGKVMLA-ERKGTDELYAVKILKKDVvIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVMEYVNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHmSPWD--EKHVLRG 175
Cdd:cd05616    87 DLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDS--EGHIKIADFGMCKE-NIWDgvTTKTFCG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRViELPlrPQLSLDCRDLLQRLLERDP 255
Cdd:cd05616   164 TPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNV-AYP--KSMSKEAVAICKGLMTKHP 240

                  ....
gi 1907200402 256 ARRI 259
Cdd:cd05616   241 GKRL 244
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-258 3.71e-29

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: 115.90  E-value: 3.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   4 PSWGLPRLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWD 83
Cdd:cd08229    16 PDMGYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  84 NDNIYLIMEFCAGGDLSRFIH----TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFG 159
Cdd:cd08229    96 DNELNIVLELADAGDLSRMIKhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGV--VKLGDLG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 160 FAQHMSP-WDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFS--ELEEKIRSNRVIELPlR 236
Cdd:cd08229   174 LGRFFSSkTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYPPLP-S 252
                         250       260
                  ....*....|....*....|..
gi 1907200402 237 PQLSLDCRDLLQRLLERDPARR 258
Cdd:cd08229   253 DHYSEELRQLVNMCINPDPEKR 274
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
30-270 3.94e-29

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: 115.12  E-value: 3.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  30 KAYAKKDTREVvaikcvakkslnKASVENlltEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRIL 109
Cdd:cd14088    32 KKFLKRDGRKV------------RKAAKN---EINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 110 PEKVARVFMQQLASALQFLHERNISHLDLKPQNIL-LSSLEKPHLKLADFGFAQHmspwdEKHVLR---GSPLYMAPEMV 185
Cdd:cd14088    97 SERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNSKIVISDFHLAKL-----ENGLIKepcGTPEYLAPEVV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 186 CRRQYDARVDLWSVGVILYEALFGQPPFasrsFSELEEKIRSNRVIEL-------------PLRPQLSLDCRDLLQRLLE 252
Cdd:cd14088   172 GRQRYGRPVDCWAIGVIMYILLSGNPPF----YDEAEEDDYENHDKNLfrkilagdyefdsPYWDDISQAAKDLVTRLME 247
                         250
                  ....*....|....*...
gi 1907200402 253 RDPARRISFKDFFAHPWV 270
Cdd:cd14088   248 VEQDQRITAEEAISHEWI 265
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
11-267 4.73e-29

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 117.04  E-value: 4.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKDtREVVAIKCVAKKSL-NKASVENLLTEIEIL-KGIRHPHIVQLKDFQWDNDNIY 88
Cdd:cd05617    14 LQDFDLIRVIGRGSYAKVLLVRLKKN-DQIYAMKVVKKELVhDDEDIDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH-MSPW 167
Cdd:cd05617    93 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD--ADGHIKLTDYGMCKEgLGPG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF--ASRSFSELEEKIRSNRVIELPLR-PQ-LSLDC 243
Cdd:cd05617   171 DTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiITDNPDMNTEDYLFQVILEKPIRiPRfLSVKA 250
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907200402 244 RDLLQRLLERDPARRI------SFKDFFAH 267
Cdd:cd05617   251 SHVLKGFLNKDPKERLgcqpqtGFSDIKSH 280
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
13-269 6.19e-29

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: 115.85  E-value: 6.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFIlterlGSGTYATVYKAYAKK-DTREVVAIKCVakkslnKASVENL-------LTEIEILKGIRHPHIVQLKDFQWDN 84
Cdd:cd07842     6 GCI-----GRGTYGRVYKAKRKNgKDGKEYAIKKF------KGDKEQYtgisqsaCREIALLRELKHENVVSLVEVFLEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DN--IYLIMEFcAGGDLSRFIH-----TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPH--LKL 155
Cdd:cd07842    75 ADksVYLLFDY-AEHDLWQIIKfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERgvVKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 156 ADFGFAQHM-SPWdeKHVLRGSPL-----YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfselEEKIRSN 228
Cdd:cd07842   154 GDLGLARLFnAPL--KPLADLDPVvvtiwYRAPElLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGR-----EAKIKKS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 229 ---------RVIE---------------LPLRPQLSLD------------------------CRDLLQRLLERDPARRIS 260
Cdd:cd07842   227 npfqrdqleRIFEvlgtptekdwpdikkMPEYDTLKSDtkastypnsllakwmhkhkkpdsqGFDLLRKLLEYDPTKRIT 306

                  ....*....
gi 1907200402 261 FKDFFAHPW 269
Cdd:cd07842   307 AEEALEHPY 315
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
20-263 6.60e-29

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 114.07  E-value: 6.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdtrEVVAIKCVAKKSLNKAsvenLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14058     1 VGRGSFGVVCKARWRN---QIVAVKIIESESEKKA----FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPE-KVARV--FMQQLASALQFLH---ERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSpwDEKHVL 173
Cdd:cd14058    74 YNVLHGKEPKPIyTAAHAmsWALQCAKGVAYLHsmkPKALIHRDLKPPNLLLTN-GGTVLKICDFGTACDIS--THMTNN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPfasrsFSELE-EKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:cd14058   151 KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKP-----FDHIGgPAFRIMWAVHNGERPPLIKNCPKPIESLMT 225
                         250
                  ....*....|....*
gi 1907200402 253 R----DPARRISFKD 263
Cdd:cd14058   226 RcwskDPEKRPSMKE 240
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
14-282 7.33e-29

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: 115.86  E-value: 7.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLlTEIEILKGIRHPHIVQLKDFQ----WDNDN-IY 88
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAV-HKPTGQKVAIKKISPFEHQTYCLRTL-REIKILLRFKHENIIGILDIQrpptFESFKdVY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGgDLSRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPwD 168
Cdd:cd07849    85 IVQELMET-DLYKLIKTQH-LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT--NCDLKICDFGLARIADP-E 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHvlrGSPL--------YMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELEEK 224
Cdd:cd07849   160 HDH---TGFLteyvatrwYRAPEiMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYlhqlnlilgilgtpsQEDLNC 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 225 IRSNR----VIELPLRPQLSL---------DCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLA 282
Cdd:cd07849   237 IISLKarnyIKSLPFKPKVPWnklfpnadpKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVA 307
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
54-260 1.15e-28

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: 113.53  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  54 ASVENLLTEIEILKGIRHPHIVQLKD-FQWDNdNIYLIMEFCAGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHE 130
Cdd:cd08219    40 SAVEDSRKEAVLLAKMKHPNIVAFKEsFEADG-HLYIVMEYCDGGDLMQKIKLQRgkLFPEDTILQWFVQMCLGVQHIHE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 131 RNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS-PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFG 209
Cdd:cd08219   119 KRVLHRDIKSKNIFLT--QNGKVKLGDFGSARLLTsPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 210 QPPFASRSFSELEEKIRSNRVIELPLrpQLSLDCRDLLQRLLERDPARRIS 260
Cdd:cd08219   197 KHPFQANSWKNLILKVCQGSYKPLPS--HYSYELRSLIKQMFKRNPRSRPS 245
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
11-269 1.44e-28

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 114.33  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVeNLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd07873     1 LETYIKLDKLGEGTYATVYKGRSKL-TDNLVALKEIRLEHEEGAPC-TAIREVSLLKDLKHANIVTLHDIIHTEKSLTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCaGGDLSRFIH-TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDE 169
Cdd:cd07873    79 FEYL-DKDLKQYLDdCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLIN--ERGELKLADFGLARAKSIPTK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPE--MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE------------LEEK---IRSN---R 229
Cdd:cd07873   156 TYSNEVVTLWYRPPdiLLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEqlhfifrilgtpTEETwpgILSNeefK 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200402 230 VIELPL---------RPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07873   236 SYNYPKyradalhnhAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
12-275 1.50e-28

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: 114.39  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENL----LTEIEILKGIRHPHIVQLKD-FQWDNDN 86
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDyFSLDTDS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILL-SSLEKPHLKLADFGFAQH 163
Cdd:cd14041    86 FCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvNGTACGEIKITDFGLSKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPwDEKHVLRGSPL---------YMAPE--MVCRR--QYDARVDLWSVGVILYEALFGQPPFASRSFSE---LEEKIRS 227
Cdd:cd14041   166 MDD-DSYNSVDGMELtsqgagtywYLPPEcfVVGKEppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQdilQENTILK 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 228 NRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVdLEHM 275
Cdd:cd14041   245 ATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL-LPHI 291
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
14-268 1.64e-28

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 112.91  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTY--ATVYKayaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd08221     2 YIPVRVLGRGAFgeAVLYR---KTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHM-SPWD 168
Cdd:cd08221    79 EYCNGGNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADL--VKLGDFGISKVLdSESS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF-ASRSFSELEEKIRSNRVIELplrPQLSLDCRDLL 247
Cdd:cd08221   157 MAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFdATNPLRLAVKIVQGEYEDID---EQYSEEIIQLV 233
                         250       260
                  ....*....|....*....|.
gi 1907200402 248 QRLLERDPARRISFKDFFAHP 268
Cdd:cd08221   234 HDCLHQDPEDRPTAEELLERP 254
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
9-258 1.69e-28

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 117.43  E-value: 1.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENllTEIEILKGIRHPHIVQ-LKDFQWDnDNI 87
Cdd:PTZ00267   64 PREHMYVLTTLVGRNPTTAAFVATRGSDPKEKVVAKFVMLNDERQAAYAR--SELHCLAACDHFGIVKhFDDFKSD-DKL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTR--RILP--EKVARVFMQQLASALQFLHERNISHLDLKPQNILLssLEKPHLKLADFGFAQH 163
Cdd:PTZ00267  141 LLIMEYGSGGDLNKQIKQRlkEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL--MPTGIIKLGDFGFSKQ 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MS---PWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLrpQLS 240
Cdd:PTZ00267  219 YSdsvSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDPFPC--PVS 296
                         250
                  ....*....|....*...
gi 1907200402 241 LDCRDLLQRLLERDPARR 258
Cdd:PTZ00267  297 SGMKALLDPLLSKNPALR 314
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
12-270 1.70e-28

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: 113.95  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVvaikcvAKKSLNkaSVENLLTEIE----ILKGIR-HPHIVQL------KDF 80
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKA------AVKILD--PIHDIDEEIEaeynILKALSdHPNVVKFygmyykKDV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QwDNDNIYLIMEFCAGG---DLSR-FIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLA 156
Cdd:cd06638    90 K-NGDQLWLVLELCNGGsvtDLVKgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTT--EGGVKLV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 157 DFGF-AQHMSPWDEKHVLRGSPLYMAPEMV-CRRQ----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV 230
Cdd:cd06638   167 DFGVsAQLTSTRLRRNTSVGTPFWMAPEVIaCEQQldstYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907200402 231 IELPlRPQL-SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06638   247 PTLH-QPELwSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
14-280 2.65e-28

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: 113.61  E-value: 2.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENL----LTEIEILKGIRHPHIVQLKD-FQWDNDNIY 88
Cdd:cd14040     8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDyFSLDTDTFC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILL-SSLEKPHLKLADFGFAQHMS 165
Cdd:cd14040    88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTACGEIKITDFGLSKIMD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 pwDEKHVLRGSPL---------YMAPE--MVCRR--QYDARVDLWSVGVILYEALFGQPPFASRSFSE---LEEKIRSNR 229
Cdd:cd14040   168 --DDSYGVDGMDLtsqgagtywYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdilQENTILKAT 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 230 VIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVdLEHMPSGES 280
Cdd:cd14040   246 EVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL-LPHMRRSNS 295
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
20-270 3.12e-28

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: 113.41  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCV--AKKSLNKAsvenlLTEIEILKGIRH------PHIVQLKD-FQWDN------ 84
Cdd:cd14210    21 LGKGSFGQVVKCLDHK-TGQLVAIKIIrnKKRFHQQA-----LVEVKILKHLNDndpddkHNIVRYKDsFIFRGhlcivf 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 ----DNIYlimefcaggDLSRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFG- 159
Cdd:cd14210    95 ellsINLY---------ELLKSNNFQG-LSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFGs 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 160 --FAQHMSpwdekHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKI------------ 225
Cdd:cd14210   165 scFEGEKV-----YTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACImevlgvppksli 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 226 ----RSNRVIELPLRPQLSLDCR-----------------------DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14210   240 dkasRRKKFFDSNGKPRPTTNSKgkkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
20-275 3.41e-28

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: 114.95  E-value: 3.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVyKAYAKKDTREVVAIKCVAKKSL-NKASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIMEFCAGG 97
Cdd:cd05629     9 IGKGAFGEV-RLVQKKDTGKIYAMKTLLKSEMfKKDQLAHVKAERDVLAESDSPWVVSLyYSFQ-DAQYLYLIMEFLPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA-----QH--------- 163
Cdd:cd05629    87 DLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDR--GGHIKLSDFGLStgfhkQHdsayyqkll 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 -----------------------MSPWDEKHVLR-----------GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFG 209
Cdd:cd05629   165 qgksnknridnrnsvavdsinltMSSKDQIATWKknrrlmaystvGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIG 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 210 QPPFASRSFSELEEKIRSNR-VIELPLRPQLSLDCRDLLQRLLERDPAR--RISFKDFFAHPW---VDLEHM 275
Cdd:cd05629   245 WPPFCSENSHETYRKIINWReTLYFPDDIHLSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFfrgVDWDTI 316
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
7-260 3.90e-28

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 117.92  E-value: 3.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402    7 GLPRLDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD--FQWDN 84
Cdd:PTZ00266     8 GESRLNEYEVIKKIGNGRFGEVFLVKHKR-TQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDrfLNKAN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   85 DNIYLIMEFCAGGDLSRFIhtrrilpEKVARVF-----------MQQLASALQFLH--------ERnISHLDLKPQNILL 145
Cdd:PTZ00266    87 QKLYILMEFCDAGDLSRNI-------QKCYKMFgkieehaivdiTRQLLHALAYCHnlkdgpngER-VLHRDLKPQNIFL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  146 SS---------------LEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCR--RQYDARVDLWSVGVILYEALF 208
Cdd:PTZ00266   159 STgirhigkitaqannlNGRPIAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHetKSYDDKSDMWALGCIIYELCS 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907200402  209 GQPPF-ASRSFSELEEKIRsnRVIELPLRPQlSLDCRDLLQRLLERDPARRIS 260
Cdd:PTZ00266   239 GKTPFhKANNFSQLISELK--RGPDLPIKGK-SKELNILIKNLLNLSAKERPS 288
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
18-263 5.19e-28

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: 111.38  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKkDTREVVAIK-CvaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd05041     1 EKIGRGNFGDVYRGVLK-PDNTEVAVKtC--RETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRR-ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGfaqhMSPWDEKHV--- 172
Cdd:cd05041    78 GSLLTFLRKKGaRLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVG--ENNVLKISDFG----MSREEEDGEytv 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 ---LRGSPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNrvIELPlRPQLS-LDCRDL 246
Cdd:cd05041   152 sdgLKQIPIkWTAPEALNYGRYTSESDVWSFGILLWEIFsLGATPYPGMSNQQTREQIESG--YRMP-APELCpEAVYRL 228
                         250
                  ....*....|....*..
gi 1907200402 247 LQRLLERDPARRISFKD 263
Cdd:cd05041   229 MLQCWAYDPENRPSFSE 245
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
19-269 6.14e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 111.49  E-value: 6.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNkasvenlltEIE-----ILKGirHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:PHA03390   23 KLIDGKFGKVS-VLKHKPTQKLFVQKIIKAKNFN---------AIEpmvhqLMKD--NPNFIKLYYSVTTLKGHVLIMDY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMspwDEKHVL 173
Cdd:PHA03390   91 IKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR-AKDRIYLCDYGLCKII---GTPSCY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELE----EKIRSNRvieLPLRPQLSLDCRDLLQR 249
Cdd:PHA03390  167 DGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDleslLKRQQKK---LPFIKNVSKNANDFVQS 243
                         250       260
                  ....*....|....*....|.
gi 1907200402 250 LLERDPARR-ISFKDFFAHPW 269
Cdd:PHA03390  244 MLKYNINYRlTNYNEIIKHPF 264
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
11-275 7.94e-28

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: 113.61  E-value: 7.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIY 88
Cdd:cd05627     1 LDDFESLKVIGRGAFGEV-RLVQKKDTGHIYAMKILRKADmLEKEQVAHIRAERDILVEADGAWVVKMfYSFQ-DKRNLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA------- 161
Cdd:cd05627    79 LIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDA--KGHVKLSDFGLCtglkkah 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 ------------------QHMSP------WDEK-----HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPP 212
Cdd:cd05627   157 rtefyrnlthnppsdfsfQNMNSkrkaetWKKNrrqlaYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 213 FASRSFSELEEKIRSNR-VIELPLRPQLSLDCRDLLQRLLErDPARRI---SFKDFFAHPW---VDLEHM 275
Cdd:cd05627   237 FCSETPQETYRKVMNWKeTLVFPPEVPISEKAKDLILRFCT-DAENRIgsnGVEEIKSHPFfegVDWEHI 305
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
11-267 1.09e-27

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: 111.50  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKDTREVvAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQL---------KDFQ 81
Cdd:cd14048     5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNY-AVKRIRLPN-NELAREKVLREVRALAKLDHPGIVRYfnawlerppEGWQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  82 WDNDNIYL--IMEFCAGGDLSRFIHTRRILPEK---VARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLA 156
Cdd:cd14048    83 EKMDEVYLyiQMQLCRKENLKDWMNRRCTMESRelfVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDV--VKVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 157 DFGFAQHM------------SPWDEKHVLR-GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFgqppfasrSFSELEE 223
Cdd:cd14048   161 DFGLVTAMdqgepeqtvltpMPAYAKHTGQvGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY--------SFSTQME 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 224 KIRS---NRVIELPLRPQLSLDC-RDLLQRLLERDPARRISFKDFFAH 267
Cdd:cd14048   233 RIRTltdVRKLKFPALFTNKYPEeRDMVQQMLSPSPSERPEAHEVIEH 280
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
11-276 1.36e-27

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 111.45  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKA-RDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCaGGDLSRFIHTRRILPE--KVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMspwd 168
Cdd:PLN00009   80 FEYL-DLDLKKHMDSSPDFAKnpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDR-RTNALKLADFGLARAF---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 ekhvlrGSPL-----------YMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRVIELP-- 234
Cdd:PLN00009  154 ------GIPVrtfthevvtlwYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGD--SEIDELFKIFRILGTPne 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 235 --------------------------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV-DLEHMP 276
Cdd:PLN00009  226 etwpgvtslpdyksafpkwppkdlatVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFkDLGDAP 294
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
4-271 1.72e-27

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: 111.48  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   4 PSWGLPrlDGFILTERLGSGTYATVYKAYaKKDTREVVAIKC---VAKKSLNKasvenlltEIEILKGIR-HPHIVQLKD 79
Cdd:cd14132    12 VEWGSQ--DDYEIIRKIGRGKYSEVFEGI-NIGNNEKVVIKVlkpVKKKKIKR--------EIKILQNLRgGPNIVKLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  80 -FQWDNDNIY-LIMEFCAGGDLSRFIHTrriLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLAD 157
Cdd:cd14132    81 vVKDPQSKTPsLIFEYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDH-EKRKLRLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 158 FGFAQHMSPWDEKHVLRGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPF-----------------ASRSFS 219
Cdd:cd14132   157 WGLAEFYHPGQEYNVRVASRYYKGPElLVDYQYYDYSLDMWSLGCMLASMIFRKEPFfhghdnydqlvkiakvlGTDDLY 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 220 ELEEKIRsnrvIELPLRPQLSLDCR----------------------DLLQRLLERDPARRISFKDFFAHPWVD 271
Cdd:cd14132   237 AYLDKYG----IELPPRLNDILGRHskkpwerfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHPYFD 306
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
20-271 1.86e-27

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 113.98  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKkDTREVVAIKcvakKSLNKASVENllTEIEILKGIRHPHIVQLKDFQW------DNDNIYL--IM 91
Cdd:PTZ00036   74 IGNGSFGVVYEAICI-DTSEKVAIK----KVLQDPQYKN--RELLIMKNLNHINIIFLKDYYYtecfkkNEKNIFLnvVM 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EF---CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPH-LKLADFGFAQHMSPW 167
Cdd:PTZ00036  147 EFipqTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDP--NTHtLKLCDFGSAKNLLAG 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLRGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRVIELPLRPQLSL----- 241
Cdd:PTZ00036  225 QRSVSYICSRFYRAPElMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQ--SSVDQLVRIIQVLGTPTEDQLKEmnpny 302
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 242 -----------------------DCRDLLQRLLERDPARRISFKDFFAHPWVD 271
Cdd:PTZ00036  303 adikfpdvkpkdlkkvfpkgtpdDAINFISQFLKYEPLKRLNPIEALADPFFD 355
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
15-260 1.88e-27

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: 110.50  E-value: 1.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTER-LGSGTYATVYKAYAKKDTREvvaikCVAKKSL--NKASVENLLTEIEILKGI-RHPHIVQLKDFQ-WDNDN--- 86
Cdd:cd13985     2 YQVTKqLGEGGFSYVYLAHDVNTGRR-----YALKRMYfnDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAiLSSEGrke 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCaGGDLSRFIHTR---RILPEKVARVFmQQLASALQFLHERN--ISHLDLKPQNILLSSLEKphLKLADFGFA 161
Cdd:cd13985    77 VLLLMEYC-PGSLVDILEKSppsPLSEEEVLRIF-YQICQAVGHLHSQSppIIHRDIKIENILFSNTGR--FKLCDFGSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 ----------QHMSPWDEKHVLRGSPLYMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPPFasrsfsELEEKIR-S 227
Cdd:cd13985   153 ttehypleraEEVNIIEEEIQKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPF------DESSKLAiV 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 228 NRVIELPLRPQLSLDCRDLLQRLLERDPARRIS 260
Cdd:cd13985   227 AGKYSIPEQPRYSPELHDLIRHMLTPDPAERPD 259
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
20-268 2.24e-27

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: 110.86  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd07848     9 VGEGAYGVVLKC-RHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNML 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFI-HTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDEKHVLR--GS 176
Cdd:cd07848    88 ELLEeMPNGVPPEKV-RSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV--LKLCDFGFARNLSEGSNANYTEyvAT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRVI-ELP---------------LR---- 236
Cdd:cd07848   165 RWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGE--SEIDQLFTIQKVLgPLPaeqmklfysnprfhgLRfpav 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907200402 237 --PQlSLDCR----------DLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd07848   243 nhPQ-SLERRylgilsgvllDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
20-213 3.00e-27

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 110.39  E-value: 3.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWD-----NDNIYLIMEFC 94
Cdd:cd14039     1 LGTGGFGNVC-LYQNQETGEKIAIK-SCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEmnflvNDVPLLAMEYC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRI---LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLE-KPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14039    79 SGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgKIVHKIIDLGYAKDLDQGSLC 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14039   159 TSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
12-269 3.57e-27

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: 112.41  E-value: 3.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVykAYAK-KDTREVVAIKCVAK-KSLNKASVENLLTEIEILKGIRHPHIVQLK-DFQwDNDNIY 88
Cdd:cd05624    72 DDFEIIKVIGRGAFGEV--AVVKmKNTERIYAMKILNKwEMLKRAETACFREERNVLVNGDCQWITTLHyAFQ-DENYLY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDL----SRFihtRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHM 164
Cdd:cd05624   149 LVMDYYVGGDLltllSKF---EDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDM--NGHIRLADFGSCLKM 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 SPwD---EKHVLRGSPLYMAPEMVCRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPL 235
Cdd:cd05624   224 ND-DgtvQSSVAVGTPDYISPEILQAMEdgmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEErFQFPS 302
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907200402 236 R-PQLSLDCRDLLQRLL-ERDpaRRI---SFKDFFAHPW 269
Cdd:cd05624   303 HvTDVSEEAKDLIQRLIcSRE--RRLgqnGIEDFKKHAF 339
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
20-270 3.74e-27

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 110.16  E-value: 3.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSlNKASVENLLTEIEI-LKGIRHPHIVQLKDFQWDNDNIYLIMEF---CA 95
Cdd:cd06618    23 IGSGTCGQVYKMRHKK-TGHVMAVKQMRRSG-NKEENKRILMDLDVvLKSHDCPYIVKCYGYFITDSDVFICMELmstCL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTrriLPEKVARVFMQQLASALQFLHER-NISHLDLKPQNILLSslEKPHLKLADFGFAQHMSpwDEKHVLR 174
Cdd:cd06618   101 DKLLKRIQGP---IPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLD--ESGNVKLCDFGISGRLV--DSKAKTR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 --GSPLYMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPPFASRSfSELE--EKIRSNRVIELPLRPQLSLDCRDLL 247
Cdd:cd06618   174 saGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYRNCK-TEFEvlTKILNEEPPSLPPNEGFSPDFCSFV 252
                         250       260
                  ....*....|....*....|...
gi 1907200402 248 QRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06618   253 DLCLTKDHRYRPKYRELLQHPFI 275
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
4-262 3.74e-27

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: 110.20  E-value: 3.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   4 PSWGLPRlDGFILTERLGSGTYATVYKAYA-----KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQL 77
Cdd:cd05053     5 PEWELPR-DRLTLGKPLGEGAFGQVVKAEAvgldnKPNEVVTVAVKML-KDDATEKDLSDLVSEMEMMKMIgKHKNIINL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  78 KDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVARV----------------FMQQLASALQFLHERNISHLDLKPQ 141
Cdd:cd05053    83 LGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDdprvpeeqltqkdlvsFAYQVARGMEYLASKKCIHRDLAAR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 142 NILLSslEKPHLKLADFGFAQ--HMSPWDEKHVLRGSPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRS 217
Cdd:cd05053   163 NVLVT--EDNVMKIADFGLARdiHHIDYYRKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 218 FSELEEKIRSNRVIElplRPQL-SLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05053   241 VEELFKLLKEGHRME---KPQNcTQELYMLMRDCWHEVPSQRPTFK 283
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
12-270 3.80e-27

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: 109.94  E-value: 3.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYaKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVL-HRPTGVTMAMKEI-RLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFI---HTRRILPEKVARVFMQQLASALQFLHER-NISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPW 167
Cdd:cd06622    79 EYMDAGSLDKLYaggVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNG--NGQVKLCDFGVSGNLVAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLrGSPLYMAPE------MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSnrVIELP---LRPQ 238
Cdd:cd06622   157 LAKTNI-GCQSYMAPEriksggPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSA--IVDGDpptLPSG 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06622   234 YSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
12-270 3.80e-27

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: 109.16  E-value: 3.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVVaikCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDfQWDNDNI-YLI 90
Cdd:cd14112     3 GRFSFGSEIFRGRFSVIVKAVDSTTETDAH---CAVKIFEVSDEASEAVREFESLRTLQHENVQRLIA-AFKPSNFaYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14112    79 MEKLQEDVFTRFSSNDYYSEEQVATT-VRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKLGKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVlRGSPLYMAPEMVCRRQY-DARVDLWSVGVILYEALFGQPPFasRSFSELEEKIRSNrVIELPLRPQL-----SLDCR 244
Cdd:cd14112   158 PV-DGDTDWASPEFHNPETPiTVQSDIWGLGVLTFCLLSGFHPF--TSEYDDEEETKEN-VIFVKCRPNLifveaTQEAL 233
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14112   234 RFATWALKKSPTRRMRTDEALEHRWL 259
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
6-262 4.88e-27

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: 109.06  E-value: 4.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRLDgFILTERLGSGTYATVYKAYAKKDTRevVAIKCVakKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDND 85
Cdd:cd05148     1 WERPREE-FTLERKLGSGYFGEVWEGLWKNRVR--VAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:cd05148    76 PVYIITELMEKGSLLAFLRSPegQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVG--EDLVCKVADFGLARL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 M-----SPWDEKHVLRgsplYMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLR- 236
Cdd:cd05148   154 IkedvyLSSDKKIPYK----WTAPEAASHGTFSTKSDVWSFGILLYEMFtYGQVPYPGMNNHEVYDQITAGYRMPCPAKc 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907200402 237 PQ----LSLDCrdllqrlLERDPARRISFK 262
Cdd:cd05148   230 PQeiykIMLEC-------WAAEPEDRPSFK 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
19-287 5.12e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 111.07  E-value: 5.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKDTREVvAIKCVAKKslNKASVENLLT-EIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:PLN00034   81 RIGSGAGGTVYKVIHRPTGRLY-ALKVIYGN--HEDTVRRQICrEIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGG 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLS-RFIHTRRILPEkVARvfmqQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFG----FAQHMSPWDEKhv 172
Cdd:PLN00034  158 SLEgTHIADEQFLAD-VAR----QILSGIAYLHRRHIVHRDIKPSNLLINS--AKNVKIADFGvsriLAQTMDPCNSS-- 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 lRGSPLYMAPEMV----CRRQYDARV-DLWSVGVILYEALFGQPPFA-SRS--FSELEEKIRSNRVIELPlrPQLSLDCR 244
Cdd:PLN00034  229 -VGTIAYMSPERIntdlNHGAYDGYAgDIWSLGVSILEFYLGRFPFGvGRQgdWASLMCAICMSQPPEAP--ATASREFR 305
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQARAL 287
Cdd:PLN00034  306 HFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQL 348
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-261 6.67e-27

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: 108.59  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKA-YAKKDTREV-VAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQwDNDNIYLIMEFCA 95
Cdd:cd05060     1 KELGHGNFGSVRKGvYLMKSGKEVeVAVK-TLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVC-KGEPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRG 175
Cdd:cd05060    79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVN--RHQAKISDFGMSRALGAGSDYYRATT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 S---PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQRL 250
Cdd:cd05060   157 AgrwPLkWYAPECINYGKFSSKSDVWSYGVTLWEAFsYGAKPYGEMKGPEVIAMLESGERLPRP--EECPQEIYSIMLSC 234
                         250
                  ....*....|.
gi 1907200402 251 LERDPARRISF 261
Cdd:cd05060   235 WKYRPEDRPTF 245
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
14-276 8.06e-27

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: 109.74  E-value: 8.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAyAKKDTREVVAIKcvaKKSLNKASV----ENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd06633    23 FVDLHEIGHGSFGAVYFA-TNSHTNEVVAIK---KMSYSGKQTnekwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAG--GDLSRfIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPW 167
Cdd:cd06633    99 VMEYCLGsaSDLLE-VHKKPLQEVEIAAITHGAL-QGLAYLHSHNMIHRDIKAGNILLT--EPGQVKLADFGSASIASPA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEkhvLRGSPLYMAPEMVC---RRQYDARVDLWSVGVILYEALFGQPP-FASRSFSELEEkIRSNRVIELPlRPQLSLDC 243
Cdd:cd06633   175 NS---FVGTPYWMAPEVILamdEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSALYH-IAQNDSPTLQ-SNEWTDSF 249
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 244 RDLLQRLLERDPARRISFKDFFAHPWVDLEHMP 276
Cdd:cd06633   250 RGFVDYCLQKIPQERPSSAELLRHDFVRRERPP 282
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
20-243 8.19e-27

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: 108.49  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREV-VAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFqWDNDNIYLIMEFCAGGD 98
Cdd:cd05115    12 LGSGNFGCVKKGVYKMRKKQIdVAIK-VLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGV-CEAEALMLVMEMASGGP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRR--ILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLssLEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05115    90 LNKFLSGKKdeITVSNVVEL-MHQVSMGMKYLEEKNFVHRDLAARNVLL--VNQHYAKISDFGLSKALGADDSYYKARSA 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 177 ---PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLR-P----QLSLDC 243
Cdd:cd05115   167 gkwPLkWYAPECINFRKFSSRSDVWSYGVTMWEAFsYGQKPYKKMKGPEVMSFIEQGKRMDCPAEcPpemyALMSDC 243
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
20-259 1.04e-26

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: 108.96  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05630     8 LGKGGFGEVC-ACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIH--TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMsPWDEKHVLR-G 175
Cdd:cd05630    87 LKFHIYhmGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLD--DHGHIRISDLGLAVHV-PEGQTIKGRvG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFS-ELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd05630   164 TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKiKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKD 243

                  ....*
gi 1907200402 255 PARRI 259
Cdd:cd05630   244 PAERL 248
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
12-269 1.20e-26

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: 107.68  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVenlLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd14108     2 DYYDIHKEIGRGAFSYL-RRVKEKSSDLSFAAKFIPVRAKKKTSA---RRELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRfIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKH 171
Cdd:cd14108    78 ELCHEELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELTPNEPQY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRS-NRVIELPLRPQLSLDCRDLLQRL 250
Cdd:cd14108   157 CKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNyNVAFEESMFKDLCREAKGFIIKV 236
                         250
                  ....*....|....*....
gi 1907200402 251 LERDPARRISfKDFFAHPW 269
Cdd:cd14108   237 LVSDRLRPDA-EETLEHPW 254
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
18-269 1.21e-26

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: 108.61  E-value: 1.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd07847     7 SKIGEGSYGVVFKC-RNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHV-LRGS 176
Cdd:cd07847    86 VLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT--KQGQIKLCDFGFARILTGPGDDYTdYVAT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEM-VCRRQYDARVDLWSVGVILYEALFGQPPFASRS-----------FSELE---EKIRSN------------- 228
Cdd:cd07847   164 RWYRAPELlVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSdvdqlylirktLGDLIprhQQIFSTnqffkglsipepe 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907200402 229 RVIELPLR-PQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07847   244 TREPLESKfPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
20-269 1.30e-26

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: 108.29  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILK----GIRHPHIVQLK-DFQwDNDNIYLIMEF 93
Cdd:cd05606     2 IGRGGFGEVYGC-RKADTGKMYAMKCLDKKRIKMKQGETLaLNERIMLSlvstGGDCPFIVCMTyAFQ-TPDKLCFILDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHVL 173
Cdd:cd05606    80 MNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLD--EHGHVRISDLGLACDFSK-KKPHAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCRRQ-YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLE 252
Cdd:cd05606   157 VGTHGYMAPEVLQKGVaYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236
                         250       260
                  ....*....|....*....|..
gi 1907200402 253 RDPARRI-----SFKDFFAHPW 269
Cdd:cd05606   237 RDVSKRLgclgrGATEVKEHPF 258
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
20-294 1.42e-26

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: 109.74  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD-------FQWDNDnIYLIME 92
Cdd:cd07877    25 VGSGAYGSVCAAFDTK-TGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDvftparsLEEFND-VYLVTH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FcAGGDLSRFIHTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSpwDEKHV 172
Cdd:cd07877   103 L-MGADLNNIVKCQKLTDDHV-QFLIYQILRGLKYIHSADIIHRDLKPSNLAVN--EDCELKILDFGLARHTD--DEMTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELEEKIRS----NRVIE 232
Cdd:cd07877   177 YVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHidqlklilrlvgtpgAELLKKISSesarNYIQS 256
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200402 233 LPLRPQLSLD---------CRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLA-------QARALVVEAVKK 294
Cdd:cd07877   257 LTQMPKMNFAnvfiganplAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVAdpydqsfESRDLLIDEWKS 334
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
6-297 1.45e-26

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: 109.75  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLP-RLDGfiLTErLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDF---- 80
Cdd:cd07878    11 WEVPeRYQN--LTP-VGSGAYGSVCSAYDTR-LRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVftpa 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 --QWDNDNIYLIMEFcAGGDLSRFIHTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADF 158
Cdd:cd07878    87 tsIENFNEVYLVTNL-MGADLNNIVKCQKLSDEHV-QFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVN--EDCELRILDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 159 GFAQHMSpwDEKHVLRGSPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELE 222
Cdd:cd07878   163 GLARQAD--DEMTGYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYidqlkrimevvgtpsPEVL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 223 EKIRSN---RVIE-LPLRPQLSLD---------CRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQARALVV 289
Cdd:cd07878   241 KKISSEharKYIQsLPHMPQQDLKkifrganplAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPEDEPEAEPYDESP 320

                  ....*...
gi 1907200402 290 EAVKKDQE 297
Cdd:cd07878   321 ENKERTIE 328
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
5-261 1.62e-26

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: 107.82  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQWDN 84
Cdd:cd05072     1 AWEIPR-ESIKLVKKLGAGQFGEVWMGYYNNSTK--VAVKTLKPGTM---SVQAFLEEANLMKTLQHDKLVRLYAVVTKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHT----RRILPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF 160
Cdd:cd05072    75 EPIYIITEYMAKGSLLDFLKSdeggKVLLPKLID--FSAQIAEGMAYIERKNYIHRDLRAANVLVS--ESLMCKIADFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSpwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRsnRVIELPL 235
Cdd:cd05072   151 ARVIE--DNEYTAREGakfPIkWTAPEAINFGSFTIKSDVWSFGILLYEIVtYGKIPYPGMSNSDVMSALQ--RGYRMPR 226
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 236 RPQLSLDCRDLLQRLLERDPARRISF 261
Cdd:cd05072   227 MENCPDELYDIMKTCWKEKAEERPTF 252
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
20-267 1.66e-26

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: 106.81  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdtrEVVAIKCVAKKSLnkasvenllTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14059     1 LGSGAQGAVFLGKFRG---EEVAVKKVRDEKE---------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDEKHVLRGSPLY 179
Cdd:cd14059    69 YEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV--LKISDFGTSKELSEKSTKMSFAGTVAW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 180 MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLrPQlslDCRDLLQRLLER----DP 255
Cdd:cd14059   147 MAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNS-LQLPV-PS---TCPDGFKLLMKQcwnsKP 221
                         250
                  ....*....|..
gi 1907200402 256 ARRISFKDFFAH 267
Cdd:cd14059   222 RNRPSFRQILMH 233
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
19-269 1.69e-26

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 108.61  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD--------FQWDNDNIYLI 90
Cdd:cd07865    19 KIGQGTFGEVFKARHRK-TGQIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEicrtkatpYNRYKGSIYLV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGgDLSRFIHTRRI---LPEKvaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS-- 165
Cdd:cd07865    98 FEFCEH-DLAGLLSNKNVkftLSEI--KKVMKMLLNGLYYIHRNKILHRDMKAANILIT--KDGVLKLADFGLARAFSla 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 --PWDEKHVLRGSPL-YMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRS-------FSELEEKIRSN------ 228
Cdd:cd07865   173 knSQPNRYTNRVVTLwYRPPELLLgERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTeqhqltlISQLCGSITPEvwpgvd 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 229 -----RVIELP----------LRPQLS-LDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07865   253 klelfKKMELPqgqkrkvkerLKPYVKdPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
20-283 1.70e-26

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: 109.48  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKslNKASVENLLTEIEILKGIRHPHIVQLKDFQWDN--------------D 85
Cdd:cd07854    13 LGCGSNGLVFSA-VDSDCDKRVAVKKIVLT--DPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSgsdltedvgsltelN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEfCAGGDLSRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMS 165
Cdd:cd07854    90 SVYIVQE-YMETDLANVLEQGP-LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINT-EDLVLKIGDFGLARIVD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 P-WDEK-HVLRG--SPLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEK---------IRSNRVI 231
Cdd:cd07854   167 PhYSHKgYLSEGlvTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPLFAGA--HELEQMqlilesvpvVREEDRN 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 232 EL-----------------PLR---PQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQ 283
Cdd:cd07854   245 ELlnvipsfvrndggeprrPLRdllPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCYSCPFDEPVSL 316
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
23-270 1.75e-26

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: 107.31  E-value: 1.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  23 GTYATVYKAYAKKDTReVVAIKCVAKKSLNKASVenlLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRF 102
Cdd:cd14110    14 GRFSVVRQCEEKRSGQ-MLAAKIIPYKPEDKQLV---LREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 103 IHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwdEKHVLRGSPLY--- 179
Cdd:cd14110    90 LAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIIT--EKNLLKIVDLGNAQPFNQ--GKVLMTDKKGDyve 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 180 -MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPARR 258
Cdd:cd14110   166 tMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCYAGLSGGAVNFLKSTLCAKPWGR 245
                         250
                  ....*....|..
gi 1907200402 259 ISFKDFFAHPWV 270
Cdd:cd14110   246 PTASECLQNPWL 257
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
20-268 2.09e-26

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 111.50  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTrEVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQL-KDFQWDNDN-------IYLIM 91
Cdd:PTZ00283   40 LGSGATGTVLCAKRVSDG-EPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKChEDFAKKDPRnpenvlmIALVL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTR----RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPW 167
Cdd:PTZ00283  119 DYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS--NGLVKLGDFGFSKMYAAT 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLR---GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCR 244
Cdd:PTZ00283  197 VSDDVGRtfcGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLP--PSISPEMQ 274
                         250       260
                  ....*....|....*....|....
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHP 268
Cdd:PTZ00283  275 EIVTALLSSDPKRRPSSSKLLNMP 298
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
6-263 2.17e-26

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 107.81  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCvAKKSLNKASVE----NLLTEIEILKGIRHPHIVQLKDFQ 81
Cdd:cd05032     1 WELPR-EKITLIRELGQGSFGMVYEGLAKGVVKGEPETRV-AIKTVNENASMreriEFLNEASVMKEFNCHHVVRLLGVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  82 WDNDNIYLIMEFCAGGDLSRFIHTRRilPEKV---------ARVFMQ---QLASALQFLHERNISHLDLKPQNILLSSLE 149
Cdd:cd05032    79 STGQPTLVVMELMAKGDLKSYLRSRR--PEAEnnpglgpptLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 150 KphLKLADFGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEKI 225
Cdd:cd05032   157 T--VKIGDFGMTRDIYETDYYRKGGKGLLpvrWMAPESLKDGVFTTKSDVWSFGVVLWEmATLAEQPYQGLSNEEVLKFV 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907200402 226 RSNRVIELPLR-PQLsldCRDLLQRLLERDPARRISFKD 263
Cdd:cd05032   235 IDGGHLDLPENcPDK---LLELMRMCWQYNPKMRPTFLE 270
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
14-270 2.21e-26

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: 107.84  E-value: 2.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVakkSLNKAS--VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd06642     6 FTKLERIGKGSFGEVYKGIDNR-TKEVVAIKII---DLEEAEdeIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWD-EK 170
Cdd:cd06642    82 EYLGGGSALDLLKPGP-LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLS--EQGDVKLADFGVAGQLTDTQiKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRviELPLRPQLSLDCRDLLQRL 250
Cdd:cd06642   159 NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNS--PPTLEGQHSKPFKEFVEAC 236
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd06642   237 LNKDPRFRPTAKELLKHKFI 256
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
14-263 3.06e-26

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: 107.38  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDtREVVAIK---CVAKKSLNKAsvenlLTEIEILKGIRHPHIVQLKDFQ-----WDND 85
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLST-GRLYALKkilCHSKEDVKEA-----MREIENYRLFNHPNILRLLDSQivkeaGGKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTRRI----LPEKVARVFMQQLASALQFLHE---RNISHLDLKPQNILLSSLEKPhlKLADF 158
Cdd:cd13986    76 EVYLLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEP--ILMDL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 159 G-------------FAQHMSPWDEKHvlrGSPLYMAPEMVCRRQY---DARVDLWSVGVILYEALFGQPPFasrsfsELE 222
Cdd:cd13986   154 GsmnparieiegrrEALALQDWAAEH---CTMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPF------ERI 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 223 EK-------IRSNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKD 263
Cdd:cd13986   225 FQkgdslalAVLSGNYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDD 272
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
6-262 3.62e-26

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: 106.67  E-value: 3.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRLDgFILTERLGSGTYATVYKAYAKKDTrevVAIKCVaKKSLNKAsvENLLTEIEILKGIRHPHIVQLKDFQWDND 85
Cdd:cd05039     1 WAINKKD-LKLGELIGKGEFGDVMLGDYRGQK---VAVKCL-KDDSTAA--QAFLAEASVMTTLRHPNLVQLLGVVLEGN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTR-RILPEKVARV-FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQh 163
Cdd:cd05039    74 GLYIVTEYMAKGSLVDYLRSRgRAVITRKDQLgFALDVCEGMEYLESKKFVHRDLAARNVLVS--EDNVAKVSDFGLAK- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 mspwDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLR-P- 237
Cdd:cd05039   151 ----EASSNQDGGKLpikWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPHVEKGYRMEAPEGcPp 226
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 238 ---QLSLDCRDLlqrllerDPARRISFK 262
Cdd:cd05039   227 evyKVMKNCWEL-------DPAKRPTFK 247
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
14-261 4.97e-26

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: 106.67  E-value: 4.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKaSVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14145     8 LVLEEIIGIGGFGKVYRAIWIGDEVAVKAARHDPDEDISQ-TIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARvFMQQLASALQFLHERNIS---HLDLKPQNILL------SSLEKPHLKLADFGFAQHm 164
Cdd:cd14145    87 ARGGPLNRVLSGKRIPPDILVN-WAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvenGDLSNKILKITDFGLARE- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 spWDE--KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLrPQlslD 242
Cdd:cd14145   165 --WHRttKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNK-LSLPI-PS---T 237
                         250       260
                  ....*....|....*....|...
gi 1907200402 243 CRDLLQRLLER----DPARRISF 261
Cdd:cd14145   238 CPEPFARLMEDcwnpDPHSRPPF 260
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-270 5.03e-26

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 106.21  E-value: 5.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNK----ASVENLLTEIEILK--GIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14100     8 LGSGGFGSVYSGIRVADGAPV-AIKHVEKDRVSEwgelPNGTRVPMEIVLLKkvGSGFRGVIRLLDWFERPDSFVLVLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAG-GDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLsSLEKPHLKLADFGFAQHMSpwDEKHV 172
Cdd:cd14100    87 PEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI-DLNTGELKLIDFGSGALLK--DTVYT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 -LRGSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFasrsfsELEEKIRSNRVIelpLRPQLSLDCRDLLQRL 250
Cdd:cd14100   164 dFDGTRVYSPPEWIRFHRYHGRsAAVWSLGILLYDMVCGDIPF------EHDEEIIRGQVF---FRQRVSSECQHLIKWC 234
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd14100   235 LALRPSDRPSFEDIQNHPWM 254
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
18-261 7.16e-26

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: 105.44  E-value: 7.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTK--VAVKTLKPGTM---SPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHT--RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQhMSPWDEKHVLRG 175
Cdd:cd05034    76 SLLDYLRTgeGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVG--ENNVCKVADFGLAR-LIEDDEYTAREG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 S--PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKI-RSNRvieLPlRPQlslDCRDLLQRL 250
Cdd:cd05034   153 AkfPIkWTAPEAALYGRFTIKSDVWSFGILLYEIVtYGRVPYPGMTNREVLEQVeRGYR---MP-KPP---GCPDELYDI 225
                         250
                  ....*....|....*
gi 1907200402 251 L----ERDPARRISF 261
Cdd:cd05034   226 MlqcwKKEPEERPTF 240
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
20-261 7.55e-26

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: 106.00  E-value: 7.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd13978     1 LGSGGFGTVSKAR-HVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRI-LPEKVARVFMQQLASALQFLH--ERNISHLDLKPQNILLSslEKPHLKLADFGFAQ------HMSPWDEK 170
Cdd:cd13978    80 KSLLEREIQdVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLD--NHFHVKISDFGLSKlgmksiSANRRRGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQY--DARVDLWSVGVILYEALFGQPPFASRSFSELE--EKIRSNRvielPLRPQLSLDCRD- 245
Cdd:cd13978   158 ENLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAINPLLImqIVSKGDR----PSLDDIGRLKQIe 233
                         250       260
                  ....*....|....*....|...
gi 1907200402 246 -------LLQRLLERDPARRISF 261
Cdd:cd13978   234 nvqelisLMIRCWDGNPDARPTF 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
16-251 7.65e-26

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: 105.90  E-value: 7.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTREVvAIKCVA---KKSLNKASVENLLTEIEILKGIRHPHIVQ----LKDFQWDNDNIY 88
Cdd:cd06652     6 LGKLLGQGAFGRVYLCYDADTGREL-AVKQVQfdpESPETSKEVNALECEIQLLKNLLHERIVQyygcLRDPQERTLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 liMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHM---- 164
Cdd:cd06652    85 --MEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVG--NVKLGDFGASKRLqtic 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 -SPWDEKHVlRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfsELEEKIRSNRVIELPLRPQL---- 239
Cdd:cd06652   161 lSGTGMKSV-TGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA-----EFEAMAAIFKIATQPTNPQLpahv 234
                         250
                  ....*....|..
gi 1907200402 240 SLDCRDLLQRLL 251
Cdd:cd06652   235 SDHCRDFLKRIF 246
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
16-261 7.98e-26

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: 105.88  E-value: 7.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKdtrEVVAIKCVAKKSLNKASV--ENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14147     7 LEEVIGIGGFGKVYRGSWRG---ELVAVKAARQDPDEDISVtaESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRIlPEKVARVFMQQLASALQFLHERNIS---HLDLKPQNILLS------SLEKPHLKLADFGFAQHm 164
Cdd:cd14147    84 AAGGPLSRALAGRRV-PPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpiendDMEHKTLKITDFGLARE- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 spWDE--KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPL-----RP 237
Cdd:cd14147   162 --WHKttQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNK-LTLPIpstcpEP 238
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 238 --QLSLDCRDllqrlleRDPARRISF 261
Cdd:cd14147   239 faQLMADCWA-------QDPHRRPDF 257
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
14-269 8.86e-26

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 108.56  E-value: 8.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVykAYAK-KDTREVVAIKCVAK-KSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd05623    74 FEILKVIGRGAFGEV--AVVKlKNADKVFAMKILNKwEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDL----SRFihtRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHM--S 165
Cdd:cd05623   152 DYYVGGDLltllSKF---EDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDM--NGHIRLADFGSCLKLmeD 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPEMV-----CRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRV-IELPLR-PQ 238
Cdd:cd05623   227 GTVQSSVAVGTPDYISPEILqamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKErFQFPTQvTD 306
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 239 LSLDCRDLLQRLLERDPAR--RISFKDFFAHPW 269
Cdd:cd05623   307 VSENAKDLIRRLICSREHRlgQNGIEDFKNHPF 339
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
20-261 1.21e-25

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: 105.04  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAK-KDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFqWDNDNIYLIMEFCAGGD 98
Cdd:cd05116     3 LGSGNFGTVKKGYYQmKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGI-CEAESWMLVMEMAELGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLssLEKPHLKLADFGFAQHMSPwDEKHVLRGS-- 176
Cdd:cd05116    82 LNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLL--VTQHYAKISDFGLSKALRA-DENYYKAQThg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 --PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQRLLE 252
Cdd:cd05116   159 kwPVkWYAPECMNYYKFSSKSDVWSFGVLMWEAFsYGQKPYKGMKGNEVTQMIEKGERMECP--AGCPPEMYDLMKLCWT 236

                  ....*....
gi 1907200402 253 RDPARRISF 261
Cdd:cd05116   237 YDVDERPGF 245
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
20-266 1.51e-25

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: 106.04  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKaSVENLLTEIEILKGIRHPHIVQLKDFQWDND--NIYLIMEFCAGG 97
Cdd:cd13988     1 LGQGATANVFRGRHKK-TGDLYAVKVFNNLSFMR-PLDVQMREFEVLKKLNHKNIVKLFAIEEELTtrHKVLVMELCPCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIH---TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLE--KPHLKLADFGFAQHMSPwDEKHV 172
Cdd:cd13988    79 SLYTVLEepsNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEdgQSVYKLTDFGAARELED-DEQFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 -LRGSPLYMAPEMVCR--------RQYDARVDLWSVGVILYEALFGQPPF----ASRSFSELEEKIRSNR---VI----- 231
Cdd:cd13988   158 sLYGTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPFrpfeGPRRNKEVMYKIITGKpsgAIsgvqk 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200402 232 ----------ELPLRPQLSLDCRDL----LQRLLERDPARRISFKDFFA 266
Cdd:cd13988   238 sengpiewsgELPVSCSLSQGLQTLltpvLANILEADQEKCWGFDQFFA 286
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
7-213 1.90e-25

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: 105.84  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   7 GLPRLDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVeNLLTEIEILKGIRHPHIVQLKDFQWDNDN 86
Cdd:cd07872     1 GFGKMETYIKLEKLGEGTYATVFKGRSKL-TENLVALKEIRLEHEEGAPC-TAIREVSLLKDLKHANIVTLHDIVHTDKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCaGGDLSRFIH-TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS 165
Cdd:cd07872    79 LTLVFEYL-DKDLKQYMDdCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLIN--ERGELKLADFGLARAKS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLRGSPLYMAPE--MVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd07872   156 VPTKTYSNEVVTLWYRPPdvLLGSSEYSTQIDMWGVGCIFFEMASGRPLF 205
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
20-269 2.19e-25

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: 104.80  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKsLNKASVENLLTEIEILKGIRHPHIVQLKDfQWDN-----DNIYLIMEFC 94
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAWCELQDRK-LTKAEQQRFKEEAEMLKGLQHPNIVRFYD-SWESvlkgkKCIVLVTELM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14031    96 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG-PTGSVKIGDLGLATLMRTSFAKSV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LrGSPLYMAPEMVcRRQYDARVDLWSVGVILYEALFGQPPfasrsFSELEEKIRSNRVIELPLRPQ-----LSLDCRDLL 247
Cdd:cd14031   175 I-GTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYP-----YSECQNAAQIYRKVTSGIKPAsfnkvTDPEVKEII 247
                         250       260
                  ....*....|....*....|..
gi 1907200402 248 QRLLERDPARRISFKDFFAHPW 269
Cdd:cd14031   248 EGCIRQNKSERLSIKDLLNHAF 269
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
20-250 2.38e-25

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: 106.66  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVyKAYAKKDTREVVAIKCVAKKS-LNKASVENLLTEIEILKGIRHPHIVQL-KDFQwDNDNIYLIMEFCAGG 97
Cdd:cd05628     9 IGRGAFGEV-RLVQKKDTGHVYAMKILRKADmLEKEQVGHIRAERDILVEADSLWVVKMfYSFQ-DKLNLYLIMEFLPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLR--- 174
Cdd:cd05628    87 DMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDS--KGHVKLSDFGLCTGLKKAHRTEFYRnln 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 ---------------------------------GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSEL 221
Cdd:cd05628   165 hslpsdftfqnmnskrkaetwkrnrrqlafstvGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQET 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907200402 222 EEKIRSNR-VIELPLRPQLSLDCRDLLQRL 250
Cdd:cd05628   245 YKKVMNWKeTLIFPPEVPISEKAKDLILRF 274
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
20-270 2.47e-25

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 104.41  E-value: 2.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKslNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd06624    16 LGKGTFGVVYAA-RDLSTQVRIAIKEIPER--DSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTR---RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPhLKLADFGFAQH---MSPWDEkhVL 173
Cdd:cd06624    93 SALLRSKwgpLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGV-VKISDFGTSKRlagINPCTE--TF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGSPLYMAPEMVCR--RQYDARVDLWSVGVILYEALFGQPPFasrsFSELEEKIRSNRV----IELPLRPQLSLDCRDLL 247
Cdd:cd06624   170 TGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPF----IELGEPQAAMFKVgmfkIHPEIPESLSEEAKSFI 245
                         250       260
                  ....*....|....*....|...
gi 1907200402 248 QRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06624   246 LRCFEPDPDKRATASDLLQDPFL 268
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
20-271 3.41e-25

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: 104.44  E-value: 3.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTrevvaiKCVAKKSL---NKASVEN-LLTEIEILKGIRHPHIVQL-KDFQWDNDNIYLIMEFC 94
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTG------TIMAKKVIhidAKSSVRKqILRELQILHECHSPYIVSFyGAFLNENNNIIICMEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLH-ERNISHLDLKPQNILLSSleKPHLKLADFGFAQHM--SPWDekh 171
Cdd:cd06620    87 DCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNS--KGQIKLCDFGVSGELinSIAD--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR-----------SFSELEEKIRSNRVIELPLRPQLS 240
Cdd:cd06620   162 TFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSnddddgyngpmGILDLLQRIVNEPPPRLPKDRIFP 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907200402 241 LDCRDLLQRLLERDPARRISFKDFFAH-PWVD 271
Cdd:cd06620   242 KDLRDFVDRCLLKDPRERPSPQLLLDHdPFIQ 273
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-247 3.57e-25

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: 106.63  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVENLL-TEIEILKGIRHPHIVQL-KDFQwDNDNI 87
Cdd:cd05622    71 KAEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLfYAFQ-DDRYL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTRRIlPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMspw 167
Cdd:cd05622   149 YMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD--KSGHLKLADFGTCMKM--- 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLR-----GSPLYMAPEmVCRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPLR 236
Cdd:cd05622   223 NKEGMVRcdtavGTPDYISPE-VLKSQggdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnSLTFPDD 301
                         250
                  ....*....|.
gi 1907200402 237 PQLSLDCRDLL 247
Cdd:cd05622   302 NDISKEAKNLI 312
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-270 3.71e-25

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: 103.97  E-value: 3.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVenLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd06645    11 EDFELIQRIGSGTYGDVYKA-RNVNTGELAAIKVIKLEPGEDFAV--VQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQHMSPWDEK 170
Cdd:cd06645    88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLT--DNGHVKLADFGVsAQITATIAKR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQ---YDARVDLWSVGVILYEALFGQPP-FASRSFSELEEKIRSN-RVIELPLRPQLSLDCRD 245
Cdd:cd06645   166 KSFIGTPYWMAPEVAAVERkggYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSNfQPPKLKDKMKWSNSFHH 245
                         250       260
                  ....*....|....*....|....*
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06645   246 FVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
12-270 3.97e-25

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 104.69  E-value: 3.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTrEVVAIKCVAKKSLNKASVEnllTEIEILKGI-RHPHIVQL-----KDFQWDND 85
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDG-SLAAVKILDPISDVDEEIE---AEYNILRSLpNHPNVVKFygmfyKADQYVGG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTRRI----LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGF- 160
Cdd:cd06639    98 QLWLVLELCNGGSVTELVKGLLKcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT--EGGVKLVDFGVs 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSPWDEKHVLRGSPLYMAPEMV-CRRQYD----ARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELpL 235
Cdd:cd06639   176 AQLTSARLRRNTSVGTPFWMAPEVIaCEQQYDysydARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTL-L 254
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907200402 236 RPQLSldCRD---LLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06639   255 NPEKW--CRGfshFISQCLIKDFEKRPSVTHLLEHPFI 290
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
11-255 4.68e-25

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 105.09  E-value: 4.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKS--LNKASVEnllteIEILKGI-RHP-----HIVQLKD-FQ 81
Cdd:cd14226    12 MDRYEIDSLIGKGSFGQVVKAYDHV-EQEWVAIKIIKNKKafLNQAQIE-----VRLLELMnKHDtenkyYIVRLKRhFM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  82 WDND----------NIYlimefcaggDLSRFIHTRRILPeKVARVFMQQLASALQFLH--ERNISHLDLKPQNILLSSLE 149
Cdd:cd14226    86 FRNHlclvfellsyNLY---------DLLRNTNFRGVSL-NLTRKFAQQLCTALLFLStpELSIIHCDLKPENILLCNPK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 150 KPHLKLADFGFA----QHMSPWDEkhvlrgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSfseleEKI 225
Cdd:cd14226   156 RSAIKIIDFGSScqlgQRIYQYIQ------SRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGAN-----EVD 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 226 RSNRVIE-LPLRPQLSLDCRDLLQRLLERDP 255
Cdd:cd14226   225 QMNKIVEvLGMPPVHMLDQAPKARKFFEKLP 255
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
18-258 5.28e-25

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: 103.99  E-value: 5.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVvAIKcvaKKSLNKASVEN--LLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14046    12 QVLGKGAFGQVVKVRNKLDGRYY-AIK---KIKLRSESKNNsrILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILP-EKVARVFmQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQ-HM--------- 164
Cdd:cd14046    88 KSTLRDLIDSGLFQDtDRLWRLF-RQILEGLAYIHSQGIIHRDLKPVNIFLDSNG--NVKIGDFGLATsNKlnvelatqd 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 --SPWD------EKHVLR-GSPLYMAPEMVCRRQ--YDARVDLWSVGVILYEALFgqpPFASRSfseleEKIRSNRVIEL 233
Cdd:cd14046   165 inKSTSaalgssGDLTGNvGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMCY---PFSTGM-----ERVQILTALRS 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 234 PlRPQLSLDCRD--------LLQRLLERDPARR 258
Cdd:cd14046   237 V-SIEFPPDFDDnkhskqakLIRWLLNHDPAKR 268
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
6-275 5.61e-25

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 103.27  E-value: 5.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRLDgFILTERLGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNkasVENLLTEIEILKGIRHPHIVQLKDFQWDND 85
Cdd:cd05052     1 WEIERTD-ITMKHKLGGGQYGEVYEGVWKKYNL-TVAVKTLKEDTME---VEEFLKEAAVMKEIKHPNLVQLLGVCTREP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTR-RILPEKVARVFMQ-QLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:cd05052    76 PFYIITEFMPYGNLLDYLRECnREELNAVVLLYMAtQIASAMEYLEKKNFIHRDLAARNCLVG--ENHLVKVADFGLSRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSpwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEKIRSNRVIELPlrPQ 238
Cdd:cd05052   154 MT--GDTYTAHAGakfPIkWTAPESLAYNKFSIKSDVWAFGVLLWEiATYGMSPYPGIDLSQVYELLEKGYRMERP--EG 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFKDFFAhpwvDLEHM 275
Cdd:cd05052   230 CPPKVYELMRACWQWNPSDRPSFAEIHQ----ALETM 262
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-269 6.26e-25

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: 105.47  E-value: 6.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVyKAYAKKDTREVVAIKCVAKKSLNKASVENLL-TEIEILKGIRHPHIVQLKDFQWDNDNIY 88
Cdd:cd05621    50 KAEDYDVVKVIGRGAFGEV-QLVRHKASQKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFCAFQDDKYLY 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRIlPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMspwD 168
Cdd:cd05621   129 MVMEYMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLD--KYGHLKLADFGTCMKM---D 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLR-----GSPLYMAPEmVCRRQ-----YDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNR-VIELPLRP 237
Cdd:cd05621   203 ETGMVHcdtavGTPDYISPE-VLKSQggdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKnSLNFPDDV 281
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 238 QLSLDCRDLLQRLLERDPAR--RISFKDFFAHPW 269
Cdd:cd05621   282 EISKHAKNLICAFLTDREVRlgRNGVEEIKQHPF 315
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
18-261 7.60e-25

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: 102.70  E-value: 7.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCvaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKSC--RETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTR--RILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGfaqhMSPWDEKHV--- 172
Cdd:cd05084    80 DFLTFLRTEgpRLKVKELIRM-VENAAAGMEYLESKHCIHRDLAARNCLVT--EKNVLKISDFG----MSREEEDGVyaa 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 ---LRGSPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRsnRVIELPLRPQLSLDCRDLL 247
Cdd:cd05084   153 tggMKQIPVkWTAPEALNYGRYSSESDVWSFGILLWETFsLGAVPYANLSNQQTREAVE--QGVRLPCPENCPDEVYRLM 230
                         250
                  ....*....|....
gi 1907200402 248 QRLLERDPARRISF 261
Cdd:cd05084   231 EQCWEYDPRKRPSF 244
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
20-269 8.39e-25

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: 103.27  E-value: 8.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd07846     9 VGEGSYGMVMKC-RHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM-SPWDEKHVLRGSPL 178
Cdd:cd07846    88 DDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS--QSGVVKLCDFGFARTLaAPGEVYTDYVATRW 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEM-VCRRQYDARVDLWSVGVILYEALFGQPPFASRS---------------FSELEEKIRSNRV---IELP----- 234
Cdd:cd07846   166 YRAPELlVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSdidqlyhiikclgnlIPRHQELFQKNPLfagVRLPevkev 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907200402 235 -----LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07846   246 eplerRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
71-269 9.65e-25

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 102.12  E-value: 9.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  71 HPHIVQLKDFQWDNDNIYLIMEFcAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK 150
Cdd:cd13976    44 HPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 151 PHLKLADFGFAQHMSPWDEK-HVLRGSPLYMAPEMVC-RRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRS 227
Cdd:cd13976   123 TKLRLESLEDAVILEGEDDSlSDKHGCPAYVSPEILNsGATYSGKaADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRR 202
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907200402 228 NRViELPLrpQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd13976   203 GQF-AIPE--TLSPRARCLIRSLLRREPSERLTAEDILLHPW 241
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
20-261 1.13e-24

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: 102.81  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKkdTREVvAIKCVAKKSLN--KASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14146     2 IGVGGFGKVYRATWK--GQEV-AVKAARQDPDEdiKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFI----------HTRRILPEKVARvFMQQLASALQFLHERN---ISHLDLKPQNILLssLEK--------PHLKLA 156
Cdd:cd14146    79 TLNRALaaanaapgprRARRIPPHILVN-WAVQIARGMLYLHEEAvvpILHRDLKSSNILL--LEKiehddicnKTLKIT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 157 DFGFAQHmspWDE--KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELP 234
Cdd:cd14146   156 DFGLARE---WHRttKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNK-LTLP 231
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 235 LRPQLSLDCRDLLQRLLERDPARRISF 261
Cdd:cd14146   232 IPSTCPEPFAKLMKECWEQDPHIRPSF 258
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
19-263 1.13e-24

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: 102.59  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKdtrevVAIKCVAKK-SLNKASVENLLTeieiLKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd13991    13 RIGRGSFGEVHRMEDKQ-----TGFQCAVKKvRLEVFRAEELMA----CAGLTSPRVVPLYGAVREGPWVNIFMDLKEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSP--WDEKHVL-- 173
Cdd:cd13991    84 SLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSS-DGSDAFLCDFGHAECLDPdgLGKSLFTgd 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 --RGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNrviELPLRpQLSLDCRDL----L 247
Cdd:cd13991   163 yiPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANE---PPPLR-EIPPSCAPLtaqaI 238
                         250
                  ....*....|....*.
gi 1907200402 248 QRLLERDPARRISFKD 263
Cdd:cd13991   239 QAGLRKEPVHRASAAE 254
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
18-270 1.26e-24

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: 102.84  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKaSVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06641    10 EKIGKGSFGEVFKGIDNR-TQKVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWD-EKHVLRGS 176
Cdd:cd06641    88 SALDLLEPGPLDETQIATI-LREILKGLDYLHSEKKIHRDIKAANVLLS--EHGEVKLADFGVAGQLTDTQiKRN*FVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvielP--LRPQLSLDCRDLLQRLLERD 254
Cdd:cd06641   165 PFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNN----PptLEGNYSKPLKEFVEACLNKE 240
                         250
                  ....*....|....*.
gi 1907200402 255 PARRISFKDFFAHPWV 270
Cdd:cd06641   241 PSFRPTAKELLKHKFI 256
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
16-261 1.58e-24

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: 101.95  E-value: 1.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd05112     8 FVQEIGSGQFGLVHLGYWLNKDK--VAIKTIREGAM---SEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFM-QQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFA------QHMSPWD 168
Cdd:cd05112    83 HGCLSDYLRTQRGLFSAETLLGMcLDVCEGMAYLEEASVIHRDLAARNCLVG--ENQVVKVSDFGMTrfvlddQYTSSTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSplymAPEMVCRRQYDARVDLWSVGVILYEALF-GQPPFASRSFSELEEKIRSNRVIelpLRPQL-SLDCRDL 246
Cdd:cd05112   161 TKFPVKWS----SPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGFRL---YKPRLaSTHVYEI 233
                         250
                  ....*....|....*
gi 1907200402 247 LQRLLERDPARRISF 261
Cdd:cd05112   234 MNHCWKERPEDRPSF 248
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
14-213 1.77e-24

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 103.48  E-value: 1.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKslnKASVENLLTEIEILKGIR-------HPHIVQLKDFQWDNDN 86
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLK-TNKLVAVKVLKNK---PAYFRQAMLEIAILTLLNtkydpedKHHIVRLLDHFMHHGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEfCAGGDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHm 164
Cdd:cd14212    77 LCIVFE-LLGVNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFGSACF- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 165 spwdEKHVLRG---SPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14212   155 ----ENYTLYTyiqSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLF 202
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
14-270 2.05e-24

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: 102.05  E-value: 2.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVakkSLNKAS--VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd06640     6 FTKLERIGKGSFGEVFKGIDNR-TQQVVAIKII---DLEEAEdeIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVArVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWD-EK 170
Cdd:cd06640    82 EYLGGGSALDLLRAGPFDEFQIA-TMLKEILKGLDYLHSEKKIHRDIKAANVLLS--EQGDVKLADFGVAGQLTDTQiKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQRL 250
Cdd:cd06640   159 NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLV--GDFSKPFKEFIDAC 236
                         250       260
                  ....*....|....*....|
gi 1907200402 251 LERDPARRISFKDFFAHPWV 270
Cdd:cd06640   237 LNKDPSFRPTAKELLKHKFI 256
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
20-269 2.18e-24

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: 102.35  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR---HPHIVQLKDF----QWDND-NIYLIM 91
Cdd:cd07863     8 IGVGAYGTVYKA-RDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVcatsRTDREtKVTLVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFcAGGDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDE 169
Cdd:cd07863    87 EH-VDQDLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTS--GGQVKLADFGLARIYSCQMA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSnrVIELPLRPQLSLDCR----- 244
Cdd:cd07863   164 LTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFD--LIGLPPEDDWPRDVTlprga 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 245 ---------------------DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07863   242 fsprgprpvqsvvpeieesgaQLLLEMLTFNPHKRISAFRALQHPF 287
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
20-263 2.93e-24

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: 101.69  E-value: 2.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAY---AKKDTREVVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWD--NDNIYLIMEFC 94
Cdd:cd05038    12 LGEGHFGSVELCRydpLGDNTGEQVAVK-SLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESpgRRSLRLIMEYL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFI--HTRRILPEKVARvFMQQLASALQFLHERNISHLDLKPQNILLSSlEKpHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd05038    91 PSGSLRDYLqrHRDQIDLKRLLL-FASQICKGMEYLGSQRYIHRDLAARNILVES-ED-LVKISDFGLAKVLPEDKEYYY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 ---LRGSPLY-MAPEMVCRRQYDARVDLWSVGVILYEAL-----FGQPPfasRSFSELEEKIRSNRVIE----------- 232
Cdd:cd05038   168 vkePGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFtygdpSQSPP---ALFLRMIGIAQGQMIVTrllellksger 244
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 233 LPLRPQLSLDCRDLLQRLLERDPARRISFKD 263
Cdd:cd05038   245 LPRPPSCPDEVYDLMKECWEYEPQDRPSFSD 275
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
11-259 4.03e-24

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 102.83  E-value: 4.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  11 LDGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRH----PHIVQLKDFQWDNDN 86
Cdd:cd05633     4 MNDFSVHRIIGRGGFGEVYGC-RKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSP 166
Cdd:cd05633    83 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD--EHGHVRISDLGLACDFSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 wDEKHVLRGSPLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRD 245
Cdd:cd05633   161 -KKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKS 239
                         250
                  ....*....|....
gi 1907200402 246 LLQRLLERDPARRI 259
Cdd:cd05633   240 LLEGLLQRDVSKRL 253
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
16-204 6.46e-24

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: 101.86  E-value: 6.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKdTREVVAIK---CVAKKSlnkasVENLLTEIEILKGI--RHPHIVQLKDFQWDNDNI--- 87
Cdd:cd13977     4 LIREVGRGSYGVVYEAVVRR-TGARVAVKkirCNAPEN-----VELALREFWALSSIqrQHPNVIQLEECVLQRDGLaqr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 ---------------------------------YLIMEFCAGGDLSRFIHTRRILPeKVARVFMQQLASALQFLHERNIS 134
Cdd:cd13977    78 mshgssksdlylllvetslkgercfdprsacylWFVMEFCDGGDMNEYLLSRRPDR-QTNTSFMLQLSSALAFLHRNQIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 135 HLDLKPQNILLS-SLEKPHLKLADFGFAQ-----HMSPWDEKHVLR-------GSPLYMAPEmVCRRQYDARVDLWSVGV 201
Cdd:cd13977   157 HRDLKPDNILIShKRGEPILKVADFGLSKvcsgsGLNPEEPANVNKhflssacGSDFYMAPE-VWEGHYTAKADIFALGI 235

                  ...
gi 1907200402 202 ILY 204
Cdd:cd13977   236 IIW 238
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
12-290 7.29e-24

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: 100.58  E-value: 7.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVaKKSLNKASVENLLTEIEI-LKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKM-RHVPTGTIMAVKRI-RATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCaggDLS-------RFIHTRRIlPEKVARVFMQQLASALQFLHER-NISHLDLKPQNILLSslEKPHLKLADFGFAQ 162
Cdd:cd06617    79 MEVM---DTSldkfykkVYDKGLTI-PEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLIN--RNGQVKLCDFGISG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMV----CRRQYDARVDLWSVGVILYEALFGQPPFAS--RSFSELEEkirsnrVIELPlR 236
Cdd:cd06617   153 YLVDSVAKTIDAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDSwkTPFQQLKQ------VVEEP-S 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 237 PQL-----SLDCRDLLQRLLERDPARRISFKDFFAHPWVDlEHMPSGESLAQARALVVE 290
Cdd:cd06617   226 PQLpaekfSPEFQDFVNKCLKKNYKERPNYPELLQHPFFE-LHLSKNTDVASFVSLILG 283
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
20-262 9.93e-24

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: 99.80  E-value: 9.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASV----ENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd05044     3 LGSGAFGEVFEGTAKDILGDGSGETKVAVKTLRKGATdqekAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRilPEKVARV---FMQQLASAL------QFLHERNISHLDLKPQNILLSSlEKPH---LKLADFGFAQH 163
Cdd:cd05044    83 GGDLLSYLRAAR--PTAFTPPlltLKDLLSICVdvakgcVYLEDMHFVHRDLAARNCLVSS-KDYRervVKIGDFGLARD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVlRGSPL----YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQ 238
Cdd:cd05044   160 IYKNDYYRK-EGEGLlpvrWMAPESLVDGVFTTQSDVWAFGVLMWEILtLGQQPYPARNNLEVLHFVRAGGRLDQP--DN 236
                         250       260
                  ....*....|....*....|....
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05044   237 CPDDLYELMLRCWSTDPEERPSFA 260
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
20-261 1.09e-23

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: 99.68  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNkASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14148     2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIA-VTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRIlPEKVARVFMQQLASALQFLHERN---ISHLDLKPQNILL------SSLEKPHLKLADFGFAQHmspWDE- 169
Cdd:cd14148    81 NRALAGKKV-PPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILIlepienDDLSGKTLKITDFGLARE---WHKt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 -KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRvIELPLrPQlslDCRDLLQ 248
Cdd:cd14148   157 tKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNK-LTLPI-PS---TCPEPFA 231
                         250
                  ....*....|....*..
gi 1907200402 249 RLLER----DPARRISF 261
Cdd:cd14148   232 RLLEEcwdpDPHGRPDF 248
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
53-268 1.22e-23

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: 99.36  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  53 KASVENLLTEIEILKGIRHPHIVQLKDFQ---------WdndNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLAS 123
Cdd:cd14012    39 KKQIQLLEKELESLKKLRHPNLVSYLAFSierrgrsdgW---KVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 124 ALQFLHERNISHLDLKPQNILLSSLE---KPhlKLADFGF---AQHMSPWDEKHVLRgSPLYMAPEMV-CRRQYDARVDL 196
Cdd:cd14012   116 ALEYLHRNGVVHKSLHAGNVLLDRDAgtgIV--KLTDYSLgktLLDMCSRGSLDEFK-QTYWLPPELAqGSKSPTRKTDV 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 197 WSVGVILYEALFGQPPFasrsfseleekIRSNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14012   193 WDLGLLFLQMLFGLDVL-----------EKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
15-215 1.38e-23

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: 99.71  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKAYAKKDtrevVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQwDNDNIYLIMEFC 94
Cdd:cd14150     3 SMLKRIGTGSFGTVFRGKWHGD----VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFM-TRPNFAIITQWC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARV-FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:cd14150    78 EGSSLYRHLHVTETRFDTMQLIdVARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EGLTVKIGDFGLATVKTRWSGSQQV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200402 174 R---GSPLYMAPEMVcRRQ----YDARVDLWSVGVILYEALFGQPPFAS 215
Cdd:cd14150   156 EqpsGSILWMAPEVI-RMQdtnpYSFQSDVYAYGVVLYELMSGTLPYSN 203
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
20-263 2.23e-23

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: 99.41  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREV---VAIKCVAKKSLNKASVEnLLTEIEILKGIRHPHIVQLKDFQWdNDNIYLIMEFCAG 96
Cdd:cd05057    15 LGSGAFGTVYKGVWIPEGEKVkipVAIKVLREETGPKANEE-ILDEAYVMASVDHPHLVRLLGICL-SSQVQLITQLMPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFI--HTRRILPEKVARvFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPwDEKHVLR 174
Cdd:cd05057    93 GCLLDYVrnHRDNIGSQLLLN-WCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPN--HVKITDFGLAKLLDV-DEKEYHA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GS---PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQR 249
Cdd:cd05057   169 EGgkvPIkWMALESIQYRIYTHKSDVWSYGVTVWELMtFGAKPYEGIPAVEIPDLLEKGERLPQP--PICTIDVYMVLVK 246
                         250
                  ....*....|....
gi 1907200402 250 LLERDPARRISFKD 263
Cdd:cd05057   247 CWMIDAESRPTFKE 260
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
14-268 2.29e-23

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: 98.88  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYAT-VYKAyaKKDTREVvAIKCVAKKSLNKASVE-NLLTEIEilkgiRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd13982     3 TFSPKVLGYGSEGTiVFRG--TFDGRPV-AVKRLLPEFFDFADREvQLLRESD-----EHPNVIRYFCTEKDRQFLYIAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGG--DLSR----FIHTRRILPEKVaRVfMQQLASALQFLHERNISHLDLKPQNILLS---SLEKPHLKLADFGFAQ 162
Cdd:cd13982    75 ELCAASlqDLVEspreSKLFLRPGLEPV-RL-LRQIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRAMISDFGLCK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSpwDEKHVLR------GSPLYMAPEMV---CRRQYDARVDLWSVGVILYEAL-FGQPPFASRsfSELEEKIRSNRVIE 232
Cdd:cd13982   153 KLD--VGRSSFSrrsgvaGTSGWIAPEMLsgsTKRRQTRAVDIFSLGCVFYYVLsGGSHPFGDK--LEREANILKGKYSL 228
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907200402 233 LPLRPQLSL--DCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd13982   229 DKLLSLGEHgpEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
16-281 2.35e-23

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 100.24  E-value: 2.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDF-----QWDNDNIYLI 90
Cdd:cd07859     4 IQEVIGKGSYGVVCSAI-DTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHImlppsRREFKDIYVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFcAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHM---SP- 166
Cdd:cd07859    83 FEL-MESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCK--LKICDFGLARVAfndTPt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 ---WDEKHVLRgspLYMAPEMvCRR---QYDARVDLWSVGVILYEALFGQPPF--------------------------- 213
Cdd:cd07859   160 aifWTDYVATR---WYRAPEL-CGSffsKYTPAIDIWSIGCIFAEVLTGKPLFpgknvvhqldlitdllgtpspetisrv 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200402 214 ----ASRSFSELEEKIRSNRVIELPLRPQLSLdcrDLLQRLLERDPARRISFKDFFAHPW----VDLEHMPSGESL 281
Cdd:cd07859   236 rnekARRYLSSMRKKQPVPFSQKFPNADPLAL---RLLERLLAFDPKDRPTAEEALADPYfkglAKVEREPSAQPI 308
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
20-259 2.42e-23

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: 100.12  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRH----PHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14223     8 IGRGGFGEVYGC-RKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMSYAFHTPDKLSFILDLMN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHVLRG 175
Cdd:cd14223    87 GGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLD--EFGHVRISDLGLACDFSK-KKPHASVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRR-QYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERD 254
Cdd:cd14223   164 THGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRD 243

                  ....*
gi 1907200402 255 PARRI 259
Cdd:cd14223   244 VNRRL 248
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-270 2.83e-23

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 98.49  E-value: 2.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTrEVVAIKCVAKKSLNKASVENLLT---EIEILK--GIRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd14102     8 LGSGGFGTVYAGSRIADG-LPVAVKHVVKERVTEWGTLNGVMvplEIVLLKkvGSGFRGVIKLLDWYERPDGFLIVMERP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 A-GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNiLLSSLEKPHLKLADFGFAQHMSpwDEKHV- 172
Cdd:cd14102    87 EpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDEN-LLVDLRTGELKLIDFGSGALLK--DTVYTd 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFasrsfsELEEKIRSNRvieLPLRPQLSLDCRDLLQRLL 251
Cdd:cd14102   164 FDGTRVYSPPEWIRYHRYHGRsATVWSLGVLLYDMVCGDIPF------EQDEEILRGR---LYFRRRVSPECQQLIKWCL 234
                         250
                  ....*....|....*....
gi 1907200402 252 ERDPARRISFKDFFAHPWV 270
Cdd:cd14102   235 SLRPSDRPTLEQIFDHPWM 253
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
20-273 4.84e-23

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: 98.97  E-value: 4.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVA---KKSLNKAsvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAG 96
Cdd:cd06635    33 IGHGSFGAVYFARDVR-TSEVVAIKKMSysgKQSNEKW--QDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 --GDLSRfIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEkhvLR 174
Cdd:cd06635   110 saSDLLE-VHKKPLQEIEIAAITHGAL-QGLAYLHSHNMIHRDIKAGNILLT--EPGQVKLADFGSASIASPANS---FV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPLYMAPEMVC---RRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPlRPQLSLDCRDLLQRLL 251
Cdd:cd06635   183 GTPYWMAPEVILamdEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQ-SNEWSDYFRNFVDSCL 261
                         250       260
                  ....*....|....*....|..
gi 1907200402 252 ERDPARRISFKDFFAHPWVDLE 273
Cdd:cd06635   262 QKIPQDRPTSEELLKHMFVLRE 283
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
9-270 4.94e-23

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: 98.18  E-value: 4.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   9 PRLDgFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVenLLTEIEILKGIRHPHIVQLKDFQWDNDNIY 88
Cdd:cd06646     7 PQHD-YELIQRVGSGTYGDVYKA-RNLHTGELAAVKIIKLEPGDDFSL--IQQEIFMVKECKHCNIVAYFGSYLSREKLW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRILPE-KVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSP- 166
Cdd:cd06646    83 ICMEYCGGGSLQDIYHVTGPLSElQIAYVCRETL-QGLAYLHSKGKMHRDIKGANILLT--DNGDVKLADFGVAAKITAt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLRGSPLYMAPEMVCRRQ---YDARVDLWSVGVILYEALFGQPP-FASRSFSELEEKIRSN-RVIELPLRPQLSL 241
Cdd:cd06646   160 IAKRKSFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNfQPPKLKDKTKWSS 239
                         250       260
                  ....*....|....*....|....*....
gi 1907200402 242 DCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06646   240 TFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
17-270 5.81e-23

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 98.83  E-value: 5.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  17 TERLGSGTYATVYKAYAKKDTREVVAIKCV-AKKSLNKASvenlLTEIEILKGIRHP------HIVQLKD-FQWDNdniY 88
Cdd:cd14135     5 YGYLGKGVFSNVVRARDLARGNQEVAIKIIrNNELMHKAG----LKELEILKKLNDAdpddkkHCIRLLRhFEHKN---H 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEF-CAGGDLsrfihtRRILPE---------KVARVFMQQLASALQFLHERNISHLDLKPQNILLSSlEKPHLKLADF 158
Cdd:cd14135    78 LCLVFeSLSMNL------REVLKKygknvglniKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNE-KKNTLKLCDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 159 GFAQHMSPWDEKHVLRgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS-------FSELEEKIrSNRVI 231
Cdd:cd14135   151 GSASDIGENEITPYLV-SRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTnnhmlklMMDLKGKF-PKKML 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 232 ----------------------------------------------------ELPLRPQLsLDCRDLLQRLLERDPARRI 259
Cdd:cd14135   229 rkgqfkdqhfdenlnfiyrevdkvtkkevrrvmsdikptkdlktlligkqrlPDEDRKKL-LQLKDLLDKCLMLDPEKRI 307
                         330
                  ....*....|.
gi 1907200402 260 SFKDFFAHPWV 270
Cdd:cd14135   308 TPNEALQHPFI 318
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
6-283 7.40e-23

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 99.21  E-value: 7.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRldGFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQW--- 82
Cdd:cd07879    11 WELPE--RYTSLKQVGSGAYGSVCSAIDKR-TGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTsav 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  83 ---DNDNIYLIMEFCAGgDLSRfIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFG 159
Cdd:cd07879    88 sgdEFQDFYLVMPYMQT-DLQK-IMGHPLSEDKVQYLVYQML-CGLKYIHSAGIIHRDLKPGNLAVN--EDCELKILDFG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 160 FAQHMSPWDEKHVLrgSPLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFASRSF-------------------S 219
Cdd:cd07879   163 LARHADAEMTGYVV--TRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYldqltqilkvtgvpgpefvQ 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 220 ELEEKIRSNRVIELP---------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQ 283
Cdd:cd07879   241 KLEDKAAKSYIKSLPkyprkdfstLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEETEQQ 313
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
20-283 8.22e-23

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: 98.87  E-value: 8.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD-FQWDND-----NIYLIMEF 93
Cdd:cd07880    23 VGSGAYGTVCSALDRR-TGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDvFTPDLSldrfhDFYLVMPF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 cAGGDLSRFIHTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:cd07880   102 -MGTDLGKLMKHEKLSEDRI-QFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVN--EDCELKILDFGLARQTDSEMTGYVV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 rgSPLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPF-ASRSFSELEE--------------KIRS----NRVIEL 233
Cdd:cd07880   178 --TRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFkGHDHLDQLMEimkvtgtpskefvqKLQSedakNYVKKL 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 234 P---------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPSGESLAQ 283
Cdd:cd07880   256 PrfrkkdfrsLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETEAP 314
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
20-277 9.94e-23

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 98.64  E-value: 9.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIV----------QLKDFQwdndNIYL 89
Cdd:cd07850     8 IGSGAQGIVCAAYDTV-TGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIgllnvftpqkSLEEFQ----DVYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFcAGGDLSRFIHtrRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ------H 163
Cdd:cd07850    83 VMEL-MDANLCQVIQ--MDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS--DCTLKILDFGLARtagtsfM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWdekHVLRgspLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF------------------ASRSF-SELEEK 224
Cdd:cd07850   158 MTPY---VVTR---YYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFpgtdhidqwnkiieqlgtPSDEFmSRLQPT 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 225 IRsNRVIELPLRPQLSLD----------------------CRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPS 277
Cdd:cd07850   232 VR-NYVENRPKYAGYSFEelfpdvlfppdseehnklkasqARDLLSKMLVIDPEKRISVDDALQHPYINVWYDPS 305
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
20-259 1.04e-22

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 97.37  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05631     8 LGKGGFGEVC-ACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHT--RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05631    87 LKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLD--DRGHIRISDLGLAVQIPEGETVRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR----SFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLE 252
Cdd:cd05631   165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkervKREEVDRRVKED---QEEYSEKFSEDAKSICRMLLT 241

                  ....*..
gi 1907200402 253 RDPARRI 259
Cdd:cd05631   242 KNPKERL 248
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
6-265 1.17e-22

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: 96.88  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQwDND 85
Cdd:cd05067     2 WEVPR-ETLKLVERLGAGQFGEVWMGYYNGHTK--VAIKSLKQGSM---SPDAFLAEANLMKQLQHQRLVRLYAVV-TQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTRRILPEKVARVF--MQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:cd05067    75 PIYIITEYMENGSLVDFLKTPSGIKLTINKLLdmAAQIAEGMAFIEERNYIHRDLRAANILVS--DTLSCKIADFGLARL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPwDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIrsNRVIELPLRPQL 239
Cdd:cd05067   153 IED-NEYTAREGAKFpikWTAPEAINYGTFTIKSDVWSFGILLTEIVtHGRIPYPGMTNPEVIQNL--ERGYRMPRPDNC 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 240 SLDCRDLLQRLLERDPARRISFK-------DFF 265
Cdd:cd05067   230 PEELYQLMRLCWKERPEDRPTFEylrsvleDFF 262
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
20-267 1.30e-22

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: 96.41  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKcvakksLNKASVE--NLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd14065     1 LGKGFFGEVYKV-THRETGKVMVMK------ELKRFDEqrSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLkLADFGFAQHMSPW-----DE 169
Cdd:cd14065    74 TLEELLKSMDEqLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreANRGRNAV-VADFGLAREMPDEktkkpDR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLR--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEAL---FGQPPFASRS--FSELEEKIRSNRVIELPLR-PQLSL 241
Cdd:cd14065   153 KKRLTvvGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIgrvPADPDYLPRTmdFGLDVRAFRTLYVPDCPPSfLPLAI 232
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 242 DCRDLlqrllerDPARRISFKDFFAH 267
Cdd:cd14065   233 RCCQL-------DPEKRPSFVELEHH 251
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
20-267 1.40e-22

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: 96.61  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKsLNKASVENLLTEIEILKGIRHPHIVQLKDfQWDND-----NIYLIMEFC 94
Cdd:cd14033     9 IGRGSFKTVYRGLDTETTVEVAWCELQTRK-LSKGERQRFSEEVEMLKGLQHPNIVRFYD-SWKSTvrghkCIILVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14033    87 TSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITG-PTGSVKIGDLGLATLKRASFAKSV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LrGSPLYMAPEMVcRRQYDARVDLWSVGVILYEALFGQPPF-----ASRSFSELEEKIRSNRVIELPLrPQLsldcRDLL 247
Cdd:cd14033   166 I-GTPEFMAPEMY-EEKYDEAVDVYAFGMCILEMATSEYPYsecqnAAQIYRKVTSGIKPDSFYKVKV-PEL----KEII 238
                         250       260
                  ....*....|....*....|
gi 1907200402 248 QRLLERDPARRISFKDFFAH 267
Cdd:cd14033   239 EGCIRTDKDERFTIQDLLEH 258
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
20-213 1.63e-22

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: 97.40  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyakKDTR--EVVAIKCVA---KKSLNKAsvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd06634    23 IGHGSFGAVYFA---RDVRnnEVVAIKKMSysgKQSNEKW--QDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYC 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AG--GDLSRfIHTRRILPEKVARVFMQQLaSALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwdeKHV 172
Cdd:cd06634    98 LGsaSDLLE-VHKKPLQEVEIAAITHGAL-QGLAYLHSHNMIHRDVKAGNILLT--EPGLVKLGDFGSASIMAP---ANS 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907200402 173 LRGSPLYMAPEMVC---RRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd06634   171 FVGTPYWMAPEVILamdEGQYDGKVDVWSLGITCIELAERKPPL 214
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
4-262 2.30e-22

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 96.96  E-value: 2.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   4 PSWGLPRlDGFILTERLGSGTYATVYKAYA------KKDTREVVAIKCVAKKSLNKaSVENLLTEIEILKGI-RHPHIVQ 76
Cdd:cd05099     5 PKWEFPR-DRLVLGKPLGEGCFGQVVRAEAygidksRPDQTVTVAVKMLKDNATDK-DLADLISEMELMKLIgKHKNIIN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  77 LKDFQWDNDNIYLIMEFCAGGDLSRFIHTRR------------------ILPEKVARVFmqQLASALQFLHERNISHLDL 138
Cdd:cd05099    83 LLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdytfditkvpeeqlSFKDLVSCAY--QVARGMEYLESRRCIHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 139 KPQNILLSslEKPHLKLADFGFAQHMSPWDE-KHVLRGS-PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFA 214
Cdd:cd05099   161 AARNVLVT--EDNVMKIADFGLARGVHDIDYyKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILMWEIFtLGGSPYP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 215 SRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05099   239 GIPVEELFKLLREGHRMDKP--SNCTHELYMLMRECWHAVPTQRPTFK 284
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
14-213 2.49e-22

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: 96.23  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVakkSLNKASVENLLTEIEILKGIRHPHIVQL-------KDFQWDNDN 86
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVK-TGQLAAIKVM---DVTEDEEEEIKLEINMLKKYSHHRNIATyygafikKSPPGHDDQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQH 163
Cdd:cd06636    94 LWLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVsAQL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 164 MSPWDEKHVLRGSPLYMAPEMV-CRRQ----YDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd06636   172 DRTVGRRNTFIGTPYWMAPEVIaCDENpdatYDYRSDIWSLGITAIEMAEGAPPL 226
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
18-264 2.71e-22

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 95.46  E-value: 2.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTRevVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDKTP--VAVK-TCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGfaqhMSPWDEKHVLRGS 176
Cdd:cd05085    79 DFLSFLRKKKDeLKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVG--ENNALKISDFG----MSRQEDDGVYSSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PL------YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLR-PQlslDCRDLLQ 248
Cdd:cd05085   153 GLkqipikWTAPEALNYGRYSSESDVWSFGILLWETFsLGVCPYPGMTNQQAREQVEKGYRMSAPQRcPE---DIYKIMQ 229
                         250
                  ....*....|....*.
gi 1907200402 249 RLLERDPARRISFKDF 264
Cdd:cd05085   230 RCWDYNPENRPKFSEL 245
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
14-268 3.48e-22

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: 95.07  E-value: 3.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGK-LYAVKRSRSRFRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKGILYIQTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGgDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14050    82 LCDT-SLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS--KDGVCKLGDFGLVVELDKEDIHDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPLYMAPEmVCRRQYDARVDLWSVGVILYE-ALFGQPPfasrSFSELEEKIRsNRVIELPLRPQLSLDCRDLLQRLL 251
Cdd:cd14050   159 QEGDPRYMAPE-LLQGSFTKAADIFSLGITILElACNLELP----SGGDGWHQLR-QGYLPEEFTAGLSPELRSIIKLMM 232
                         250
                  ....*....|....*..
gi 1907200402 252 ERDPARRISFKDFFAHP 268
Cdd:cd14050   233 DPDPERRPTAEDLLALP 249
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
6-265 4.13e-22

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: 95.55  E-value: 4.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLNKasvENLLTEIEILKGIRHPHIVQLKDFQWDND 85
Cdd:cd05068     3 WEIDR-KSLKLLRKLGSGQFGEVWEGLWNNTTP--VAVKTLKPGTMDP---EDFLREAQIMKKLRHPKLIQLYAVCTLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIHTRR---ILPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQ 162
Cdd:cd05068    77 PIYIITELMKHGSLLEYLQGKGrslQLPQLID--MAAQVASGMAYLESQNYIHRDLAARNVLVG--ENNICKVADFGLAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNrvIELPLRPQ 238
Cdd:cd05068   153 VIKVEDEYEAREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVtYGRIPYPGMTNAEVLQQVERG--YRMPCPPN 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISF-------KDFF 265
Cdd:cd05068   231 CPPQLYDIMLECWKADPMERPTFetlqwklEDFF 264
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
20-269 5.29e-22

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: 95.14  E-value: 5.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKsLNKASVENLLTEIEILKGIRHPHIVQLKDFqWDNDN-----IYLIMEFC 94
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWVEVAWCELQDRK-LTKVERQRFKEEAEMLKGLQHPNIVRFYDF-WESCAkgkrcIVLVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14032    87 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITG-PTGSVKIGDLGLATLKRASFAKSV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LrGSPLYMAPEMVcRRQYDARVDLWSVGVILYEALFGQPPfasrsFSELEEKIRSNRVIELPLRPQL-----SLDCRDLL 247
Cdd:cd14032   166 I-GTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYP-----YSECQNAAQIYRKVTCGIKPASfekvtDPEIKEII 238
                         250       260
                  ....*....|....*....|..
gi 1907200402 248 QRLLERDPARRISFKDFFAHPW 269
Cdd:cd14032   239 GECICKNKEERYEIKDLLSHAF 260
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
10-213 5.60e-22

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: 95.92  E-value: 5.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVYKAYAKKDTReVVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd07869     3 KADSYEKLEKLGEGSYATVYKGKSKVNGK-LVALK-VIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFcAGGDLSRFI--HTRRILPEKVaRVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPW 167
Cdd:cd07869    81 VFEY-VHTDLCQYMdkHPGGLHPENV-KLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS--DTGELKLADFGLARAKSVP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 168 DEKHVLRGSPLYMAPE--MVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd07869   157 SHTYSNEVVTLWYRPPdvLLGSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
5-262 7.13e-22

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: 94.71  E-value: 7.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQwDN 84
Cdd:cd05073     5 AWEIPR-ESLKLEKKLGAGQFGEVWMATYNKHTK--VAVKTMKPGSM---SVEAFLAEANVMKTLQHDKLVKLHAVV-TK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHT----RRILPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGF 160
Cdd:cd05073    78 EPIYIITEFMAKGSLLDFLKSdegsKQPLPKLID--FSAQIAEGMAFIEQRNYIHRDLRAANILVSASLV--CKIADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSpwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELeekIRS-NRVIELP 234
Cdd:cd05073   154 ARVIE--DNEYTAREGakfPIkWTAPEAINFGSFTIKSDVWSFGILLMEIVtYGRIPYPGMSNPEV---IRAlERGYRMP 228
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 235 LRPQLSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05073   229 RPENCPEELYNIMMRCWKNRPEERPTFE 256
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
23-267 7.18e-22

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: 94.31  E-value: 7.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  23 GTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVEnllteieILKGIRHPHIVQLKD-FQWDnDNIYLIMEFCAGGDLSR 101
Cdd:cd13995    15 GAFGKVYLAQDTK-TKKRMACKLIPVEQFKPSDVE-------IQACFRHENIAELYGaLLWE-ETVHLFMEAGEGGSVLE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 102 FIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphlKLADFGFAQHMS-----PWDekhvLRGS 176
Cdd:cd13995    86 KLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKA---VLVDFGLSVQMTedvyvPKD----LRGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASR-------SFSELEEKirsnrviELPLRPQLSLDC----RD 245
Cdd:cd13995   159 EIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRyprsaypSYLYIIHK-------QAPPLEDIAQDCspamRE 231
                         250       260
                  ....*....|....*....|..
gi 1907200402 246 LLQRLLERDPARRISFKDFFAH 267
Cdd:cd13995   232 LLEAALERNPNHRSSAAELLKH 253
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
20-205 7.43e-22

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: 94.88  E-value: 7.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKksLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14154     1 LGKGFFGQAIKV-THRETGEVMVMKELIR--FDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTR-RILP--EKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQ----------HMSP 166
Cdd:cd14154    78 KDVLKDMaRPLPwaQRVR--FAKDIASGMAYLHSMNIIHRDLNSHNCLVR--EDKTVVVADFGLARliveerlpsgNMSP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 WDEKHVLR-----------GSPLYMAPEMVCRRQYDARVDLWSVGVILYE 205
Cdd:cd14154   154 SETLRHLKspdrkkrytvvGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCE 203
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
16-263 1.02e-21

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: 94.36  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTREV--VAIKCVAKKSLNKASVeNLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd05033     8 IEKVIGGGEFGEVCSGSLKLPGKKEidVAIKTLKSGYSDKQRL-DFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFI--HTRRILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILLSSlekpHL--KLADFGFAQHMSPWDE 169
Cdd:cd05033    87 MENGSLDKFLreNDGKFTVTQLVGM-LRGIASGMKYLSEMNYVHRDLAARNILVNS----DLvcKVSDFGLSRRLEDSEA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRG--SPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELeekIRSnrvIELPLRPQLSLDCRD 245
Cdd:cd05033   162 TYTTKGgkIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEVMsYGERPYWDMSNQDV---IKA---VEDGYRLPPPMDCPS 235
                         250       260
                  ....*....|....*....|..
gi 1907200402 246 LLQRLL----ERDPARRISFKD 263
Cdd:cd05033   236 ALYQLMldcwQKDRNERPTFSQ 257
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
20-269 1.22e-21

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 95.04  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05632    10 LGKGGFGEVC-ACQVRATGKMYACKRLEKKRIKKRKGESMaLNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHT--RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05632    89 LKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLD--DYGHIRISDLGLAVKIPEGESIRGRVGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIrSNRVIELP--LRPQLSLDCRDLLQRLLERD 254
Cdd:cd05632   167 VGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEV-DRRVLETEevYSAKFSEEAKSICKMLLTKD 245
                         250       260
                  ....*....|....*....|
gi 1907200402 255 PARRISFKDFFA-----HPW 269
Cdd:cd05632   246 PKQRLGCQEEGAgevkrHPF 265
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
6-251 1.22e-21

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: 94.36  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPrlDGFI-LTERLGSGTYATVYKAYAKKDtrevVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQwDN 84
Cdd:cd14151     3 WEIP--DGQItVGQRIGSGSFGTVYKGKWHGD----VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS-TK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTRRILPEKVARV-FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQH 163
Cdd:cd14151    76 PQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIdIARQTAQGMDYLHAKSIIHRDLKSNNIFLH--EDLTVKIGDFGLATV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKH---VLRGSPLYMAPEMVcRRQ----YDARVDLWSVGVILYEALFGQPPFASRSfseleekiRSNRVIELPLR 236
Cdd:cd14151   154 KSRWSGSHqfeQLSGSILWMAPEVI-RMQdknpYSFQSDVYAFGIVLYELMTGQLPYSNIN--------NRDQIIFMVGR 224
                         250       260
                  ....*....|....*....|..
gi 1907200402 237 PQLSLD-------CRDLLQRLL 251
Cdd:cd14151   225 GYLSPDlskvrsnCPKAMKRLM 246
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
20-214 1.30e-21

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: 93.61  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDtrevVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQwDNDNIYLIMEFCAGGDL 99
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD----VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYM-TKPQLAIVTQWCEGSSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPE-----KVARvfmqQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLR 174
Cdd:cd14062    76 YKHLHVLETKFEmlqliDIAR----QTAQGMDYLHAKNIIHRDLKSNNIFLH--EDLTVKIGDFGLATVKTRWSGSQQFE 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 175 ---GSPLYMAPE---MVCRRQYDARVDLWSVGVILYEALFGQPPFA 214
Cdd:cd14062   150 qptGSILWMAPEvirMQDENPYSFQSDVYAFGIVLYELLTGQLPYS 195
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
20-272 1.57e-21

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: 93.99  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVA--IKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDN--DNIYLIMEFCA 95
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAkqVQFDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH-----MSPWDEK 170
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS--AGNVKLGDFGASKRlqticMSGTGIR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVlRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfsELEEKIRSNRVIELPLRPQL----SLDCRDL 246
Cdd:cd06651   173 SV-TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA-----EYEAMAAIFKIATQPTNPQLpshiSEHARDF 246
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 247 LQRLLErDPARRISFKDFFAHPWVDL 272
Cdd:cd06651   247 LGCIFV-EARHRPSAEELLRHPFAQL 271
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
14-180 1.63e-21

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: 93.68  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKasveNLLTEIEILKGIR-HPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLK-TGEEVAIKIEKKDSKHP----QLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCaGGDLSR-FIHTRRILPEKVarVFM--QQLASALQFLHERNISHLDLKPQNILLSSLEKPH-LKLADFGFA------- 161
Cdd:cd14016    77 LL-GPSLEDlFNKCGRKFSLKT--VLMlaDQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkVYLIDFGLAkkyrdpr 153
                         170       180
                  ....*....|....*....|.
gi 1907200402 162 --QHMsPWDEKHVLRGSPLYM 180
Cdd:cd14016   154 tgKHI-PYREGKSLTGTARYA 173
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
20-269 2.15e-21

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: 93.94  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIR---HPHIVQLKDF----QWDNDN-IYLIM 91
Cdd:cd07862     9 IGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVctvsRTDRETkLTLVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFcAGGDLSRFIHT--RRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDE 169
Cdd:cd07862    89 EH-VDQDLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTS--SGQIKLADFGLARIYSFQMA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFasRSFSELEEKIRSNRVIELP--------------- 234
Cdd:cd07862   166 LTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLF--RGSSDVDQLGKILDVIGLPgeedwprdvalprqa 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 235 -----------LRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07862   244 fhsksaqpiekFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
14-270 2.37e-21

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: 94.02  E-value: 2.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKdTREVVAIKCVakkSLNKASVENLLTEIEILKGIRHPHIVQL-------KDFQWDNDN 86
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVK-TGQLAAIKVM---DVTGDEEEEIKQEINMLKKYSHHRNIATyygafikKNPPGMDDQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF-AQH 163
Cdd:cd06637    84 LWLVMEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT--ENAEVKLVDFGVsAQL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVLRGSPLYMAPEMV-CRRQ----YDARVDLWSVGVILYEALFGQPPFASRsfseleEKIRSNRVIELPLRPQ 238
Cdd:cd06637   162 DRTVGRRNTFIGTPYWMAPEVIaCDENpdatYDFKSDLWSLGITAIEMAEGAPPLCDM------HPMRALFLIPRNPAPR 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 239 L-----SLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06637   236 LkskkwSKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
20-258 2.57e-21

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: 93.45  E-value: 2.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdtrEVVAIKCVAKKSLNKASVENLLT-------------------EIEILKGIRHPHIVQLkdF 80
Cdd:cd14000     2 LGDGGFGSVYRASYKG---EPVAVKIFNKHTSSNFANVPADTmlrhlratdamknfrllrqELTVLSHLHHPSIVYL--L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QWDNDNIYLIMEFCAGGDLS--------RFIHTRRILPEKVArvfmQQLASALQFLHERNISHLDLKPQNILLSSLEKP- 151
Cdd:cd14000    77 GIGIHPLMLVLELAPLGSLDhllqqdsrSFASLGRTLQQRIA----LQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNs 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 152 --HLKLADFGFAQHMSPWDEKHVlRGSPLYMAPEMVCRR-QYDARVDLWSVGVILYEALFGQPPFasrsfsELEEKIRSN 228
Cdd:cd14000   153 aiIIKIADYGISRQCCRMGAKGS-EGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPM------VGHLKFPNE 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 229 RVIELPLRPQLS-------LDCRDLLQRLLERDPARR 258
Cdd:cd14000   226 FDIHGGLRPPLKqyecapwPEVEVLMKKCWKENPQQR 262
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
10-264 3.96e-21

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: 92.91  E-value: 3.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  10 RLDGFILTERLGSGTYATVYKAYAKKDTRE----VVAIKCVAKKSLNKASvENLLTEIEILKGIRHPHIVQLKDFQWDND 85
Cdd:cd05049     3 KRDTIVLKRELGEGAFGKVFLGECYNLEPEqdkmLVAVKTLKDASSPDAR-KDFEREAELLTNLQHENIVKFYGVCTEGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFIhtRRILPEKVARVFM----------------QQLASALQFLHERNISHLDLKPQNILLSslE 149
Cdd:cd05049    82 PLLMVFEYMEHGDLNKFL--RSHGPDAAFLASEdsapgeltlsqllhiaVQIASGMVYLASQHFVHRDLATRNCLVG--T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 150 KPHLKLADFGFAQHMSPWDEKHVlRGSPL----YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEK 224
Cdd:cd05049   158 NLVVKIGDFGMSRDIYSTDYYRV-GGHTMlpirWMPPESILYRKFTTESDVWSFGVVLWEIFtYGKQPWFQLSNTEVIEC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907200402 225 IRSNRVIElplRPQlslDC----RDLLQRLLERDPARRISFKDF 264
Cdd:cd05049   237 ITQGRLLQ---RPR---TCpsevYAVMLGCWKREPQQRLNIKDI 274
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
20-271 4.17e-21

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: 94.43  E-value: 4.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD---------FQwdndNIYLI 90
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRV-ALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDilqpphidpFE----EIYVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGgDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd07853    83 TELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS--NCVLKICDFGLARVEEPDESK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRG--SPLYMAPE-MVCRRQYDARVDLWSVGVILYEALFGQPPF-ASRSFSELE-----------EKIRS------NR 229
Cdd:cd07853   160 HMTQEvvTQYYRAPEiLMGSRHYTSAVDIWSVGCIFAELLGRRILFqAQSPIQQLDlitdllgtpslEAMRSacegarAH 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 230 VIELPLRP-----------QLSLDCRDLLQRLLERDPARRISFKDFFAHPWVD 271
Cdd:cd07853   240 ILRGPHKPpslpvlytlssQATHEAVHLLCRMLVFDPDKRISAADALAHPYLD 292
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
18-263 4.30e-21

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: 92.56  E-value: 4.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLkdFQWDNDNIYLIMEFCAGG 97
Cdd:cd14025     2 EKVGSGGFGQVYKVRHKH-WKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPV--YGICSEPVGLVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRILPEKVARVfMQQLASALQFLHERN--ISHLDLKPQNILLSSleKPHLKLADFGFAQHM----SPWDEKH 171
Cdd:cd14025    79 SLEKLLASEPLPWELRFRI-IHETAVGMNFLHCMKppLLHLDLKPANILLDA--HYHVKISDFGLAKWNglshSHDLSRD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCR--RQYDARVDLWSVGVILYEALFGQPPFASRS-FSELEEKIRSNRVIELPL----RPQLSLDCR 244
Cdd:cd14025   156 GLRGTIAYLPPERFKEknRCPDTKHDVYSFAIVIWGILTQKKPFAGENnILHIMVKVVKGHRPSLSPiprqRPSECQQMI 235
                         250
                  ....*....|....*....
gi 1907200402 245 DLLQRLLERDPARRISFKD 263
Cdd:cd14025   236 CLMKRCWDQDPRKRPTFQD 254
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
6-262 4.66e-21

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: 92.93  E-value: 4.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYA----KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDF 80
Cdd:cd05055    30 WEFPR-NNLSFGKTLGAGAFGKVVEATAyglsKSDAVMKVAVKML-KPTAHSSEREALMSELKIMSHLgNHENIVNLLGA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QWDNDNIYLIMEFCAGGDLSRFIHTRR--ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADF 158
Cdd:cd05055   108 CTIGGPILVITEYCCYGDLLNFLRRKResFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLT--HGKIVKICDF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 159 GFAQH-MSpwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYE--ALFGQP----PFASRSFSELEEKIRS 227
Cdd:cd05055   186 GLARDiMN--DSNYVVKGNarlPVkWMAPESIFNCVYTFESDVWSYGILLWEifSLGSNPypgmPVDSKFYKLIKEGYRM 263
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907200402 228 NRVIELPlrpqlsLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05055   264 AQPEHAP------AEIYDIMKTCWDADPLKRPTFK 292
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
20-259 7.15e-21

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: 92.27  E-value: 7.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkAYAKKDTREVVAIKCVAKKSLNKASVENL-LTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05607    10 LGKGGFGEVC-AVQVKNTGQMYACKKLDKKRLKKKSGEKMaLLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARV--FMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWDEKHVLRGS 176
Cdd:cd05607    89 LKYHIYNVGERGIEMERVifYSAQITCGILHLHSLKIVYRDMKPENVLLDDNG--NCRLSDLGLAVEVKEGKPITQRAGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 177 PLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFasRSFSE---LEEKIRsnRVIELPLR---PQLSLDCRDLLQRL 250
Cdd:cd05607   167 NGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPF--RDHKEkvsKEELKR--RTLEDEVKfehQNFTEEAKDICRLF 242

                  ....*....
gi 1907200402 251 LERDPARRI 259
Cdd:cd05607   243 LAKKPENRL 251
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
15-214 7.85e-21

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: 92.02  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKAYAKKDtrevVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQwDNDNIYLIMEFC 94
Cdd:cd14149    15 MLSTRIGSGSFGTVYKGKWHGD----VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARV-FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWD---EK 170
Cdd:cd14149    90 EGSSLYKHLHVQETKFQMFQLIdIARQTAQGMDYLHAKNIIHRDMKSNNIFLH--EGLTVKIGDFGLATVKSRWSgsqQV 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 171 HVLRGSPLYMAPEMVcRRQ----YDARVDLWSVGVILYEALFGQPPFA 214
Cdd:cd14149   168 EQPTGSILWMAPEVI-RMQdnnpFSFQSDVYSYGIVLYELMTGELPYS 214
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
20-273 8.39e-21

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: 92.04  E-value: 8.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKsLNKASVENLLTEIEILKGIRHPHIVQLKDfQWDNDN-----IYLIMEFC 94
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAWCELQDRK-LSKSERQRFKEEAGMLKGLQHPNIVRFYD-SWESTVkgkkcIVLVTELM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN--ISHLDLKPQNILLSSlEKPHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd14030   111 TSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG-PTGSVKIGDLGLATLKRASFAKSV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LrGSPLYMAPEMVcRRQYDARVDLWSVGVILYEALFGQPPfasrsFSELEEKIRSNRVIELPLRPQlSLD------CRDL 246
Cdd:cd14030   190 I-GTPEFMAPEMY-EEKYDESVDVYAFGMCMLEMATSEYP-----YSECQNAAQIYRRVTSGVKPA-SFDkvaipeVKEI 261
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 247 LQRLLERDPARRISFKDFFAHPWVDLE 273
Cdd:cd14030   262 IEGCIRQNKDERYAIKDLLNHAFFQEE 288
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
18-258 1.79e-20

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: 90.81  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyakKDTRevVAIKCVAKKSL--NKASVENLLTEIEILKGIR-HPHIVQ--------LKDFQWDndn 86
Cdd:cd14037     9 KYLAEGGFAHVYLV---KTSN--GGNRAALKRVYvnDEHDLNVCKREIEIMKRLSgHKNIVGyidssanrSGNGVYE--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  87 IYLIMEFCAGGDLSRFIHTR---RILPEKVARVFmQQLASALQFLHERN--ISHLDLKPQNILLSslEKPHLKLADFGFA 161
Cdd:cd14037    81 VLLLMEYCKGGGVIDLMNQRlqtGLTESEILKIF-CDVCEAVAAMHYLKppLIHRDLKVENVLIS--DSGNYKLCDFGSA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 QHMSPWDEKH---------VLRGSPL-YMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPPFA-SRSFSELEEKirs 227
Cdd:cd14037   158 TTKILPPQTKqgvtyveedIKKYTTLqYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPFEeSGQLAILNGN--- 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 228 nrvIELPLRPQLSLDCRDLLQRLLERDPARR 258
Cdd:cd14037   235 ---FTFPDNSRYSKRLHKLIRYMLEEDPEKR 262
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
15-263 1.81e-20

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: 91.18  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKA----YAKKDTREVVAIKcvAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd05092     8 VLKWELGEGAFGKVFLAechnLLPEQDKMLVAVK--ALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTR----RILPEKVARVFMQ-----------QLASALQFLHERNISHLDLKPQNILLSslEKPHLKL 155
Cdd:cd05092    86 FEYMRHGDLNRFLRSHgpdaKILDGGEGQAPGQltlgqmlqiasQIASGMVYLASLHFVHRDLATRNCLVG--QGLVVKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 156 ADFGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVI 231
Cdd:cd05092   164 GDFGMSRDIYSTDYYRVGGRTMLpirWMPPESILYRKFTTESDIWSFGVVLWEIFtYGKQPWYQLSNTEAIECITQGREL 243
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 232 ElplRPQL-SLDCRDLLQRLLERDPARRISFKD 263
Cdd:cd05092   244 E---RPRTcPPEVYAIMQGCWQREPQQRHSIKD 273
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
71-269 4.73e-20

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 88.94  E-value: 4.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  71 HPHIVQLKDFQWDNDNIYLIMEFcAGGDLSRFIHT-RRILPEKVARVFMQqLASALQFLHERNISHLDLKPQNILLSSLE 149
Cdd:cd14022    44 HSNINQITEIILGETKAYVFFER-SYGDMHSFVRTcKKLREEEAARLFYQ-IASAVAHCHDGGLVLRDLKLRKFVFKDEE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 150 KPHLKLAD----FGFAQHMSPWDEKHvlrGSPLYMAPEMV-CRRQYDARV-DLWSVGVILYEALFGQPPFASRSFSELEE 223
Cdd:cd14022   122 RTRVKLESledaYILRGHDDSLSDKH---GCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFS 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 224 KIRSNRvIELPlrPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14022   199 KIRRGQ-FNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
19-258 4.86e-20

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: 89.87  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKDTrEVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDfQWDND---NIYLIMEFCA 95
Cdd:cd14049    13 RLGKGGYGKVYKVRNKLDG-QYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHT-AWMEHvqlMLYIQMQLCE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GgDLSRFIHTRRILPE--------------KVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKpHLKLADFGFA 161
Cdd:cd14049    91 L-SLWDWIVERNKRPCeeefksapytpvdvDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDI-HVRIGDFGLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 -----QHMSPWDEKHVLR--------GSPLYMAPEMVCRRQYDARVDLWSVGVILYEaLFgqPPFAsrsfSELE--EKIR 226
Cdd:cd14049   169 cpdilQDGNDSTTMSRLNglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGVILLE-LF--QPFG----TEMEraEVLT 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 227 SNRVIELPlrpqLSLDCR-----DLLQRLLERDPARR 258
Cdd:cd14049   242 QLRNGQIP----KSLCKRwpvqaKYIKLLTSTEPSER 274
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
20-210 5.56e-20

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: 89.62  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKksLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14222     1 LGKGFFGQAIKV-THKATGKVMVMKELIR--CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLsSLEKPHLkLADFGFAQHM----------SPWDE 169
Cdd:cd14222    78 KDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI-KLDKTVV-VADFGLSRLIveekkkpppdKPTTK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 170 KHVLR-----------GSPLYMAPEMVCRRQYDARVDLWSVGVILYEaLFGQ 210
Cdd:cd14222   156 KRTLRkndrkkrytvvGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCE-IIGQ 206
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
4-262 8.45e-20

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: 89.69  E-value: 8.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   4 PSWGLPRlDGFILTERLGSGTYATVYKAYA------KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQ 76
Cdd:cd05098     6 PRWELPR-DRLVLGKPLGEGCFGQVVLAEAigldkdKPNRVTKVAVKML-KSDATEKDLSDLISEMEMMKMIgKHKNIIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  77 LKDFQWDNDNIYLIMEFCAGGDLSRFIHTRR-------ILPEKVARVFMQ---------QLASALQFLHERNISHLDLKP 140
Cdd:cd05098    84 LLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycYNPSHNPEEQLSskdlvscayQVARGMEYLASKKCIHRDLAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 141 QNILLSslEKPHLKLADFGFAQ---HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASR 216
Cdd:cd05098   164 RNVLVT--EDNVMKIADFGLARdihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPYPGV 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 217 SFSELEEKIRSNRVIELP--LRPQLSLDCRDLLQRLlerdPARRISFK 262
Cdd:cd05098   242 PVEELFKLLKEGHRMDKPsnCTNELYMMMRDCWHAV----PSQRPTFK 285
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
20-214 9.18e-20

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: 88.36  E-value: 9.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdtrEVVAIKCV-AKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM-EFCAGG 97
Cdd:cd14064     1 IGSGSFGKVYKGRCRN---KIVAIKRYrANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVtQYVSGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIH-TRRILPEKVARVFMQQLASALQFLHE--RNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLR 174
Cdd:cd14064    78 SLFSLLHeQKRVIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLY--EDGHAVVADFGESRFLQSLDEDNMTK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 175 --GSPLYMAPEMVCR-RQYDARVDLWSVGVILYEALFGQPPFA 214
Cdd:cd14064   156 qpGNLRWMAPEVFTQcTRYSIKADVFSYALCLWELLTGEIPFA 198
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
29-263 9.51e-20

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: 88.60  E-value: 9.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  29 YKAYAKKDTREVVAIKCVAKKSLNKASVenlLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRI 108
Cdd:cd13992    16 YVKKVGVYGGRTVAIKHITFSRTEKRTI---LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 109 lpeKVARVFMQQ----LASALQFLHERNI-SHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWdEKHVLRGSP-----L 178
Cdd:cd13992    93 ---KMDWMFKSSfikdIVKGMNYLHSSSIgYHGRLKSSNCLVDS--RWVVKLTDFGLRNLLEEQ-TNHQLDEDAqhkklL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEMVcrRQYDARV------DLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRviELPLRP-------QLSLDCRD 245
Cdd:cd13992   167 WTAPELL--RGSLLEVrgtqkgDVYSFAIILYEILFRSDPFALEREVAIVEKVISGG--NKPFRPelavlldEFPPRLVL 242
                         250
                  ....*....|....*...
gi 1907200402 246 LLQRLLERDPARRISFKD 263
Cdd:cd13992   243 LVKQCWAENPEKRPSFKQ 260
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
14-264 1.02e-19

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 88.82  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKD--TREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNI---- 87
Cdd:cd05074    11 FTLGRMLGKGEFGSVREAQLKSEdgSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKgrlp 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 --YLIMEFCAGGDLSRFIHTRRI------LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFG 159
Cdd:cd05074    91 ipMVILPFMKHGDLHTFLLMSRIgeepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLN--ENMTVCVADFG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 160 FAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEK-IRSNRVIELP 234
Cdd:cd05074   169 LSKKIYSGDYYRQGCASKLpvkWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGVENSEIYNYlIKGNRLKQPP 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907200402 235 LRPQlslDCRDLLQRLLERDPARRISFKDF 264
Cdd:cd05074   249 DCLE---DVYELMCQCWSPEPKCRPSFQHL 275
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
18-265 1.07e-19

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: 88.31  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKAS---VENLLTEIEILKGIRHPHIVQLKDFQWDNDNIyLIMEFC 94
Cdd:cd05037     5 EHLGQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDHrdiSESFFETASLMSQISHKHLVKLYGVCVADENI-MVQEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVAR-VFMQQLASALQFLHERNISHLDLKPQNILLSSLE----KPHLKLADFGFAQHMSPWDE 169
Cdd:cd05037    84 RYGPLDKYLRRMGNNVPLSWKlQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGldgyPPFIKLSDPGVPITVLSREE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 KhVLRgSPlYMAPEmvCRRQYDARV----DLWSVGVILYEALFGQP-PFASRSFSELEEKIRSNRVIELPLRPQLSLdcr 244
Cdd:cd05037   164 R-VDR-IP-WIAPE--CLRNLQANLtiaaDKWSFGTTLWEICSGGEePLSALSSQEKLQFYEDQHQLPAPDCAELAE--- 235
                         250       260
                  ....*....|....*....|.
gi 1907200402 245 dLLQRLLERDPARRISFKDFF 265
Cdd:cd05037   236 -LIMQCWTYEPTKRPSFRAIL 255
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
18-266 1.16e-19

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 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: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 88.92  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAY----AKKDTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd05091    12 EELGEDRFGKVYKGHlfgtAPGEQTQAVAIKTLKDKA-EGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRilP---------EKVARVFMQ---------QLASALQFLHERNISHLDLKPQNILLssLEKPHLKL 155
Cdd:cd05091    91 CSHGDLHEFLVMRS--PhsdvgstddDKTVKSTLEpadflhivtQIAAGMEYLSSHHVVHKDLATRNVLV--FDKLNVKI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 156 ADFGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVI 231
Cdd:cd05091   167 SDLGLFREVYAADYYKLMGNSLLpirWMSPEAIMYGKFSIDSDIWSYGVVLWEVFsYGLQPYCGYSNQDVIEMIRNRQVL 246
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907200402 232 ELPlrpqlsLDCRDLLQRLL----ERDPARRISFKDFFA 266
Cdd:cd05091   247 PCP------DDCPAWVYTLMlecwNEFPSRRPRFKDIHS 279
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
20-205 1.19e-19

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: 88.47  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKksLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14221     1 LGKGCFGQAIKV-THRETGEVMVMKELIR--FDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARV-FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM-----SPWDEKHVL 173
Cdd:cd14221    78 RGIIKSMDSHYPWSQRVsFAKDIASGMAYLHSMNIIHRDLNSHNCLVR--ENKSVVVADFGLARLMvdektQPEGLRSLK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907200402 174 R----------GSPLYMAPEMVCRRQYDARVDLWSVGVILYE 205
Cdd:cd14221   156 KpdrkkrytvvGNPYWMAPEMINGRSYDEKVDVFSFGIVLCE 197
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
4-262 1.36e-19

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: 88.92  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   4 PSWGLPRlDGFILTERLGSGTYATVYKAYA----KKDTREVVAIKC-VAKKSLNKASVENLLTEIEILKGI-RHPHIVQL 77
Cdd:cd05101    17 PKWEFPR-DKLTLGKPLGEGCFGQVVMAEAvgidKDKPKEAVTVAVkMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  78 KDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEK----VARVFMQ------------QLASALQFLHERNISHLDLKPQ 141
Cdd:cd05101    96 LGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEysydINRVPEEqmtfkdlvsctyQLARGMEYLASQKCIHRDLAAR 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 142 NILLSslEKPHLKLADFGFAQHMSPWDE-KHVLRGS-PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRS 217
Cdd:cd05101   176 NVLVT--ENNVMKIADFGLARDINNIDYyKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLMWEIFtLGGSPYPGIP 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907200402 218 FSELEEKIRSNRVIELPlrpqlsLDCRDLLQRLLeRD-----PARRISFK 262
Cdd:cd05101   254 VEELFKLLKEGHRMDKP------ANCTNELYMMM-RDcwhavPSQRPTFK 296
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
14-268 1.62e-19

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: 88.23  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKA--------YAKKDTREVVAIKCVAKKSLNKASVENLLTeieilkgiRHPHIVQLKDFQWDND 85
Cdd:cd14051     2 FHEVEKIGSGEFGSVYKCinrldgcvYAIKKSKKPVAGSVDEQNALNEVYAHAVLG--------KHPHVVRYYSAWAEDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFI--HTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPH--------- 152
Cdd:cd14051    74 HMIIQNEYCNGGSLADAIseNEKagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVsseeeeedf 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 153 -------------LKLADFGfaqHMSPWDEKHVLRGSPLYMAPEmVCRRQYD--ARVDLWSVGVILYEALFGQP-PfasR 216
Cdd:cd14051   154 egeednpesnevtYKIGDLG---HVTSISNPQVEEGDCRFLANE-ILQENYShlPKADIFALALTVYEAAGGGPlP---K 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 217 SFSELeEKIRSNRvieLPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14051   227 NGDEW-HEIRQGN---LPPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
15-265 2.65e-19

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 87.76  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKA--YAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd05094     8 VLKRELGEGAFGKVFLAecYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIhtRRILPEKVARVFMQ------------------QLASALQFLHERNISHLDLKPQNILLSSleKPHLK 154
Cdd:cd05094    88 YMKHGDLNKFL--RAHGPDAMILVDGQprqakgelglsqmlhiatQIASGMVYLASQHFVHRDLATRNCLVGA--NLLVK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 155 LADFGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRV 230
Cdd:cd05094   164 IGDFGMSRDVYSTDYYRVGGHTMLpirWMPPESIMYRKFTTESDVWSFGVILWEIFtYGKQPWFQLSNTEVIECITQGRV 243
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907200402 231 IElplRPQL-SLDCRDLLQRLLERDPARRISFKDFF 265
Cdd:cd05094   244 LE---RPRVcPKEVYDIMLGCWQREPQQRLNIKEIY 276
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
18-266 2.86e-19

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: 87.01  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREV--VAIKCVAKKSLNKASV-ENLLTEIEILKGIRHPHIVQLKDFQWDNdNIYLIMEFC 94
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSGKViqVAVKCLKSDVLSQPNAmDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDL-SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDEKHVL 173
Cdd:cd05040    80 PLGSLlDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK--VKIGDFGLMRALPQNEDHYVM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 ---RGSPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRviELPLRPQlslDC-RDLL 247
Cdd:cd05040   158 qehRKVPFaWCAPESLKTRKFSHASDVWMFGVTLWEMFtYGEEPWLGLNGSQILEKIDKEG--ERLERPD---DCpQDIY 232
                         250       260
                  ....*....|....*....|....*
gi 1907200402 248 QRLLE---RDPARRISF---KDFFA 266
Cdd:cd05040   233 NVMLQcwaHKPADRPTFvalRDFLP 257
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
20-266 2.98e-19

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: 88.16  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREV---VAIKCVAKKSLNKASVEnLLTEIEILKGIRHPHIVQLKDFQWdNDNIYLIMEFCAG 96
Cdd:cd05108    15 LGSGAFGTVYKGLWIPEGEKVkipVAIKELREATSPKANKE-ILDEAYVMASVDNPHVCRLLGICL-TSTVQLITQLMPF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFI--HTRRILPEKVARvFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWDEKHVLR 174
Cdd:cd05108    93 GCLLDYVreHKDNIGSQYLLN-WCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ--HVKITDFGLAKLLGAEEKEYHAE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 GSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRviELPLRPQLSLDCRDLLQRL 250
Cdd:cd05108   170 GGKVpikWMALESILHRIYTHQSDVWSYGVTVWELMtFGSKPYDGIPASEISSILEKGE--RLPQPPICTIDVYMIMVKC 247
                         250
                  ....*....|....*.
gi 1907200402 251 LERDPARRISFKDFFA 266
Cdd:cd05108   248 WMIDADSRPKFRELII 263
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
14-264 3.11e-19

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: 87.38  E-value: 3.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAY---AKKDTREVVAIKcvakkSLNKASVENLLT---EIEILKGIRHPHIVQLKD--FQWDND 85
Cdd:cd14205     6 LKFLQQLGKGNFGSVEMCRydpLQDNTGEVVAVK-----KLQHSTEEHLRDferEIEILKSLQHDNIVKYKGvcYSAGRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  86 NIYLIMEFCAGGDLSRFI--HTRRILPEKVARvFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQH 163
Cdd:cd14205    81 NLRLIMEYLPYGSLRDYLqkHKERIDHIKLLQ-YTSQICKGMEYLGTKRYIHRDLATRNILVENENR--VKIGDFGLTKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWDEKHVLRG---SPLY-MAPEMVCRRQYDARVDLWSVGVILYEaLFGQPPFASRSFSELEEKIRSNR--------VI 231
Cdd:cd14205   158 LPQDKEYYKVKEpgeSPIFwYAPESLTESKFSVASDVWSFGVVLYE-LFTYIEKSKSPPAEFMRMIGNDKqgqmivfhLI 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907200402 232 ELPLR----PQLSlDCRDLLQRLLER----DPARRISFKDF 264
Cdd:cd14205   237 ELLKNngrlPRPD-GCPDEIYMIMTEcwnnNVNQRPSFRDL 276
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
16-276 3.32e-19

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 87.37  E-value: 3.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTREV-VAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD--FQWDNDNIY---- 88
Cdd:cd05075     4 LGKTLGEGEFGSVMEGQLNQDDSVLkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGvcLQNTESEGYpspv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTRRI------LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQ 162
Cdd:cd05075    84 VILPFMKHGDLHSFLLYSRLgdcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLN--ENMNVCVADFGLSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEKIRS-NRVIELPlrp 237
Cdd:cd05075   162 KIYNGDYYRQGRISKMpvkWIAIESLADRVYTTKSDVWSFGVTMWEiATRGQTPYPGVENSEIYDYLRQgNRLKQPP--- 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 238 qlslDCRDLLQRLLER----DPARRISFKDFFAHPWVDLEHMP 276
Cdd:cd05075   239 ----DCLDGLYELMSScwllNPKDRPSFETLRCELEKILKDLP 277
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-312 3.54e-19

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: 87.24  E-value: 3.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd06619     7 EILGHGNGGTVYKAYHLL-TRRILAVK-VIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFihtrRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLrGSP 177
Cdd:cd06619    85 SLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNT--RGQVKLCDFGVSTQLVNSIAKTYV-GTN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 178 LYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAsrsfseleeKIRSNRVIELPLRpqlsldcrdLLQRLLERDPAR 257
Cdd:cd06619   158 AYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYP---------QIQKNQGSLMPLQ---------LLQCIVDEDPPV 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200402 258 RI--SFKDFFAHPWVDLEHMPSGESLAQARALVVEAVKKDQEGDAAAALSLYCKALD 312
Cdd:cd06619   220 LPvgQFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYNDGNAEVVSMWVCRALE 276
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
27-271 3.83e-19

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: 87.38  E-value: 3.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  27 TVYKAYaKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKG-------IRHPHIVQLKD-FQWDNDNIYLIME--FCAg 96
Cdd:cd14011    11 KIYNGS-KKSTKQEVSVFVFEKKQLEEYSKRDREQILELLKRgvkqltrLRHPRILTVQHpLEESRESLAFATEpvFAS- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 gdLSRFIHTRRILP------------EKVARVFMQQLASALQFLHER-NISHLDLKPQNILLSSleKPHLKLADFGFAQH 163
Cdd:cd14011    89 --LANVLGERDNMPspppelqdyklyDVEIKYGLLQISEALSFLHNDvKLVHGNICPESVVINS--NGEWKLAGFDFCIS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSP----------WDEK--HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYeALF--GQPPFAS-RSFSELEEKIRSN 228
Cdd:cd14011   165 SEQatdqfpyfreYDPNlpPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIY-AIYnkGKPLFDCvNNLLSYKKNSNQL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 229 RVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWVD 271
Cdd:cd14011   244 RQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPFFD 286
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
58-269 4.84e-19

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 86.25  E-value: 4.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  58 NLLTEIEILKGIRHPHIVQLKDFqwdndniylimefcagGDLSRFIHTR-RILPEKVARVFmQQLASALQFLHERNISHL 136
Cdd:cd14023    46 NITGIVEVILGDTKAYVFFEKDF----------------GDMHSYVRSCkRLREEEAARLF-KQIVSAVAHCHQSAIVLG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 137 DLKPQNILLSSLEKPHLKLADFGFAQHMSPWDE----KHvlrGSPLYMAPEMV-CRRQYDAR-VDLWSVGVILYEALFGQ 210
Cdd:cd14023   109 DLKLRKFVFSDEERTQLRLESLEDTHIMKGEDDalsdKH---GCPAYVSPEILnTTGTYSGKsADVWSLGVMLYTLLVGR 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 211 PPFASRSFSELEEKIRSNrviELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14023   186 YPFHDSDPSALFSKIRRG---QFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
18-267 5.59e-19

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror 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: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 86.66  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKA----YAKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd05048    11 EELGEGAFGKVYKGellgPSSEESAISVAIKTL-KENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTR--------RILPEKVARVFMQ--------QLASALQFLHERNISHLDLKPQNILLSslEKPHLKLAD 157
Cdd:cd05048    90 MAHGDLHEFLVRHsphsdvgvSSDDDGTASSLDQsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVG--DGLTVKISD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 158 FGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIEL 233
Cdd:cd05048   168 FGLSRDIYSSDYYRVQSKSLLpvrWMPPEAILYGKFTTESDVWSFGVVLWEIFsYGLQPYYGYSNQEVIEMIRSRQLLPC 247
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907200402 234 PlrpqlsLDCRDLLQRLL----ERDPARRISFKDFFAH 267
Cdd:cd05048   248 P------EDCPARVYSLMvecwHEIPSRRPRFKEIHTR 279
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
20-275 5.68e-19

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 86.90  E-value: 5.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKCVAKKSLNKASVEN-LLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd14026     5 LSRGAFGTVSRA-RHADWRVTVAIKCLKLDSPVGDSERNcLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEkVA-----RVfMQQLASALQFLHERN--ISHLDLKPQNILLSslEKPHLKLADFGfaqhMSPWDEKH 171
Cdd:cd14026    84 LNELLHEKDIYPD-VAwplrlRI-LYEIALGVNYLHNMSppLLHHDLKTQNILLD--GEFHVKIADFG----LSKWRQLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSP----------LYMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPPFasrsfselEEKIRSNRVIELPL--- 235
Cdd:cd14026   156 ISQSRSsksapeggtiIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSRKIPF--------EEVTNPLQIMYSVSqgh 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907200402 236 RPQLSLDC-------RDLLQRLLERDPARRISFKDFFAHPWVDLEHM 275
Cdd:cd14026   228 RPDTGEDSlpvdiphRATLINLIESGWAQNPDERPSFLKCLIELEPV 274
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
14-275 7.16e-19

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: 86.56  E-value: 7.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYA----KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYL 89
Cdd:cd05045     2 LVLGKTLGEGEFGKVVKATAfrlkGRAGYTTVAVKML-KENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIH-TRRILPEKVAR-----------------------VFMQQLASALQFLHERNISHLDLKPQNILL 145
Cdd:cd05045    81 IVEYAKYGSLRSFLReSRKVGPSYLGSdgnrnssyldnpderaltmgdliSFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 146 SSLEKphLKLADFGFAQHMspWDEKHVLRGS----PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFS 219
Cdd:cd05045   161 AEGRK--MKISDFGLSRDV--YEEDSYVKRSkgriPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIAPE 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 220 ELEEKIRSNRVIElplRPQlslDCRDLLQRLLER----DPARRISFKDFFAhpwvDLEHM 275
Cdd:cd05045   237 RLFNLLKTGYRME---RPE---NCSEEMYNLMLTcwkqEPDKRPTFADISK----ELEKM 286
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
71-270 8.08e-19

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 85.32  E-value: 8.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  71 HPHIVQLKDFQWDNDNIYLIMEfCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEK 150
Cdd:cd14024    44 HEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 151 PHLKLADF-----GFAQHMSPWDeKHvlrGSPLYMAPEMV-CRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEE 223
Cdd:cd14024   123 TKLVLVNLedscpLNGDDDSLTD-KH---GCPAYVGPEILsSRRSYSGKaADVWSLGVCLYTMLLGRYPFQDTEPAALFA 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907200402 224 KIRSNrVIELPlrPQLSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14024   199 KIRRG-AFSLP--AWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
20-213 8.25e-19

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: 86.01  E-value: 8.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyaKKDTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14664     1 IGRGGAGTVYKG--VMPNGTLVAVKRLKGEG-TQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKV-----ARVFMQQlASALQFLHER---NISHLDLKPQNILLSSLEKPHLklADFGFAQHMSPwDEKH 171
Cdd:cd14664    78 GELLHSRPESQPPLdwetrQRIALGS-ARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHV--ADFGLAKLMDD-KDSH 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907200402 172 V---LRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14664   154 VmssVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
8-262 8.80e-19

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: 85.70  E-value: 8.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   8 LPRLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCvakkslnKASVENLLTEIEILKGIRHPHIVQLKDFQWDNdNI 87
Cdd:cd05083     2 LLNLQKLTLGEIIGEGEFGAVLQGEYMGQKVAVKNIKC-------DVTAQAFLEETAVMTKLQHKNLVRLLGVILHN-GL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  88 YLIMEFCAGGDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMS 165
Cdd:cd05083    74 YIVMELMSKGNLVNFLRSRgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVS--EDGVAKISDFGLAKVGS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 166 PWDEKHVLrgsPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrPQLSLDC 243
Cdd:cd05083   152 MGVDNSRL---PVkWTAPEALKNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSVKEVKEAVEKGYRMEPP--EGCPPDV 226
                         250
                  ....*....|....*....
gi 1907200402 244 RDLLQRLLERDPARRISFK 262
Cdd:cd05083   227 YSIMTSCWEAEPGKRPSFK 245
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
6-211 1.09e-18

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: 86.00  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYA----KKDTREVVAIKCV---AKKSLNKAsvenLLTEIEILKGI-RHPHIVQL 77
Cdd:cd05054     2 WEFPR-DRLKLGKPLGRGAFGKVIQASAfgidKSATCRTVAVKMLkegATASEHKA----LMTELKILIHIgHHLNVVNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  78 -KDFQWDNDNIYLIMEFCAGGDLSRFIHTRR--ILPEKVARV-----------FMQ-------------QLASALQFLHE 130
Cdd:cd05054    77 lGACTKPGGPLMVIVEFCKFGNLSNYLRSKReeFVPYRDKGArdveeeedddeLYKepltledlicysfQVARGMEFLAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 131 RNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYE- 205
Cdd:cd05054   157 RKCIHRDLAARNILLS--ENNVVKICDFGLARDIYK-DPDYVRKGDarlPLkWMAPESIFDKVYTTQSDVWSFGVLLWEi 233

                  ....*..
gi 1907200402 206 -ALFGQP 211
Cdd:cd05054   234 fSLGASP 240
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-262 1.10e-18

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: 85.19  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLNKasvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd05059     8 FLKELGSGQFGVVHLGKWRGKID--VAIKMIKEGSMSE---DDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFM-QQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFA------QHMSPWD 168
Cdd:cd05059    83 NGCLLNYLRERRGKFQTEQLLEMcKDVCEAMEYLESNGFIHRDLAARNCLVG--EQNVVKVSDFGLAryvlddEYTSSVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVLRGSPlymaPEMVCRRQYDARVDLWSVGVILYEaLF--GQPPFASRSFSELEEKIrsNRVIELPlRPQL-SLDCRD 245
Cdd:cd05059   161 TKFPVKWSP----PEVFMYSKFSSKSDVWSFGVLMWE-VFseGKMPYERFSNSEVVEHI--SQGYRLY-RPHLaPTEVYT 232
                         250
                  ....*....|....*..
gi 1907200402 246 LLQRLLERDPARRISFK 262
Cdd:cd05059   233 IMYSCWHEKPEERPTFK 249
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
20-266 1.47e-18

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 85.89  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREV---VAIKCVAKKSLNKASVEnLLTEIEILKGIRHPHIVQLKDFQWdNDNIYLIMEFCAG 96
Cdd:cd05110    15 LGSGAFGTVYKGIWVPEGETVkipVAIKILNETTGPKANVE-FMDEALIMASMDHPHLVRLLGVCL-SPTIQLVTQLMPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLRG 175
Cdd:cd05110    93 GCLLDYVHEHKDnIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKS--PNHVKITDFGLARLLEGDEKEYNADG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 176 SPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPF---ASRSFSELEEKIRsnrviELPLRPQLSLDCRDLLQ 248
Cdd:cd05110   171 GKMpikWMALECIHYRKFTHQSDVWSYGVTIWELMtFGGKPYdgiPTREIPDLLEKGE-----RLPQPPICTIDVYMVMV 245
                         250
                  ....*....|....*...
gi 1907200402 249 RLLERDPARRISFKDFFA 266
Cdd:cd05110   246 KCWMIDADSRPKFKELAA 263
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
20-205 1.55e-18

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: 84.83  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAyAKKDTREVVAIKcVAKKSLNKAsveNLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14155     1 IGSGFFSEVYKV-RHRTSGQVMALK-MNTLSSNRA---NMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKL-ADFGFAQHMSPWD---EKHVLRG 175
Cdd:cd14155    76 EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVvGDFGLAEKIPDYSdgkEKLAVVG 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907200402 176 SPLYMAPEMVCRRQYDARVDLWSVGVILYE 205
Cdd:cd14155   156 SPYWMAPEVLRGEPYNEKADVFSYGIILCE 185
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
36-266 2.10e-18

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 84.98  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  36 DTREVVAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDF-QWDNDN-IYLIMEFCAGGDLSRFihtrriLPEKV 113
Cdd:cd05079    31 NTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGIcTEDGGNgIKLIMEFLPSGSLKEY------LPRNK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 114 ARV-FMQQLASALQ------FLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVL---RGSPLY-MAP 182
Cdd:cd05079   104 NKInLKQQLKYAVQickgmdYLGSRQYVHRDLAARNVLVES--EHQVKIGDFGLTKAIETDKEYYTVkddLDSPVFwYAP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 183 EMVCRRQYDARVDLWSVGVILYEALfgqpPFASRSFSELEEKI-------------RSNRVIE----LPLRPQLSLDCRD 245
Cdd:cd05079   182 ECLIQSKFYIASDVWSFGVTLYELL----TYCDSESSPMTLFLkmigpthgqmtvtRLVRVLEegkrLPRPPNCPEEVYQ 257
                         250       260
                  ....*....|....*....|.
gi 1907200402 246 LLQRLLERDPARRISFKDFFA 266
Cdd:cd05079   258 LMRKCWEFQPSKRTTFQNLIE 278
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
6-264 2.21e-18

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 84.65  E-value: 2.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRLDgFILTERLGSGTYATVYKAyakkDTREV-VAIKCVAkkslNKASVENLLTEIEILKGIRHPHIVQLKD-FQWD 83
Cdd:cd05082     1 WALNMKE-LKLLQTIGKGEFGDVMLG----DYRGNkVAVKCIK----NDATAQAFLAEASVMTQLRHSNLVQLLGvIVEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  84 NDNIYLIMEFCAGGDLSRFIHTR--RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFA 161
Cdd:cd05082    72 KGGLYIVTEYMAKGSLVDYLRSRgrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVS--EDNVAKVSDFGLT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 162 QHMSPWDEKHVLrgsPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLR-PQ 238
Cdd:cd05082   150 KEASSTQDTGKL---PVkWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPRVEKGYKMDAPDGcPP 226
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 239 LsldCRDLLQRLLERDPARRISFKDF 264
Cdd:cd05082   227 A---VYDVMKNCWHLDAAMRPSFLQL 249
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
20-159 4.79e-18

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: 80.18  E-value: 4.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTrEVVAIKCVakKSLNKASVENLLTEIEILK--GIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd13968     1 MGEGASAKVFWAEGECTT-IGVAVKIG--DDVNNEEGEDLESEMDILRrlKGLELNIPKVLVTEDVDGPNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402  98 DLSRFIhTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFG 159
Cdd:cd13968    78 TLIAYT-QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS--EDGNVKLIDFG 136
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
8-223 4.99e-18

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 83.98  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   8 LPRlDGFILTERLGSGTYATVYKAYAKKDTREVVAIKcVAKKSL----NKASVENLLTEIEILKGIRHPHIVQLKDFQWD 83
Cdd:cd05036     3 VPR-KNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQ-VAVKTLpelcSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  84 NDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFM-------QQLASALQFLHERNISHLDLKPQNILLSSLEKPHL-KL 155
Cdd:cd05036    81 RLPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMldllqlaQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVaKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 156 ADFGFAQHMspWDEKHVLRGS----PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEE 223
Cdd:cd05036   161 GDFGMARDI--YRADYYRKGGkamlPVkWMPPEAFLDGIFTSKTDVWSFGVLLWEIFsLGYMPYPGKSNQEVME 232
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
19-213 1.13e-17

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 82.93  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKDTrevVAIKCVAkkSLNKASVENLL----TEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd14158    22 KLGEGGFGVVFKGYINDKN---VAVKKLA--AMVDISTEDLTkqfeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRILPEKVARV---FMQQLASALQFLHERNISHLDLKPQNILLSSLEKPhlKLADFGFAQhMSPWDEKH 171
Cdd:cd14158    97 PNGSLLDRLACLNDTPPLSWHMrckIAQGTANGINYLHENNHIHRDIKSANILLDETFVP--KISDFGLAR-ASEKFSQT 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 172 VLR----GSPLYMAPEMVcRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14158   174 IMTerivGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPPV 218
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
19-262 1.20e-17

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: 82.27  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQwDNDNIYLIMEFCAGGD 98
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGTTK--VAIKTLKPGTM---SPEAFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFI------HTRriLPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHV 172
Cdd:cd14203    76 LLDFLkdgegkYLK--LPQLVD--MAAQIASGMAYIERMNYIHRDLRAANILVG--DNLVCKIADFGLARLIED-NEYTA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGS--PL-YMAPEMVCRRQYDARVDLWSVGVILYEALF-GQPPFASRSFSELEEKIrsNRVIELPLRPQLSLDCRDLLQ 248
Cdd:cd14203   149 RQGAkfPIkWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV--ERGYRMPCPPGCPESLHELMC 226
                         250
                  ....*....|....
gi 1907200402 249 RLLERDPARRISFK 262
Cdd:cd14203   227 QCWRKDPEERPTFE 240
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
20-277 1.25e-17

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 83.98  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQL----------KDFQwdndNIYL 89
Cdd:cd07874    25 IGSGAQGIVCAAYDAVLDRNV-AIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLlnvftpqkslEEFQ----DVYL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFcAGGDLSRFIHTRriLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ------H 163
Cdd:cd07874   100 VMEL-MDANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS--DCTLKILDFGLARtagtsfM 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 164 MSPWdekHVLRgspLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF-------------------SELEEK 224
Cdd:cd07874   175 MTPY---VVTR---YYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYidqwnkvieqlgtpcpefmKKLQPT 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 225 IRS---NRVIELPLR-PQLSLD----------------CRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPS 277
Cdd:cd07874   249 VRNyveNRPKYAGLTfPKLFPDslfpadsehnklkasqARDLLSKMLVIDPAKRISVDEALQHPYINVWYDPA 321
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
20-211 1.70e-17

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 83.15  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYaKKDTREVVAIKCV-----------------AKKSLNKASVENLLTEIEILKGIRHPHIVqlkdFQW 82
Cdd:cd14229     8 LGRGTFGQVVKCW-KRGTNEIVAVKILknhpsyarqgqievgilARLSNENADEFNFVRAYECFQHRNHTCLV----FEM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  83 DNDNIYlimEFCAGGDLSRfihtrriLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL-SSLEKPH-LKLADFGF 160
Cdd:cd14229    83 LEQNLY---DFLKQNKFSP-------LPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvDPVRQPYrVKVIDFGS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 161 AQHMSPWDEKHVLRgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQP 211
Cdd:cd14229   153 ASHVSKTVCSTYLQ-SRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 202
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
20-264 1.72e-17

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: 82.38  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREV---VAIKCVAKKSLNKASVEnLLTEIEILKGIRHPHIVQLKDFQWdNDNIYLIMEFCAG 96
Cdd:cd05109    15 LGSGAFGTVYKGIWIPDGENVkipVAIKVLRENTSPKANKE-ILDEAYVMAGVGSPYVCRLLGICL-TSTVQLVTQLMPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRR-ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPwDEK--HVL 173
Cdd:cd05109    93 GCLLDYVRENKdRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKS--PNHVKITDFGLARLLDI-DETeyHAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 RGS-PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRviELPLRPQLSLDCRDLLQRL 250
Cdd:cd05109   170 GGKvPIkWMALESILHRRFTHQSDVWSYGVTVWELMtFGAKPYDGIPAREIPDLLEKGE--RLPQPPICTIDVYMIMVKC 247
                         250
                  ....*....|....
gi 1907200402 251 LERDPARRISFKDF 264
Cdd:cd05109   248 WMIDSECRPRFREL 261
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
18-270 1.77e-17

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 83.21  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKdTREVVAIKCV--AKKSLNKAsvenlLTEIEILKGIRHP------HIVQLKDFQWDNDNIYL 89
Cdd:cd14225    49 EVIGKGSFGQVVKALDHK-TNEHVAIKIIrnKKRFHHQA-----LVEVKILDALRRKdrdnshNVIHMKEYFYFRNHLCI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFcAGGDLSRFI--HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGfaqhMSPW 167
Cdd:cd14225   123 TFEL-LGMNLYELIkkNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKVIDFG----SSCY 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLR--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEE--------KIRSNRVIELPLRP 237
Cdd:cd14225   198 EHQRVYTyiQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGE--NEVEQlacimevlGLPPPELIENAQRR 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200402 238 QLSLDCR---------------------------------DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd14225   276 RLFFDSKgnprcitnskgkkrrpnskdlasalktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
5-262 1.90e-17

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: 82.04  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQwDN 84
Cdd:cd05071     3 AWEIPR-ESLRLEVKLGQGCFGEVWMGTWNGTTR--VAIKTLKPGTM---SPEAFLQEAQVMKKLRHEKLVQLYAVV-SE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIH----TRRILPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGF 160
Cdd:cd05071    76 EPIYIVTEYMSKGSLLDFLKgemgKYLRLPQLVD--MAAQIASGMAYVERMNYVHRDLRAANILVG--ENLVCKVADFGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSpwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEKIRsnRVIELPL 235
Cdd:cd05071   152 ARLIE--DNEYTARQGakfPIkWTAPEAALYGRFTIKSDVWSFGILLTElTTKGRVPYPGMVNREVLDQVE--RGYRMPC 227
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 236 RPQLSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05071   228 PPECPESLHDLMCQCWRKEPEERPTFE 254
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
20-213 1.99e-17

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 81.75  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKA-YAKKDTREvvaIKCvAKKSLNK----ASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI-MEF 93
Cdd:cd05058     3 IGKGHFGCVYHGtLIDSDGQK---IHC-AVKSLNRitdiEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVvLPY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPE-KVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHM------SP 166
Cdd:cd05058    79 MKHGDLRNFIRSETHNPTvKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLD--ESFTVKVADFGLARDIydkeyySV 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200402 167 WDEKHVlRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALF-GQPPF 213
Cdd:cd05058   157 HNHTGA-KLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPY 203
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
18-268 2.03e-17

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: 81.99  E-value: 2.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTReVVAIKCVAKKSLNKASVENLLTEI---EILKgiRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd14138    11 EKIGSGEFGSVFKCVKRLDGC-IYAIKRSKKPLAGSVDEQNALREVyahAVLG--QHSHVVRYYSAWAEDDHMLIQNEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFI----HTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPH-----------------L 153
Cdd:cd14138    88 NGGSLADAIsenyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNaaseegdedewasnkviF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 154 KLADFGfaqHMSPWDEKHVLRGSPLYMAPEmVCRRQYD--ARVDLWSVGVILYEALfGQPPFASRsfSELEEKIRSNRvi 231
Cdd:cd14138   168 KIGDLG---HVTRVSSPQVEEGDSRFLANE-VLQENYThlPKADIFALALTVVCAA-GAEPLPTN--GDQWHEIRQGK-- 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907200402 232 eLPLRPQ-LSLDCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd14138   239 -LPRIPQvLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
5-262 2.06e-17

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: 82.04  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   5 SWGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQwDN 84
Cdd:cd05070     3 VWEIPR-ESLQLIKRLGNGQFGEVWMGTWNGNTK--VAIKTLKPGTM---SPESFLEEAQIMKKLKHDKLVQLYAVV-SE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTRRILPEKVARV--FMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ 162
Cdd:cd05070    76 EPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLvdMAAQVAAGMAYIERMNYIHRDLRSANILVGN--GLICKIADFGLAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPwDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEALF-GQPPFASRSFSELEEKIRsnRVIELPLRPQ 238
Cdd:cd05070   154 LIED-NEYTARQGAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVE--RGYRMPCPQD 230
                         250       260
                  ....*....|....*....|....
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05070   231 CPISLHELMIHCWKKDPEERPTFE 254
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
20-261 2.37e-17

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: 81.63  E-value: 2.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEIL-KGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARV----------------FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQ 162
Cdd:cd05047    83 LLDFLRKSRVLETDPAFAianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVG--ENYVAKIADFGLSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLrpQLSL 241
Cdd:cd05047   161 GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQGYRLEKPL--NCDD 238
                         250       260
                  ....*....|....*....|
gi 1907200402 242 DCRDLLQRLLERDPARRISF 261
Cdd:cd05047   239 EVYDLMRQCWREKPYERPSF 258
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
103-260 2.85e-17

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 82.07  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 103 IHTRRiLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKpHLKLADFGFAQHMSpwDEKHVL---RGSPLY 179
Cdd:cd13974   124 IREKR-LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR-KITITNFCLGKHLV--SEDDLLkdqRGSPAY 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 180 MAPEMVCRRQYDAR-VDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIeLPLRPQLSLDCRDLLQRLLERDPARR 258
Cdd:cd13974   200 ISPDVLSGKPYLGKpSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYT-IPEDGRVSENTVCLIRKLLVLNPQKR 278

                  ..
gi 1907200402 259 IS 260
Cdd:cd13974   279 LT 280
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
16-276 3.26e-17

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 81.24  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYAKKDtrevVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd14063     4 IKEVIGKGRFGRVHRGRWHGD----VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRI-LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILlssLEKPHLKLADFGF---AQHMSPWDEKH 171
Cdd:cd14063    80 GRTLYSLIHERKEkFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIF---LENGRVVITDFGLfslSGLLQPGRRED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VL---RGSPLYMAPEMV------CRRQ----YDARVDLWSVGVILYEALFGQPPFASRSfseLEEKIRSNRVIELPLRPQ 238
Cdd:cd14063   157 TLvipNGWLCYLAPEIIralspdLDFEeslpFTKASDVYAFGTVWYELLAGRWPFKEQP---AESIIWQVGCGKKQSLSQ 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907200402 239 LSL--DCRDLLQRLLERDPARRISFKDFFAHpwvdLEHMP 276
Cdd:cd14063   234 LDIgrEVKDILMQCWAYDPEKRPTFSDLLRM----LERLP 269
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
30-277 3.32e-17

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: 82.77  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  30 KAYAKKDTREVVAIKCVAKKslNKASVENLLTEIEilkgirhphivQLKDFQwdndNIYLIMEFcAGGDLSRFIHTRriL 109
Cdd:cd07876    61 QTHAKRAYRELVLLKCVNHK--NIISLLNVFTPQK-----------SLEEFQ----DVYLVMEL-MDANLCQVIHME--L 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 110 PEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQ------HMSPWdekHVLRgspLYMAPE 183
Cdd:cd07876   121 DHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS--DCTLKILDFGLARtactnfMMTPY---VVTR---YYRAPE 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 184 MVCRRQYDARVDLWSVGVILYEALFGQPPF-------------------ASRSFSELEEKIRsNRVIELPLRPQLSLD-- 242
Cdd:cd07876   193 VILGMGYKENVDIWSVGCIMGELVKGSVIFqgtdhidqwnkvieqlgtpSAEFMNRLQPTVR-NYVENRPQYPGISFEel 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 243 -------------------CRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPS 277
Cdd:cd07876   272 fpdwifpseserdklktsqARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPA 325
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
62-212 3.34e-17

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 81.55  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  62 EIEILKGIRHPHIVQLKDFqwdndNIY---LIMEFCAGGDL----------SRFIHTRRILPEKVArvfmQQLASALQFL 128
Cdd:cd14067    60 EASMLHSLQHPCIVYLIGI-----SIHplcFALELAPLGSLntvleenhkgSSFMPLGHMLTFKIA----YQIAAGLAYL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 129 HERNISHLDLKPQNILLSSLE-KPHL--KLADFGFAQHmSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYE 205
Cdd:cd14067   131 HKKNIIFCDLKSDNILVWSLDvQEHIniKLSDYGISRQ-SFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYE 209

                  ....*..
gi 1907200402 206 ALFGQPP 212
Cdd:cd14067   210 LLSGQRP 216
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
20-207 3.94e-17

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: 81.03  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAikcvaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVV-----KIYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIhTRRILP----EKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLK---LADFGFAQHM------SP 166
Cdd:cd14156    76 EELL-AREELPlswrEKVE--LACDISRGMVYLHSKNIYHRDLNSKNCLIR--VTPRGReavVTDFGLAREVgempanDP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907200402 167 wDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEAL 207
Cdd:cd14156   151 -ERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
15-263 4.29e-17

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: 81.24  E-value: 4.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  15 ILTERLGSGTYATVYKA--YAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:cd05093     8 VLKRELGEGAFGKVFLAecYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGGDLSRFIhtRRILPEKVARV---------------FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLAD 157
Cdd:cd05093    88 YMKHGDLNKFL--RAHGPDAVLMAegnrpaeltqsqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVG--ENLLVKIGD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 158 FGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIEL 233
Cdd:cd05093   164 FGMSRDVYSTDYYRVGGHTMLpirWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQGRVLQR 243
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907200402 234 PLR-PQlslDCRDLLQRLLERDPARRISFKD 263
Cdd:cd05093   244 PRTcPK---EVYDLMLGCWQREPHMRLNIKE 271
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
21-263 5.14e-17

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: 80.39  E-value: 5.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  21 GSGTYATVYKAYAKKDTREVvaikcvAKKSLNKASvenllTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLS 100
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEV------AVKKLLKIE-----KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 101 RFIHTRRILPEKVARV--FMQQLASALQFLHER---NISHLDLKPQNILLSSleKPHLKLADFGFAQ------HMSpwde 169
Cdd:cd14060    71 DYLNSNESEEMDMDQImtWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAA--DGVLKICDFGASRfhshttHMS---- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 170 khvLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASrsfseLEEKIRSNRVIELPLRPQLSLDC----RD 245
Cdd:cd14060   145 ---LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG-----LEGLQVAWLVVEKNERPTIPSSCprsfAE 216
                         250
                  ....*....|....*...
gi 1907200402 246 LLQRLLERDPARRISFKD 263
Cdd:cd14060   217 LMRRCWEADVKERPSFKQ 234
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
20-268 6.71e-17

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 80.87  E-value: 6.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKaSVENLLTEIEILKGIRH-PHIVQLKDFQWDNDNIYLIMEFCaggD 98
Cdd:cd06616    14 IGRGAFGTVNKMLHKP-SGTIMAVKRIRSTVDEK-EQKRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWICMELM---D 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LS-----RFIH--TRRILPEKVARVFMQQLASALQFLHER-NISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd06616    89 ISldkfyKYVYevLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLD--RNGNIKLCDFGISGQLVDSIAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HVLRGSPLYMAPEMV----CRRQYDARVDLWSVGVILYEALFGQPPFasRSFSELEEKIRSNRVIELP-LRP----QLSL 241
Cdd:cd06616   167 TRDAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPY--PKWNSVFDQLTQVVKGDPPiLSNseerEFSP 244
                         250       260
                  ....*....|....*....|....*..
gi 1907200402 242 DCRDLLQRLLERDPARRISFKDFFAHP 268
Cdd:cd06616   245 SFVNFVNLCLIKDESKRPKYKELLKHP 271
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
281-346 7.90e-17

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


Pssm-ID: 461228  Cd Length: 66  Bit Score: 74.50  E-value: 7.90e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200402 281 LAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKA 346
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
14-261 8.47e-17

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 80.27  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  14 FILTERLGSGTYATVYKAYAKKDTREV--VAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKD--FQWDNDNIY- 88
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDDGSQlkVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGvcFTASDLNKPp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 ---LIMEFCAGGDLSRFIHTRRI------LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFG 159
Cdd:cd05035    81 spmVILPFMKHGDLHSYLLYSRLgglpekLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLD--ENMTVCVADFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 160 FAQHMSPWD---EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEKIRSNRVIELPl 235
Cdd:cd05035   159 LSRKIYSGDyyrQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEiATRGQTPYPGVENHEIYDYLRNGNRLKQP- 237
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 236 rPQLSLDCRDLLQRLLERDPARRISF 261
Cdd:cd05035   238 -EDCLDEVYFLMYFCWTVDPKDRPTF 262
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
20-262 8.63e-17

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: 80.33  E-value: 8.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATV----YKAyAKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWD--NDNIYLIMEF 93
Cdd:cd05080    12 LGEGHFGKVslycYDP-TNDGTGEMVAVKAL-KADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQLIMEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVArVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVL 173
Cdd:cd05080    90 VPLGSLRDYLPKHSIGLAQLL-LFAQQICEGMAYLHSQHYIHRDLAARNVLLDN--DRLVKIGDFGLAKAVPEGHEYYRV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 174 R---GSPLY-MAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFAS--RSFSEL----EEKIRSNRVIE-------LPLR 236
Cdd:cd05080   167 RedgDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSppTKFLEMigiaQGQMTVVRLIEllergerLPCP 246
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 237 PQLSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05080   247 DKCPQEVYHLMKNCWETEASFRPTFE 272
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
20-209 8.69e-17

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: 79.61  E-value: 8.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKA-YAKKDtrevvaikcVAKKSLNK-ASVENLLTEIEILKGIRHPHIVQLkdFQWDNDNIYLIMEFCAGG 97
Cdd:cd14068     2 LGDGGFGSVYRAvYRGED---------VAVKIFNKhTSFRLLRQELVVLSHLHHPSLVAL--LAAGTAPRMLVMELAPKG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSR-FIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLeKPH----LKLADFGFAQHMSPWDEKhV 172
Cdd:cd14068    71 SLDAlLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTL-YPNcaiiAKIADYGIAQYCCRMGIK-T 148
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907200402 173 LRGSPLYMAPEmVCRRQ--YDARVDLWSVGVILYEALFG 209
Cdd:cd14068   149 SEGTPGFRAPE-VARGNviYNQQADVYSFGLLLYDILTC 186
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
19-269 1.32e-16

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: 80.50  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAK--KDTREVvAIKCVAKKSLNKASVEnlltEIEILKGIRHPHIVQLKD--FQWDNDNIYLIMEFc 94
Cdd:cd07867     9 KVGRGTYGHVYKAKRKdgKDEKEY-ALKQIEGTGISMSACR----EIALLRELKHPNVIALQKvfLSHSDRKVWLLFDY- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRI---------LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQ- 162
Cdd:cd07867    83 AEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgEGPERGRVKIADMGFARl 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 ---HMSPWDEKHVLRGSPLYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASRsfselEEKIRSNR--------- 229
Cdd:cd07867   163 fnsPLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCR-----QEDIKTSNpfhhdqldr 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 230 ---------------VIELPLRPQLSLDCRD-------------------------LLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd07867   238 ifsvmgfpadkdwedIRKMPEYPTLQKDFRRttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 317
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
12-269 1.37e-16

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 80.31  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYAKKDTREVvAIKCVakKSlnkASV--ENLLTEIEILKGIR-----HP---HIVQLKD-F 80
Cdd:cd14136    10 GRYHVVRKLGWGHFSTVWLCWDLQNKRFV-ALKVV--KS---AQHytEAALDEIKLLKCVReadpkDPgreHVVQLLDdF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QWDNDN-IYLIMEFCAGGD--LSRFIHTR-RILPEKVARVFMQQLASALQFLHER-NISHLDLKPQNILLSSLeKPHLKL 155
Cdd:cd14136    84 KHTGPNgTHVCMVFEVLGPnlLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCIS-KIEVKI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 156 ADFGFAQhmspWDEKHV-----LRGsplYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS------------- 217
Cdd:cd14136   163 ADLGNAC----WTDKHFtediqTRQ---YRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDPHSgedysrdedhlal 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 218 FSEL----------------------EEKIRSNRVIELPL----------RPQLSLDCRDLLQRLLERDPARRISFKDFF 265
Cdd:cd14136   236 IIELlgriprsiilsgkysreffnrkGELRHISKLKPWPLedvlvekykwSKEEAKEFASFLLPMLEYDPEKRATAAQCL 315

                  ....
gi 1907200402 266 AHPW 269
Cdd:cd14136   316 QHPW 319
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
2-262 1.65e-16

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: 80.45  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   2 AGPSWGLPRlDGFILTERLGSGTYATVYKAYA------KKDTREVVAIKCVAKKSLNKaSVENLLTEIEILKGI-RHPHI 74
Cdd:cd05100     3 ADPKWELSR-TRLTLGKPLGEGCFGQVVMAEAigidkdKPNKPVTVAVKMLKDDATDK-DLSDLVSEMEMMKMIgKHKNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  75 VQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRI-----------LPEK-------VARVFmqQLASALQFLHERNISHL 136
Cdd:cd05100    81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPpgmdysfdtckLPEEqltfkdlVSCAY--QVARGMEYLASQKCIHR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 137 DLKPQNILLSslEKPHLKLADFGFAQHMSPWDE-KHVLRGS-PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPP 212
Cdd:cd05100   159 DLAARNVLVT--EDNVMKIADFGLARDVHNIDYyKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907200402 213 FASRSFSELEEKIRSNRVIELPlrPQLSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05100   237 YPGIPVEELFKLLKEGHRMDKP--ANCTHELYMIMRECWHAVPSQRPTFK 284
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
20-263 1.78e-16

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 79.08  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKkdTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd14027     1 LDSGGFGKVSLCFHR--TQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRRIlPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQhMSPW----DEKHVLR- 174
Cdd:cd14027    79 MHVLKKVSV-PLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVD--NDFHIKIADLGLAS-FKMWskltKEEHNEQr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 175 ----------GSPLYMAPEMVcrRQYDAR----VDLWSVGVILYEALFGQPPFA-SRSFSELEEKIRS-NRVIELPLRPQ 238
Cdd:cd14027   155 evdgtakknaGTLYYMAPEHL--NDVNAKptekSDVYSFAIVLWAIFANKEPYEnAINEDQIIMCIKSgNRPDVDDITEY 232
                         250       260
                  ....*....|....*....|....*
gi 1907200402 239 LSLDCRDLLQRLLERDPARRISFKD 263
Cdd:cd14027   233 CPREIIDLMKLCWEANPEARPTFPG 257
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
47-270 1.95e-16

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: 79.79  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  47 AKKSLN---KASVEN-LLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKV-ARVFMQQL 121
Cdd:cd06615    30 ARKLIHleiKPAIRNqIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPENIlGKISIAVL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 122 aSALQFLHE-RNISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWDEKHVlrGSPLYMAPEMVCRRQYDARVDLWSV 199
Cdd:cd06615   110 -RGLTYLREkHKIMHRDVKPSNILVNS--RGEIKLCDFGVSgQLIDSMANSFV--GTRSYMSPERLQGTHYTVQSDIWSL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 200 GVILYEALFGQPPFASRSFSELE------------------------EKIRSNRVIEL---------PLRPQ--LSLDCR 244
Cdd:cd06615   185 GLSLVEMAIGRYPIPPPDAKELEamfgrpvsegeakeshrpvsghppDSPRPMAIFELldyivneppPKLPSgaFSDEFQ 264
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 245 DLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06615   265 DFVDKCLKKNPKERADLKELTKHPFI 290
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-270 2.21e-16

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: 79.71  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSlnKASVEN-LLTEIEILKGIRHPHIVQLKDFQWDNDNIYLI 90
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKV-SHKPSGLVMARKLIHLEI--KPAIRNqIIRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  91 MEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN-ISHLDLKPQNILLSSleKPHLKLADFGFA-QHMSPWD 168
Cdd:cd06650    82 MEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNS--RGEIKLCDFGVSgQLIDSMA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 EKHVlrGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELE---------EKIRSNRVIELPLRPQ- 238
Cdd:cd06650   160 NSFV--GTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELElmfgcqvegDAAETPPRPRTPGRPLs 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 239 -------------------------------LSLDCRDLLQRLLERDPARRISFKDFFAHPWV 270
Cdd:cd06650   238 sygmdsrppmaifelldyivnepppklpsgvFSLEFQDFVNKCLIKNPAERADLKQLMVHAFI 300
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
20-269 2.34e-16

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 79.67  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVakKSLNKASvENLLTEIEILKGIRHPH------IVQLKDfqWDNDNIYLIMEF 93
Cdd:cd14214    21 LGEGTFGKVVECLDHARGKSQVALKII--RNVGKYR-EAARLEINVLKKIKEKDkenkflCVLMSD--WFNFHGHMCIAF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 -CAGGDLSRFIHTRRILPEKVARV--FMQQLASALQFLHERNISHLDLKPQNILL------------SSLEKPHLK---- 154
Cdd:cd14214    96 eLLGKNTFEFLKENNFQPYPLPHIrhMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlynesKSCEEKSVKntsi 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 155 -LADFGFAQhmspWDEKH--VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSE---LEEKI--- 225
Cdd:cd14214   176 rVADFGSAT----FDHEHhtTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREhlvMMEKIlgp 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 226 --------------------------RSNRVIE---LPLRPQLSLDCR------DLLQRLLERDPARRISFKDFFAHPW 269
Cdd:cd14214   252 ipshmihrtrkqkyfykgslvwdensSDGRYVSencKPLMSYMLGDSLehtqlfDLLRRMLEFDPALRITLKEALLHPF 330
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
20-263 2.50e-16

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 79.05  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVAKKSLNKASVENLLT----EIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd05046    13 LGRGEFGEVFLAKAKG-IEEEGGETLVLVKALQKTKDENLQSefrrELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKV--------ARVFM-QQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSP 166
Cdd:cd05046    92 LGDLKQFLRATKSKDEKLkppplstkQKVALcTQIALGMDHLSNARFVHRDLAARNCLVSSQRE--VKVSLLSLSKDVYN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 167 wDEKHVLRGS--PL-YMAPEMVCRRQYDARVDLWSVGVILYEaLF--GQPPFASRSFSELEEKIRSNRvIELPLRPQLSL 241
Cdd:cd05046   170 -SEYYKLRNAliPLrWLAPEAVQEDDFSTKSDVWSFGVLMWE-VFtqGELPFYGLSDEEVLNRLQAGK-LELPVPEGCPS 246
                         250       260
                  ....*....|....*....|..
gi 1907200402 242 DCRDLLQRLLERDPARRISFKD 263
Cdd:cd05046   247 RLYKLMTRCWAVNPKDRPSFSE 268
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
20-262 3.26e-16

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: 78.89  E-value: 3.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEIL-KGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05089    10 IGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLcKLGHHPNIINLLGACENRGYLYIAIEYAPYGN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARV----------------FMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQ 162
Cdd:cd05089    90 LLDFLRKSRVLETDPAFAkehgtastltsqqllqFASDVAKGMQYLSEKQFIHRDLAARNVLVG--ENLVSKIADFGLSR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrpqlsL 241
Cdd:cd05089   168 GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYEKLPQGYRMEKP------R 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907200402 242 DCRDLLQRLL---------ERDPARRISFK 262
Cdd:cd05089   242 NCDDEVYELMrqcwrdrpyERPPFSQISVQ 271
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
20-263 3.63e-16

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: 78.09  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAikcVAKKSLNKASVE----NLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd05063    13 IGAGEFGEVFRGILKMPGRKEVA---VAIKTLKPGYTEkqrqDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFI--HTRRILPEKVARVfMQQLASALQFLHERNISHLDLKPQNILL-SSLEkphLKLADFGFAQHMSPWDE-KH 171
Cdd:cd05063    90 NGALDKYLrdHDGEFSSYQLVGM-LRGIAAGMKYLSDMNYVHRDLAARNILVnSNLE---CKVSDFGLSRVLEDDPEgTY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIrsNRVIELPlrpqLSLDCRDLL 247
Cdd:cd05063   166 TTSGGKIpirWTAPEAIAYRKFTSASDVWSFGIVMWEVMsFGERPYWDMSNHEVMKAI--NDGFRLP----APMDCPSAV 239
                         250       260
                  ....*....|....*....|
gi 1907200402 248 QRLL----ERDPARRISFKD 263
Cdd:cd05063   240 YQLMlqcwQQDRARRPRFVD 259
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
35-265 3.69e-16

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: 78.53  E-value: 3.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  35 KDTREVVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVA 114
Cdd:cd05051    43 KDEPVLVAVK-MLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGAS 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 115 R-----------VFM-QQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDeKHVLRGS---PL- 178
Cdd:cd05051   122 AtnsktlsygtlLYMaTQIASGMKYLESLNFVHRDLATRNCLVGPNYT--IKIADFGMSRNLYSGD-YYRIEGRavlPIr 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 YMAPEMVCRRQYDARVDLWSVGVILYEAL-FG--QPpfasrsFSELEEKirsnRVIE--------------LPLRPQLSL 241
Cdd:cd05051   199 WMAWESILLGKFTTKSDVWAFGVTLWEILtLCkeQP------YEHLTDE----QVIEnageffrddgmevyLSRPPNCPK 268
                         250       260
                  ....*....|....*....|....
gi 1907200402 242 DCRDLLQRLLERDPARRISFKDFF 265
Cdd:cd05051   269 EIYELMLECWRRDEEDRPTFREIH 292
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
20-221 6.50e-16

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: 77.94  E-value: 6.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKA------YAKKDTREVVAIKCVAKKslnkasvENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd14159     1 IGEGGFGCVYQAvmrnteYAVKRLKEDSELDWSVVK-------NSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPekvARVFMQQL------ASALQFLHERNIS--HLDLKPQNILLSSLEKPhlKLADFGFAQ--- 162
Cdd:cd14159    74 LPNGSLEDRLHCQVSCP---CLSWSQRLhvllgtARAIQYLHSDSPSliHGDVKSSNILLDAALNP--KLGDFGLARfsr 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 163 ------HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSEL 221
Cdd:cd14159   149 rpkqpgMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPT 213
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
18-266 6.98e-16

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 77.74  E-value: 6.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAY---AKKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFC 94
Cdd:cd05090    11 EELGECAFGKIYKGHlylPGMDHAQLVAIKTL-KDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRR------ILPEKVARV--------FMQ---QLASALQFLHERNISHLDLKPQNILLSslEKPHLKLAD 157
Cdd:cd05090    90 NQGDLHEFLIMRSphsdvgCSSDEDGTVkssldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILVG--EQLHVKISD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 158 FGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIEL 233
Cdd:cd05090   168 LGLSREIYSSDYYRVQNKSLLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQLLPC 247
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907200402 234 PlrpqlsLDC----RDLLQRLLERDPARRISFKDFFA 266
Cdd:cd05090   248 S------EDCpprmYSLMTECWQEIPSRRPRFKDIHA 278
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
13-281 7.10e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.88  E-value: 7.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAYAKKdTREVVAIKCVAKkslnkasvENLLTEIEILKGIRHPHIVQLK-DFQWDNDNIYLIM 91
Cdd:PHA03212   93 GFSILETFTPGAEGFAFACIDNK-TCEHVVIKAGQR--------GGTATEAHILRAINHPSIIQLKgTFTYNKFTCLILP 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAggDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHmsPWD--- 168
Cdd:PHA03212  164 RYKT--DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFIN--HPGDVCLGDFGAACF--PVDina 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 169 -EKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRVI------------ELPL 235
Cdd:PHA03212  238 nKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEK--DGLDGDCDSDRQIkliirrsgthpnEFPI 315
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 236 RPQLSLDcrDLLQRLLE---RDPARRISFKDFFAHPwVDLE------------HMPSGESL 281
Cdd:PHA03212  316 DAQANLD--EIYIGLAKkssRKPGSRPLWTNLYELP-IDLEylickmlafdahHRPSAEAL 373
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
1-262 7.73e-16

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: 77.42  E-value: 7.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   1 MAGPSWGLPRlDGFILTERLGSGTYATVYKAYAKKDTRevVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDF 80
Cdd:cd05069     2 LAKDAWEIPR-ESLRLDVKLGQGCFGEVWMGTWNGTTK--VAIKTLKPGTM---MPEAFLQEAQIMKKLRHDKLVPLYAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QwDNDNIYLIMEFCAGGDLSRFI------HTRriLPEKVArvFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLK 154
Cdd:cd05069    76 V-SEEPIYIVTEFMGKGSLLDFLkegdgkYLK--LPQLVD--MAAQIADGMAYIERMNYIHRDLRAANILVG--DNLVCK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 155 LADFGFAQHMSpwDEKHVLRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYEALF-GQPPFASRSFSELEEKIrsNR 229
Cdd:cd05069   149 IADFGLARLIE--DNEYTARQGakfPIkWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQV--ER 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907200402 230 VIELPLRPQLSLDCRDLLQRLLERDPARRISFK 262
Cdd:cd05069   225 GYRMPCPQGCPESLHELMKLCWKKDPDERPTFE 257
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
19-216 1.16e-15

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 77.79  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  19 RLGSGTYATVYKAYAK--KDTREVvAIKCVAKKSLNKASVEnlltEIEILKGIRHPHIVQLKD--FQWDNDNIYLIMEFc 94
Cdd:cd07868    24 KVGRGTYGHVYKAKRKdgKDDKDY-ALKQIEGTGISMSACR----EIALLRELKHPNVISLQKvfLSHADRKVWLLFDY- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGGDLSRFIHTRRI---------LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQ- 162
Cdd:cd07868    98 AEHDLWHIIKFHRAskankkpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgEGPERGRVKIADMGFARl 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200402 163 ---HMSPWDEKHVLRGSPLYMAPEMVC-RRQYDARVDLWSVGVILYEALFGQPPFASR 216
Cdd:cd07868   178 fnsPLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCR 235
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
12-255 1.85e-15

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 77.44  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAYaKKDTREVVAIKCVAKKS--LNKASVE-NLLTEIEILKGIRHPHIVQLKDFQWDNDNIy 88
Cdd:cd14228    15 NSYEVLEFLGRGTFGQVAKCW-KRSTKEIVAIKILKNHPsyARQGQIEvSILSRLSSENADEYNFVRSYECFQHKNHTC- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGgDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL-SSLEKPH-LKLADFGFAQHM 164
Cdd:cd14228    93 LVFEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvDPVRQPYrVKVIDFGSASHV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 165 SPWDEKHVLRgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRsfSELEEKIRSNRVIELPLRPQLSLDCR 244
Cdd:cd14228   172 SKAVCSTYLQ-SRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGA--SEYDQIRYISQTQGLPAEYLLSAGTK 248
                         250
                  ....*....|.
gi 1907200402 245 DllQRLLERDP 255
Cdd:cd14228   249 T--SRFFNRDP 257
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
20-277 1.87e-15

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 77.39  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIV----------QLKDFQwdndNIYL 89
Cdd:cd07875    32 IGSGAQGIVCAAYDAILERNV-AIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIgllnvftpqkSLEEFQ----DVYI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFcAGGDLSRFIHTRriLPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQH--MSPW 167
Cdd:cd07875   107 VMEL-MDANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS--DCTLKILDFGLARTagTSFM 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 168 DEKHVLrgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSF---------------SELEEKIRSNRVIE 232
Cdd:cd07875   182 MTPYVV--TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHidqwnkvieqlgtpcPEFMKKLQPTVRTY 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 233 LPLRPQL------------------------SLDCRDLLQRLLERDPARRISFKDFFAHPWVDLEHMPS 277
Cdd:cd07875   260 VENRPKYagysfeklfpdvlfpadsehnklkASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPS 328
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
279-350 2.16e-15

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


Pssm-ID: 239121  Cd Length: 75  Bit Score: 70.80  E-value: 2.16e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 279 ESLAQARALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSS 350
Cdd:cd02656     1 ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKELLKK 72
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
18-211 2.63e-15

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 76.72  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYaKKDTREVVAIKcVAKKSLNKASVENLltEIEILKGIRHP-----HIVQLKDFQWDNDNIYLIME 92
Cdd:cd14211     5 EFLGRGTFGQVVKCW-KRGTNEIVAIK-ILKNHPSYARQGQI--EVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGgDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL-SSLEKPH-LKLADFGFAQHMSPWD 168
Cdd:cd14211    81 MLEQ-NLYDFLKQNKFspLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLvDPVRQPYrVKVIDFGSASHVSKAV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 169 EKHVLRgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQP 211
Cdd:cd14211   160 CSTYLQ-SRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 201
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
16-264 3.30e-15

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: 76.58  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVYKAYA----KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDFQWDNDN-IYL 89
Cdd:cd14207    11 LGKSLGRGAFGKVVQASAfgikKSPTCRVVAVKML-KEGATASEYKALMTELKILIHIgHHLNVVNLLGACTKSGGpLMV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  90 IMEFCAGGDLSRFIHTRR--ILPEKVARVFMQ------------------------------------------------ 119
Cdd:cd14207    90 IVEYCKYGNLSNYLKSKRdfFVTNKDTSLQEElikekkeaeptggkkkrlesvtssesfassgfqedkslsdveeeeeds 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 120 ------------------QLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHVLRGS---PL 178
Cdd:cd14207   170 gdfykrpltmedlisysfQVARGMEFLSSRKCIHRDLAARNILLS--ENNVVKICDFGLARDIYK-NPDYVRKGDarlPL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 179 -YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRS-----FSELEEKIRSnRVIELPLRP--QLSLDCrdllqr 249
Cdd:cd14207   247 kWMAPESIFDKIYSTKSDVWSYGVLLWEIFsLGASPYPGVQidedfCSKLKEGIRM-RAPEFATSEiyQIMLDC------ 319
                         330
                  ....*....|....*
gi 1907200402 250 lLERDPARRISFKDF 264
Cdd:cd14207   320 -WQGDPNERPRFSEL 333
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
20-264 3.46e-15

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 75.28  E-value: 3.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYkaYAKKDTREVVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDL 99
Cdd:cd05114    12 LGSGLFGVVR--LGKWRAQYKVAIKAIREGAM---SEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 100 SRFIHTRR-ILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFA------QHMSPWDEKHV 172
Cdd:cd05114    87 LNYLRQRRgKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGV--VKVSDFGMTryvlddQYTSSSGAKFP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGSPlymaPEMVCRRQYDARVDLWSVGVILYEALF-GQPPFASRSFSELEEKI-RSNRVielpLRPQL-SLDCRDLLQR 249
Cdd:cd05114   165 VKWSP----PEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVsRGHRL----YRPKLaSKSVYEVMYS 236
                         250
                  ....*....|....*
gi 1907200402 250 LLERDPARRISFKDF 264
Cdd:cd05114   237 CWHEKPEGRPTFADL 251
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
20-221 3.73e-15

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: 75.38  E-value: 3.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAY--AKKDTREV-VAIKCVAKKSlNKASVENLLTEIEILKGIRHPHIVQLKDFqWDNDNIYLIMEFCAG 96
Cdd:cd05111    15 LGSGVFGTVHKGIwiPEGDSIKIpVAIKVIQDRS-GRQSFQAVTDHMLAIGSLDHAYIVRLLGI-CPGASLQLVTQLLPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  97 GDLSRFIHTRR--ILPEKVARvFMQQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPWDEKHVLR 174
Cdd:cd05111    93 GSLLDHVRQHRgsLGPQLLLN-WCVQIAKGMYYLEEHRMVHRNLAARNVLLKS--PSQVQVADFGVADLLYPDDKKYFYS 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907200402 175 --GSPL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSEL 221
Cdd:cd05111   170 eaKTPIkWMALESIHFGKYTHQSDVWSYGVTVWEMMtFGAEPYAGMRLAEV 220
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
8-261 4.57e-15

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: 75.40  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   8 LPRlDGFILTERLGSGTYATVYKAYAK-------------KDTREVVAIKCVaKKSLNKASVENLLTEIEILKGIRHPHI 74
Cdd:cd05097     2 FPR-QQLRLKEKLGEGQFGEVHLCEAEglaeflgegapefDGQPVLVAVKML-RADVTKTARNDFLKEIKIMSRLKNPNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  75 VQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPE--------KVAR---VFMQ-QLASALQFLHERNISHLDLKPQN 142
Cdd:cd05097    80 IRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTfthannipSVSIanlLYMAvQIASGMKYLASLNFVHRDLATRN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 143 ILLSSleKPHLKLADFGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYE--ALFGQPPFASRS 217
Cdd:cd05097   160 CLVGN--HYTIKIADFGMSRNLYSGDYYRIQGRAVLpirWMAWESILLGKFTTASDVWAFGVTLWEmfTLCKEQPYSLLS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200402 218 FSELEEK----IRSN-RVIELPLRPQLSLDCRDLLQRLLERDPARRISF 261
Cdd:cd05097   238 DEQVIENtgefFRNQgRQIYLSQTPLCPSPVFKLMMRCWSRDIKDRPTF 286
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
18-205 4.74e-15

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 75.44  E-value: 4.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAyakKDTREVVAIKCVAKKslNKASvenLLTEIEI--LKGIRHPHIVQ----LKDFQWDNDNIYLIM 91
Cdd:cd14053     1 EIKARGRFGAVWKA---QYLNRLVAVKIFPLQ--EKQS---WLTEREIysLPGMKHENILQfigaEKHGESLEAEYWLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRrILPEKVARVFMQQLASALQFLHER----------NISHLDLKPQNILLssleKPHLK--LADFG 159
Cdd:cd14053    73 EFHERGSLCDYLKGN-VISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLL----KSDLTacIADFG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907200402 160 FAQHMSPWDEK---HVLRGSPLYMAPEMV---CRRQYDA--RVDLWSVGVILYE 205
Cdd:cd14053   148 LALKFEPGKSCgdtHGQVGTRRYMAPEVLegaINFTRDAflRIDMYAMGLVLWE 201
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
20-226 5.44e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 74.93  E-value: 5.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATV----YKAYAKkDTREVVAIKCVAKKSLNKasVENLLTEIEILKGIRHPHIVQLKDFQWD--NDNIYLIMEF 93
Cdd:cd05081    12 LGKGNFGSVelcrYDPLGD-NTGALVAVKQLQHSGPDQ--QRDFQREIQILKALHSDFIVKYRGVSYGpgRRSLRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIH-TRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWDEKHV 172
Cdd:cd05081    89 LPSGCLRDFLQrHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEA--HVKIADFGLAKLLPLDKDYYV 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200402 173 LR---GSPLY-MAPEMVCRRQYDARVDLWSVGVILYEaLFgqpPFASRSFSELEEKIR 226
Cdd:cd05081   167 VRepgQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYE-LF---TYCDKSCSPSAEFLR 220
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-222 5.46e-15

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: 75.86  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKsLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIM 91
Cdd:cd06649     5 DDFERISELGAGNGGVVTKV-QHKPSGLIMARKLIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERN-ISHLDLKPQNILLSSleKPHLKLADFGFAQHMSPwDEK 170
Cdd:cd06649    83 EHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNS--RGEIKLCDFGVSGQLID-SMA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 171 HVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELE 222
Cdd:cd06649   160 NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELE 211
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
20-213 6.57e-15

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: 74.85  E-value: 6.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVvAIK--CVAKKSLNKAsvenLLTEIEILKGIR-HPHIVQL--------KDFQWDNDNIY 88
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEY-ALKrlLSNEEEKNKA----IIQEINFMKKLSgHPNIVQFcsaasigkEESDQGQAEYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  89 LIMEFCAGGDLSRFIHTR---RILPEKVARVFMQqLASALQFLHERN--ISHLDLKPQNILLSSleKPHLKLADFGFA-- 161
Cdd:cd14036    83 LLTELCKGQLVDFVKKVEapgPFSPDTVLKIFYQ-TCRAVQHMHKQSppIIHRDLKIENLLIGN--QGQIKLCDFGSAtt 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200402 162 QHMSP---WD-------EKHVLRGS-PLYMAPEMV---CRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14036   160 EAHYPdysWSaqkrslvEDEITRNTtPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPF 225
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
20-261 7.37e-15

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: 75.03  E-value: 7.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDFQWDNDNIYLIMEFCAGGD 98
Cdd:cd05088    15 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  99 LSRFIHTRRILPEKVARVFMQQLASALQ----------------FLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQ 162
Cdd:cd05088    95 LLDFLRKSRVLETDPAFAIANSTASTLSsqqllhfaadvargmdYLSQKQFIHRDLAARNILVG--ENYVAKIADFGLSR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 163 HMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPLrpQLSL 241
Cdd:cd05088   173 GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQGYRLEKPL--NCDD 250
                         250       260
                  ....*....|....*....|
gi 1907200402 242 DCRDLLQRLLERDPARRISF 261
Cdd:cd05088   251 EVYDLMRQCWREKPYERPSF 270
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
18-239 1.03e-14

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: 74.40  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTrevvaikcVAKKSLNKASVENLLTEIEILK--GIRHPHIVQ-LKDFQWDND---NIYLIM 91
Cdd:cd13998     1 EVIGKGRFGEVWKASLKNEP--------VAVKIFSSRDKQSWFREKEIYRtpMLKHENILQfIAADERDTAlrtELWLVT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGGDLSRFIHTRRILPEKVARVfMQQLASALQFLHER---------NISHLDLKPQNILLssleKPHLK--LADFGF 160
Cdd:cd13998    73 AFHPNGSL*DYLSLHTIDWVSLCRL-ALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILV----KNDGTccIADFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 161 AQHMSPWDEK-----HVLRGSPLYMAPEM----VCRRQYDA--RVDLWSVGVILYE------ALFG-----QPPFASR-- 216
Cdd:cd13998   148 AVRLSPSTGEednanNGQVGTKRYMAPEVlegaINLRDFESfkRVDIYAMGLVLWEmasrctDLFGiveeyKPPFYSEvp 227
                         250       260
                  ....*....|....*....|....*.
gi 1907200402 217 ---SFSELEEKirsnrVIELPLRPQL 239
Cdd:cd13998   228 nhpSFEDMQEV-----VVRDKQRPNI 248
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
6-220 1.74e-14

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: 74.25  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYA----KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQL-KD 79
Cdd:cd05102     2 WEFPR-DRLRLGKVLGHGAFGKVVEASAfgidKSSSCETVAVKML-KEGATASEHKALMSELKILIHIgNHLNVVNLlGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  80 FQWDNDNIYLIMEFCAGGDLSRFIHTRR--ILP--EKVARVFMQ------------------------------------ 119
Cdd:cd05102    80 CTKPNGPLMVIVEFCKYGNLSNFLRAKRegFSPyrERSPRTRSQvrsmveavradrrsrqgsdrvasftestsstnqprq 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 120 --------------------QLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHVLRGS--- 176
Cdd:cd05102   160 evddlwqspltmedlicysfQVARGMEFLASRKCIHRDLAARNILLS--ENNVVKICDFGLARDIYK-DPDYVRKGSarl 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 177 PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSE 220
Cdd:cd05102   237 PLkWMAPESIFDKVYTTQSDVWSFGVLLWEIFsLGASPYPGVQINE 282
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
18-217 2.66e-14

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 73.97  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYaKKDTREVVAIKCVAKKS--LNKASVE-NLLTEIEILKGIRHPHIVQLKDFQWDNDNIyLIMEFC 94
Cdd:cd14227    21 EFLGRGTFGQVVKCW-KRGTNEIVAIKILKNHPsyARQGQIEvSILARLSTESADDYNFVRAYECFQHKNHTC-LVFEML 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  95 AGgDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILL--SSLEKPHLKLADFGFAQHMSPWDEK 170
Cdd:cd14227    99 EQ-NLYDFLKQNKFspLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdPSRQPYRVKVIDFGSASHVSKAVCS 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907200402 171 HVLRgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRS 217
Cdd:cd14227   178 TYLQ-SRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGAS 223
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
16-242 2.99e-14

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 72.61  E-value: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  16 LTERLGSGTYATVykAYAKKDTREVVAIKCVAKKSLnkaSVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCA 95
Cdd:cd05113     8 FLKELGTGQFGVV--KYGKWRGQYDVAIKMIKEGSM---SEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  96 GGDLSRFIHTRRILPEKVARVFM-QQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFA------QHMSPWD 168
Cdd:cd05113    83 NGCLLNYLREMRKRFQTQQLLEMcKDVCEAMEYLESKQFLHRDLAARNCLVND--QGVVKVSDFGLSryvlddEYTSSVG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 169 EKHVLRGSPlymaPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIelpLRPQLSLD 242
Cdd:cd05113   161 SKFPVRWSP----PEVLMYSKFSSKSDVWAFGVLMWEVYsLGKMPYERFTNSETVEHVSQGLRL---YRPHLASE 228
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
18-263 3.15e-14

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: 72.59  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVaikCVAKKSLNKASVE----NLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd05065    10 EVIGAGEFGEVCRGRLKLPGKREI---FVAIKTLKSGYTEkqrrDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRILPEKVARVFM-QQLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQHM--SPWDEK 170
Cdd:cd05065    87 MENGALDSFLRQNDGQFTVIQLVGMlRGIAAGMKYLSEMNYVHRDLAARNILVNS--NLVCKVSDFGLSRFLedDTSDPT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 171 HV--LRGS-PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlrpqlsLDCRD 245
Cdd:cd05065   165 YTssLGGKiPIrWTAPEAIAYRKFTSASDVWSYGIVMWEVMsYGERPYWDMSNQDVINAIEQDYRLPPP------MDCPT 238
                         250       260
                  ....*....|....*....|..
gi 1907200402 246 LLQRLL----ERDPARRISFKD 263
Cdd:cd05065   239 ALHQLMldcwQKDRNLRPKFGQ 260
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
114-260 3.25e-14

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 73.30  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 114 ARVFMQQLASALQFLHERNISHLDLKPQNILLS--SLEKPHLKLADFGFAQHmspwDEKHVLR-----------GSPLYM 180
Cdd:cd14018   140 ARVMILQLLEGVDHLVRHGIAHRDLKSDNILLEldFDGCPWLVIADFGCCLA----DDSIGLQlpfsswyvdrgGNACLM 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 181 APEMVCRR-------QYdARVDLWSVGVILYEaLFGQP-PFASRSFSELEEkiRSNRVIELPLRPQ-LSLDCRDLLQRLL 251
Cdd:cd14018   216 APEVSTAVpgpgvviNY-SKADAWAVGAIAYE-IFGLSnPFYGLGDTMLES--RSYQESQLPALPSaVPPDVRQVVKDLL 291

                  ....*....
gi 1907200402 252 ERDPARRIS 260
Cdd:cd14018   292 QRDPNKRVS 300
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
48-268 4.56e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 73.34  E-value: 4.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  48 KKSLNKASV--ENLLTEIEILKGIRHPHIVQLKD-FQWDNdNIYLIMEF--CaggDLSRFIHTRRILPEKVARVFMQQLA 122
Cdd:PHA03207  120 KKVIVKAVTggKTPGREIDILKTISHRAIINLIHaYRWKS-TVCMVMPKykC---DLFTYVDRSGPLPLEQAITIQRRLL 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 123 SALQFLHERNISHLDLKPQNILLSSLEkpHLKLADFGFAQHMSPWDEK---HVLRGSPLYMAPEMVCRRQYDARVDLWSV 199
Cdd:PHA03207  196 EALAYLHGRGIIHRDVKTENIFLDEPE--NAVLGDFGAACKLDAHPDTpqcYGWSGTLETNSPELLALDPYCAKTDIWSA 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 200 GVILYEALFGQPPFASR----SFSELEEKIRSNRVIEL-------------------PLRPQ-----------LSLDCRD 245
Cdd:PHA03207  274 GLVLFEMSVKNVTLFGKqvksSSSQLRSIIRCMQVHPLefpqngstnlckhfkqyaiVLRPPytippvirkygMHMDVEY 353
                         250       260
                  ....*....|....*....|...
gi 1907200402 246 LLQRLLERDPARRISFKDFFAHP 268
Cdd:PHA03207  354 LIAKMLTFDQEFRPSAQDILSLP 376
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
8-266 6.70e-14

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: 72.27  E-value: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   8 LPRlDGFILTERLGSGTYATV---------------YKAYAKKDTREVVAIKcVAKKSLNKASVENLLTEIEILKGIRHP 72
Cdd:cd05096     2 FPR-GHLLFKEKLGEGQFGEVhlcevvnpqdlptlqFPFNVRKGRPLLVAVK-ILRPDANKNARNDFLKEVKILSRLKDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  73 HIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRIL------------------PEKVARVFMQ-QLASALQFLHERNI 133
Cdd:cd05096    80 NIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHLDdkeengndavppahclpaISYSSLLHVAlQIASGMKYLSSLNF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 134 SHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLRGSPL---YMAPEMVCRRQYDARVDLWSVGVILYEALF-- 208
Cdd:cd05096   160 VHRDLATRNCLVG--ENLTIKIADFGMSRNLYAGDYYRIQGRAVLpirWMAWECILMGKFTTASDVWAFGVTLWEILMlc 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 209 GQPPFASRSFSELEEKI-----RSNRVIELPLRPQLSLDCRDLLQRLLERDPARRISFKDFFA 266
Cdd:cd05096   238 KEQPYGELTDEQVIENAgeffrDQGRQVYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHA 300
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
12-234 8.00e-14

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 71.71  E-value: 8.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  12 DGFILTERLGSGTYATVYKA---YAKKDTREVVaIKCVAkkslNKAS---VENLLTEIEILKGIRHPHIVQ-LKDFQWDN 84
Cdd:cd05043     6 ERVTLSDLLQEGTFGRIFHGilrDEKGKEEEVL-VKTVK----DHASeiqVTMLLQESSLLYGLSHQNLLPiLHVCIEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  85 DNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQ--------QLASALQFLHERNISHLDLKPQNILLSslEKPHLKLA 156
Cdd:cd05043    81 EKPMVLYPYMNWGNLKLFLQQCRLSEANNPQALSTqqlvhmalQIACGMSYLHRRGVIHKDIAARNCVID--DELQVKIT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 157 DFGFAQHMSPWDeKHVL---RGSPL-YMAPEMVCRRQYDARVDLWSVGVILYE-ALFGQPPFASRSFSELEEKIRSNRVI 231
Cdd:cd05043   159 DNALSRDLFPMD-YHCLgdnENRPIkWMSLESLVNKEYSSASDVWSFGVLLWElMTLGQTPYVEIDPFEMAAYLKDGYRL 237

                  ...
gi 1907200402 232 ELP 234
Cdd:cd05043   238 AQP 240
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
13-272 8.85e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.22  E-value: 8.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  13 GFILTERLGSGTYATVYKAyAKKDTREVVAIKCVAKKSLnkasvenlLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIME 92
Cdd:PHA03209   67 GYTVIKTLTPGSEGRVFVA-TKPGQPDPVVLKIGQKGTT--------LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLP 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  93 FCAGgDLSRFIHTR-RILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKphLKLADFGFAQHMSPWDEKH 171
Cdd:PHA03209  138 HYSS-DLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQ--VCIGDLGAAQFPVVAPAFL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYE------ALFGQPP-----FASRSFSELEEKIRSNRV--IELPLRPQ 238
Cdd:PHA03209  215 GLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEmlaypsTIFEDPPstpeeYVKSCHSHLLKIISTLKVhpEEFPRDPG 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200402 239 ----------------------------LSLDCRDLLQRLLERDPARRISFKDFFAHP-WVDL 272
Cdd:PHA03209  295 srlvrgfieyaslerqpytrypcfqrvnLPIDGEFLVHKMLTFDAAMRPSAEEILNYPmFAQL 357
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
6-211 1.13e-13

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 71.15  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYAKK------DTRevVAIKCVAKKSLNKASVEnLLTEIEILKGIRHPHIVQLKD 79
Cdd:cd05061     1 WEVSR-EKITLLRELGQGSFGMVYEGNARDiikgeaETR--VAVKTVNESASLRERIE-FLNEASVMKGFTCHHVVRLLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  80 FQWDNDNIYLIMEFCAGGDLSRFIHTRRI-------LPEKVARVFMQ---QLASALQFLHERNISHLDLKPQNILLSslE 149
Cdd:cd05061    77 VVSKGQPTLVVMELMAHGDLKSYLRSLRPeaennpgRPPPTLQEMIQmaaEIADGMAYLNAKKFVHRDLAARNCMVA--H 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200402 150 KPHLKLADFGFAQHMspWDEKHVLRGS----PL-YMAPEMVCRRQYDARVDLWSVGVILYE--ALFGQP 211
Cdd:cd05061   155 DFTVKIGDFGMTRDI--YETDYYRKGGkgllPVrWMAPESLKDGVFTTSSDMWSFGVVLWEitSLAEQP 221
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
20-263 1.55e-13

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 70.63  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYA------KKDTreVVAIKcVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEF 93
Cdd:cd05050    13 IGQGAFGRVFQARApgllpyEPFT--MVAVK-MLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  94 CAGGDLSRFIHTRRI----------------------LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSslEKP 151
Cdd:cd05050    90 MAYGDLNEFLRHRSPraqcslshstssarkcglnplpLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVG--ENM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 152 HLKLADFGFAQHMSPWDekhVLRGS-----PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSELEEK 224
Cdd:cd05050   168 VVKIADFGLSRNIYSAD---YYKASendaiPIrWMPPESIFYNRYTTESDVWAYGVVLWEIFsYGMQPYYGMAHEEVIYY 244
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907200402 225 IRSNRVIELPLRPQLSLdcRDLLQRLLERDPARRISFKD 263
Cdd:cd05050   245 VRDGNVLSCPDNCPLEL--YNLMRLCWSKLPSDRPSFAS 281
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
6-261 2.48e-13

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: 71.21  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYK--AYAKKDTREV--VAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQLKDF 80
Cdd:cd05105    32 WEFPR-DGLVLGRILGSGAFGKVVEgtAYGLSRSQPVmkVAVKML-KPTARSSEKQALMSELKIMTHLgPHLNIVNLLGA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  81 QWDNDNIYLIMEFCAGGDLSRFIHTRR-----ILPEKVAR---------------------------------------- 115
Cdd:cd05105   110 CTKSGPIYIITEYCFYGDLVNYLHKNRdnflsRHPEKPKKdldifginpadestrsyvilsfenkgdymdmkqadttqyv 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 116 ---------------------------------------------------VFMQQLASALQFLHERNISHLDLKPQNIL 144
Cdd:cd05105   190 pmleikeaskysdiqrsnydrpasykgsndsevknllsddgseglttldllSFTYQVARGMEFLASKNCVHRDLAARNVL 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 145 LSslEKPHLKLADFGFAQHMSPwDEKHVLRGSPL----YMAPEMVCRRQYDARVDLWSVGVILYE--ALFGQPPFASRSF 218
Cdd:cd05105   270 LA--QGKIVKICDFGLARDIMH-DSNYVSKGSTFlpvkWMAPESIFDNLYTTLSDVWSYGILLWEifSLGGTPYPGMIVD 346
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1907200402 219 SELEEKIRSNRVIELPlrPQLSLDCRDLLQRLLERDPARRISF 261
Cdd:cd05105   347 STFYNKIKSGYRMAKP--DHATQEVYDIMVKCWNSEPEKRPSF 387
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
6-267 2.95e-13

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: 70.78  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402   6 WGLPRlDGFILTERLGSGTYATVYKAYA----KKDTREVVAIKCVaKKSLNKASVENLLTEIEILKGI-RHPHIVQL-KD 79
Cdd:cd05103     2 WEFPR-DRLKLGKPLGRGAFGQVIEADAfgidKTATCRTVAVKML-KEGATHSEHRALMSELKILIHIgHHLNVVNLlGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  80 FQWDNDNIYLIMEFCAGGDLSRFIHTRR---------------------ILPEKVAR----------------------- 115
Cdd:cd05103    80 CTKPGGPLMVIVEFCKFGNLSAYLRSKRsefvpyktkgarfrqgkdyvgDISVDLKRrldsitssqssassgfveeksls 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 116 -----------------------VFMQQLASALQFLHERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPwDEKHV 172
Cdd:cd05103   160 dveeeeagqedlykdfltledliCYSFQVAKGMEFLASRKCIHRDLAARNILLS--ENNVVKICDFGLARDIYK-DPDYV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 173 LRGS---PL-YMAPEMVCRRQYDARVDLWSVGVILYEAL-FGQPPFASRSFSE-----LEEKIRSnRVIEL--PLRPQLS 240
Cdd:cd05103   237 RKGDarlPLkWMAPETIFDRVYTIQSDVWSFGVLLWEIFsLGASPYPGVKIDEefcrrLKEGTRM-RAPDYttPEMYQTM 315
                         330       340
                  ....*....|....*....|....*..
gi 1907200402 241 LDCrdllqrlLERDPARRISFKDFFAH 267
Cdd:cd05103   316 LDC-------WHGEPSQRPTFSELVEH 335
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
18-263 4.41e-13

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: 69.15  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  18 ERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGG 97
Cdd:cd05042     1 QEIGNGWFGKVLLGEIYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  98 DLSRFIHTRRIlPEKVARVFMQ------QLASALQFLHERNISHLDLKPQNILLSSleKPHLKLADFGFAQhmSPWDEKH 171
Cdd:cd05042    81 DLKAYLRSERE-HERGDSDTRTlqrmacEVAAGLAHLHKLNFVHSDLALRNCLLTS--DLTVKIGDYGLAH--SRYKEDY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 172 VLRGS----PL-YMAPEMVCRRQYDARV-------DLWSVGVILYEAL-FGQPPFASRSFSELEEKIRSNRVIELPlRPQ 238
Cdd:cd05042   156 IETDDklwfPLrWTAPELVTEFHDRLLVvdqtkysNIWSLGVTLWELFeNGAQPYSNLSDLDVLAQVVREQDTKLP-KPQ 234
                         250       260
                  ....*....|....*....|....*...
gi 1907200402 239 LSLDCRDLLQRLLE---RDPARRISFKD 263
Cdd:cd05042   235 LELPYSDRWYEVLQfcwLSPEQRPAAED 262
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
72-269 4.83e-13

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 69.11  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  72 PHIVQLKDFQWDNDNIYLIMEFCAGGDL----SRFIH------------------TRRILPEKVARVFMQQLASALQFLH 129
Cdd:cd05576    51 PNMVCLRKYIISEESVFLVLQHAEGGKLwsylSKFLNdkeihqlfadlderlaaaSRFYIPEECIQRWAAEMVVALDALH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402 130 ERNISHLDLKPQNILLSslEKPHLKLADFGFAQHMSPWDEKHVLrgSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFG 209
Cdd:cd05576   131 REGIVCRDLNPNNILLN--DRGHIQLTYFSRWSEVEDSCDSDAI--ENMYCAPEVGGISEETEACDWWSLGALLFELLTG 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200402 210 QPPFASRSfseleEKIRSNRVIELPlrPQLSLDCRDLLQRLLERDPARRI-----SFKDFFAHPW 269
Cdd:cd05576   207 KALVECHP-----AGINTHTTLNIP--EWVSEEARSLLQQLLQFNPTERLgagvaGVEDIKSHPF 264
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
20-213 4.93e-13

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 70.16  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  20 LGSGTYATVYKAYAKKdTREVVAIKCVA-KKSLNKASVEnlltEIEILKGIR-------HPHIVQLKDFQWDNdNIYLIM 91
Cdd:cd14224    73 IGKGSFGQVVKAYDHK-THQHVALKMVRnEKRFHRQAAE----EIRILEHLKkqdkdntMNVIHMLESFTFRN-HICMTF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200402  92 EFCAGgDLSRFIHTRRI--LPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGfaqhMSPWDE 169
Cdd:cd14224   147 ELLSM-NLYELIKKNKFqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFG----SSCYEH 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200402 170 KHVLR--GSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPF 213
Cdd:cd14224   222 QRIYTyiQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLF 267
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
374-425 4.67e-05

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


Pssm-ID: 239121  Cd Length: 75  Bit Score: 41.53  E-value: 4.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907200402 374 PRLLAALEVASAALaKEEEAGKEQDALDLYQHSLGELLVLLAGKAPALVRAL 425
Cdd:cd02656     1 ELLQQAKELIKQAV-KEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKL 51
 
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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