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Conserved domains on  [gi|89898773|ref|YP_515883|]
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serine/threonine protein kinase [Chlamydophila felis Fe/C-56]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
28-248 1.42e-52

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 178.58  E-value: 1.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  28 STVYHGVHPVTLQPTVIKVLvtPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILS 107
Cdd:cd00180   7 GTVYLARDKKTGKKVAIKII--KKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSLKDLLKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 108 QLIPLS--RAVDIILQIAQALEYLHSRGILHRDIKPENILIT-PQGEIKLIDFGLAASSSMANDPYPVCLGTPSYMSPEQ 184
Cdd:cd00180  85 NEGKLSedEILRILLQILEGLEYLHSNGIIHRDLKPENILLDsDNGKVKLADFGLSKLLTSDKSLLKTIVGTPAYMAPEV 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89898773 185 -RQGDKISENSEIYSLGLIAYELilgnlalgkvilslvpERMSKILAKALQPSPKDRYaSMKEFL 248
Cdd:cd00180 165 lLGKGYYSEKSDIWSLGVILYEL----------------PELKDLIRKMLQKDPEKRP-SAKEIL 212
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
28-248 6.57e-52

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 178.11  E-value: 6.57e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773     28 STVYHGVHPVTLQPTVIKVLvtPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILS 107
Cdd:smart00220  13 GKVYLARDKKTGKLVAIKVI--KKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    108 Q-LIPLSRAVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYPVClGTPSYMSPEQRQ 186
Cdd:smart00220  91 RgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV-GTPEYMAPEVLL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    187 GDKISENSEIYSLGLIAYELILGN---------LALGKVILSLVPERMSK----------ILAKALQPSPKDRYaSMKEF 247
Cdd:smart00220 170 GKGYGKAVDIWSLGVILYELLTGKppfpgddqlLELFKKIGKPKPPFPPPewdispeakdLIRKLLVKDPEKRL-TAEEA 248

                   .
gi 89898773    248 L 248
Cdd:smart00220 249 L 249
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
28-248 1.42e-52

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 178.58  E-value: 1.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  28 STVYHGVHPVTLQPTVIKVLvtPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILS 107
Cdd:cd00180   7 GTVYLARDKKTGKKVAIKII--KKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSLKDLLKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 108 QLIPLS--RAVDIILQIAQALEYLHSRGILHRDIKPENILIT-PQGEIKLIDFGLAASSSMANDPYPVCLGTPSYMSPEQ 184
Cdd:cd00180  85 NEGKLSedEILRILLQILEGLEYLHSNGIIHRDLKPENILLDsDNGKVKLADFGLSKLLTSDKSLLKTIVGTPAYMAPEV 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89898773 185 -RQGDKISENSEIYSLGLIAYELilgnlalgkvilslvpERMSKILAKALQPSPKDRYaSMKEFL 248
Cdd:cd00180 165 lLGKGYYSEKSDIWSLGVILYEL----------------PELKDLIRKMLQKDPEKRP-SAKEIL 212
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
93-168 1.11e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 51.06  E-value: 1.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89898773   93 MEHIQGVSLrKYILSQLIPlsRAVDIILQIAQALEYLHSRGILHRDIKPENILITpQGEIKLIDFGLAASSSMAND 168
Cdd:PRK14879  78 MEYIEGEPL-KDLINSNGM--EELELSREIGRLVGKLHSAGIIHGDLTTSNMILS-GGKIYLIDFGLAEFSKDLED 149
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
49-200 1.40e-07

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 51.88  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   49 TPLVADTLRVHNFLKEARI-----IEQISHPNIVKLYQYG---QCR--------EGLYMAMEHIqgvslRKYILSQLIPL 112
Cdd:PHA02882  53 ETIVMETLVYNNIYDIDKIalwknIHNIDHLGIPKYYGCGsfkRCRmyyrfillEKLVENTKEI-----FKRIKCKNKKL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  113 SRavDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAA-------SSSMANDPYPVCLGTPSYMSPEQR 185
Cdd:PHA02882 128 IK--NIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIIDYGIAShfiihgkHIEYSKEQKDLHRGTLYYAGLDAH 205
                        170
                 ....*....|....*
gi 89898773  186 QGDKISENSEIYSLG 200
Cdd:PHA02882 206 NGACVTRRGDLESLG 220
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
56-168 1.88e-07

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 50.36  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  56 LRVHNFLKEARIIEqishpnivKLYQYGQCREGLY--------MAMEHIQGVSLRKYILSQLIPLSRAVDIilQIAQale 127
Cdd:COG3642  41 LRRERTRREARILA--------KAREAGVPVPIVYdvdpdnglIVMEYIEGELLKDALEEARPDLLREVGR--LVGK--- 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 89898773 128 yLHSRGILHRDIKPENILITpQGEIKLIDFGLAASSSMAND 168
Cdd:COG3642 108 -LHKAGIVHGDLTTSNIILS-GGRIYFIDFGLGEFSDEVED 146
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
118-212 1.55e-06

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 47.01  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    118 IILQIAQALEYLHSRGilhrdiKPENILITPQGEIKLidFGLAASSSMANDpypvcLGTPSYMSPEQRQGDKISENSEIY 197
Cdd:smart00750  22 VCLQCLGALRELHRQA------KSGNILLTWDGLLKL--DGSVAFKTPEQS-----RPDPYFMAPEVIQGQSYTEKADIY 88
                           90
                   ....*....|....*
gi 89898773    198 SLGLIAYELILGNLA 212
Cdd:smart00750  89 SLGITLYEALDYELP 103
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
91-164 3.69e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine [Unknown function, General].


Pssm-ID: 234331  Cd Length: 199  Bit Score: 46.44  E-value: 3.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89898773    91 MAMEHIQGVSLrKYILSQLIPlsravDIILQIAQALEYLHSRGILHRDIKPENILITpQGEIKLIDFGLAASSS 164
Cdd:TIGR03724  74 IVMEYIEGKPL-KDVIEEGND-----ELLREIGRLVGKLHKAGIVHGDLTTSNIIVR-DDKLYLIDFGLGKYSD 140
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
118-240 1.11e-04

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 258671  Cd Length: 289  Bit Score: 42.79  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   118 IILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFG--LAASSSMANDPYPVCLGTPSYMSPEQRQGD---KISE 192
Cdd:pfam14531 151 LTLQLIRLAAGLQHRGLVHGDFRPDNFFLDQKGGVFLGGFTalVRAGTKVVVSEVDVAFAPPELFASRGYTGKnttTMTH 230
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 89898773   193 NSEIYSLGLIAYELILGNLALGKV--------ILSL---VPERMSKILAKALQPSPKDR 240
Cdd:pfam14531 231 KTDAWQLGLVIYRIWCLRLPFTLDtpeggsewKFGRcvnMPEPVKALLAGFLNRSQEAR 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
28-248 6.57e-52

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 178.11  E-value: 6.57e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773     28 STVYHGVHPVTLQPTVIKVLvtPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILS 107
Cdd:smart00220  13 GKVYLARDKKTGKLVAIKVI--KKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    108 Q-LIPLSRAVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYPVClGTPSYMSPEQRQ 186
Cdd:smart00220  91 RgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV-GTPEYMAPEVLL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    187 GDKISENSEIYSLGLIAYELILGN---------LALGKVILSLVPERMSK----------ILAKALQPSPKDRYaSMKEF 247
Cdd:smart00220 170 GKGYGKAVDIWSLGVILYELLTGKppfpgddqlLELFKKIGKPKPPFPPPewdispeakdLIRKLLVKDPEKRL-TAEEA 248

                   .
gi 89898773    248 L 248
Cdd:smart00220 249 L 249
Pkinase pfam00069
Protein kinase domain;
16-248 2.41e-48

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 168.96  E-value: 2.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    16 YCIKRIMSKKEGSTVYHGVHPVTLQPTVIKVLVTPLVADTLRVHNFLkEARIIEQISHPNIVKLYQYGQCREGLYMAMEH 95
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTARR-EIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    96 IQGVSLRKYIlSQLIPLSR--AVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYPVC 173
Cdd:pfam00069  80 CEGGDLFDYL-SRGGPLSEdeAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLTTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   174 LGTPSYMSPEQ-RQGDKISENSEIYSLGLIAYELILGNL-----------------ALGKVILS-----LVPERMSKILA 230
Cdd:pfam00069 159 VGTPEYMAPEVlLGGNGYGPKVDVWSLGVILYELLTGKPpfsgesildqlqlirriLGPPLEFDepksdSGSEEAKDLIK 238
                         250
                  ....*....|....*...
gi 89898773   231 KALQPSPKDRYaSMKEFL 248
Cdd:pfam00069 239 KCLNKDPSKRP-TAEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
28-251 4.74e-38

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 143.34  E-value: 4.74e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  28 STVYHGVHPvtlQPTVIKVLVTPLVADTLRVHNFLKEARIIEQISHP-NIVKLYQYGQCREGLYMAMEHIQGVSLRKYI- 105
Cdd:COG0515  14 GEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEYVDGGSLEDLLk 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 106 ---LSQLIPLSRAVDIILQIAQALEYLHSRGILHRDIKPENILITPQG-EIKLIDFGLAA------SSSMANDPYPVCLG 175
Cdd:COG0515  91 kigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKllpdpgSTSSIPALPSTSVG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 176 TPSYMSPEQRQG---DKISENSEIYSLGLIAYELILGNLALGKVILSLVPERMSKILAKALQPS-----PKDRYASMKEF 247
Cdd:COG0515 171 TPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILELPTPSlasplSPSNPELISKA 250

                ....
gi 89898773 248 LIDL 251
Cdd:COG0515 251 ASDL 254
pknD PRK13184
serine/threonine-protein kinase; Reviewed
13-258 2.64e-34

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 136.44  E-value: 2.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   13 IGEYCIKRIMSKKEGSTVYHGVHPVTLQPTVIKVLVTPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMA 92
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   93 MEHIQGVSLR--------KYILSQLIPLSRAV----DIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLA 160
Cdd:PRK13184  81 MPYIEGYTLKsllksvwqKESLSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  161 ASSSMAND-------PYPVCL-----------GTPSYMSPEQRQGDKISENSEIYSLGLIAYE-LILGN---------LA 212
Cdd:PRK13184 161 IFKKLEEEdlldidvDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQmLTLSFpyrrkkgrkIS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89898773  213 LGKVILSL--------VPERMSKILAKALQPSPKDRYASMKEFLIDLYKYRHGE 258
Cdd:PRK13184 241 YRDVILSPievapyreIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGS 294
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
38-243 1.53e-30

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 125.34  E-value: 1.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773     38 TLQPTVIKVLVTPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAM-EHIQGVSLRKYILSQ-LIPLSRA 115
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVfEYVPGRTLREVLAADgALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773    116 VDIILQIAQALEYLHSRGILHRDIKPENILITPQG---EIKLIDFGLAASSSMANDPYPV-------CLGTPSYMSPEQR 185
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGVRDADVAtltrtteVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89898773    186 QGDKISENSEIYSLGLIAYELILGNLA-------------LGKVILSLVP----ERMSKILAKALQPSPKDRYAS 243
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQRVvqgasvaeilyqqLSPVDVSLPPwiagHPLGQVLRKALNKDPRQRAAS 236
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
35-274 5.46e-23

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 98.35  E-value: 5.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   35 HPVTLQPTVIKVLVTPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILSQ-LIPLS 113
Cdd:PTZ00263  39 HKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGELFTHLRKAgRFPND 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  114 RAVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAasSSMANDPYPVClGTPSYMSPEQRQGDKISEN 193
Cdd:PTZ00263 119 VAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA--KKVPDRTFTLC-GTPEYLAPEVIQSKGHGKA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  194 SEIYSLGLIAYELILG--------------NLALGKVIL-SLVPERMSKILAKALQPSPKDRYASMKEFLIDL--YKYRH 256
Cdd:PTZ00263 196 VDWWTMGVLLYEFIAGyppffddtpfriyeKILAGRLKFpNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVknHPYFH 275
                        250
                 ....*....|....*...
gi 89898773  257 GEDLQKdIRYKDHTAKIH 274
Cdd:PTZ00263 276 GANWDK-LYARYYPAPIP 292
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
18-214 2.00e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 97.20  E-value: 2.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   18 IKRIMSKKeGSTVYHGVHPVTLQPTVIKVLVTPLvADTLRvHNFLKEARIIEQISHPNIVKLYQ-YGQCREgLYMAMEHI 96
Cdd:PLN00034  79 VNRIGSGA-GGTVYKVIHRPTGRLYALKVIYGNH-EDTVR-RQICREIEILRDVNHPNVVKCHDmFDHNGE-IQVLLEFM 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   97 QGVSLRKYILSQLIPLSravDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYPVCLGT 176
Cdd:PLN00034 155 DGGSLEGTHIADEQFLA---DVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGT 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 89898773  177 PSYMSPEQ-----RQGDKISENSEIYSLGLIAYELILGNLALG 214
Cdd:PLN00034 232 IAYMSPERintdlNHGAYDGYAGDIWSLGVSILEFYLGRFPFG 274
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
63-213 7.05e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 81.04  E-value: 7.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773   63 KEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQgVSLRKYI-LSQLIPLSRAVDIILQIAQALEYLHSRGILHRDIKP 141
Cdd:PHA03207 135 REIDILKTISHRAIINLIHAYRWKSTVCMVMPKYK-CDLFTYVdRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKT 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89898773  142 ENILITPQGEIKLIDFGLAASSSMANDPyPVC---LGTPSYMSPEQRQGDKISENSEIYSLGLIAYELILGNLAL 213
Cdd:PHA03207 214 ENIFLDEPENAVLGDFGAACKLDAHPDT-PQCygwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
28-248 1.42e-52

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 178.58  E-value: 1.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  28 STVYHGVHPVTLQPTVIKVLvtPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILS 107
Cdd:cd00180   7 GTVYLARDKKTGKKVAIKII--KKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSLKDLLKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 108 QLIPLS--RAVDIILQIAQALEYLHSRGILHRDIKPENILIT-PQGEIKLIDFGLAASSSMANDPYPVCLGTPSYMSPEQ 184
Cdd:cd00180  85 NEGKLSedEILRILLQILEGLEYLHSNGIIHRDLKPENILLDsDNGKVKLADFGLSKLLTSDKSLLKTIVGTPAYMAPEV 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89898773 185 -RQGDKISENSEIYSLGLIAYELilgnlalgkvilslvpERMSKILAKALQPSPKDRYaSMKEFL 248
Cdd:cd00180 165 lLGKGYYSEKSDIWSLGVILYEL----------------PELKDLIRKMLQKDPEKRP-SAKEIL 212
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
44-240 4.80e-41

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 148.44  E-value: 4.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  44 IKVLVTPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILSQL-IPLSRAVDIILQI 122
Cdd:cd05123  23 MKVLKKKKIIKRKEVEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVLEYAPGGELFSHLSKEGrFSEERARFYAAEI 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 123 AQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMAND-PYPVClGTPSYMSPEQRQGDKISENSEIYSLGL 201
Cdd:cd05123 103 VLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLAKELSSEGSrTNTFC-GTPEYLAPEVLLGKGYGKAVDWWSLGV 181
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 89898773 202 IAYELILGNL--------ALGKVILSL-------VPERMSKILAKALQPSPKDR 240
Cdd:cd05123 182 LLYEMLTGKPpfyaedrkEIYEKILKDplrfpefLSPEARDLISGLLQKDPTKR 235
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
29-240 3.38e-39

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 143.12  E-value: 3.38e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  29 TVYHGVHPVTLQPTVIKVLvtPLVADTlRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILSQ 108
Cdd:cd05122  15 EVYKARHKRTGKEVAIKVI--KLESKE-KKEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKST 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 109 LIPLSR---AVdIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAA--SSSMANDpypVCLGTPSYMSPE 183
Cdd:cd05122  92 NQTLTEsqiAY-VCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDFGLSAqlSDTKARN---TMVGTPYWMAPE 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89898773 184 QRQGDKISENSEIYSLGLIAYELILGN---------LALGKVILSLVP-----ERMSKI----LAKALQPSPKDR 240
Cdd:cd05122 168 VINGKPYDYKADIWSLGITAIELAEGKppyselppmKALFKIATNGPPglrnpEKWSDEfkdfLKKCLQKNPEKR 242
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
62-240 1.93e-38

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 141.10  E-value: 1.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  62 LKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILSQ-----LIPLSRAVDIILQIAQALEYLHSRGILH 136
Cdd:cd08215  47 LNEVKILKKLNHPNIIKYYESFEEKGKLCIVMEYADGGDLSQKIKKQkkegkPFPEEQILDWFVQLCLALKYLHSRKILH 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 137 RDIKPENILITPQGEIKLIDFGLA----ASSSMANdpypVCLGTPSYMSPEQRQGDKISENSEIYSLGLIAYELILGNLA 212
Cdd:cd08215 127 RDIKPQNIFLTSNGLVKLGDFGISkvlsSTVDLAK----TVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHP 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 89898773 213 -LGKVILSLV---------------PERMSKILAKALQPSPKDR 240
Cdd:cd08215 203 fEGENLLELAlkilkgqyppipsqySSELRNLVSSLLQKDPEER 246
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
61-240 1.50e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 130.37  E-value: 1.50e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  61 FLKEARIIEQISHPNIVKlYqYGQCRE----GLYMAMEHIQGVSLRKyILSQLIPLSRAVDIIL--QIAQALEYLHSRGI 134
Cdd:cd06606  46 LEREIRILSSLQHPNIVR-Y-YGSERDeeknTLNIFLEYVSGGSLSS-LLKKFGKLPEPVIRKYtrQILEGLAYLHSNGI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 135 LHRDIKPENILITPQGEIKLIDFGLA---ASSSMANDPYPVClGTPSYMSPEQRQGDKISENSEIYSLGLIAYELI---- 207
Cdd:cd06606 123 VHRDIKGANILVDSDGVVKLADFGCAkrlGDIETGEGTGSVR-GTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMAtgkp 201
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 89898773 208 ----LGNL--ALGKVILSL----VPERMSKI----LAKALQPSPKDR 240
Cdd:cd06606 202 pwseLGNPmaALYKIGSSGeppeIPEHLSEEakdfLRKCLRRDPKKR 248
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
57-209 2.54e-34

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, 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 also contains an insert relative to MAST kinases like MASTL. 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. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 129.68  E-value: 2.54e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  57 RVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKyILSQL--IPLSRAVDIILQIAQALEYLHSRGI 134
Cdd:cd05579  36 QVDQVLTERDILSQAQSPYVVKLYYSFQGKKNLYLVMEYLPGGDLAS-LLENVgsLDEDVARIYIAEIVLALEYLHSNGI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 135 LHRDIKPENILITPQGEIKLIDFGLA---ASSSMANDPYPV-----CLGTPSYMSPEQRQGDKISENSEIYSLGLIAYEL 206
Cdd:cd05579 115 IHRDLKPDNILIDSNGHLKLTDFGLSkvgLVRRQINLNDDEkedkrIVGTPDYIAPEVILGQGHSKTVDWWSLGCILYEF 194

                ...
gi 89898773 207 ILG 209
Cdd:cd05579 195 LVG 197
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
57-209 1.15e-33

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


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 127.43  E-value: 1.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  57 RVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRkYILSQLIPLSRAVD--IILQIAQALEYLHSRGI 134
Cdd:cd05578  43 SVRNVLNERRILQELNHPFLVNLWYSFQDEENMYLVVDLLLGGDLR-YHLSQKVKFSEEQVkfWICEIVLALEYLHSKGI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 135 LHRDIKPENILITPQGEIKLIDFGLAA-------SSSMAndpypvclGTPSYMSPEQRQGDKISENSEIYSLGLIAYELI 207
Cdd:cd05578 122 IHRDIKPDNILLDEQGHVHITDFNIATkvtpdtlTTSTS--------GTPGYMAPEVLCRQGYSVAVDWWSLGVTAYECL 193

                ..
gi 89898773 208 LG 209
Cdd:cd05578 194 RG 195
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
27-248 2.56e-33

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 126.94  E-value: 2.56e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  27 GSTVYHGVHPVTLQPTVIKVLvtPLVADTLRVHNFLKEARIIEQISHPNIVKLYQ-YgqCREG-LYMAMEHIQGVSLRKy 104
Cdd:cd06623  14 SGVVYKVRHKPTGKIYALKKI--HVDGDEEFRKQLLRELKTLRSCESPYVVKCYGaF--YKEGeISIVLEYMDGGSLAD- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 105 ILSQLIPLSRAV--DIILQIAQALEYLHS-RGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYPVCLGTPSYMS 181
Cdd:cd06623  89 LLKKVGKIPEPVlaYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFVGTVTYMS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 182 PEQRQGDKISENSEIYSLGLIAYELILGN---LALGKV-------------ILSLVPERMSK----ILAKALQPSPKDRy 241
Cdd:cd06623 169 PERIQGESYSYAADIWSLGLTLLECALGKfpfLPPGQPsffelmqaicdgpPPSLPAEEFSPefrdFISACLQKDPKKR- 247

                ....*..
gi 89898773 242 ASMKEFL 248
Cdd:cd06623 248 PSAAELL 254
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
64-211 3.34e-33

Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cGMP-dependent protein kinase (cGK or PKG) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 126.19  E-value: 3.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  64 EARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYILSQ-LIPLSRAVDIILQIAQALEYLHSRGILHRDIKPE 142
Cdd:cd05572  43 EKEILEECNHPFIVKLYRTFKDKKYIYMLMEYCLGGELWTILRDRgLFDEYTARFYIACVVLAFEYLHNRGIIYRDLKPE 122
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89898773 143 NILITPQGEIKLIDFGLAASSSMANDPYPVClGTPSYMSPEQRQGDKISENSEIYSLGLIAYELILGNL 211
Cdd:cd05572 123 NLLLDSNGYVKLVDFGFAKKLKSGQKTWTFC-GTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRP 190
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
29-210 1.87e-32

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. 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. 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.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 123.90  E-value: 1.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  29 TVYHGVHPVTLQPTVIK-VLVTPLVADTLRVhnFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLRKyILS 107
Cdd:cd06627  15 VVYKGLNLETGDFVAIKqISLEKIKEEALKS--IMQEIDLLKNLKHPNIVKYIGSIETSDSLYIILEYAENGSLRQ-IIK 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 108 QLIPL--SRAVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYPVCLGTPSYMSPEQR 185
Cdd:cd06627  92 KFGPFpeSLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGVVKLADFGVATKLNDVSKDDASVVGTPYWMAPEVI 171
                       170       180
                ....*....|....*....|....*
gi 89898773 186 QGDKISENSEIYSLGLIAYELILGN 210
Cdd:cd06627 172 EMSGASTASDIWSLGCTVIELLTGN 196
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
62-209 4.95e-31

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. 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.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 120.11  E-value: 4.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  62 LKEARIIEQISHPNIVKLYQ--YGQCRegLYMAMEHIQGVSLRKYI--LSQLIPLSRAVDIILQIAQALEYLHS-RGILH 136
Cdd:cd06605  47 LRELDILHKCNSPYIVGFYGafYNNGD--ISICMEYMDGGSLDKILkeVQGRIPERILGKIAVAVLKGLTYLHEkHKIIH 124
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89898773 137 RDIKPENILITPQGEIKLIDFGLaaSSSMANDPYPVCLGTPSYMSPEQRQGDKISENSEIYSLGLIAYELILG 209
Cdd:cd06605 125 RDVKPSNILVNSRGQIKLCDFGV--SGQLVNSLAKTFVGTSSYMAPERIQGNDYSVKSDIWSLGLSLIELATG 195
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
28-209 7.92e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 117.30  E-value: 7.92e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  28 STVYHGVHPVTLQPTVIKVLVTPLVADTLRVHNFLKEARIIEQIS-HPNIVKLYQYGQCREGLYMAMEHIQGVSLRKYI- 105
Cdd:cd05581  15 STVVLAKEKETNKEYAIKILDKRQLIKEKKVKYVKIEKEVLTRLNgHPGIIKLYYTFQDEENLYFVLEYAPNGELLQYIr 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 106 ----LSQLIplsrAVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAA-----SSSMANDPYPVCL-- 174
Cdd:cd05581  95 kygsLDEKC----TRFYAAEILLALEYLHSKGIIHRDLKPENILLDKDMHIKITDFGTAKvldpnSSPESNKGDATNIds 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 89898773 175 -------------GTPSYMSPEQRQGDKISENSEIYSLGLIAYELILG 209
Cdd:cd05581 171 qieknrrrfasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTG 218
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
64-209 3.10e-29

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 115.13  E-value: 3.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  64 EARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLrkyilSQLIPLSRAVDII------LQIAQALEYLHSRGILHR 137
Cdd:cd06626  49 EMKVLELLKHPNLVKYYGVEVHREKVYIFMEYCSGGTL-----EELLEHGRILDEHvirvytLQLLEGLAYLHSHGIVHR 123
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89898773 138 DIKPENILITPQGEIKLIDFGLAASSSMANDPYPVCL----GTPSYMSPEQRQGDKISEN---SEIYSLGLIAYELILG 209
Cdd:cd06626 124 DIKPANIFLDHNGVIKLGDFGCAVKLKNNTTTMGEEVqslaGTPAYMAPEVITGGKGKGHgraADIWSLGCVVLEMATG 202
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
34-209 1.11e-28

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a 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). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) 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 C 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.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 114.18  E-value: 1.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  34 VHPVTLQPT----VIKVLVTPLVADTLRVHNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQG----VSLRKyi 105
Cdd:cd05580  17 VMLVRHKGSgkyyALKILSKAKIVKLKQVEHVLNEKRILQSIRHPFLVNLYGSFQDDSNLYLVMEYVPGgelfSHLRK-- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773 106 lSQLIPLSRAVDIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAasSSMANDPYPVClGTPSYMSPE-- 183
Cdd:cd05580  95 -SGRFPEPVARFYAAQVVLALEYLHSLDIVYRDLKPENLLLDSDGYIKITDFGFA--KRVKGRTYTLC-GTPEYLAPEii 170
                       170       180
                ....*....|....*....|....*.
gi 89898773 184 QRQGDKISenSEIYSLGLIAYELILG 209
Cdd:cd05580 171 LSKGYGKA--VDWWALGILIYEMLAG 194
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine ...
26-209 1.22e-28

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase (CDK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK-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. 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.


Pssm-ID: 173733 [Multi-domain]  Cd Length: 282  Bit Score: 113.73  E-value: 1.22e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  26 EGS--TVYHGVHPVTLQPTVIKVLVTPLVAD-----TLRvhnflkEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQg 98
Cdd:cd07829   9 EGTygVVYKARDKKTGEIVALKKIRLDNEEEgipstALR------EISLLKELKHPNIVKLLDVIHTERKLYLVFEYCD- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  99 VSLRKYILSQLIPLSRAV--DIILQIAQALEYLHSRGILHRDIKPENILITPQGEIKLIDFGLAASSSMANDPYpvclgT 176
Cdd:cd07829  82 MDLKKYLDKRPGPLSPNLikSIMYQLLRGLAYCHSHRILHRDLKPQNILINRDGVLKLADFGLARAFGIPLRTY-----T 156
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 89898773 177 PS-----YMSPEQRQGDKISENS-EIYSLGLIAYELILG 209
Cdd:cd07829 157 HEvvtlwYRAPEILLGSKHYSTAvDIWSVGCIFAEMITG 195
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
26-248 1.24e-28

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, 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 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.


Pssm-ID: 173728 [Multi-domain]  Cd Length: 286  Bit Score: 113.85  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89898773  26 EGST--VYHGVHPVTLQPTVIKVLvtPLVADTLRvhNFLKEARIIEQISHPNIVKLYQYGQCREGLYMAMEHIQGVSLrK 103
Cdd:cd06614  29 EGASgeVYKATDRATGKEVAIKKM--RLRKQNKE--LIINEILIMKDCKHPNIVDYYDSYLVGDELWVVMEYMDGGSL-T 103