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Conserved domains on  [gi|31793271|ref|NP_855764|]
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Ser/Thr protein kinase [Mycobacterium bovis AF2122/97]

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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 ...
20-209 3.80e-44

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: 156.63  E-value: 3.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  20 LGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNA 99
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKII--KKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 100 EDALRA--ATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaagGDERVLLSDFGIARALGDTGLTSTGSVl 177
Cdd:cd00180  79 KDLLKEneGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDS---DNGKVKLADFGLSKLLTSDKSLLKTIV- 154
                       170       180       190
                ....*....|....*....|....*....|...
gi 31793271 178 ATLAYAAPEVLAGQGFDGR-ADLYSLGCALFRL 209
Cdd:cd00180 155 GTPAYMAPEVLLGKGYYSEkSDIWSLGVILYEL 187
PknH_C pfam14032
PknH-like extracellular domain; This domain is functionally uncharacterized. It is found as ...
394-587 5.82e-33

PknH-like extracellular domain; This domain is functionally uncharacterized. It is found as the periplasmic domain of the bacterial protein kinase PknH. The domain is also found in isolation in numerous proteins, for example the lipoproteins lpqQ, lprH, lppH and lpqA from M. tuberculosis. This family of proteins is found in bacteria. Proteins in this family are typically between 214 and 268 amino acids in length. There are two completely conserved C residues that are likely to form a disulphide bond. A second pair of cysteines are less well conserved probably form a second disulphide bond. It seems likely that this domain functions to bind some as yet unknown ligand.


:

Pssm-ID: 258267  Cd Length: 189  Bit Score: 124.83  E-value: 5.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   394 VTRSRLPGLLPPLDDVKNFVGIQNLVAHEPMLQPQTPNGSINPAECWPAVGGGVPSAYDLGtVIGFYGLTIDEPPTGTAP 473
Cdd:pfam14032   3 VTPAALDSLLLTPAEVAAILGAPELAVDAPSTPGTDGAASVDPPECLGVAGPAQASVYASG-YTAFRGQTLQETGPDGDH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   474 nQVGQLIVAFRDAATAQRHLADLASIWRRCGGRTVTLfrSEWRRPVELSTSVPEVVDGITTMVLTAQGPVLRvREDHAIA 553
Cdd:pfam14032  82 -LVSQAVVVFPSADAAQAFFASLADRWRGCAGQTVTV--SDDGPTETWTVGDVTADDGVVAWTLTQEGGDGW-SCQRALR 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 31793271   554 AKNNVLVDVDIMtpDTSRGQQAVIGITNYILAKI 587
Cdd:pfam14032 158 VRGNVVVDVTVC--GAGDGGDAAVAIADAIAAKV 189
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-266 1.91e-61

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 205.46  E-value: 1.91e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271     14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQF 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVI--KKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271     94 VDGGNAEDALRAA-TMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGDTGLTS 172
Cdd:smart00220  79 CEGGDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE----DGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271    173 TgsVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPFaaGAGAAVAVVAGHLHQPPPTVSDRVPGLSAAMDAV 252
Cdd:smart00220 155 T--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPF--PGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....
gi 31793271    253 IATAMAKDPMRRFT 266
Cdd:smart00220 231 IRKLLVKDPEKRLT 244
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
20-209 3.80e-44

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: 156.63  E-value: 3.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  20 LGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNA 99
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKII--KKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 100 EDALRA--ATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaagGDERVLLSDFGIARALGDTGLTSTGSVl 177
Cdd:cd00180  79 KDLLKEneGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDS---DNGKVKLADFGLSKLLTSDKSLLKTIV- 154
                       170       180       190
                ....*....|....*....|....*....|...
gi 31793271 178 ATLAYAAPEVLAGQGFDGR-ADLYSLGCALFRL 209
Cdd:cd00180 155 GTPAYMAPEVLLGKGYYSEkSDIWSLGVILYEL 187
PknH_C pfam14032
PknH-like extracellular domain; This domain is functionally uncharacterized. It is found as ...
394-587 5.82e-33

PknH-like extracellular domain; This domain is functionally uncharacterized. It is found as the periplasmic domain of the bacterial protein kinase PknH. The domain is also found in isolation in numerous proteins, for example the lipoproteins lpqQ, lprH, lppH and lpqA from M. tuberculosis. This family of proteins is found in bacteria. Proteins in this family are typically between 214 and 268 amino acids in length. There are two completely conserved C residues that are likely to form a disulphide bond. A second pair of cysteines are less well conserved probably form a second disulphide bond. It seems likely that this domain functions to bind some as yet unknown ligand.


Pssm-ID: 258267  Cd Length: 189  Bit Score: 124.83  E-value: 5.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   394 VTRSRLPGLLPPLDDVKNFVGIQNLVAHEPMLQPQTPNGSINPAECWPAVGGGVPSAYDLGtVIGFYGLTIDEPPTGTAP 473
Cdd:pfam14032   3 VTPAALDSLLLTPAEVAAILGAPELAVDAPSTPGTDGAASVDPPECLGVAGPAQASVYASG-YTAFRGQTLQETGPDGDH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   474 nQVGQLIVAFRDAATAQRHLADLASIWRRCGGRTVTLfrSEWRRPVELSTSVPEVVDGITTMVLTAQGPVLRvREDHAIA 553
Cdd:pfam14032  82 -LVSQAVVVFPSADAAQAFFASLADRWRGCAGQTVTV--SDDGPTETWTVGDVTADDGVVAWTLTQEGGDGW-SCQRALR 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 31793271   554 AKNNVLVDVDIMtpDTSRGQQAVIGITNYILAKI 587
Cdd:pfam14032 158 VRGNVVVDVTVC--GAGDGGDAAVAIADAIAAKV 189
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
56-163 1.22e-05

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 45.35  E-value: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  56 RARFVREADV-----AAGLDHPNIVAVhqrgqFEGRLWIAMQFVDGGNAEDALRAATMTTARAVyviGE-VAKAldyaHQ 129
Cdd:COG3642  43 RERTRREARIlakarEAGVPVPIVYDV-----DPDNGLIVMEYIEGELLKDALEEARPDLLREV---GRlVGKL----HK 110
                        90       100       110
                ....*....|....*....|....*....|....
gi 31793271 130 QGVIHRDIKPANFLLSraaggDERVLLSDFGIAR 163
Cdd:COG3642 111 AGIVHGDLTTSNIILS-----GGRIYFIDFGLGE 139
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
56-163 1.34e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 45.28  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   56 RARFVREADV-----AAGLDHPNIVAVhqrgqFEGRLWIAMQFVDGGNAEDALRAATMTTARAVYVIGEVAKALdyaHQQ 130
Cdd:PRK14879  43 RERTRREARImsrarKAGVNVPAVYFV-----DPENFIIVMEYIEGEPLKDLINSNGMEELELSREIGRLVGKL---HSA 114
                         90       100       110
                 ....*....|....*....|....*....|...
gi 31793271  131 GVIHRDIKPANFLLSraaggDERVLLSDFGIAR 163
Cdd:PRK14879 115 GIIHGDLTTSNMILS-----GGKIYLIDFGLAE 142
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
89-163 7.85e-04

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: 39.89  E-value: 7.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31793271    89 IAMQFVDGGNAEDALRAATMTTARAvyvIGEVAKALdyaHQQGVIHRDIKPANFLLSraaggDERVLLSDFGIAR 163
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIEEGNDELLRE---IGRLVGKL---HKAGIVHGDLTTSNIIVR-----DDKLYLIDFGLGK 137
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
126-216 1.64e-03

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: 39.32  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   126 YAHQQGVIHRDIKPANFLLSRAAGgderVLLSDFGIARALGDTGLTSTGSVlatlAYAAPEVLAGQGFDGRA-------- 197
Cdd:pfam14531 161 GLQHRGLVHGDFRPDNFFLDQKGG----VFLGGFTALVRAGTKVVVSEVDV----AFAPPELFASRGYTGKNtttmthkt 232
                          90
                  ....*....|....*....
gi 31793271   198 DLYSLGCALFRLLTGEAPF 216
Cdd:pfam14531 233 DAWQLGLVIYRIWCLRLPF 251
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
14-206 3.30e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 38.39  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   14 YRIERMLGAGGMGTVY---LARNPDLPRSEALKVLAAE----LSRDLDFRARFvrEADVAA------GLDHPNIVAVHQR 80
Cdd:PHA02882  14 WKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLEnetiVMETLVYNNIY--DIDKIAlwknihNIDHLGIPKYYGC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   81 GQFEG-----RLWIAMQFVDGGNaEDALRAATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSraagGDERVL 155
Cdd:PHA02882  92 GSFKRcrmyyRFILLEKLVENTK-EIFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVD----GNNRGY 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 31793271  156 LSDFGIARALGDTG------LTSTGSVLATLAYAAPEVLAGQGFDGRADLYSLG-CAL 206
Cdd:PHA02882 167 IIDYGIASHFIIHGkhieysKEQKDLHRGTLYYAGLDAHNGACVTRRGDLESLGyCML 224
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
116-215 4.38e-03

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: 37.38  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271    116 VIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggdervllsdFGIARALGDTGLTSTGSVLAtlayaaPEVLAGQGFDG 195
Cdd:smart00750  22 VCLQCLGALRELHRQAKSGNILLTWDGLLKL------------DGSVAFKTPEQSRPDPYFMA------PEVIQGQSYTE 83
                           90       100
                   ....*....|....*....|
gi 31793271    196 RADLYSLGCALFRLLTGEAP 215
Cdd:smart00750  84 KADIYSLGITLYEALDYELP 103
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-266 1.91e-61

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 205.46  E-value: 1.91e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271     14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQF 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVI--KKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271     94 VDGGNAEDALRAA-TMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGDTGLTS 172
Cdd:smart00220  79 CEGGDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE----DGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271    173 TgsVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPFaaGAGAAVAVVAGHLHQPPPTVSDRVPGLSAAMDAV 252
Cdd:smart00220 155 T--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPF--PGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....
gi 31793271    253 IATAMAKDPMRRFT 266
Cdd:smart00220 231 IRKLLVKDPEKRLT 244
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
13-267 5.25e-50

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: 178.40  E-value: 5.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  13 GYRIERMLGAGGMGTVYLARNPdlpRSEALKVLAAELSRDLDFRARFVREADVAAGLDHP-NIVAVHQRGQFEGRLWIAM 91
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  92 QFVDGGNAEDALR----AATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaagGDERVLLSDFGIARALGD 167
Cdd:COG0515  78 EYVDGGSLEDLLKkigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR---DGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 168 TGLTS-----TGSVLATLAYAAPEVLAGQGF---DGRADLYSLGCALFRLLTGEAPFAAGAGAAVAVVAG-HLHQ----- 233
Cdd:COG0515 155 PGSTSsipalPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkIILElptps 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 31793271 234 -PPPTVSDRVPGLSAAMDAVIATAMAKDPMRRFTS 267
Cdd:COG0515 235 lASPLSPSNPELISKAASDLLKKLLAKDPKNRLSS 269
Pkinase pfam00069
Protein kinase domain;
14-266 6.47e-48

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 168.96  E-value: 6.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271    14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLAAElSRDLDFRARFVREADVAAGLDHPNIVAVHqrGQFE--GRLWIAM 91
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLI--DAFEdkDHLYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271    92 QFVDGGNAEDALRAAT-MTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGDTGl 170
Cdd:pfam00069  78 EYCEGGDLFDYLSRGGpLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDE----NGVVKIADFGLAKKLTKSS- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   171 TSTGSVLATLAYAAPEVLA-GQGFDGRADLYSLGCALFRLLTGEAPFAAGAGAAVAVVAGHLHQPPPTVSDR--VPGLSA 247
Cdd:pfam00069 153 SSLTTFVGTPEYMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDEPksDSGSEE 232
                         250
                  ....*....|....*....
gi 31793271   248 AMDaVIATAMAKDPMRRFT 266
Cdd:pfam00069 233 AKD-LIKKCLNKDPSKRPT 250
pknD PRK13184
serine/threonine-protein kinase; Reviewed
14-267 1.81e-26

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 113.33  E-value: 1.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLAAELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQF 93
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   94 VDGGNAEDALRA-----------ATMTTARAVYVI-GEVAKALDYAHQQGVIHRDIKPANFLLsraaGGDERVLLSDFGI 161
Cdd:PRK13184  84 IEGYTLKSLLKSvwqkeslskelAEKTSVGAFLSIfHKICATIEYVHSKGVLHRDLKPDNILL----GLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  162 ARA-------LGD----------TGLTSTGSVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPFaaGAGAAV 224
Cdd:PRK13184 160 AIFkkleeedLLDidvdernicySSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY--RRKKGR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 31793271  225 AVVAGHLHQPPPTVS---DRVPGLSaamdAVIATAMAKDPMRRFTS 267
Cdd:PRK13184 238 KISYRDVILSPIEVApyrEIPPFLS----QIAMKALAVDPAERYSS 279
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
41-213 1.20e-23

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: 104.93  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271     41 ALKVLAAELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFE-GRLWIAMQFVDGGNAEDALRA-ATMTTARAVYVIG 118
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAAdGALPAGETGRLML 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271    119 EVAKALDYAHQQGVIHRDIKPANFLLSrAAGGDERVLLSDFGIARALGDTG------LTSTGSVLATLAYAAPEVLAGQG 192
Cdd:TIGR03903   87 QVLDALACAHNQGIVHRDLKPQNIMVS-QTGVRPHAKVLDFGIGTLLPGVRdadvatLTRTTEVLGTPTYCAPEQLRGEP 165
                          170       180
                   ....*....|....*....|.
gi 31793271    193 FDGRADLYSLGCALFRLLTGE 213
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTGQ 186
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
15-216 3.23e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 97.20  E-value: 3.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   15 RIERmLGAGGMGTVYLARNPDLPRSEALKVLAAelSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFV 94
Cdd:PLN00034  78 RVNR-IGSGAGGTVYKVIHRPTGRLYALKVIYG--NHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFM 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   95 DGGNAEDALRAATMTTARavyVIGEVAKALDYAHQQGVIHRDIKPANFLLSRAaggdERVLLSDFGIARALGDTgLTSTG 174
Cdd:PLN00034 155 DGGSLEGTHIADEQFLAD---VARQILSGIAYLHRRHIVHRDIKPSNLLINSA----KNVKIADFGVSRILAQT-MDPCN 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 31793271  175 SVLATLAYAAPEVL---AGQG-FDGRA-DLYSLGCALFRLLTGEAPF 216
Cdd:PLN00034 227 SSVGTIAYMSPERIntdLNHGaYDGYAgDIWSLGVSILEFYLGRFPF 273
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
20-216 8.89e-21

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 92.57  E-value: 8.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   20 LGAGGMGTVYLARNPDLPRSEALKVLAAELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNA 99
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  100 EDALR-AATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSraagGDERVLLSDFGIARALGDTGLTSTGsvla 178
Cdd:PTZ00263 106 FTHLRkAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLD----NKGHVKVTDFGFAKKVPDRTFTLCG---- 177
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 31793271  179 TLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:PTZ00263 178 TPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
13-210 3.91e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 63.74  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   13 GYRIERMLGAGGMGTVYLARNPDLPRSEALKVlaaelsrdlDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAM- 91
Cdd:PHA03209  67 GYTVIKTLTPGSEGRVFVATKPGQPDPVVLKI---------GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLp 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   92 QFVDGGNAEDALRAATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRAaggdERVLLSDFGIAR----ALGD 167
Cdd:PHA03209 138 HYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDV----DQVCIGDLGAAQfpvvAPAF 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 31793271  168 TGLTstgsvlATLAYAAPEVLAGQGFDGRADLYSLGCALFRLL 210
Cdd:PHA03209 214 LGLA------GTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
20-209 3.80e-44

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: 156.63  E-value: 3.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  20 LGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNA 99
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKII--KKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 100 EDALRA--ATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaagGDERVLLSDFGIARALGDTGLTSTGSVl 177
Cdd:cd00180  79 KDLLKEneGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDS---DNGKVKLADFGLSKLLTSDKSLLKTIV- 154
                       170       180       190
                ....*....|....*....|....*....|...
gi 31793271 178 ATLAYAAPEVLAGQGFDGR-ADLYSLGCALFRL 209
Cdd:cd00180 155 GTPAYMAPEVLLGKGYYSEkSDIWSLGVILYEL 187
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
14-216 3.18e-42

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: 152.75  E-value: 3.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLAAELSRDldfRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQF 93
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEK---KEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  94 VDGGNAEDALRAA--TMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGDTGLT 171
Cdd:cd05122  79 CSGGSLKDLLKSTnqTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTS----DGEVKLIDFGLSAQLSDTKAR 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 31793271 172 STgsVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd05122 155 NT--MVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPY 197
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
14-216 3.52e-38

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: 141.16  E-value: 3.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFV-READVAAGLDHPNIVAV--HQRGQFEGRLWIA 90
Cdd:cd06606   2 WTRGELLGRGSFGSVYLALDKDTGELMAVKSV--ELSGDSEEELEALeREIRILSSLQHPNIVRYygSERDEEKNTLNIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  91 MQFVDGGNAEDALR---AATMTTARaVYVIgEVAKALDYAHQQGVIHRDIKPANFLLSraagGDERVLLSDFGIARALGD 167
Cdd:cd06606  80 LEYVSGGSLSSLLKkfgKLPEPVIR-KYTR-QILEGLAYLHSNGIVHRDIKGANILVD----SDGVVKLADFGCAKRLGD 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 31793271 168 TGLT-STGSVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd06606 154 IETGeGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPW 203
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
14-216 1.03e-37

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: 139.94  E-value: 1.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSR-DLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQ 92
Cdd:cd08215   2 YEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEI--DLSNmSEKEREDALNEVKILKKLNHPNIIKYYESFEEKGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  93 FVDGGNAEDALRAAT-----MTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGD 167
Cdd:cd08215  80 YADGGDLSQKIKKQKkegkpFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTS----NGLVKLGDFGISKVLSS 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 31793271 168 TG-LTSTgsVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd08215 156 TVdLAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPF 203
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
20-216 5.13e-34

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: 129.18  E-value: 5.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  20 LGAGGMGTVYLARNPDLPRSEALKVLAAELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNA 99
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLKKKKIIKRKEVEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVLEYAPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 100 EDALRAA-TMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLsraaGGDERVLLSDFGIARALGDTGlTSTGSVLA 178
Cdd:cd05123  81 FSHLSKEgRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL----DADGHIKLTDFGLAKELSSEG-SRTNTFCG 155
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 31793271 179 TLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd05123 156 TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF 193
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
14-267 1.22e-33

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3-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. 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.


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 128.89  E-value: 1.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDHPNIVAVHqrGQFEG--RLWIAM 91
Cdd:cd06609   3 FTLLECIGKGSFGEVYKAIDKRTNQVVAIKVI--DLEEAEDEIEDIQQEIQFLSQCRSPYITKYY--GSFLKgsKLWIIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  92 QFVDGGNAEDALRAATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSraAGGDerVLLSDFGIARALGDTGL- 170
Cdd:cd06609  79 EYCGGGSCLDLLKPGKLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANILLS--EEGD--VKLADFGVSGQLTSTMSk 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 171 --TSTGsvlaTLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPFaagagaavavvaGHLH----------QPPPTV 238
Cdd:cd06609 155 rnTFVG----TPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPL------------SDLHpmrvlflipkNNPPSL 218
                       250       260
                ....*....|....*....|....*....
gi 31793271 239 SDRvpGLSAAMDAVIATAMAKDPMRRFTS 267
Cdd:cd06609 219 EGN--KFSKPFKDFVSLCLNKDPKERPSA 245
PknH_C pfam14032
PknH-like extracellular domain; This domain is functionally uncharacterized. It is found as ...
394-587 5.82e-33

PknH-like extracellular domain; This domain is functionally uncharacterized. It is found as the periplasmic domain of the bacterial protein kinase PknH. The domain is also found in isolation in numerous proteins, for example the lipoproteins lpqQ, lprH, lppH and lpqA from M. tuberculosis. This family of proteins is found in bacteria. Proteins in this family are typically between 214 and 268 amino acids in length. There are two completely conserved C residues that are likely to form a disulphide bond. A second pair of cysteines are less well conserved probably form a second disulphide bond. It seems likely that this domain functions to bind some as yet unknown ligand.


Pssm-ID: 258267  Cd Length: 189  Bit Score: 124.83  E-value: 5.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   394 VTRSRLPGLLPPLDDVKNFVGIQNLVAHEPMLQPQTPNGSINPAECWPAVGGGVPSAYDLGtVIGFYGLTIDEPPTGTAP 473
Cdd:pfam14032   3 VTPAALDSLLLTPAEVAAILGAPELAVDAPSTPGTDGAASVDPPECLGVAGPAQASVYASG-YTAFRGQTLQETGPDGDH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271   474 nQVGQLIVAFRDAATAQRHLADLASIWRRCGGRTVTLfrSEWRRPVELSTSVPEVVDGITTMVLTAQGPVLRvREDHAIA 553
Cdd:pfam14032  82 -LVSQAVVVFPSADAAQAFFASLADRWRGCAGQTVTV--SDDGPTETWTVGDVTADDGVVAWTLTQEGGDGW-SCQRALR 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 31793271   554 AKNNVLVDVDIMtpDTSRGQQAVIGITNYILAKI 587
Cdd:pfam14032 158 VRGNVVVDVTVC--GAGDGGDAAVAIADAIAAKV 189
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase-like Protein Serine ...
14-264 1.18e-32

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 3 (MAPKKKK3 or MAP4K3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K3-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. 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, similar to MAP4K4/6. MAP4Ks are involved in some MAPK signaling pathways that are important in mediating cellular responses to extracellular signals by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). 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. 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).


Pssm-ID: 173727 [Multi-domain]  Cd Length: 262  Bit Score: 125.87  E-value: 1.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNpdLPRSE--ALKVLAAELSRDLDFrarFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAM 91
Cdd:cd06613   5 YELIQRIGSGTYGDVYKARD--IATGElvAIKVIKLEPGDDFEI---IQQEISMLKECRHPNIVAYFGSYLRRDKLWIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  92 QFVDGGNAEDALRA--ATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaGGDerVLLSDFGIARALGDTg 169
Cdd:cd06613  80 EYCGGGSLQDIYQVtrGPLSELQIAYVCRETLKGLAYLHETGKIHRDIKGANILLTE--DGD--VKLADFGVSAQLTAT- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 170 LTSTGSVLATLAYAAPEVLA---GQGFDGRADLYSLGCALFRLLTGEAPFAAGAGAAVAVVAGHLHQPPPTVSDRvPGLS 246
Cdd:cd06613 155 IAKRKSFIGTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLISKSNFPPPKLKDK-EKWS 233
                       250
                ....*....|....*...
gi 31793271 247 AAMDAVIATAMAKDPMRR 264
Cdd:cd06613 234 PVFHDFIKKCLTKDPKKR 251
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
14-216 2.71e-31

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: 121.97  E-value: 2.71e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSRDL-DFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQ 92
Cdd:cd06627   2 YQLGDLIGRGAFGVVYKGLNLETGDFVAIKQI--SLEKIKeEALKSIMQEIDLLKNLKHPNIVKYIGSIETSDSLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  93 FVDGGNAEDALRAATMTTAR--AVYVIgEVAKALDYAHQQGVIHRDIKPANFLLSraagGDERVLLSDFGIARALGDTGL 170
Cdd:cd06627  80 YAENGSLRQIIKKFGPFPESlvAVYVY-QVLQGLAYLHEQGVIHRDIKAANILTT----KDGVVKLADFGVATKLNDVSK 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31793271 171 TSTgSVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd06627 155 DDA-SVVGTPYWMAPEVIEMSGASTASDIWSLGCTVIELLTGNPPY 199
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
20-266 1.32e-30

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: 120.00  E-value: 1.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  20 LGAGGMGTVYLARNPDLPRSEALKVLAaeLSRDLDFRARFVREADVAAGLDHPNIVAVHqrGQF--EGRLWIAMQFVDGG 97
Cdd:cd06623   9 LGQGSSGVVYKVRHKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRSCESPYVVKCY--GAFykEGEISIVLEYMDGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  98 NAEDALRAATMTTARAV-YVIGEVAKALDYAHQQ-GVIHRDIKPANFLLSRAagGDerVLLSDFGIARALgDTGLTSTGS 175
Cdd:cd06623  85 SLADLLKKVGKIPEPVLaYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSK--GE--VKIADFGISKVL-ENTLDQCNT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 176 VLATLAYAAPEVLAGQ--GFDgrADLYSLGCALFRLLTGEAPFAAGAGAAVAVVAGHL-HQPPPTVSDRvpGLSAAMDAV 252
Cdd:cd06623 160 FVGTVTYMSPERIQGEsySYA--ADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAIcDGPPPSLPAE--EFSPEFRDF 235
                       250
                ....*....|....
gi 31793271 253 IATAMAKDPMRRFT 266
Cdd:cd06623 236 ISACLQKDPKKRPS 249
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
14-216 2.50e-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: 119.61  E-value: 2.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLAAELSRDLDfRARFV-READVAAGLD-HPNIVAVHQRGQFEGRLWIAM 91
Cdd:cd05581   3 FKFGKIIGEGSFSTVVLAKEKETNKEYAIKILDKRQLIKEK-KVKYVkIEKEVLTRLNgHPGIIKLYYTFQDEENLYFVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  92 QFVDGGNAEDALR---AATMTTARavYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGDT 168
Cdd:cd05581  82 EYAPNGELLQYIRkygSLDEKCTR--FYAAEILLALEYLHSKGIIHRDLKPENILLDK----DMHIKITDFGTAKVLDPN 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31793271 169 GLTS-------------------TGSVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd05581 156 SSPEsnkgdatnidsqieknrrrFASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPF 222
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
14-267 2.62e-30

Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; Serine/threonine kinases (STKs), oxidative stress response kinase (OSR1) and Ste20-related proline alanine-rich kinase (SPAK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 119.38  E-value: 2.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNpdLPRSE--ALKVLAAELSR-DLDFrarFVREADVAAGLDHPNIVAVHqrGQF-EGR-LW 88
Cdd:cd06610   3 YELIEVIGVGATAVVYAAIC--LPNNEkvAIKRIDLEKCQtSVDE---LRKEVQAMSQCNHPNVVKYY--TSFvVGDeLW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  89 IAMQFVDGGNAEDALRAA----TMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLsraaGGDERVLLSDFGIARA 164
Cdd:cd06610  76 LVMPYLSGGSLLDIMKSSyprgGLDEAIIATVLKEVLKGLEYLHSNGQIHRDIKAGNILL----GEDGSVKIADFGVSAS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 165 LGDTGLTSTGS---VLATLAYAAPEVLA-GQGFDGRADLYSLGCALFRLLTGEAPFAagagaavavvaghlHQPPP---- 236
Cdd:cd06610 152 LADGGDRTRKVrktFVGTPCWMAPEVMEqVHGYDFKADIWSFGITAIELATGAAPYS--------------KYPPMkvlm 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 31793271 237 -TVSDRVPGL---------SAAMDAVIATAMAKDPMRRFTS 267
Cdd:cd06610 218 lTLQNDPPSLetgadykkySKSFRKMISLCLQKDPSKRPTA 258
STKc_RSK_N cd05582
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, 90 kDa ribosomal protein ...
18-216 3.11e-30

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; Serine/Threonine Kinases (STKs), 90 kDa ribosomal protein S6 kinase (RSK) subfamily, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173673 [Multi-domain]  Cd Length: 318  Bit Score: 120.29  E-value: 3.11e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  18 RMLGAGGMGTVYLARN---PDLPRSEALKVL-AAELS-RDldfRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQ 92
Cdd:cd05582   2 KVLGQGSFGKVFLVRKitgPDAGQLYAMKVLkKATLKvRD---RVRTKMERDILAEVNHPFIVKLHYAFQTEGKLYLILD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  93 FVDGGNAEDALRAATMTTARAV-YVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARALGDtGLT 171
Cdd:cd05582  79 FLRGGDLFTRLSKEVMFTEEDVkFYLAELALALDHLHSLGIIYRDLKPENILLDE----EGHIKLTDFGLSKESID-HEK 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 31793271 172 STGSVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd05582 154 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPF 198
STKc_Sid2p_Dbf2p cd05600
Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine ...
20-216 3.81e-30

Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ROCK- and NDR-like subfamily, fungal Sid2p- and Dbf2p-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sid2p- and Dbf2p-like group is part of a 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 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.


Pssm-ID: 173691 [Multi-domain]  Cd Length: 333  Bit Score: 120.20  E-value: 3.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  20 LGAGGMGTVYLARNPDLPRSEALKVLAAELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNA 99
Cdd:cd05600   9 VGQGGYGQVFLAKKKDTGEIVALKRMKKSLLFKLNEVRHVLTERDILTTTKSEWLVKLLYAFQDDEYLYLAMEYVPGGDF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 100 EDALRA-ATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRaaggDERVLLSDFGIARAlgdtGLTSTGSVLA 178
Cdd:cd05600  89 RTLLNNlGVLSEDHARFYMAEMFEAVDALHELGYIHRDLKPENFLIDA----SGHIKLTDFGLSKG----IVTYANSVVG 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 31793271 179 TLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPF 216
Cdd:cd05600 161 SPDYMAPEVLRGKGYDFTVDYWSLGCMLYEFLCGFPPF 198
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine ...
14-267 7.26e-30

Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Nak1 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nak1 subfamily is part of a 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 is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also known as 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.


Pssm-ID: 132991 [Multi-domain]  Cd Length: 277  Bit Score: 118.31  E-value: 7.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  14 YRIERMLGAGGMGTVYLARNPDLPRSEALKVLaaELSRDLDFRARFVREADVAAGLDH---PNIVAVHQRGQFEGRLWIA 90
Cdd:cd06917   3 YQRLELIGRGAYGAVYRGKHVPTGRVVALKII--NLDTPDDDVSDIQREVALLSQLRQsqpPNITKYYGSYLKGPRLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271  91 MQFVDGGNAEDALRAATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRAAggdeRVLLSDFGIARALGDTGL 170
Cdd:cd06917  81 MEYAEGGSVRTLMKAGPIAEKYISVIIREVLVALKYIHKVGVIHRDIKAANILVTNTG----NVKLCDFGVAALLNQNSS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31793271 171 TSTgSVLATLAYAAPEV-LAGQGFDGRADLYSLGCALFRLLTGEAPFAAGAGAAVAVVAGhlHQPPPTVSDRvpGLSAAM 249
Cdd:cd06917 157 KRS-TFVGTPYWMAPEViTEGKYYDTKADIWSLGITIYEMATGNPPYSDVDAFRAMMLIP--KSKPPRLEDN--GYSKLL 231
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