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Conserved domains on  [gi|75906659|ref|YP_320955|]
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serine/threonine protein kinase [Anabaena variabilis ATCC 29413]

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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 ...
40-299 9.61e-33

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: 125.81  E-value: 9.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  40 LGGGGFGKTFAVNDTRTQTAKVLKVL-INNHPKAVELFQREAEVLALLNYPGIptVEANGYFvyfprnSQEPMHCLVMEK 118
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIkKEDSSSLLEELLREIEILKKLNHPNI--VKLYGVF------EDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 119 IEGLDLGQYLRQRDyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIML-RADGRLVLIDFGTARSVTGTYIAKQ 197
Cdd:cd00180  73 CEGGSLKDLLKENE-GKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLdSDNGKVKLADFGLSKLLTSDKSLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 198 avgqvTGVISAGYTPSEQINGQAV--QQSDFFALGRTFIYlltgkepsdptiynylndelrwrdgllssgsnsvtptvgd 275
Cdd:cd00180 152 -----TIVGTPAYMAPEVLLGKGYysEKSDIWSLGVILYE---------------------------------------- 186
                       250       260
                ....*....|....*....|....
gi 75906659 276 rpniLPQFADLLDQMMERLPAQRP 299
Cdd:cd00180 187 ----LPELKDLIRKMLQKDPEKRP 206
Pectinesterase super family cl01911
Pectinesterase;
361-582 3.71e-06

Pectinesterase;


The actual alignment was detected with superfamily member pfam01095:

Pssm-ID: 261113  Cd Length: 298  Bit Score: 47.99  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   361 IVSQEGGGDYKTISAAIeNAQP---GMR--ILVRPGLYQESLVLDKALK---IIGDGVKAEIIIESKDAgclvvktdqae 432
Cdd:pfam01095   3 VVAKDGSGQFKTINEAV-AAAPkksSKRfvIYVKAGVYKENVEVPKKKTnvmFVGDGPGKTIITGSLNF----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   433 VRGL-TFRSRVgtenkqyFAVdisQGQVILADcDITSDSLSGIGVHGATA------NPVIQKCQIhDGKQSGIYLYENsR 505
Cdd:pfam01095  71 IDGGtTFRTAT-------FAV---VGDGFIAR-DITFENTAGPEKHQAVAlrvgadLSVFYRCSF-DGYQDTLYVHSN-R 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   506 GTIEDCDFFGnttteiTVD----AAQPIIRRCKIHQDKEGgilfRNQ-----AQGIVEDcdifnNNLSGIeirdssnpTI 576
Cdd:pfam01095 138 QFYRDCDITG------TVDfifgNAAAVFQNCNIVARKPL----PGQkntvtAQGRTDP-----NQNTGI--------VI 194

                  ....*.
gi 75906659   577 QKCRIH 582
Cdd:pfam01095 195 QNCRIT 200
para_beta_helix TIGR03804
parallel beta-helix repeat (two copies); This model represents a tandem pair of an ...
565-610 1.27e-03

parallel beta-helix repeat (two copies); This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences.


:

Pssm-ID: 234360  Cd Length: 44  Bit Score: 37.52  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 75906659   565 GIEIRDSSNPTIQKCRIHDNqqGDGILVHLNGRGTVEDCNIFSNGF 610
Cdd:TIGR03804   1 GIYLESSSNNTLENNTASNN--SYGIYLTDSSNNTLSNNTASSNSY 44
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-299 2.65e-36

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 136.89  E-value: 2.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659     34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNH-PKAVELFQREAEVLALLNYPGIPTVeangYFVYFPRNSqepmH 112
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKiKKDRERILREIKILKKLKHPNIVRL----YDVFEDEDK----L 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659    113 CLVMEKIEGLDLGQYLRQRDYRPIDQklALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSVTGT 192
Cdd:smart00220  73 YLVMEYCEGGDLFDLLKKRGRLSEDE--ARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659    193 YIAKQAVGqvtgviSAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEP--SDPTIYNYLNdelrwrdgLLSSGSNSV 269
Cdd:smart00220 151 EKLTTFVG------TPEYMAPEVLLGKGYgKAVDIWSLGVILYELLTGKPPfpGDDQLLELFK--------KIGKPKPPF 216
                          250       260       270
                   ....*....|....*....|....*....|
gi 75906659    270 TPtvgDRPNILPQFADLLDQMMERLPAQRP 299
Cdd:smart00220 217 PP---PEWDISPEAKDLIRKLLVKDPEKRL 243
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
472-628 2.08e-25

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 257587 [Multi-domain]  Cd Length: 157  Bit Score: 103.36  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   472 SGIGVHGATaNPVIQKCQIHDGKQSGIYLYENSRGTIEDCDFFGNTTTEITVDAAQPIIRRCKIHQDKEGGILFRNQAQG 551
Cdd:pfam13229   1 SGILINGSS-NVTIENNTISNNGGNGIYIGGSSNVTIENNTITNGGTGIYILGSSNNTISNNTISNNGGGGIYLRGSSNN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75906659   552 IVEDCDIFNNNLSGIEIRDSSNPTIQKCRIHDNqQGDGILVHLNGRG-TVEDCNIFSNGFSGVEIRDRG-NPVIRRCSI 628
Cdd:pfam13229  80 TIENNTISNNGGYGIYLSNSSNNTIENNTISNN-GGYGIYLEDSSNNiTITNNTISNNGGYGIYLIGGSsNNTISNNTI 157
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
588-673 5.49e-08

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 257587 [Multi-domain]  Cd Length: 157  Bit Score: 51.75  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   588 DGILVHLNGRGTVEDCNI----------------------FSNGFSGVEIRDRGNPVIRRCSINKNKYYGVYAYKNSTGT 645
Cdd:pfam13229   1 SGILINGSSNVTIENNTIsnnggngiyiggssnvtienntITNGGTGIYILGSSNNTISNNTISNNGGGGIYLRGSSNNT 80
                          90       100
                  ....*....|....*....|....*...
gi 75906659   646 VENCDLTGNIRSAINVDETSQLQRSGNV 673
Cdd:pfam13229  81 IENNTISNNGGYGIYLSNSSNNTIENNT 108
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
40-299 9.61e-33

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: 125.81  E-value: 9.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  40 LGGGGFGKTFAVNDTRTQTAKVLKVL-INNHPKAVELFQREAEVLALLNYPGIptVEANGYFvyfprnSQEPMHCLVMEK 118
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIkKEDSSSLLEELLREIEILKKLNHPNI--VKLYGVF------EDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 119 IEGLDLGQYLRQRDyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIML-RADGRLVLIDFGTARSVTGTYIAKQ 197
Cdd:cd00180  73 CEGGSLKDLLKENE-GKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLdSDNGKVKLADFGLSKLLTSDKSLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 198 avgqvTGVISAGYTPSEQINGQAV--QQSDFFALGRTFIYlltgkepsdptiynylndelrwrdgllssgsnsvtptvgd 275
Cdd:cd00180 152 -----TIVGTPAYMAPEVLLGKGYysEKSDIWSLGVILYE---------------------------------------- 186
                       250       260
                ....*....|....*....|....
gi 75906659 276 rpniLPQFADLLDQMMERLPAQRP 299
Cdd:cd00180 187 ----LPELKDLIRKMLQKDPEKRP 206
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
78-187 1.24e-09

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 57.29  E-value: 1.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  78 REAEVLALLNYPGIPT--VeangYFVYfPRNSQepmhcLVMEKIEGLDLGQYLRQRDYrpidqklalQWFKEVMIILHQV 155
Cdd:COG3642  48 REARILAKAREAGVPVpiV----YDVD-PDNGL-----IVMEYIEGELLKDALEEARP---------DLLREVGRLVGKL 108
                        90       100       110
                ....*....|....*....|....*....|..
gi 75906659 156 HQQGLFHRDIKPSNIMLRaDGRLVLIDFGTAR 187
Cdd:COG3642 109 HKAGIVHGDLTTSNIILS-GGRIYFIDFGLGE 139
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
114-187 1.23e-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: 48.37  E-value: 1.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75906659   114 LVMEKIEGLDLGQYLRQRDYrpidqklalQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRaDGRLVLIDFGTAR 187
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIEEGND---------ELLREIGRLVGKLHKAGIVHGDLTTSNIIVR-DDKLYLIDFGLGK 137
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
33-186 1.79e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 48.79  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   33 RYRVVSVLGGGGFGKTFAVN------DTRTQTAK---------VLKVLINNH---PKAVELFQREAEVlallNYPGIPTV 94
Cdd:PHA02882  13 EWKIDKLIGCGGFGCVYETQcasdhcINNQAVAKienlenetiVMETLVYNNiydIDKIALWKNIHNI----DHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   95 EANGYF----VYFprnsqepmHCLVMEKIEgLDLGQYLRQRDYRPidQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNI 170
Cdd:PHA02882  89 YGCGSFkrcrMYY--------RFILLEKLV-ENTKEIFKRIKCKN--KKLIKNIMKDMLTTLEYIHEHGISHGDIKPENI 157
                        170
                 ....*....|....*.
gi 75906659  171 MLRADGRLVLIDFGTA 186
Cdd:PHA02882 158 MVDGNNRGYIIDYGIA 173
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
78-187 2.45e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 47.59  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   78 REAEVLALLNYPGIPTVEAngYFVyFPRNSQepmhcLVMEKIEGLDLGQYLRQRDYRpidqklALQWFKEVMIILHQVHQ 157
Cdd:PRK14879  48 REARIMSRARKAGVNVPAV--YFV-DPENFI-----IVMEYIEGEPLKDLINSNGME------ELELSREIGRLVGKLHS 113
                         90       100       110
                 ....*....|....*....|....*....|
gi 75906659  158 QGLFHRDIKPSNIMLRaDGRLVLIDFGTAR 187
Cdd:PRK14879 114 AGIIHGDLTTSNMILS-GGKIYLIDFGLAE 142
Pectinesterase pfam01095
Pectinesterase;
361-582 3.71e-06

Pectinesterase;


Pssm-ID: 250360  Cd Length: 298  Bit Score: 47.99  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   361 IVSQEGGGDYKTISAAIeNAQP---GMR--ILVRPGLYQESLVLDKALK---IIGDGVKAEIIIESKDAgclvvktdqae 432
Cdd:pfam01095   3 VVAKDGSGQFKTINEAV-AAAPkksSKRfvIYVKAGVYKENVEVPKKKTnvmFVGDGPGKTIITGSLNF----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   433 VRGL-TFRSRVgtenkqyFAVdisQGQVILADcDITSDSLSGIGVHGATA------NPVIQKCQIhDGKQSGIYLYENsR 505
Cdd:pfam01095  71 IDGGtTFRTAT-------FAV---VGDGFIAR-DITFENTAGPEKHQAVAlrvgadLSVFYRCSF-DGYQDTLYVHSN-R 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   506 GTIEDCDFFGnttteiTVD----AAQPIIRRCKIHQDKEGgilfRNQ-----AQGIVEDcdifnNNLSGIeirdssnpTI 576
Cdd:pfam01095 138 QFYRDCDITG------TVDfifgNAAAVFQNCNIVARKPL----PGQkntvtAQGRTDP-----NQNTGI--------VI 194

                  ....*.
gi 75906659   577 QKCRIH 582
Cdd:pfam01095 195 QNCRIT 200
PLN02432 PLN02432
putative pectinesterase
360-491 8.10e-06

putative pectinesterase


Pssm-ID: 178051  Cd Length: 293  Bit Score: 46.75  E-value: 8.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  360 LIVSQEGGGDYKTISAAIENAQP----GMRILVRPGLYQESLVL--DKA-LKIIGDGVKAEIII-----ESKDAGCLVVK 427
Cdd:PLN02432  13 IRVDQSGKGDFRKIQDAIDAVPSnnsqLVFIWVKPGIYREKVVVpaDKPfITLSGTQASNTIITwndggDIFESPTLSVL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  428 TDQAEVRGLTFRSRVGTENKQyFAVDISQGQVILADCDITS--DSL---------SGIGVHGAT------ANPVIQKCQI 490
Cdd:PLN02432  93 ASDFVGRFLTIQNTFGSSGKA-VALRVAGDRAAFYGCRILSyqDTLlddtgrhyyRNCYIEGATdficgnAASLFEKCHL 171

                 .
gi 75906659  491 H 491
Cdd:PLN02432 172 H 172
para_beta_helix TIGR03804
parallel beta-helix repeat (two copies); This model represents a tandem pair of an ...
542-584 4.63e-04

parallel beta-helix repeat (two copies); This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences.


Pssm-ID: 234360  Cd Length: 44  Bit Score: 38.68  E-value: 4.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 75906659   542 GILFRNQAQGIVEDCDIFNNNLsGIEIRDSSNPTIQKCRIHDN 584
Cdd:TIGR03804   1 GIYLESSSNNTLENNTASNNSY-GIYLTDSSNNTLSNNTASSN 42
para_beta_helix TIGR03804
parallel beta-helix repeat (two copies); This model represents a tandem pair of an ...
565-610 1.27e-03

parallel beta-helix repeat (two copies); This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences.


Pssm-ID: 234360  Cd Length: 44  Bit Score: 37.52  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 75906659   565 GIEIRDSSNPTIQKCRIHDNqqGDGILVHLNGRGTVEDCNIFSNGF 610
Cdd:TIGR03804   1 GIYLESSSNNTLENNTASNN--SYGIYLTDSSNNTLSNNTASSNSY 44
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
114-183 1.36e-03

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in Escherichia coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 253661  Cd Length: 206  Bit Score: 39.27  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75906659   114 LVMEKIEGL-DLGQYLRQRDYRPIDQKLALqWFKeVMIILHQVHQQGLFHRDIKPSNIMLRADG---RLVLIDF 183
Cdd:pfam06293  94 LLTERLEGAqDLVTWLAQWADPAEELRRAL-WRA-VGRLIARMHRAGVNHTDLNAHNILLDTGEggfKVWLIDF 165
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-299 2.65e-36

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 136.89  E-value: 2.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659     34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNH-PKAVELFQREAEVLALLNYPGIPTVeangYFVYFPRNSqepmH 112
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKiKKDRERILREIKILKKLKHPNIVRL----YDVFEDEDK----L 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659    113 CLVMEKIEGLDLGQYLRQRDYRPIDQklALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSVTGT 192
Cdd:smart00220  73 YLVMEYCEGGDLFDLLKKRGRLSEDE--ARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659    193 YIAKQAVGqvtgviSAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEP--SDPTIYNYLNdelrwrdgLLSSGSNSV 269
Cdd:smart00220 151 EKLTTFVG------TPEYMAPEVLLGKGYgKAVDIWSLGVILYELLTGKPPfpGDDQLLELFK--------KIGKPKPPF 216
                          250       260       270
                   ....*....|....*....|....*....|
gi 75906659    270 TPtvgDRPNILPQFADLLDQMMERLPAQRP 299
Cdd:smart00220 217 PP---PEWDISPEAKDLIRKLLVKDPEKRL 243
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
472-628 2.08e-25

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 257587 [Multi-domain]  Cd Length: 157  Bit Score: 103.36  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   472 SGIGVHGATaNPVIQKCQIHDGKQSGIYLYENSRGTIEDCDFFGNTTTEITVDAAQPIIRRCKIHQDKEGGILFRNQAQG 551
Cdd:pfam13229   1 SGILINGSS-NVTIENNTISNNGGNGIYIGGSSNVTIENNTITNGGTGIYILGSSNNTISNNTISNNGGGGIYLRGSSNN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75906659   552 IVEDCDIFNNNLSGIEIRDSSNPTIQKCRIHDNqQGDGILVHLNGRG-TVEDCNIFSNGFSGVEIRDRG-NPVIRRCSI 628
Cdd:pfam13229  80 TIENNTISNNGGYGIYLSNSSNNTIENNTISNN-GGYGIYLEDSSNNiTITNNTISNNGGYGIYLIGGSsNNTISNNTI 157
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
34-316 1.08e-42

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: 158.37  E-value: 1.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNHPKAVELFQREAEVLALLNYPG-IPTVeangYFVYFPRNSqepmH 112
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKLVALKVLAKKLESKSKEVERFLREIQILASLNHPPnIVKL----YDFFQDEGS----L 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 113 CLVMEKIEGLDLGQYLRQRDYR-PIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLV-LIDFGTARSVT 190
Cdd:COG0515  74 YLVMEYVDGGSLEDLLKKIGRKgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVkLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 191 GTYIAKQAVGQVTGVI-SAGYTPSEQINGQ----AVQQSDFFALGRTFIYLLTGKEPSDptIYNYLNDELRWRDGLLSSG 265
Cdd:COG0515 154 DPGSTSSIPALPSTSVgTPGYMAPEVLLGLslayASSSSDIWSLGITLYELLTGLPPFE--GEKNSSATSQTLKIILELP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 75906659 266 SNSVTPTVGDR--PNILPQFADLLDQMMERLPAQRPQNTHIILQRLADIEKSL 316
Cdd:COG0515 232 TPSLASPLSPSnpELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLK 284
Pkinase pfam00069
Protein kinase domain;
34-299 3.62e-28

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 113.88  E-value: 3.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659    34 YRVVSVLGGGGFGKTF-AVN-DTRTQTA-KVLKVLiNNHPKAVELFQREAEVLALLNYPGIptVEANGYFVYFPRNsqep 110
Cdd:pfam00069   1 YELLRKLGSGSFGTVYkAKHkGTGKIVAvKILKKR-SEKSKKDQTARREIRILRRLSHPNI--VRLIDAFEDKDHL---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   111 mhCLVMEKIEGLDLGQYLRQrdYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSVT 190
Cdd:pfam00069  74 --YLVMEYCEGGDLFDYLSR--GGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   191 GTYiakqaVGQVTGVISAGYTPSEQINGQAV--QQSDFFALGRTFIYLLTGKEP-SDPTIYN--YLNDELRWRDgLLSSG 265
Cdd:pfam00069 150 KSS-----SSLTTFVGTPEYMAPEVLLGGNGygPKVDVWSLGVILYELLTGKPPfSGESILDqlQLIRRILGPP-LEFDE 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 75906659   266 SNSvtptvgdrPNILPQFADLLDQMMERLPAQRP 299
Cdd:pfam00069 224 PKS--------DSGSEEAKDLIKKCLNKDPSKRP 249
pknD PRK13184
serine/threonine-protein kinase; Reviewed
32-242 1.61e-13

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 72.88  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   32 GRYRVVSVLGGGGFGKTFAVNDT----RTQTAKVLKVLINNhPKAVELFQREAEVLALLNYPGI-P--TVEANGYFVYFp 104
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPvcsrRVALKKIREDLSEN-PLLKKRFLREAKIAADLIHPGIvPvySICSDGDPVYY- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  105 rnsqepmhclVMEKIEGLDLGQYLR---QRDYRPIDQ------KLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRAD 175
Cdd:PRK13184  80 ----------TMPYIEGYTLKSLLKsvwQKESLSKELaektsvGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  176 GRLVLIDFGTARS--------------VTGTYIAKQAV-GQVTGVISagYTPSEQING-QAVQQSDFFALGRTFIYLLTG 239
Cdd:PRK13184 150 GEVVILDWGAAIFkkleeedlldidvdERNICYSSMTIpGKIVGTPD--YMAPERLLGvPASESTDIYALGVILYQMLTL 227

                 ...
gi 75906659  240 KEP 242
Cdd:PRK13184 228 SFP 230
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
33-299 4.86e-13

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 70.67  E-value: 4.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNHPKAVELFQREAEVLALLNYPGIPTVEANGYFVYFPRNSQE--P 110
Cdd:PTZ00283  33 KYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKCHEDFAKKDPRNPEnvL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  111 MHCLVMEKIEGLDLGQYLRQRDY--RPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARS 188
Cdd:PTZ00283 113 MIALVLDYANAGDLRQEIKSRAKtnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKM 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  189 VTGTyiAKQAVGQVtgVISAGYTPSEQI--NGQAVQQSDFFALGRTFIYLLTGKEPSD-PTIYNYLNDELrwrdgllsSG 265
Cdd:PTZ00283 193 YAAT--VSDDVGRT--FCGTPYYVAPEIwrRKPYSKKADMFSLGVLLYELLTLKRPFDgENMEEVMHKTL--------AG 260
                        250       260       270
                 ....*....|....*....|....*....|....
gi 75906659  266 SNSVTPtvgdrPNILPQFADLLDQMMERLPAQRP 299
Cdd:PTZ00283 261 RYDPLP-----PSISPEMQEIVTALLSSDPKRRP 289
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
56-240 6.64e-13

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: 71.03  E-value: 6.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659     56 TQTAKVLKVLINNHPKAVEL---FQREAEVLALLNYPGIPTV----EANGYFVYfprnsqepmhcLVMEKIEGLDLGQYL 128
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQrarFRRETALCARLYHPNIVALldsgEAPPGLLF-----------AVFEYVPGRTLREVL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659    129 RQRDYRPIDQKLALqwFKEVMIILHQVHQQGLFHRDIKPSNIMLRADG---RLVLIDFGTARSVTGTYIAKQAVGQVTG- 204
Cdd:TIGR03903   71 AADGALPAGETGRL--MLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGVRDADVATLTRTTe 148
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 75906659    205 -VISAGYTPSEQINGQAVQ-QSDFFALGRTFIYLLTGK 240
Cdd:TIGR03903  149 vLGTPTYCAPEQLRGEPVTpNSDLYAWGLIFLECLTGQ 186
NosD_copper_fam TIGR04247
nitrous oxide reductase family maturation protein NosD; Members of this family include NosD, a ...
373-661 8.21e-10

nitrous oxide reductase family maturation protein NosD; Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase.


Pssm-ID: 234521 [Multi-domain]  Cd Length: 377  Bit Score: 59.91  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   373 ISAAIENAQPGMRILVRPGLYQESLVLDKALKIIGDG--------------VKAE-------IIIES------KDAGCLV 425
Cdd:TIGR04247   1 LQEAIDAARPGDTIRLAPGTYKGNIVIDKPLTLIGEGgavidgegkgtvitIKAPdvtieglTVRNSgtslteDDAGIKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   426 VKTDQAEVRGLTFRSRvgtenkqYFAVDISQGQ-VILADCDITSD-----SLSGIGVH-GATANPVIQKCQIHDGkQSGI 498
Cdd:TIGR04247  81 EKADRAVIENNRLEDN-------LFGIYLQEAHdSLIENNRITGKpdlrsNDRGNGIHlWNSPGNVIEGNTVRGG-RDGI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   499 YLyENSRGTIedcdFFGNTTTEItvdaaqpiirRCKIHqdkeggilFRNQAQGIVEDcDIFNNNLSGIEIRDSSNPTIQK 578
Cdd:TIGR04247 153 YI-EFSHHNL----IRNNTSHNL----------RYGLH--------FMYSNDNLVED-NVFRGNSVGYALMYSKRLTVRG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   579 CRIHDNQ--QGDGILVHLNGRGTVEDcNIFSNGFSGVEIRD------RGNpVIRRCSInknkyyGVYAYKNSTG-TVENC 649
Cdd:TIGR04247 209 NVFLNNWgdAGYGILLKEINDSEIEG-NTVLGNTKGLFIDNsprnvfRDN-DFEYNGI------GIHFTAGSERnRFEGN 280
                         330
                  ....*....|..
gi 75906659   650 DLTGNIRSAINV 661
Cdd:TIGR04247 281 AFIGNREQVKYV 292
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
34-186 1.71e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 58.85  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVlinnhpkavelFQR-----EAEVLALLNYPGIptVEANGYFVYfprNSq 108
Cdd:PHA03212  94 FSILETFTPGAEGFAFACIDNKTCEHVVIKA-----------GQRggtatEAHILRAINHPSI--IQLKGTFTY---NK- 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75906659  109 epMHCLVMEKIEgLDLGQYLRQRDYRPIDQKLALQwfKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTA 186
Cdd:PHA03212 157 --FTCLILPRYK-TDLYCYLAAKRNIAICDILAIE--RSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAA 229
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
588-673 5.49e-08

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 257587 [Multi-domain]  Cd Length: 157  Bit Score: 51.75  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   588 DGILVHLNGRGTVEDCNI----------------------FSNGFSGVEIRDRGNPVIRRCSINKNKYYGVYAYKNSTGT 645
Cdd:pfam13229   1 SGILINGSSNVTIENNTIsnnggngiyiggssnvtienntITNGGTGIYILGSSNNTISNNTISNNGGGGIYLRGSSNNT 80
                          90       100
                  ....*....|....*....|....*...
gi 75906659   646 VENCDLTGNIRSAINVDETSQLQRSGNV 673
Cdd:pfam13229  81 IENNTISNNGGYGIYLSNSSNNTIENNT 108
PLN02301 PLN02301
pectinesterase/pectinesterase inhibitor
357-558 7.96e-08

pectinesterase/pectinesterase inhibitor


Pssm-ID: 215170 [Multi-domain]  Cd Length: 548  Bit Score: 54.11  E-value: 7.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  357 KTTLIVSQEGGGDYKTISAAI----ENAQPGMRILVRPGLYQESLVLDKALK---IIGDGVKAEIIieskdAGCLVVktd 429
Cdd:PLN02301 235 KANVVVAKDGSGKYKTVKEAVasapDNSKTRYVIYVKKGTYKENVEIGKKKKnlmLVGDGMDSTII-----TGSLNV--- 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  430 qaeVRG-LTFRSRVGTENKQYFavdISQgqviladcDITSDSLSGIGVHGATA------NPVIQKCQIhDGKQSGIYLYE 502
Cdd:PLN02301 307 ---IDGsTTFRSATVAAVGDGF---IAQ--------DIWFQNTAGPEKHQAVAlrvsadQAVINRCRI-DAYQDTLYAHS 371
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75906659  503 NsRGTIEDC------DF-FGNttteitvdaAQPIIRRCKIHQDKEG----------GILFRNQAQGI-VEDCDI 558
Cdd:PLN02301 372 L-RQFYRDSyitgtvDFiFGN---------AAVVFQNCKIVARKPMagqknmvtaqGRTDPNQNTGIsIQKCDI 435
PLN02990 PLN02990
Probable pectinesterase/pectinesterase inhibitor
357-581 1.97e-07

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215535 [Multi-domain]  Cd Length: 572  Bit Score: 52.72  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  357 KTTLIVSQEGGGDYKTISAAIeNAQPGMR-----ILVRPGLYQESLVLDKAL---KIIGDGVKAEIIIESKDAGCLVVKT 428
Cdd:PLN02990 258 KANVVVAQDGSGQYKTINEAL-NAVPKANqkpfvIYIKQGVYNEKVDVTKKMthvTFIGDGPTKTKITGSLNFYIGKVKT 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  429 ----------DQAEVRGLTFRSRVGTENKQYFAVDISQGQVILADCDItsdslsgigvhgatanpviqkcqihDGKQSGI 498
Cdd:PLN02990 337 yltatvaingDHFTAKNIGFENTAGPEGHQAVALRVSADYAVFYNCQI-------------------------DGYQDTL 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  499 YLYENsRGTIEDCDFFGntTTEITVDAAQPIIRRCKihqdkeggILFRNQAQGivEDCDIFNNNLSgiEIRDSSNPTIQK 578
Cdd:PLN02990 392 YVHSH-RQFFRDCTVSG--TVDFIFGDAKVVLQNCN--------IVVRKPMKG--QSCMITAQGRS--DVRESTGLVLQN 456

                 ...
gi 75906659  579 CRI 581
Cdd:PLN02990 457 CHI 459
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
146-216 1.06e-06

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 50.45  E-value: 1.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75906659  146 KEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSV-TGTYIakqavGQVTGVISAGYTPSEQI 216
Cdd:PLN03224 316 RQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAAVDMcTGINF-----NPLYGMLDPRYSPPEEL 382
ZntA COG2217
Cation transport ATPase [Inorganic ion transport and metabolism]
350-391 6.05e-03

Cation transport ATPase [Inorganic ion transport and metabolism]


Pssm-ID: 225127 [Multi-domain]  Cd Length: 713  Bit Score: 38.35  E-value: 6.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 75906659 350 ALSRLLPKTTLIVSqeggGDYKTISAAIENAQPGMRILVRPG 391
Cdd:COG2217 204 ALLDLAPKTATVVR----GDGEEEEVPVEEVQVGDIVLVRPG 241
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
40-299 9.61e-33

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: 125.81  E-value: 9.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  40 LGGGGFGKTFAVNDTRTQTAKVLKVL-INNHPKAVELFQREAEVLALLNYPGIptVEANGYFvyfprnSQEPMHCLVMEK 118
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIkKEDSSSLLEELLREIEILKKLNHPNI--VKLYGVF------EDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 119 IEGLDLGQYLRQRDyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIML-RADGRLVLIDFGTARSVTGTYIAKQ 197
Cdd:cd00180  73 CEGGSLKDLLKENE-GKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLdSDNGKVKLADFGLSKLLTSDKSLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 198 avgqvTGVISAGYTPSEQINGQAV--QQSDFFALGRTFIYlltgkepsdptiynylndelrwrdgllssgsnsvtptvgd 275
Cdd:cd00180 152 -----TIVGTPAYMAPEVLLGKGYysEKSDIWSLGVILYE---------------------------------------- 186
                       250       260
                ....*....|....*....|....
gi 75906659 276 rpniLPQFADLLDQMMERLPAQRP 299
Cdd:cd00180 187 ----LPELKDLIRKMLQKDPEKRP 206
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-308 6.49e-29

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: 116.06  E-value: 6.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLKV--LINNHPKAVELFQREAEVLALLNYPGI----PTVEANGYFvyfprn 106
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEidLSNMSEKEREDALNEVKILKKLNHPNIikyyESFEEKGKL------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 107 sqepmhCLVMEKIEGLDLGQYLRQR--DYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFG 184
Cdd:cd08215  75 ------CIVMEYADGGDLSQKIKKQkkEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 185 TARSVTGTYI-AKQAVGqvtgvisagyTPS----EQINGQAV-QQSDFFALGRTFIYLLTGKEPSDPT-----IYNYLNd 253
Cdd:cd08215 149 ISKVLSSTVDlAKTVVG----------TPYylspELCQNKPYnYKSDIWSLGCVLYELCTLKHPFEGEnllelALKILK- 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75906659 254 elrwrdgllssgsnsvtptvGDRPNILPQF----ADLLDQMMERLPAQRPqNTHIILQR 308
Cdd:cd08215 218 --------------------GQYPPIPSQYsselRNLVSSLLQKDPEERP-SIAQILQS 255
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
34-299 4.43e-23

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: 99.19  E-value: 4.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAV--NDTRTQTA-KVL-KVLINNHpKAVELFQREAEVLALLN-YPGIPTV------EANGYFVy 102
Cdd:cd05581   3 FKFGKIIGEGSFSTVVLAkeKETNKEYAiKILdKRQLIKE-KKVKYVKIEKEVLTRLNgHPGIIKLyytfqdEENLYFV- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 103 fprnsqepmhclvMEKIEGLDLGQYLRQrdYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLID 182
Cdd:cd05581  81 -------------LEYAPNGELLQYIRK--YGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDKDMHIKITD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 183 FGTARSVTGTYIAKQAVGQVTGVIS---------------AGYTPSEQINGQAV-QQSDFFALGrTFIY-LLTGKEP-SD 244
Cdd:cd05581 146 FGTAKVLDPNSSPESNKGDATNIDSqieknrrrfasfvgtAEYVSPELLNEKPAgKSSDLWALG-CIIYqMLTGKPPfRG 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75906659 245 PTIY----NYLNDELRWrdgllssgsnsvtptvgdRPNILPQFADLLDQMMERLPAQRP 299
Cdd:cd05581 225 SNEYltfqKILKLEYSF------------------PPNFPPDAKDLIEKLLVLDPQDRL 265
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
40-302 2.51e-22

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: 96.43  E-value: 2.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  40 LGGGGFGKTFAVNDTRTQTAKVLKVL----INNHpKAVELFQREAEVLALLNYPGIPTVeangYFvYFprnsQEPMH-CL 114
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLkkkkIIKR-KEVEHTLTERNILSRINHPFIVKL----HY-AF----QTEEKlYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 115 VMEKIEGLDLGQYLRQRdyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTAR------- 187
Cdd:cd05123  71 VLEYAPGGELFSHLSKE--GRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLAKelssegs 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 188 ---SVTGT--YIAKQavgqvtgVI-SAGYTPSeqingqavqqSDFFALGRTFIYLLTGKEP---SDP-TIYNY-LNDELR 256
Cdd:cd05123 149 rtnTFCGTpeYLAPE-------VLlGKGYGKA----------VDWWSLGVLLYEMLTGKPPfyaEDRkEIYEKiLKDPLR 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 75906659 257 WrdgllssgsnsvtptvgdrPNIL-PQFADLLDQMMERLPAQRPQNT 302
Cdd:cd05123 212 F-------------------PEFLsPEARDLISGLLQKDPTKRLGSG 239
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
40-298 1.83e-21

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: 94.22  E-value: 1.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  40 LGGGGFGKTFAVNDTRTQTAKVLKVLINNH---PKAVELFQREAEVLALLNYPGIPTVEA---NGYFVYFprnsqepmhc 113
Cdd:cd05572   1 LGVGGFGRVELVKVKSKNRTFALKCVKKRHiveTGQQEHIFSEKEILEECNHPFIVKLYRtfkDKKYIYM---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 114 lVMEKIEGLDLGQYLRQRDYrpIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSVTGTY 193
Cdd:cd05572  71 -LMEYCLGGELWTILRDRGL--FDEYTARFYIACVVLAFEYLHNRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLKSGQ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 194 IAKQAVGqvtgviSAGYTPSEQINGQAVQQS-DFFALGrTFIY-LLTGKEP---SDPTIYNYLNDELRWRDGLLSsgsns 268
Cdd:cd05572 148 KTWTFCG------TPEYVAPEIILNKGYDFSvDYWSLG-ILLYeLLTGRPPfgeDDEDPMEIYNDILKGNGKLEF----- 215
                       250       260       270
                ....*....|....*....|....*....|.
gi 75906659 269 vtptvgdrPNILPQFA-DLLDQMMERLPAQR 298
Cdd:cd05572 216 --------PNYIDKAAkDLIKQLLRRNPEER 238
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-305 6.87e-21

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 92.34  E-value: 6.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLK-VLINNHPKAVELFQREAEVLALLNYPGIPT----VEANGYFVyfprns 107
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKeIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAfkesFEADGHLY------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 108 qepmhcLVMEKIEGLDLGQYLRQRDYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTAR 187
Cdd:cd08219  75 ------IVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 188 SVT--GTYiakqavgQVTGVISAGYTPSE-QINGQAVQQSDFFALGRTFIYLLTGKEPSDPTiynylndelRWRDGLLSS 264
Cdd:cd08219 149 LLTspGAY-------ACTYVGTPYYVPPEiWENMPYNNKSDIWSLGCILYELCTLKHPFQAN---------SWKNLILKV 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 75906659 265 GSNSVTPtvgdrpniLP-----QFADLLDQMMERLPAQRPQNTHII 305
Cdd:cd08219 213 CQGSYKP--------LPshysyELRSLIKQMFKRNPRSRPSATTIL 250
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
34-242 7.82e-21

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: 92.27  E-value: 7.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNHPKAVELFQREAEVLALLNYPGIptVEANGYFVYfprnSQEPMhc 113
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKKEKIINEIQILKKCKHPNI--VKYYGSYLK----KDELW-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 114 LVMEKIEGLDLGQYLRQRDYRpidqklalqwFKEVMI--ILHQV-------HQQGLFHRDIKPSNIMLRADGRLVLIDFG 184
Cdd:cd05122  74 IVMEFCSGGSLKDLLKSTNQT----------LTESQIayVCKELlkgleylHSNGIIHRDIKAANILLTSDGEVKLIDFG 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75906659 185 TARSVTGTYIAKQAVGqvtgviSAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEP 242
Cdd:cd05122 144 LSAQLSDTKARNTMVG------TPYWMAPEVINGKPYdYKADIWSLGITAIELAEGKPP 196
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
33-299 4.64e-19

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: 86.84  E-value: 4.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLKV--LINNHPKAVELFQREAEVLALLNYPGIptVEangyFVYFPRNSQEP 110
Cdd:cd06606   1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSveLSGDSEEELEALEREIRILSSLQHPNI--VR----YYGSERDEEKN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 111 MHCLVMEKIEGLDLGQYLRQrdYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSVT 190
Cdd:cd06606  75 TLNIFLEYVSGGSLSSLLKK--FGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 191 GTYIAKQaVGQVTGviSAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEPsdptIYNYLN-DELRWRDGllSSGSNS 268
Cdd:cd06606 153 DIETGEG-TGSVRG--TPYWMAPEVIRGEEYgRAADIWSLGCTVIEMATGKPP----WSELGNpMAALYKIG--SSGEPP 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 75906659 269 VTPTvgdrpNILPQFADLLDQMMERLPAQRP 299
Cdd:cd06606 224 EIPE-----HLSEEAKDFLRKCLRRDPKKRP 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
33-299 8.52e-18

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: 83.07  E-value: 8.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTF-AVNDTRTQTAKVLKVLINNHPK-AVELFQREAEVLALLNYPGIPTVEA---NGYFVYFprns 107
Cdd:cd06627   1 NYQLGDLIGRGAFGVVYkGLNLETGDFVAIKQISLEKIKEeALKSIMQEIDLLKNLKHPNIVKYIGsieTSDSLYI---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 108 qepmhclVMEKIEGLDLGQYLRQrdYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTAr 187
Cdd:cd06627  77 -------ILEYAENGSLRQIIKK--FGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGVVKLADFGVA- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 188 svtgTYIAKQAVGQVTGVISAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEPsdptiYNYLNDelrwrdgllssgs 266
Cdd:cd06627 147 ----TKLNDVSKDDASVVGTPYWMAPEVIEMSGAsTASDIWSLGCTVIELLTGNPP-----YYDLNP------------- 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75906659 267 nsvTPT----VGDR-----PNILPQFADLLDQMMERLPAQRP 299
Cdd:cd06627 205 ---MAAlfriVQDDhpplpEGISPELKDFLMQCFQKDPNLRP 243
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-309 2.61e-17

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


Pssm-ID: 173760 [Multi-domain]  Cd Length: 256  Bit Score: 81.44  E-value: 2.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGkTFAVNDTRTQTAKVLKVLINNH---PKAVELFQREAEVLALLNYPGIPtveanGYFVYFPRNSQe 109
Cdd:cd08220   1 KYEKIRVVGRGAFG-IVHLCRRKADQKLVIIKQIPVEqmtKDERLAAQNECQVLKLLSHPNII-----EYYENFLEDKA- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 110 pmHCLVMEKIEGLDLGQYLRQRDYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLI-DFGTARS 188
Cdd:cd08220  74 --LMIVMEYAPGGTLAEYIQKRCNSLLDEDTILHFFVQILLALHHVHTKLILHRDLKTQNILLDKHKMVVKIgDFGISKI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 189 VTGTYIAKQAVGqvtgviSAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEPSD----PTIynylndelrwrdgLLS 263
Cdd:cd08220 152 LSSKSKAYTVVG------TPCYISPELCEGKPYnQKSDIWALGCVLYELASLKRAFEaanlPAL-------------VLK 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 75906659 264 SGSNSVTPtVGDRpnILPQFADLLDQMMERLPAQRPQNTHIILQRL 309
Cdd:cd08220 213 IMSGTFAP-ISDR--YSPDLRQLILSMLNLDPSKRPQLSQIMAQPI 255
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
34-298 4.27e-17

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: 80.82  E-value: 4.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVlINN----HPKAVELFQREAEVLALLNYPGIptveANGYFVYfprNSQE 109
Cdd:cd05578   2 FELLRVIGKGAFGKVCIVQKRDTKKMFAMKY-MNKqkcvEKGSVRNVLNERRILQELNHPFL----VNLWYSF---QDEE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 110 PMHcLVMEKIEGLDLGQYLRQRdyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSV 189
Cdd:cd05578  74 NMY-LVVDLLLGGDLRYHLSQK--VKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNILLDEQGHVHITDFNIATKV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 190 TGTYIAKQAVGqvtgviSAGYTPSEQINGQ----AVqqsDFFALGRTFIYLLTGKEPsdptiynYLNDELRWRDGLLSS- 264
Cdd:cd05578 151 TPDTLTTSTSG------TPGYMAPEVLCRQgysvAV---DWWSLGVTAYECLRGKRP-------YRGHSRTIRDQIRAKq 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 75906659 265 GSNSVTPTVGDRPNILpqfaDLLDQMMERLPAQR 298
Cdd:cd05578 215 ETADVLYPATWSTEAI----DAINKLLERDPQKR 244
STKc_CRIK cd05601
Catalytic domain of the Protein Serine/Threonine Kinase, Citron Rho-interacting kinase; Serine ...
34-200 5.22e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Citron Rho-interacting kinase; Serine/Threonine Kinases (STKs), Citron Rho-interacting kinase (CRIK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. CRIK is also called citron kinase. It contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. CRIK, an effector of the small GTPase Rho, plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension.


Pssm-ID: 173692 [Multi-domain]  Cd Length: 330  Bit Score: 81.40  E-value: 5.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAVNDTRTQ---TAKVLKVLINNHPKAVELFQREAEVLALLNYPGIPTVEangyFVYfprnsQEP 110
Cdd:cd05601   3 FDVKSLVGRGHFGEVQVVREKATGdiyAMKVMKKSVLLAQETVSFFEEERDILSISNSPWIPQLQ----YAF-----QDK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 111 MHC-LVMEKIEGLDLGQYLRQRDyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSV 189
Cdd:cd05601  74 DNLyLVMEYQPGGDLLSLLNRYE-DQFDEDMAQFYLAELVLAIHSVHQMGYVHRDIKPENVLIDRTGHIKLADFGSAARL 152
                       170
                ....*....|...
gi 75906659 190 T--GTYIAKQAVG 200
Cdd:cd05601 153 TanKMVNSKLPVG 165
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-240 1.26e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 1; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 1 (Nek1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek1 subfamily is one of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair.


Pssm-ID: 173758 [Multi-domain]  Cd Length: 256  Bit Score: 79.49  E-value: 1.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVL--INNHPKAVELFQREAEVLALLNYPGIPTVeangyfvyfpRNSQEP 110
Cdd:cd08218   1 KYVKVKKIGEGSFGKAILVKSKEDGKQYVIKEIniSKMSPKEREESRKEVAVLSNMKHPNIVQY----------QESFEE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 111 MHCL--VMEKIEGLDLGQYLRQRDYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARS 188
Cdd:cd08218  71 NGNLyiVMDYCEGGDLYKKINAQRGVLFPEDQILDWFVQICLALKHVHDRKILHRDIKSQNIFLTKDGTIKLGDFGIARV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75906659 189 VTGTY-IAKQAVGqvtgvisAGYTPSEQI--NGQAVQQSDFFALGRTFIYLLTGK 240
Cdd:cd08218 151 LNSTVeLARTCIG-------TPYYLSPEIceNRPYNNKSDIWALGCVLYEMCTLK 198
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
113-299 1.57e-16

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: 79.21  E-value: 1.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 113 CLVMEKIEGLDLGQYLRQRDYrpIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFG------TA 186
Cdd:cd05579  69 YLVMEYLPGGDLASLLENVGS--LDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNILIDSNGHLKLTDFGlskvglVR 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 187 RSVTGTYIAKQAVgQVTGviSAGYTPSEQINGQAV-QQSDFFALGRTFIYLLTGKEP-----SDPTIYNYLNDELRWRDG 260
Cdd:cd05579 147 RQINLNDDEKEDK-RIVG--TPDYIAPEVILGQGHsKTVDWWSLGCILYEFLVGIPPfhgetPEEIFQNILNGKIEWPED 223
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75906659 261 llssgsnsvtptvgdrPNILPQFADLLDQMMERLPAQRP 299
Cdd:cd05579 224 ----------------VEVSDEAIDLISKLLVPDPEKRL 246
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Protein Serine/Threonine Kinases; Serine/Threonine ...
33-183 2.12e-16

Catalytic domain of Phototropin-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Phototropin-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The phototropin-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. Included in this subfamily are plant phototropins and predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. Neurospora crassa nrc-2 plays a role in growth and development by controlling entry into the conidiation program.


Pssm-ID: 173665 [Multi-domain]  Cd Length: 316  Bit Score: 79.25  E-value: 2.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNhpkavELFQR--------EAEVLALLNYPGIPTVEANgyfvyfp 104
Cdd:cd05574   2 HFKKIKLLGKGDVGRVFLVRLKGTGKLFALKVLDKK-----EMIKRnkvkrvltEQEILATLDHPFLPTLYAS------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 105 rnSQEPMH-CLVMEKIEGLDLGQYLRQRDYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDF 183
Cdd:cd05574  70 --FQTETYlCLVMDYCPGGELFRLLQRQPGKCLSEEVARFYAAEVLLALEYLHLLGIVYRDLKPENILLHESGHIMLSDF 147
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
113-298 2.25e-16

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, 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. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 78.68  E-value: 2.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 113 CLVMEKIEGLDLGQYLRQRDYRPIDqkLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSVtgt 192
Cdd:cd05611  73 YLVMEYLNGGDCASLIKTLGGLPED--WAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNG--- 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 193 YIAKQAVGqvtgviSAGYTPSEQINGQA-VQQSDFFALGRTFIYLLTGKEP-----SDPTIYNYLNDELRWRDGLLSSGS 266
Cdd:cd05611 148 LENKKFVG------TPDYLAPETILGVGdDKMSDWWSLGCVIFEFLFGYPPfhaetPDAVFDNILSRRINWPEEVKEFCS 221
                       170       180       190
                ....*....|....*....|....*....|..
gi 75906659 267 nsvtptvgdrpnilPQFADLLDQMMERLPAQR 298
Cdd:cd05611 222 --------------PEAVDLINRLLCMDPAKR 239
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-305 6.06e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 5; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 5 (Nek5) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek5 subfamily is one of a family of 11 different Neks (Nek1-11). 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. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 77.31  E-value: 6.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  33 RYRVVSVLGGGGFGKTFAVNDTRTQTAKVLKV--LINNHPKAVELFQREAEVLALLNYPGIPTveangYFVYFPRNSQep 110
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEidLTKMPVKEKEASKKEVILLAKMKHPNIVT-----FFASFQENGR-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 111 mHCLVMEKIEGLDLGQYLRQRDYRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLV-LIDFGTARSV 189
Cdd:cd08225  74 -LFIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGIARQL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 190 TGTY-IAKQAVGqvtgvisAGYTPSEQI--NGQAVQQSDFFALGRTFIYLLTGKEPSDPTIYNYLndelrwrdgLLSSGS 266
Cdd:cd08225 153 NDSMeLAYTCVG-------TPYYLSPEIcqNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQL---------VLKICQ 216
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75906659 267 NSVTPTvgdRPNILPQFADLLDQMMERLPAQRPQNTHII 305
Cdd:cd08225 217 GYFAPI---SPNFSRDLRSLISQLFKVSPRDRPSITSIL 252
STKc_ROCK cd05596
Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing ...
34-242 2.91e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; Serine/Threonine Kinases (STKs), Rho-associated coiled-coil containing protein kinase (ROCK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development.


Pssm-ID: 173687 [Multi-domain]  Cd Length: 370  Bit Score: 76.74  E-value: 2.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVL-----INNHPKAveLFQREAEVLALLNYPGIptVEANGYFvyfprnsQ 108
Cdd:cd05596  45 FDVIKVIGRGAFGEVQLVRHKSSKQVYAMKLLskfemIKRSDSA--FFWEERDIMAHANSEWI--VQLHYAF-------Q 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 109 EPMHC-LVMEKIEGLDLGQYLRQRDyrpIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTAR 187
Cdd:cd05596 114 DDKYLyMVMEYMPGGDLVNLMSNYD---IPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75906659 188 SV--TGTYIAKQAVGqVTGVISAGYTPSEQINGQAVQQSDFFALGrTFIY-LLTGKEP 242
Cdd:cd05596 191 KMdaNGMVRCDTAVG-TPDYISPEVLKSQGGDGYYGRECDWWSVG-VFLYeMLVGDTP 246
STKc_ROCK2 cd05621
Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing ...
7-242 3.74e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; Serine/Threonine Kinases (STKs), ROCK subfamily, ROCK2 (or ROK-alpha) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction.


Pssm-ID: 173711 [Multi-domain]  Cd Length: 370  Bit Score: 76.21  E-value: 3.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659   7 PQCSKPQNPDNVLfcqNCGSELLLEGR--------YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVL-----INNHPKAv 73
Cdd:cd05621  13 PALRKNKNIDNFL---NRYEKIVRKIRklqmkaedYDVVKVIGRGAFGEVQLVRHKSSQKVYAMKLLskfemIKRSDSA- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  74 eLFQREAEVLALLNYPGIPTVeangyFVYFprnsQEPMHC-LVMEKIEGLDLGQYLRQRDyrpIDQKLALQWFKEVMIIL 152
Cdd:cd05621  89 -FFWEERDIMAFANSPWVVQL-----FCAF----QDDKYLyMVMEYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLAL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 153 HQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARSV--TGTYIAKQAVGqVTGVISAGYTPSEQINGQAVQQSDFFALG 230
Cdd:cd05621 156 DAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMdeTGMVRCDTAVG-TPDYISPEVLKSQGGDGYYGRECDWWSVG 234
                       250
                ....*....|..
gi 75906659 231 RTFIYLLTGKEP 242
Cdd:cd05621 235 VFLFEMLVGDTP 246
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
40-299 4.33e-15

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: 74.68  E-value: 4.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  40 LGGGGFGKTF-AVN-DTRTQTA-KVLKvLINNHPKAVELFQREAEVLALLNYPGIptVEANGYFVYfprnsQEPMhCLVM 116
Cdd:cd06626   8 IGGGTFGKVYtAVNlDTGELMAvKEIR-IQDNDPKTIKEIADEMKVLELLKHPNL--VKYYGVEVH-----REKV-YIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 117 EKIEGLDLGQYLRQRdyRPIDQKLALQWFKEVMIILHQVHQQGLFHRDIKPSNIMLRADGRLVLIDFGTARsvtgtYIAK 196
Cdd:cd06626  79 EYCSGGTLEELLEHG--RILDEHVIRVYTLQLLEGLAYLHSHGIVHRDIKPANIFLDHNGVIKLGDFGCAV-----KLKN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 197 QAVGQVTGVISAGYTPS----EQINGQA----VQQSDFFALGRTFIYLLTGKEPsdptiYNYLNDELR--WRdglLSSGS 266
Cdd:cd06626 152 NTTTMGEEVQSLAGTPAymapEVITGGKgkghGRAADIWSLGCVVLEMATGKRP-----WSELDNEFQimFH---VGAGH 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 75906659 267 nsvTPTVGDRPNILPQFADLLDQMMERLPAQRP 299
Cdd:cd06626 224 ---KPPIPDSLQLSPEGKDFLDRCLESDPKKRP 253
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
34-307 1.00e-14

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


Pssm-ID: 173757 [Multi-domain]  Cd Length: 265  Bit Score: 73.44  E-value: 1.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659  34 YRVVSVLGGGGFGKTFAVNDTRTQTAKVLKVLINNHPKAVELFQREAEVLAL--LNYPGIptVeanGYFVYFPRNSQEPM 111
Cdd:cd08217   2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGNMTEKEKQQLVSEVNILreLKHPNI--V---RYYDRIIDRSNQTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906659 112 HcLVMEKIEGLDLGQYLR--QRDYRPIDQKLALQWFKEVMIILHQVH-----QQGLFHRDIKPSNIM