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Conserved domains on  [gi|32473469|ref|NP_866463|]
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serine/threonine-protein kinase pknB [Rhodopirellula baltica SH 1]

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
46-306 1.83e-95

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 310.67  E-value: 1.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   46 RYRVVRRIGSGGFGSVFHAKDESLNRDVAIKVPLrsLDDVNDEFQWSS---EARMVAKLDHPNIVPVYDVGKSDQFPFFV 122
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLR--PELAEDEEFRERflrEARALARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  123 VsRFIQGVDLRERILKGKP-SLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLAMSDDAPRPTR 201
Cdd:cd14014   79 M-EYVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  202 AGLLIGTYSYMSPEQARGEGhlVDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLRQFNPQLPIELERI 281
Cdd:cd14014  158 TGSVLGTPAYMAPEQARGGP--VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAI 235
                        250       260
                 ....*....|....*....|....*
gi 32473469  282 CLKALAQRVSDRYSNAAAMAADLRT 306
Cdd:cd14014  236 ILRALAKDPEERPQSAAELLAALRA 260
FGE-sulfatase super family cl19582
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
1550-1803 6.03e-31

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


The actual alignment was detected with superfamily member pfam03781:

Pssm-ID: 276271  Cd Length: 259  Bit Score: 124.92  E-value: 6.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1550 FVMGSPGHELFRDhslEVPIQTKIPRSFAISDSEVTLEQFRRFDPDASYATQYTTQ-----------------------P 1606
Cdd:pfam03781   13 FEMGSAERTGNDN---EAPAHDVTVRPFAIDKYPVTNAQYAAFVEATGYTTEVYPQwwaeveganwrhpsgglsdiddgA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1607 DCPMTSVGWFDAIKYCRWLSEQehvpeaemcypsieeiqrdyqspggikrpknflERTGYRLPTEAEWEFACRAGTNTPR 1686
Cdd:pfam03781   90 DHPVTGVSWYDAVAYARWLGKR---------------------------------TGNGYRLPTEAEWEYAARGGSKGRR 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1687 Y------YGYAPELLPQYAWTTESSAKSAQVLFRPVRQLLPNSFGLFDTLGNVMEWCETHDSSRRHNKRMIVDNSDgliD 1760
Cdd:pfam03781  137 YpwgdelYPAGNIWQGADFPNEHAGADSFNGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRD---N 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 32473469   1761 NQSAYRVARGSAVFYIATT--MRSAKRE-QEKLYTFHPYLGFRVAR 1803
Cdd:pfam03781  214 FGGGYRVVRGGSWACSVYPsrLRPAFRGnCQTPGTRADDVGFRLVR 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
47-301 1.38e-58

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 205.07  E-value: 1.38e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469      47 YRVVRRIGSGGFGSVFHAKDESLNRDVAIKVpLRSLDDVNDEFQWSSEARMVAKLDHPNIVPVYDVGKSDQFPFFVVSrF 126
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV-IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME-Y 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     127 IQGVDLRERILKgKPSLEEGLIW--TASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLAMSDDAPRPTRAgl 204
Cdd:smart00220   79 CEGGDLFDLLKK-RGRLSEDEARfyLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT-- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     205 LIGTYSYMSPEQARGEGHlvDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLRQFNPQLPIELERICLK 284
Cdd:smart00220  156 FVGTPEYMAPEVLLGKGY--GKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRK 233
                           250
                    ....*....|....*..
gi 32473469     285 ALAQRVSDRYSNAAAMA 301
Cdd:smart00220  234 LLVKDPEKRLTAEEALQ 250
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
1522-1806 1.91e-33

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 224182 [Multi-domain]  Cd Length: 314  Bit Score: 133.46  E-value: 1.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469 1522 NLSDDEFSPIWNRNGQGQTMVHLrGPVDFVMGSPGHELFRDHSLEVPIQTKIPRSFAISDSEVTLEQFRRFDPDASYATQ 1601
Cdd:COG1262   34 NEVGLLGSAPAETLVIAPEMVLI-PGGEFTMGSPDDEWERFDRNEAPVHKVTVPPFEIDKYPVTNAQFARFVEAGGYTTA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469 1602 YT-----------------TQPDCPMTSVGWFDAIKYCRWLSEQEHVpeaemcypsieeiqrdyqspggikrpknflert 1664
Cdd:COG1262  113 WEedgepvypsywkgeggrLRLEHPVVGVSWYDAQAYAAWLGVKTGE--------------------------------- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469 1665 gYRLPTEAEWEFACRAGTNTPRYY--GYAPELLPQYAWT----TESSAKSAQVLFRPVRQL-LPNSFGLFDTLGNVMEWC 1737
Cdd:COG1262  160 -YRLPTEAEWEYAARAGTTTDSYPwgDELEPGLNAYAGTweylRAAAGWARERETAPVGAFpPNAAYGLYDMHGNVWEWT 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32473469 1738 ET--------HDSSRRHNKRMIVDNSDGLIDNQSaYRVARGSAVFYIATTMRSAKREQEKLYTFHPYLGFRVARTLK 1806
Cdd:COG1262  239 ADwekewhydNYGPAPSDGSAWYDGNSGSKFFGS-LRVVRGGSWASYPGVLRPAFRNFLVPDYRQAHVGFRCARLIK 314
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
46-306 1.83e-95

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 310.67  E-value: 1.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   46 RYRVVRRIGSGGFGSVFHAKDESLNRDVAIKVPLrsLDDVNDEFQWSS---EARMVAKLDHPNIVPVYDVGKSDQFPFFV 122
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLR--PELAEDEEFRERflrEARALARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  123 VsRFIQGVDLRERILKGKP-SLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLAMSDDAPRPTR 201
Cdd:cd14014   79 M-EYVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  202 AGLLIGTYSYMSPEQARGEGhlVDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLRQFNPQLPIELERI 281
Cdd:cd14014  158 TGSVLGTPAYMAPEQARGGP--VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAI 235
                        250       260
                 ....*....|....*....|....*
gi 32473469  282 CLKALAQRVSDRYSNAAAMAADLRT 306
Cdd:cd14014  236 ILRALAKDPEERPQSAAELLAALRA 260
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
1550-1803 6.03e-31

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


Pssm-ID: 252159  Cd Length: 259  Bit Score: 124.92  E-value: 6.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1550 FVMGSPGHELFRDhslEVPIQTKIPRSFAISDSEVTLEQFRRFDPDASYATQYTTQ-----------------------P 1606
Cdd:pfam03781   13 FEMGSAERTGNDN---EAPAHDVTVRPFAIDKYPVTNAQYAAFVEATGYTTEVYPQwwaeveganwrhpsgglsdiddgA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1607 DCPMTSVGWFDAIKYCRWLSEQehvpeaemcypsieeiqrdyqspggikrpknflERTGYRLPTEAEWEFACRAGTNTPR 1686
Cdd:pfam03781   90 DHPVTGVSWYDAVAYARWLGKR---------------------------------TGNGYRLPTEAEWEYAARGGSKGRR 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1687 Y------YGYAPELLPQYAWTTESSAKSAQVLFRPVRQLLPNSFGLFDTLGNVMEWCETHDSSRRHNKRMIVDNSDgliD 1760
Cdd:pfam03781  137 YpwgdelYPAGNIWQGADFPNEHAGADSFNGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRD---N 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 32473469   1761 NQSAYRVARGSAVFYIATT--MRSAKRE-QEKLYTFHPYLGFRVAR 1803
Cdd:pfam03781  214 FGGGYRVVRGGSWACSVYPsrLRPAFRGnCQTPGTRADDVGFRLVR 259
GldK TIGR03525
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
1607-1800 4.85e-10

gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. There is a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture and is represented by a separate model. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 274629  Cd Length: 450  Bit Score: 62.57  E-value: 4.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1607 DCPMTSVGWFDAIKYCRWLSEQEHvpeaemcypsieeiqrDYQspggikRPKNFLERTGYRLPTEAEWEFACRAGTNTPR 1686
Cdd:TIGR03525  263 DYPVVGVTWKQARAFCNWRTKYKN----------------DFR------KKKGPANVNTFRLPTEAEWEYAARGGLEGAT 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1687 YygyapellPQYAWTTESSAKSAQVLFRPVR------QLL---------PNSFGLFDTLGNVMEWCET--HDSSRRHNKR 1749
Cdd:TIGR03525  321 Y--------PWGGPYTKNDRGCFMANFKPVRgdyaadEALytveaksyePNDYGLYNMAGNVSEWTNSsyDPSSYEYMST 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 32473469   1750 MivdNSDGlIDNQSAYRVARGSAVFYIATTMRSAKREQEKLYTFHPYLGFR 1800
Cdd:TIGR03525  393 M---NPNV-NDSENTRKVVRGGSWKDVAYFLQVSTRDYEYADSARSYIGFR 439
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
46-191 1.34e-08

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 56.88  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469    46 RYRVVRRIGSGGFGSVFH---AKDESLNRDVAIKVP-------------LRSLDDVNDEFQWSSearmVAKLDHPNIVPV 109
Cdd:PHA02882   13 EWKIDKLIGCGGFGCVYEtqcASDHCINNQAVAKIEnlenetivmetlvYNNIYDIDKIALWKN----IHNIDHLGIPKY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   110 YDVGKSDQ----FPFFVVSRFIQGV-DLRERIL-KGKPSLEEgliWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRA 183
Cdd:PHA02882   89 YGCGSFKRcrmyYRFILLEKLVENTkEIFKRIKcKNKKLIKN---IMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165

                  ....*...
gi 32473469   184 WLTDFGLA 191
Cdd:PHA02882  166 YIIDYGIA 173
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
94-195 9.21e-07

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: 274749  Cd Length: 199  Bit Score: 49.90  E-value: 9.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     94 EARMVAKL-DHPNIVP-VYDVgksDQFPFFVVSRFIQGVDLRERILKGKPSLEEgliwtaSIADALDHAHSNGLVHRDVK 171
Cdd:TIGR03724   47 EARLLSRArKAGVNTPvIYDV---DPDNKTIVMEYIEGKPLKDVIEENGDELAR------EIGRLVGKLHKAGIVHGDLT 117
                           90       100
                   ....*....|....*....|....*
gi 32473469    172 PSNILIDTqDRAWLTDFGLA-MSDD 195
Cdd:TIGR03724  118 TSNIIVRD-DKVYLIDFGLGkYSDE 141
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
94-197 1.11e-04

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168  Cd Length: 204  Bit Score: 43.81  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   94 EARMVAKLDHPNI-VP-VYDVgksDQFPFFVVSRFIQGVDLRERILKGKPSLEEgliwtaSIADALDHAHSNGLVHRDVK 171
Cdd:COG3642   49 EARILAKAREAGVpVPiVYDV---DPDNGLIVMEYIEGELLKDALEEARPDLLR------EVGRLVGKLHKAGIVHGDLT 119
                         90       100
                 ....*....|....*....|....*.
gi 32473469  172 PSNILIdTQDRAWLTDFGLAMSDDAP 197
Cdd:COG3642  120 TSNIIL-SGGRIYFIDFGLGEFSDEV 144
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
47-301 1.38e-58

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 205.07  E-value: 1.38e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469      47 YRVVRRIGSGGFGSVFHAKDESLNRDVAIKVpLRSLDDVNDEFQWSSEARMVAKLDHPNIVPVYDVGKSDQFPFFVVSrF 126
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV-IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME-Y 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     127 IQGVDLRERILKgKPSLEEGLIW--TASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLAMSDDAPRPTRAgl 204
Cdd:smart00220   79 CEGGDLFDLLKK-RGRLSEDEARfyLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT-- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     205 LIGTYSYMSPEQARGEGHlvDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLRQFNPQLPIELERICLK 284
Cdd:smart00220  156 FVGTPEYMAPEVLLGKGY--GKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRK 233
                           250
                    ....*....|....*..
gi 32473469     285 ALAQRVSDRYSNAAAMA 301
Cdd:smart00220  234 LLVKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
47-295 4.42e-51

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 183.60  E-value: 4.42e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     47 YRVVRRIGSGGFGSVFHAKDESLNRDVAIK-VPLRSLDDVNDEFQWsSEARMVAKLDHPNIVPVYDVGKSDQFPFFVVSr 125
Cdd:pfam00069    1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKiLKKRSEKSKKDQTAR-REIRILRRLSHPNIVRLIDAFEDKDHLYLVME- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469    126 FIQGVDLRERILKGKPsLEEGLI--WTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLAMSDDAPRPTRAG 203
Cdd:pfam00069   79 YCEGGDLFDYLSRGGP-LSEDEAkkIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLTT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469    204 lLIGTYSYMSPEQ-ARGEGHlvDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPL---RQFNPQLPIELE 279
Cdd:pfam00069  158 -FVGTPEYMAPEVlLGGNGY--GPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLefdEPKSDSGSEEAK 234
                          250
                   ....*....|....*.
gi 32473469    280 RICLKALAQRVSDRYS 295
Cdd:pfam00069  235 DLIKKCLNKDPSKRPT 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
47-363 6.70e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 169.54  E-value: 6.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   47 YRVVRRIGSGGFGSVFHAKDeslNRDVAIKVPLRSL-DDVNDEFQWSSEARMVAKLDHP-NIVPVYDVGKSDQfPFFVVS 124
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLeSKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEG-SLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  125 RFIQGVDLRE----RILKGKPSLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAW-LTDFGLA-----MSD 194
Cdd:COG0515   78 EYVDGGSLEDllkkIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVkLIDFGLAkllpdPGS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  195 DAPRPTRAGLLIGTYSYMSPEQARG-EGHLVDGRADIFALGIVLYELLVGRRPFGGGSS---QQLLQDIVRAEPTPLRQF 270
Cdd:COG0515  158 TSSIPALPSTSVGTPGYMAPEVLLGlSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNssaTSQTLKIILELPTPSLAS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  271 N------PQLPIELERICLKALAQRVSDRYSNAAAMAADLRTFQSNETTVDYTDDLSAEFVPVANQWAPPGVEANAKGDE 344
Cdd:COG0515  238 PlspsnpELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNS 317
                        330
                 ....*....|....*....
gi 32473469  345 SESRVIPKGLRAFDRHDRR 363
Cdd:COG0515  318 LAISGSDLKLDDSNFSKEL 336
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
1522-1806 1.91e-33

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224182 [Multi-domain]  Cd Length: 314  Bit Score: 133.46  E-value: 1.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469 1522 NLSDDEFSPIWNRNGQGQTMVHLrGPVDFVMGSPGHELFRDHSLEVPIQTKIPRSFAISDSEVTLEQFRRFDPDASYATQ 1601
Cdd:COG1262   34 NEVGLLGSAPAETLVIAPEMVLI-PGGEFTMGSPDDEWERFDRNEAPVHKVTVPPFEIDKYPVTNAQFARFVEAGGYTTA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469 1602 YT-----------------TQPDCPMTSVGWFDAIKYCRWLSEQEHVpeaemcypsieeiqrdyqspggikrpknflert 1664
Cdd:COG1262  113 WEedgepvypsywkgeggrLRLEHPVVGVSWYDAQAYAAWLGVKTGE--------------------------------- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469 1665 gYRLPTEAEWEFACRAGTNTPRYY--GYAPELLPQYAWT----TESSAKSAQVLFRPVRQL-LPNSFGLFDTLGNVMEWC 1737
Cdd:COG1262  160 -YRLPTEAEWEYAARAGTTTDSYPwgDELEPGLNAYAGTweylRAAAGWARERETAPVGAFpPNAAYGLYDMHGNVWEWT 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32473469 1738 ET--------HDSSRRHNKRMIVDNSDGLIDNQSaYRVARGSAVFYIATTMRSAKREQEKLYTFHPYLGFRVARTLK 1806
Cdd:COG1262  239 ADwekewhydNYGPAPSDGSAWYDGNSGSKFFGS-LRVVRGGSWASYPGVLRPAFRNFLVPDYRQAHVGFRCARLIK 314
pknD PRK13184
serine/threonine-protein kinase; Reviewed
44-304 1.69e-31

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 133.36  E-value: 1.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469    44 IGRYRVVRRIGSGGFGSVFHAKDESLNRDVAIKvplRSLDDVND----EFQWSSEARMVAKLDHPNIVPVYDVgKSDQFP 119
Cdd:PRK13184    1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALK---KIREDLSEnpllKKRFLREAKIAADLIHPGIVPVYSI-CSDGDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   120 FFVVSRFIQGVDLRErILKG---KPSLEEGLIWTASIADAL----------DHAHSNGLVHRDVKPSNILIDTQDRAWLT 186
Cdd:PRK13184   77 VYYTMPYIEGYTLKS-LLKSvwqKESLSKELAEKTSVGAFLsifhkicatiEYVHSKGVLHRDLKPDNILLGLFGEVVIL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   187 DFGLAMSD----------DAPRP-------TRAGLLIGTYSYMSPEQARgeGHLVDGRADIFALGIVLYELLVGRRPFGG 249
Cdd:PRK13184  156 DWGAAIFKkleeedlldiDVDERnicyssmTIPGKIVGTPDYMAPERLL--GVPASESTDIYALGVILYQMLTLSFPYRR 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 32473469   250 GSSQQLLQDIVRAEP---TPLRqfnpQLPIELERICLKALAQRVSDRYSNAAAMAADL 304
Cdd:PRK13184  234 KKGRKISYRDVILSPievAPYR----EIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
73-305 5.25e-26

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: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 115.71  E-value: 5.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469     73 VAIKVpLRSlDDVNDEFQ---WSSEARMVAKLDHPNIVPVYDVGKSDQFPFFVVSRFIQGVDLRERIL-KGKPSLEEGLI 148
Cdd:TIGR03903    6 VAIKL-LRT-DAPEEEHQrarFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLREVLAaDGALPAGETGR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469    149 WTASIADALDHAHSNGLVHRDVKPSNILIDTQD---RAWLTDFGL------AMSDDAPRPTRAGLLIGTYSYMSPEQARG 219
Cdd:TIGR03903   84 LMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIgtllpgVRDADVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469    220 EGhlVDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLRQFNPQLPieLERICLKALAQRVSDRYSNAAA 299
Cdd:TIGR03903  164 EP--VTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLPPWIAGHP--LGQVLRKALNKDPRQRAASAPA 239

                   ....*.
gi 32473469    300 MAADLR 305
Cdd:TIGR03903  240 LAERFR 245
GldK_short TIGR03529
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
1593-1804 2.02e-13

gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. This model represents a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture than that found in Flavobacterium johnsoniae and related species (represented by (TIGR03525). Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 274632 [Multi-domain]  Cd Length: 344  Bit Score: 72.26  E-value: 2.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1593 DPDASYATQYTTQPDCPMTSVGWFDAIKYCRWLSEQehvpeaeMCYPSIEEIQrdYQSPGgikrpknflertgYRLPTEA 1672
Cdd:TIGR03529  143 DPLMEYYFDHPAFDNYPVVGVDWNAAKQFCEWRTYH-------MNAYRNEESQ--YDMPR-------------FRLPSEA 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   1673 EWEFACRAGTNTPRYYGYAPEL-------LPQYAWTTESSAKSAQVLFRPVRQLLPNSFGLFDTLGNVMEWCEthDSSRR 1745
Cdd:TIGR03529  201 EWEYAARGGRDMAKYPWGGPYLrnkrgcmLANFKPGRGNYYDDGFPYTAPVAVYFPNDFGLYDMAGNVAEWVL--DAYAA 278
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 32473469   1746 HNKRMIVDNSDGLIDNQSAYRVARGSAVFYIATTMRSAKREQEKLYTFHPYLGFRVART 1804
Cdd:TIGR03529  279 TSVPIVWDLNPVYEDPNEVRKIIRGGSWKDIAYYLETGTRTFEYEDVSQAHIGFRTVMT 337
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
377-432 1.77e-03

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 41.50  E-value: 1.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 32473469    377 GVPEVLRQLKIRIDAREaedafRVALIyGPSGSGKSSLMQAgLVPLLDPAVEVVSV 432
Cdd:TIGR02857  333 GRRPALRPVSFTVPPGE-----RVALV-GPSGAGKSTLLNL-LLGFVDPTEGSIAV 381
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
46-306 1.83e-95

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 310.67  E-value: 1.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   46 RYRVVRRIGSGGFGSVFHAKDESLNRDVAIKVPLrsLDDVNDEFQWSS---EARMVAKLDHPNIVPVYDVGKSDQFPFFV 122
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLR--PELAEDEEFRERflrEARALARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  123 VsRFIQGVDLRERILKGKP-SLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLAMSDDAPRPTR 201
Cdd:cd14014   79 M-EYVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  202 AGLLIGTYSYMSPEQARGEGhlVDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLRQFNPQLPIELERI 281
Cdd:cd14014  158 TGSVLGTPAYMAPEQARGGP--VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAI 235
                        250       260
                 ....*....|....*....|....*
gi 32473469  282 CLKALAQRVSDRYSNAAAMAADLRT 306
Cdd:cd14014  236 ILRALAKDPEERPQSAAELLAALRA 260
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
53-284 2.30e-44

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 163.48  E-value: 2.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   53 IGSGGFGSVFHAKdeSLNRDVAIKV--PLRSLDDVNDEFQwsSEARMVAKLDHPNIVPVYDVGKSDQfPFFVVSRFIQGV 130
Cdd:cd13999    1 IGSGSFGEVYKGK--WRGTDVAIKKlkVEDDNDELLKEFR--REVSILSKLRHPNIVQFIGACLSPP-PLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  131 DLRERILKGKP--SLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLA--MSDDAPRPTRAgllI 206
Cdd:cd13999   76 SLYDLLHKKKIplSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSriKNSTTEKMTGV---V 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32473469  207 GTYSYMSPEQARGEGhlVDGRADIFALGIVLYELLVGRRPFGG-GSSQQLLQDIVRAEPTPLRQFNPQLPIELERICLK 284
Cdd:cd13999  153 GTPRWMAPEVLRGEP--YTEKADVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWN 229
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
53-240 3.13e-44

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 162.05  E-value: 3.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   53 IGSGGFGSVFHAKDESLNRDVAIKV-PLRSLDDVNDEFQWssEARMVAKLDHPNIVPVYDVGKSDQFpFFVVSRFIQGVD 131
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKViPKEKLKKLLEELLR--EIEILKKLNHPNIVKLYDVFETENF-LYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  132 LRERI--LKGKPSLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLA--MSDDAPRPTRAGLLIG 207
Cdd:cd00180   78 LKDLLkeNKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAkdLDSDDSLLKTTGGTTP 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 32473469  208 TYsYMSPEQARGEGHlvDGRADIFALGIVLYEL 240
Cdd:cd00180  158 PY-YAPPELLGGRYY--GPKVDIWSLGVILYEL 187
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
46-263 1.35e-42

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 158.79  E-value: 1.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   46 RYRVVRRIGSGGFGSVFHAKDESLNRDVAIKVPLRSLDDVNDEFQWSSEARMVAKLDHPNIVPVYDVGKSDQFpFFVVSR 125
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKN-LYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  126 FIQGVDLRERIL-KGKPSLEEGLIWTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAW---LTDFGLA--MSDDAPRP 199
Cdd:cd05117   80 LCTGGELFDRIVkKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSpikIIDFGLAkiFEEGEKLK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32473469  200 TRAglliGTYSYMSPEQARGEGHlvDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAE 263
Cdd:cd05117  160 TVC----GTPYYVAPEVLKGKGY--GKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGK 217
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
46-295 7.00e-40

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 151.08  E-value: 7.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   46 RYRVVRRIGSGGFGSVFHAKDESLNRDVAIK-VPLRSLD--DVNDEFQwssEARMVAKLDHPNIVPVYDVGKSDQFpFFV 122
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeIDLSNMSekEREEALN---EVKLLSKLKHPNIVKYYESFEENGK-LCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  123 VSRFIQGVDLRERILKGKPS---LEEGLI--WTASIADALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLA---MSD 194
Cdd:cd08215   77 VMEYADGGDLAQKIKKQKKKgqpFPEEQIldWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISkvlEST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  195 DAprptRAGLLIGTYSYMSPEQARGEGHlvDGRADIFALGIVLYELLVGRRPFGGGSSQQLLQDIVRAEPTPLrqfNPQL 274
Cdd:cd08215  157 TD----LAKTVVGTPYYLSPELCENKPY--NYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPI---PSQY 227
                        250       260
                 ....*....|....*....|.
gi 32473469  275 PIELERICLKALAQRVSDRYS 295
Cdd:cd08215  228 SSELRDLVNSMLQKDPEKRPS 248
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
47-247 5.59e-39

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 148.12  E-value: 5.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469   47 YRVVRRIGSGGFGSVFHAKDESLNRDVAIKV-PLRSLDDVNDEFQwssEARMVAKLDHPNIVPVYDVGKSDQFPFfVVSR 125
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKiNLESKEKKESILN---EIAILKKCKHPNIVKYYGSYLKKDELW-IVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32473469  126 FIQGVDLRERILKGKPSLEEGliWTASIAD----ALDHAHSNGLVHRDVKPSNILIDTQDRAWLTDFGLA--MSDDAPRP 199
Cdd:cd05122   78 FCSGGSLKDLLKNTNKTLTEQ--QIAYVCKevlkGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSaqLSDGKTRN 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 32473469  200 TRagllIGTYSYMSPEQARGEGHlvDGRADIFALGIVLYELLVGRRPF 247
Cdd:cd05122  156 TF----VGTPYWMAPEVIQGKPY--GFKADIWSLGITAIEMAEGKPPY 197