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Conserved domains on  [gi|37523641|ref|NP_927018|]
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serine/threonine kinase [Gloeobacter violaceus PCC 7421]

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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 ...
87-366 2.32e-82

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: 268.30  E-value: 2.32e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  87 YRLVGELGRGGMGVVYLAEraDGLFSKRVAIKVLQPGRGA-PLLLERFVQERQILANLEHPHIARLIDGGTsEEGLPYLV 165
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 166 MEYIDGEPIDCYCRKQQ-LPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDeqapEAE 244
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG----DSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 245 QTATEWRMLTPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRPagLNVGPLDEMLWTLGEQAAVPPSRAVAagtdag 324
Cdd:cd14014 155 LTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPP--FDGDSPAAVLAKHLQEAPPPPSPLNP------ 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 37523641 325 lladpqkvQIDGSIDPLVLCALAKAPADRYTSALAMAEAIRG 366
Cdd:cd14014 227 --------DVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
574-684 7.56e-14

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 68.95  E-value: 7.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 574 YDYYLKGRDYLGRRsraDNDLAIELFKRALALDPNYALAHAGLGSAYGSKatrygqeERWEaESLKAIKKALVLDPNLSQ 653
Cdd:cd00189   1 EALLNLGNLYYKLG---DYDEALEYYEKALELDPDNADAYYNLAAAYYKL-------GKYE-EALEDYEKALELDPDNAK 69
                        90       100       110
                ....*....|....*....|....*....|.
gi 37523641 654 AHKALGSYYYGRGRYRQALASFKRGAELNPS 684
Cdd:cd00189  70 AYYNLGLAYYKLGKYEEALEAYEKALELDPN 100
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
746-816 8.00e-08

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 51.23  E-value: 8.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37523641 746 VSIQPDNVYALSYLSTLHKLRGQYDEARKTAQKILARDPQEVFGLTAAGDAERFAGRWSEAKAHYEKVLKI 816
Cdd:cd00189  27 LELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNLGLAYYKLGKYEEALEAYEKALEL 97
TolB_N super family cl21526
TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent ...
421-557 1.79e-39

TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent translocation system. This function of this amino terminal domain is uncertain.


The actual alignment was detected with superfamily member COG5616:

Pssm-ID: 276345  Cd Length: 152  Bit Score: 144.41  E-value: 1.79e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 421 FGSPASAAAR-TIAVLPFANIDGDSRSAYFSDGMTFDITNQLGKIADLTVIASSAAMQYRGTTKALREVARELGAGTILT 499
Cdd:COG5616  15 TAPGTSIPAKpSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAVDVREVGEELGVRYVLE 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37523641 500 GSVRRNGNRVRIVSQLVDPATGQQLWSQDYERQLKDVFAIQAEVSEQIARRLQARLSA 557
Cdd:COG5616  95 GSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYGI 152
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
87-361 3.47e-49

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.41  E-value: 3.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641     87 YRLVGELGRGGMGVVYLA-ERADGlfsKRVAIKVLQPGRgAPLLLERFVQERQILANLEHPHIARLIDGGTSEEGLpYLV 165
Cdd:smart00220   1 YEILEKLGEGSFGKVYLArDKKTG---KLVAIKVIKKKK-IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    166 MEYIDGEPI-DCYCRKQQLPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDEqapeaE 244
Cdd:smart00220  76 MEYCEGGDLfDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP-----G 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    245 QTATEwRMLTPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRP-AGLNvgPLDEMLWTLGEQAAVPPSRAVAAGTDA 323
Cdd:smart00220 151 EKLTT-FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPfPGDD--QLLELFKKIGKPKPPFPPPEWDISPEA 227
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 37523641    324 glladpqkvqIDgsidpLVLCALAKAPADRYTSALAMA 361
Cdd:smart00220 228 ----------KD-----LIRKLLVKDPEKRLTAEEALQ 250
NrfG COG0457
FOG: TPR repeat [General function prediction only]
528-812 1.98e-11

FOG: TPR repeat [General function prediction only]


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 64.48  E-value: 1.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 528 DYERQLKDVFAIQAEVSEQIARRLQARLSATEKLRLTQVPTASITAYDYYLKGRDYLGRRS-RADNDLAIELFKRALALD 606
Cdd:COG0457   3 DLLLALAILLEALAKLLAEALALLEAGLALLELLGELAEALELLEEALELLPNSDLAGLLLlLALALLKLGRLEEALELL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 607 PNYA--LAHAGLGSAYGSKATRYGQEERWEaESLKAIKKALVLDPNLSQAHKALG-SYYYGRGRYRQALASFKRGAELNP 683
Cdd:COG0457  83 EKALelELLPNLAEALLNLGLLLEALGKYE-EALELLEKALALDPDPDLAEALLAlGALYELGDYEEALELYEKALELDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 684 SLPVVAGAY---GGLSAAMGNLEEGVRWSKRSIALNPTRNG--YPNLGMIYTILGEDARARRALEAAVSIQPDNVYALSY 758
Cdd:COG0457 162 ELNELAEALlalGALLEALGRYEEALELLEKALKLNPDDDAeaLLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYN 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523641 759 LSTLHKLRGQYDEARKTAQKILARDPQEvfgltaAGDAERFAGRWSEAKAHYEK 812
Cdd:COG0457 242 LALLLLELGRYEEALEALEKALELDPDL------YNLGLALLLLLAEALELLEK 289
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
87-366 2.32e-82

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: 268.30  E-value: 2.32e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  87 YRLVGELGRGGMGVVYLAEraDGLFSKRVAIKVLQPGRGA-PLLLERFVQERQILANLEHPHIARLIDGGTsEEGLPYLV 165
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 166 MEYIDGEPIDCYCRKQQ-LPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDeqapEAE 244
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG----DSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 245 QTATEWRMLTPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRPagLNVGPLDEMLWTLGEQAAVPPSRAVAagtdag 324
Cdd:cd14014 155 LTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPP--FDGDSPAAVLAKHLQEAPPPPSPLNP------ 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 37523641 325 lladpqkvQIDGSIDPLVLCALAKAPADRYTSALAMAEAIRG 366
Cdd:cd14014 227 --------DVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
574-684 7.56e-14

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 68.95  E-value: 7.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 574 YDYYLKGRDYLGRRsraDNDLAIELFKRALALDPNYALAHAGLGSAYGSKatrygqeERWEaESLKAIKKALVLDPNLSQ 653
Cdd:cd00189   1 EALLNLGNLYYKLG---DYDEALEYYEKALELDPDNADAYYNLAAAYYKL-------GKYE-EALEDYEKALELDPDNAK 69
                        90       100       110
                ....*....|....*....|....*....|.
gi 37523641 654 AHKALGSYYYGRGRYRQALASFKRGAELNPS 684
Cdd:cd00189  70 AYYNLGLAYYKLGKYEEALEAYEKALELDPN 100
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
746-816 8.00e-08

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 51.23  E-value: 8.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37523641 746 VSIQPDNVYALSYLSTLHKLRGQYDEARKTAQKILARDPQEVFGLTAAGDAERFAGRWSEAKAHYEKVLKI 816
Cdd:cd00189  27 LELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNLGLAYYKLGKYEEALEAYEKALEL 97
COG5616 COG5616
Predicted integral membrane protein [Function unknown]
421-557 1.79e-39

Predicted integral membrane protein [Function unknown]


Pssm-ID: 227903  Cd Length: 152  Bit Score: 144.41  E-value: 1.79e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 421 FGSPASAAAR-TIAVLPFANIDGDSRSAYFSDGMTFDITNQLGKIADLTVIASSAAMQYRGTTKALREVARELGAGTILT 499
Cdd:COG5616  15 TAPGTSIPAKpSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAVDVREVGEELGVRYVLE 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37523641 500 GSVRRNGNRVRIVSQLVDPATGQQLWSQDYERQLKDVFAIQAEVSEQIARRLQARLSA 557
Cdd:COG5616  95 GSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYGI 152
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
88-230 1.07e-06

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: 48.90  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    88 RLVGELG--RGGMGVVYLAERADG--LFSKRVAIKVLQPGRGAPLLLERFVQERQILANLEHPHIA--RLIDGGTSEEGL 161
Cdd:pfam06293   9 DVVGEPNgrRTTWFVVARKDNGALrhYYRGGMWGKLNRDRYRFPLGRTRSFREFRLLRRLREAGVPvpKPVAAGAVKVGG 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37523641   162 PY---LVMEYIDG--EPIDCYCRKQQLPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVD-GAGEPK--LLDF 230
Cdd:pfam06293  89 EYqadLLTERLEGaqDLVTWLAQWADPAEELRRALWRAVGRLIARMHRAGVNHTDLNAHNILLDtGEGGFKvwLIDF 165
Probable_serine/threonine-protein_kinase TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
164-238 6.00e-05

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: 43.74  E-value: 6.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37523641   164 LVMEYIDGEPIdcycrKQQLPVReRLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGaGEPKLLDFGIAKLLDE 238
Cdd:TIGR03724  74 IVMEYIEGKPL-----KDVIEEN-GDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRD-DKVYLIDFGLGKYSDE 141
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
87-361 3.47e-49

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.41  E-value: 3.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641     87 YRLVGELGRGGMGVVYLA-ERADGlfsKRVAIKVLQPGRgAPLLLERFVQERQILANLEHPHIARLIDGGTSEEGLpYLV 165
Cdd:smart00220   1 YEILEKLGEGSFGKVYLArDKKTG---KLVAIKVIKKKK-IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    166 MEYIDGEPI-DCYCRKQQLPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDEqapeaE 244
Cdd:smart00220  76 MEYCEGGDLfDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP-----G 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    245 QTATEwRMLTPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRP-AGLNvgPLDEMLWTLGEQAAVPPSRAVAAGTDA 323
Cdd:smart00220 151 EKLTT-FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPfPGDD--QLLELFKKIGKPKPPFPPPEWDISPEA 227
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 37523641    324 glladpqkvqIDgsidpLVLCALAKAPADRYTSALAMA 361
Cdd:smart00220 228 ----------KD-----LIRKLLVKDPEKRLTAEEALQ 250
NrfG COG0457
FOG: TPR repeat [General function prediction only]
528-812 1.98e-11

FOG: TPR repeat [General function prediction only]


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 64.48  E-value: 1.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 528 DYERQLKDVFAIQAEVSEQIARRLQARLSATEKLRLTQVPTASITAYDYYLKGRDYLGRRS-RADNDLAIELFKRALALD 606
Cdd:COG0457   3 DLLLALAILLEALAKLLAEALALLEAGLALLELLGELAEALELLEEALELLPNSDLAGLLLlLALALLKLGRLEEALELL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 607 PNYA--LAHAGLGSAYGSKATRYGQEERWEaESLKAIKKALVLDPNLSQAHKALG-SYYYGRGRYRQALASFKRGAELNP 683
Cdd:COG0457  83 EKALelELLPNLAEALLNLGLLLEALGKYE-EALELLEKALALDPDPDLAEALLAlGALYELGDYEEALELYEKALELDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 684 SLPVVAGAY---GGLSAAMGNLEEGVRWSKRSIALNPTRNG--YPNLGMIYTILGEDARARRALEAAVSIQPDNVYALSY 758
Cdd:COG0457 162 ELNELAEALlalGALLEALGRYEEALELLEKALKLNPDDDAeaLLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYN 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523641 759 LSTLHKLRGQYDEARKTAQKILARDPQEvfgltaAGDAERFAGRWSEAKAHYEK 812
Cdd:COG0457 242 LALLLLELGRYEEALEALEKALELDPDL------YNLGLALLLLLAEALELLEK 289
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
87-364 1.79e-45

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: 168.77  E-value: 1.79e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  87 YRLVGELGRGGMGVVYLAERadglfSKRVAIKVLQPGR-GAPLLLERFVQERQILANL-EHPHIARLIDGGTSEEGLpYL 164
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD-----RKLVALKVLAKKLeSKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSL-YL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 165 VMEYIDGEPIDCYCRKQQ----LPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAG-EPKLLDFGIAKLL-DE 238
Cdd:COG0515  76 VMEYVDGGSLEDLLKKIGrkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLpDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 239 QAPEAEQTATEWRMLTPSYASPEQIRG---EAAGPSSDVFSLGVVLYELLTARRP-----AGLNVGPLDEMLWTLGEQAA 310
Cdd:COG0515 156 GSTSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPfegekNSSATSQTLKIILELPTPSL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523641 311 VPPSRavaagtdagllaDPQKVQIDGSIDPLVLCALAKAPADRYTSALAMAEAI 364
Cdd:COG0515 236 ASPLS------------PSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDL 277
Pkinase pfam00069
Protein kinase domain;
87-290 3.93e-44

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 161.26  E-value: 3.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    87 YRLVGELGRGGMGVVYLAERADGlfSKRVAIKVLQPGRGAPLLLERFVQERQILANLEHPHIARLIDggTSEEG-LPYLV 165
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGT--GKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLID--AFEDKdHLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   166 MEYIDGEPIDCYCRKQQ-LPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDEQAPEA- 243
Cdd:pfam00069  77 MEYCEGGDLFDYLSRGGpLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLt 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 37523641   244 EQTATEWrmltpsYASPEQIR-GEAAGPSSDVFSLGVVLYELLTARRP 290
Cdd:pfam00069 157 TFVGTPE------YMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPP 198
pknD PRK13184
serine/threonine-protein kinase; Reviewed
84-409 6.90e-33

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 136.05  E-value: 6.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   84 LGAYRLVGELGRGGMGVVYLAEraDGLFSKRVAIKVLQPG-RGAPLLLERFVQERQILANLEHPHIARlIDGGTSEEGLP 162
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAY--DPVCSRRVALKKIREDlSENPLLKKRFLREAKIAADLIHPGIVP-VYSICSDGDPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  163 YLVMEYIDGEPIDCYCR----KQQLP--------VRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDF 230
Cdd:PRK13184  78 YYTMPYIEGYTLKSLLKsvwqKESLSkelaektsVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  231 GIAK--------LLDEQAPEAEQTATEWRML-----TPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRPAGLNVG- 296
Cdd:PRK13184 158 GAAIfkkleeedLLDIDVDERNICYSSMTIPgkivgTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGr 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  297 --PLDEMLWTLGEqaaVPPSRavaagtdaglladpqkvQIDGSIDPLVLCALAKAPADRYTSALAMAEAIRGYLadhtpa 374
Cdd:PRK13184 238 kiSYRDVILSPIE---VAPYR-----------------EIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHL------ 291
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 37523641  375 SGPLSFPPKA---PRPALTGRLRQPAAIAAGIGVLAVS 409
Cdd:PRK13184 292 QGSPEWTVKAtlmTKKKSCWKFYEPILLSKYFPMLESS 329
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
112-289 5.15e-25

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: 111.09  E-value: 5.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    112 SKRVAIKVLQ--PGRGAPLLlERFVQERQILANLEHPHIARLIDGGTSEEGLPYLVMEYIDGEPI-DCYCRKQQLPVRER 188
Cdd:TIGR03903    3 GHEVAIKLLRtdAPEEEHQR-ARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLrEVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641    189 LALIEKVCRAVHHAHTLQVLHRDLKASNILV---DGAGEPKLLDFGIAKLLDEQAPEAEQTAT-EWRML-TPSYASPEQI 263
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGTLLPGVRDADVATLTrTTEVLgTPTYCAPEQL 161
                          170       180
                   ....*....|....*....|....*.
gi 37523641    264 RGEAAGPSSDVFSLGVVLYELLTARR 289
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQR 187
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
79-290 6.83e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 84.87  E-value: 6.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   79 VAGRRLGAYRLVGELGRGGMGVVYLAERADGlfSKRVAIKVLqpgRGAPLL----LERFVQERQILANLEHPHIARLIDG 154
Cdd:PTZ00263  12 TSSWKLSDFEMGETLGTGSFGRVRIAKHKGT--GEYYAIKCL---KKREILkmkqVQHVAQEKSILMELSHPFIVNMMCS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  155 GTSEEGLpYLVMEYIDGEPIDCYCRKQ-QLPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIA 233
Cdd:PTZ00263  87 FQDENRV-YFLLEFVVGGELFTHLRKAgRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 37523641  234 KlldeQAPEAEQTATEwrmlTPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRP 290
Cdd:PTZ00263 166 K----KVPDRTFTLCG----TPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPP 214
mod_pep_cyc TIGR04510
putative peptide modification system cyclase; Members of this family show homology to ...
381-941 9.74e-14

putative peptide modification system cyclase; Members of this family show homology to mononucleotidyl cyclases and to tetratricopeptide repeat (TPR) proteins. Members occur in next to two other markers of ribosomal peptide modification systems. One is a dehydrogenase related to SagB proteins from thiazole/oxazole modification systems. The other is the putative precursor, related to the nitrile hydratase-related leader peptide (NHLP) and nitrile hydratase alpha subunit families. These systems occur in many species of Xanthomonas and Stenotrophomonas, among others.


Pssm-ID: 275303 [Multi-domain]  Cd Length: 814  Bit Score: 73.93  E-value: 9.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   381 PPKAPRPALTGR-----LRQPAAIAAGIGVLavsLGVGGFWWTSNFGSPASA-AARTIAVL-PFANIDGDSR-------- 445
Cdd:TIGR04510 192 PLRMPRPNAKARrdlplWRRPAALAAEALLV---LAAGLGLWLLLRPEPAIAfAERDWVVVgDVRNLTGNVVlddsldqa 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   446 -------SAY---FSDGMTFDITNQLGKIADLTVIASSAAmqyrgttkalrEVARELGAGTILTGSVRRNGNRVRIVSQL 515
Cdd:TIGR04510 269 frisleqSRYvnvLSDMKVRDTLTRMRRDPDTTLDRATAS-----------EVALRDGARAVLLPSVSEVGGRLRVSVEV 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   516 VDPATGQQLWSQDYE-RQLKDVFAIQAEVSEQIARRLQARLSATEK--LRLTQVPTASITAYDYYLKGRDYLGRRsraDN 592
Cdd:TIGR04510 338 VDPATQQTVYVESADgRGLESVLASVDDVTGQLRERLGEALASIRRnsKPLPQVTTSSLDALRAYALGQEAYGQG---DF 414
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   593 DLAIELFKRALALDPNYALAHAGLGSAYGSKATRygqeerweAESLKAIKKALVLDPNLSqAHKALgsYYYGR----GRY 668
Cdd:TIGR04510 415 REALALFQRAVEIDPDFALAYLGQARAHFANSDY--------ADARPLLAKAQRLRGRLP-ARERL--YLDAWaaelGDP 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   669 RQALASFKRGAELNPSLPVVAGAYGGLSAAMGNLEEGVRWSKRS-IALNPTRN-GYPNLGMIYTILGEDARARRALEAAV 746
Cdd:TIGR04510 484 GAALEAWKQLARLYPDYFAAQANAAWALFVANRYADALPYARAAaVSQNPLRSiALDLLGRIQLAQGKYAQALRAFERAA 563
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   747 SIqpDNVYALSYLSTLHKLRGQYDEarktAQKILARDPQEvfGLTAAGDAERFA---GRWSEAKAHYEKVLKITDRLDGE 823
Cdd:TIGR04510 564 LL--GGGGALRRLAAVLAAQGDYAE----ADAVLARLDKN--GFANRLERTSIAldqGKWEAARAAAAAAAAAAGQAAPF 635
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   824 SGQL-----QSTTILADIARREGQPTRAAQLLARSFQIDREAIDGGNEYYFYpFDLAAAYAVQ--GDKSSALRWLrraik 896
Cdd:TIGR04510 636 DRRLygvvqLAVRAATGRRAAAADVARLAATALLAALQADNPDEPDRGDRLV-AALAAAYLAQrlGDDALAARVL----- 709
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 37523641   897 agwRDYRWLKLDPVFERLRgdgefeQLVAQLKAQVEAMRQRVIAA 941
Cdd:TIGR04510 710 ---AQLGVLALASGDPALA------QLRAVVDAEQLLLSGDPEAA 745
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
134-286 1.91e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 71.95  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  134 VQERQILANLEHPHIARLIDGGTSEEGLPYLVMEYidgePIDCYC---RKQQLPVRERLALIEKVCRAVHHAHTLQVLHR 210
Cdd:PHA03212 131 ATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRY----KTDLYCylaAKRNIAICDILAIERSVLRAIQYLHENRIIHR 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37523641  211 DLKASNILVDGAGEPKLLDFGIAKLldeqapEAEQTATEWRMLTPSYA--SPEQIRGEAAGPSSDVFSLGVVLYELLT 286
Cdd:PHA03212 207 DIKAENIFINHPGDVCLGDFGAACF------PVDINANKYYGWAGTIAtnAPELLARDPYGPAVDIWSAGIVLFEMAT 278
PRK12370 PRK12370
invasion protein regulator; Provisional
425-792 1.18e-12

invasion protein regulator; Provisional


Pssm-ID: 237080 [Multi-domain]  Cd Length: 553  Bit Score: 70.27  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  425 ASAAARTIAVLPF-------------ANIDGDSRSAYFS-DGMTFDITNQLGKIADLTviassaamqyrgttkalrEVAR 490
Cdd:PRK12370 117 PQPTTHTLAILPFqmqdqvqseslhySIVKGLSQYAPFGlSVLPVTITKNCRSVKDIL------------------ELMD 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  491 ELGAGTILTGSVRRNGNRVRIVSQLVDpATGQQLWSQDYERQLKD--VFAIQAEVSEQIARRLQArlsatekLRLTQVPT 568
Cdd:PRK12370 179 QLRPDYYISGQMIPDGNDNIVQIEIVR-VKGYHLLHQESIKLIEHqpASLLQNKIANLLLRCIPG-------LRWDTKQI 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  569 ASITAYD---YYLKGRDYLGRRSRADNDLAIELFKRALALDPNYALAHAGLGSAYGSKAtRYGQEERWEA--ESLKAIKK 643
Cdd:PRK12370 251 SELNSIDstmVYLRGKHELNQYTPYSLQQALKLLTQCVNMSPNSIAPYCALAECYLSMA-QMGIFDKQNAmiKAKEHAIK 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  644 ALVLDPNLSQAHKALGSYYYGRGRYRQALASFKRGAELNPSLPVVAGAYGGLSAAMGNLEEGVRWSKRSIALNPTRNGYP 723
Cdd:PRK12370 330 ATELDHNNPQALGLLGLINTIHSEYIVGSLLFKQANLLSPISADIKYYYGWNLFMAGQLEEALQTINECLKLDPTRAAAG 409
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37523641  724 NLGMI--YTILGEDARARRALEAAVSIQPDNVYALSYLSTLHKLRGQYDEARKTAQKIlarDPQEVFGLTA 792
Cdd:PRK12370 410 ITKLWitYYHTGIDDAIRLGDELRSQHLQDNPILLSMQVMFLSLKGKHELARKLTKEI---STQEITGLIA 477
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
50-293 1.33e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 66.00  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641   50 QQDGFLSTPIlgsPLESLLANRSPTDVSWVAGRRLGAYRLVGEL------GRGGMGVVYLA-ERADGlfsKRVAIKVLQp 122
Cdd:PLN00034  36 QRDPSLAVPL---PLPPPSSSSSSSSSSSASGSAPSAAKSLSELervnriGSGAGGTVYKViHRPTG---RLYALKVIY- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  123 GRGAPLLLERFVQERQILANLEHPHIARLIDGgTSEEGLPYLVMEYIDGEPIDcycrKQQLPVRERLA-LIEKVCRAVHH 201
Cdd:PLN00034 109 GNHEDTVRRQICREIEILRDVNHPNVVKCHDM-FDHNGEIQVLLEFMDGGSLE----GTHIADEQFLAdVARQILSGIAY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  202 AHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDEQAPEAEQTATewrmlTPSYASPEQI-----RGEAAGPSSDVFS 276
Cdd:PLN00034 184 LHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVG-----TIAYMSPERIntdlnHGAYDGYAGDIWS 258
                        250
                 ....*....|....*..
gi 37523641  277 LGVVLYELLTARRPAGL 293
Cdd:PLN00034 259 LGVSILEFYLGRFPFGV 275
TPR_11 pfam13414
TPR repeat;
573-649 3.88e-07

TPR repeat;


Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 48.85  E-value: 3.88e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37523641   573 AYDYYLKGRDYLGRRsraDNDLAIELFKRALALDPNYALAHAGLGSAYgskatrYGQEERWEaESLKAIKKALVLDP 649
Cdd:pfam13414   3 AEALKNLGNALFKLG---DYDEAIEAYEKALELDPDNAEAYLNLALAY------LKLGKDYE-EALEDLEKALELDP 69
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
87-366 2.32e-82

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: 268.30  E-value: 2.32e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641  87 YRLVGELGRGGMGVVYLAEraDGLFSKRVAIKVLQPGRGA-PLLLERFVQERQILANLEHPHIARLIDGGTsEEGLPYLV 165
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 166 MEYIDGEPIDCYCRKQQ-LPVRERLALIEKVCRAVHHAHTLQVLHRDLKASNILVDGAGEPKLLDFGIAKLLDeqapEAE 244
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG----DSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523641 245 QTATEWRMLTPSYASPEQIRGEAAGPSSDVFSLGVVLYELLTARRPagLNVGPLDEMLWTLGEQAAVPPSRAVAagtdag 324
Cdd:cd14014 155 LTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPP--FDGDSPAAVLAKHLQEAPPPPSPLNP------ 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 37523641 325 lladpqkvQIDGSIDPLVLCALAKAPADRYTSALAMAEAIRG 366
Cdd:cd14014 227 --------DVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
574-684 7.56e-14

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals,