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Conserved domains on  [gi|1223536500|ref|WP_091573145|]
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AAA family ATPase [Melghirimyces thermohalophilus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
84-392 1.45e-64

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 209.97  E-value: 1.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500  84 RDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKldsrdevevnfawaQGKVIAFYSGKGGCGQSLVASTLAQ 163
Cdd:COG4963    60 PNLILLEALSESAALLADVLPLSPDELRAALARLLDPGAAR--------------RGRVIAVVGAKGGVGATTLAVNLAW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 164 TIGLDSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVPVINELNDNHIRSVTSVEEySQIEVLSSPVDAETAENITEEH 243
Cdd:COG4963   126 ALARESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHS-SGLSVLAAPADLERAEEVSPEA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 244 VERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNVLDLFSKLNIdPTDRLHLLLNRVSRDT 323
Cdd:COG4963   205 VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGL-PDDKVRLVLNRVPKRG 283
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1223536500 324 ELMPKDVNRHFSFPVVASFREDYKRIQQLLNKGKLIRKSRRERALpnfARDVQKLASWLLSRQGNNQSA 392
Cdd:COG4963   284 EISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAPKSPL---AKAIRKLAARLTGRPAAAAAK 349
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
6-130 4.23e-09

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 54.59  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   6 KLLIVSEDPSQAEDIVEQIGSLyPQHHHIEP----DEVRKEIVRLQPDIVLL-CERKDGSGVQLLPYLSKEVPDAITIYL 80
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERL-PGFEVVGVassgEEALALLAEHRPDLILLdIYLPDGDGLELLRELRARGPDVDVIVI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1223536500  81 TNRRDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKLDSRDE 130
Cdd:COG4565    84 TAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEE 133
 
Name Accession Description Interval E-value
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
84-392 1.45e-64

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 209.97  E-value: 1.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500  84 RDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKldsrdevevnfawaQGKVIAFYSGKGGCGQSLVASTLAQ 163
Cdd:COG4963    60 PNLILLEALSESAALLADVLPLSPDELRAALARLLDPGAAR--------------RGRVIAVVGAKGGVGATTLAVNLAW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 164 TIGLDSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVPVINELNDNHIRSVTSVEEySQIEVLSSPVDAETAENITEEH 243
Cdd:COG4963   126 ALARESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHS-SGLSVLAAPADLERAEEVSPEA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 244 VERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNVLDLFSKLNIdPTDRLHLLLNRVSRDT 323
Cdd:COG4963   205 VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGL-PDDKVRLVLNRVPKRG 283
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1223536500 324 ELMPKDVNRHFSFPVVASFREDYKRIQQLLNKGKLIRKSRRERALpnfARDVQKLASWLLSRQGNNQSA 392
Cdd:COG4963   284 EISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAPKSPL---AKAIRKLAARLTGRPAAAAAK 349
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
141-379 4.56e-43

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 150.12  E-value: 4.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQTIGLDSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVPVINELNDNHIRS-VTSVE 219
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSaVTRHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 220 eySQIEVLSSPVDAETAENITEEHVERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNVLD 299
Cdd:cd03111    81 --SGLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 300 LFSKLNIDpTDRLHLLLNRVSRDTELMPKDVNRHFSFPVVASFREDYKRIQQLLNKGKLIRKSrRERALpnFARDVQKLA 379
Cdd:cd03111   159 SLRELEGS-SDRLRLVLNRYDKKSEISPKDIEEALGLEVFATLPNDYKAVSESANTGRPLVEV-APRSA--LVRALQDLA 234
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
6-130 4.23e-09

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 54.59  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   6 KLLIVSEDPSQAEDIVEQIGSLyPQHHHIEP----DEVRKEIVRLQPDIVLL-CERKDGSGVQLLPYLSKEVPDAITIYL 80
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERL-PGFEVVGVassgEEALALLAEHRPDLILLdIYLPDGDGLELLRELRARGPDVDVIVI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1223536500  81 TNRRDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKLDSRDE 130
Cdd:COG4565    84 TAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEE 133
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
140-299 6.13e-09

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 54.90  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 140 GKVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLVDLNMQ-----YGGIETilnVDNPRNLYDLvpvinELNDNHIRS 214
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALA-KKGKKVLLIDLDPQgnatsGLGIDK---NNVEKTIYEL-----LIGECNIEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 215 VTSVEEYSQIEVLSSPVD-----AETAENITEEHV-ERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADhisYVMVP-- 286
Cdd:pfam13614  72 AIIKTVIENLDLIPSNIDlagaeIELIGIENRENIlKEALEPVKDNYDYIIIDCPPSLGLLTINALTASD---SVLIPvq 148
                         170
                  ....*....|....
gi 1223536500 287 -DMLSLRVLSNVLD 299
Cdd:pfam13614 149 cEYYALEGLSQLLN 162
PRK09841 PRK09841
tyrosine-protein kinase;
99-263 7.24e-08

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 54.53  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500  99 DILFLPdeINALEDVLNRAVKALQTKLdsrdevevNFAW--AQGKVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLV 176
Cdd:PRK09841  498 NIPFLA--VDNPADSAVEAVRALRTSL--------HFAMmeTENNILMITGATPDSGKTFVSSTLAAVIA-QSDQKVLFI 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 177 DLNMQYGGIETILNVDNPRNLYDLVPVINELNDnhirsvtSVEEYSQ--IEVLS-SPVDAETAENITEEHVERLIRTARL 253
Cdd:PRK09841  567 DADLRRGYSHNLFTVSNEHGLSEYLAGKDELNK-------VIQHFGKggFDVITrGQVPPNPSELLMRDRMRQLLEWAND 639
                         170
                  ....*....|
gi 1223536500 254 YYDYILIDLP 263
Cdd:PRK09841  640 HYDLVIVDTP 649
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
138-263 5.77e-05

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 45.10  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 138 AQGKVIAFYSGKGGCGQSLVASTLAQTIGLdSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVpvineLNDNHIRSVTS 217
Cdd:TIGR01005 551 AENNLIAIAGALPDEGKSFIAANFAALIAA-GGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLL-----AGEASIEAGIH 624
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1223536500 218 VEEYSQIEVLSSPVDAETAENITE----EHVERLIRTARLYYDYILIDLP 263
Cdd:TIGR01005 625 RDQRPGLAFIAAGGASHFPHNPNEllanPAMAELIDNARNAFDLVLVDLA 674
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
6-116 1.10e-03

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 38.38  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   6 KLLIVSEDPSQAE---DIVEQIgslyPQHHHI----EPDEVRKEIVRLQPDIVLLCER-KDGSGVQLLPYLSKEVPDAIT 77
Cdd:cd19925     2 NVLIVEDDPMVAEihrAYVEQV----PGFTVIgtagTGEEALKLLKERQPDLILLDIYlPDGNGLDLLRELRAAGHDVDV 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1223536500  78 IYLTNRRDPVRTRDVNRAGAFDILFLPDEINALEDVLNR 116
Cdd:cd19925    78 IVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
 
Name Accession Description Interval E-value
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
84-392 1.45e-64

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 209.97  E-value: 1.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500  84 RDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKldsrdevevnfawaQGKVIAFYSGKGGCGQSLVASTLAQ 163
Cdd:COG4963    60 PNLILLEALSESAALLADVLPLSPDELRAALARLLDPGAAR--------------RGRVIAVVGAKGGVGATTLAVNLAW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 164 TIGLDSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVPVINELNDNHIRSVTSVEEySQIEVLSSPVDAETAENITEEH 243
Cdd:COG4963   126 ALARESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHS-SGLSVLAAPADLERAEEVSPEA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 244 VERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNVLDLFSKLNIdPTDRLHLLLNRVSRDT 323
Cdd:COG4963   205 VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGL-PDDKVRLVLNRVPKRG 283
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1223536500 324 ELMPKDVNRHFSFPVVASFREDYKRIQQLLNKGKLIRKSRRERALpnfARDVQKLASWLLSRQGNNQSA 392
Cdd:COG4963   284 EISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAPKSPL---AKAIRKLAARLTGRPAAAAAK 349
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
141-379 4.56e-43

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 150.12  E-value: 4.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQTIGLDSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVPVINELNDNHIRS-VTSVE 219
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSaVTRHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 220 eySQIEVLSSPVDAETAENITEEHVERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNVLD 299
Cdd:cd03111    81 --SGLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 300 LFSKLNIDpTDRLHLLLNRVSRDTELMPKDVNRHFSFPVVASFREDYKRIQQLLNKGKLIRKSrRERALpnFARDVQKLA 379
Cdd:cd03111   159 SLRELEGS-SDRLRLVLNRYDKKSEISPKDIEEALGLEVFATLPNDYKAVSESANTGRPLVEV-APRSA--LVRALQDLA 234
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
172-385 2.78e-18

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 83.02  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 172 SVLLVDLNMQYGGIETILNVDNPRNLYDLvpvinelndnhIRSVTSVEEY-----SQIEVLSSPVDAETAENIT-EEHVE 245
Cdd:COG0455    16 RVLLVDADLGLANLDVLLGLEPKATLADV-----------LAGEADLEDAivqgpGGLDVLPGGSGPAELAELDpEERLI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 246 RLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNVLDLFSKLNidPTDRLHLLLNRVSRDTEL 325
Cdd:COG0455    85 RVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRL--GVRRAGVVVNRVRSEAEA 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1223536500 326 MP------KDVNRHFSF--PVVASFREDyKRIQQLLNKGKLIRKSRRERAlpnFARDVQKLASWLLSR 385
Cdd:COG0455   163 RDvferleQVAERFLGVrlRVLGVIPED-PAVREAVRRGRPLVLAAPDSP---AARAIRELAARLAGW 226
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
141-385 3.05e-17

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 80.67  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQS----LVASTLAQTiGLDssssVLLVDLNMQyGGIETILNVDN---PRNLYDLVpvineLNDNHIR 213
Cdd:COG1192     2 KVIAVANQKGGVGKTttavNLAAALARR-GKR----VLLIDLDPQ-GNLTSGLGLDPddlDPTLYDLL-----LDDAPLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 214 SVTSVEEYSQIEVLSSPVDAETAENIT------EEHVERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPD 287
Cdd:COG1192    71 DAIVPTEIPGLDLIPANIDLAGAEIELvsrpgrELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 288 MLSLRVLSNVLDLFSKL--NIDPT-DRLHLLLNRVSRDTEL---MPKDVNRHFSFPVVASFREDYKRIQQLLNKGKLIRK 361
Cdd:COG1192   151 YLSLEGLAQLLETIEEVreDLNPKlEILGILLTMVDPRTRLsreVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFE 230
                         250       260
                  ....*....|....*....|....*
gi 1223536500 362 -SRRERAlpnfARDVQKLASWLLSR 385
Cdd:COG1192   231 yDPKSKG----AKAYRALAEELLER 251
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
142-324 1.52e-14

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 73.30  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 142 VIAFYSGKGGCGQSLVASTLAQTIGLdSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVpvineLNDNHIRSVTSVEEY 221
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPGLSDVL-----AGEASLEDVIQPTEV 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 222 SQIEVLSS-PVDAETAENITEEHVERLIRTARLYYDYILIDLP--TEMTPMTyTVLEEADHISYVMVPDMLSLRVLSNVL 298
Cdd:COG0489   168 EGLDVLPAgPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPpgLGVADAT-LLASLVDGVLLVVRPGKTALDDVRKAL 246
                         170       180
                  ....*....|....*....|....*.
gi 1223536500 299 DLFSKLNIDPtdrLHLLLNRVSRDTE 324
Cdd:COG0489   247 EMLEKAGVPV---LGVVLNMVCPKGE 269
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
141-357 3.81e-12

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 65.30  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLVDLNMQYGGIETILNVDNpRNLYDLVPVINE---LNDNHIRSvts 217
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALA-KLGKKVLLIDADIGLRNLDLILGLEN-RIVYTLVDVLEGecrLEQALIKD--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 218 vEEYSQIEVLSSPVDAETaENITEEHVERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSNV 297
Cdd:cd02036    76 -KRWENLYLLPASQTRDK-DALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1223536500 298 LDLFSKLNIDPtdrLHLLLNR-----VSRDTELMPKDVNRHFSFPVVASFREDyKRIQQLLNKGK 357
Cdd:cd02036   154 IGLLESKGIVN---IGLIVNRyrpemVKSGDMLSVEDIQEILGIPLLGVIPED-PEVIVATNRGE 214
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
138-263 2.39e-10

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 59.51  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 138 AQGKVIAFYSGKGGCGQSLVASTLAQTIGLdSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLvpvineLNDNH-IRSVT 216
Cdd:cd05387    17 AGPKVIAVTSASPGEGKSTVAANLAVALAQ-SGKRVLLIDADLRRPSLHRLLGLPNEPGLSEV------LSGQAsLEDVI 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1223536500 217 SVEEYSQIEVL-SSPVDAETAENITEEHVERLIRTARLYYDYILIDLP 263
Cdd:cd05387    90 QSTNIPNLDVLpAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTP 137
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
6-130 4.23e-09

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 54.59  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   6 KLLIVSEDPSQAEDIVEQIGSLyPQHHHIEP----DEVRKEIVRLQPDIVLL-CERKDGSGVQLLPYLSKEVPDAITIYL 80
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERL-PGFEVVGVassgEEALALLAEHRPDLILLdIYLPDGDGLELLRELRARGPDVDVIVI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1223536500  81 TNRRDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKLDSRDE 130
Cdd:COG4565    84 TAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEE 133
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
140-299 6.13e-09

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 54.90  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 140 GKVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLVDLNMQ-----YGGIETilnVDNPRNLYDLvpvinELNDNHIRS 214
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALA-KKGKKVLLIDLDPQgnatsGLGIDK---NNVEKTIYEL-----LIGECNIEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 215 VTSVEEYSQIEVLSSPVD-----AETAENITEEHV-ERLIRTARLYYDYILIDLPTEMTPMTYTVLEEADhisYVMVP-- 286
Cdd:pfam13614  72 AIIKTVIENLDLIPSNIDlagaeIELIGIENRENIlKEALEPVKDNYDYIIIDCPPSLGLLTINALTASD---SVLIPvq 148
                         170
                  ....*....|....
gi 1223536500 287 -DMLSLRVLSNVLD 299
Cdd:pfam13614 149 cEYYALEGLSQLLN 162
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
141-319 9.01e-09

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 55.27  E-value: 9.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVPVINELNDnhirSVTSVEE 220
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALS-KLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLED----IIVEGPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 221 ysQIEVLSSPVDAETAENITEEHVERLIR---TARLYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLrvlsnv 297
Cdd:cd02038    76 --GLDIIPGGSGMEELANLDPEQKAKLIEelsSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSI------ 147
                         170       180
                  ....*....|....*....|....*.
gi 1223536500 298 LDLFS--KLNI--DPTDRLHLLLNRV 319
Cdd:cd02038   148 TDAYAliKVLSrrGGKKNFRLIVNMA 173
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
141-323 1.11e-08

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 53.31  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQTIGLDSSSsVLLVDLNMQyggietilnvdnprnlydlvpvinelndnhiRSVTSvee 220
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLDPQ-------------------------------GSLTS--- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 221 ysqievlsspvdaetaeniteehverlirtarLYYDYILIDLPTEMTPMTYTVLEEADhisYVMVP---DMLSLRVLSNV 297
Cdd:cd02042    46 --------------------------------WLYDYILIDTPPSLGLLTRNALAAAD---LVLIPvqpSPFDLDGLAKL 90
                         170       180
                  ....*....|....*....|....*....
gi 1223536500 298 LDLFSKLNID---PTDRLHLLLNRVSRDT 323
Cdd:cd02042    91 LDTLEELKKQlnpPLLILGILLTRVDPRT 119
PRK09841 PRK09841
tyrosine-protein kinase;
99-263 7.24e-08

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 54.53  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500  99 DILFLPdeINALEDVLNRAVKALQTKLdsrdevevNFAW--AQGKVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLV 176
Cdd:PRK09841  498 NIPFLA--VDNPADSAVEAVRALRTSL--------HFAMmeTENNILMITGATPDSGKTFVSSTLAAVIA-QSDQKVLFI 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 177 DLNMQYGGIETILNVDNPRNLYDLVPVINELNDnhirsvtSVEEYSQ--IEVLS-SPVDAETAENITEEHVERLIRTARL 253
Cdd:PRK09841  567 DADLRRGYSHNLFTVSNEHGLSEYLAGKDELNK-------VIQHFGKggFDVITrGQVPPNPSELLMRDRMRQLLEWAND 639
                         170
                  ....*....|
gi 1223536500 254 YYDYILIDLP 263
Cdd:PRK09841  640 HYDLVIVDTP 649
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-132 3.20e-07

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 51.89  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   3 NKEKLLIVSEDPSQAEDIVEQigsLYPQHHHIE----PDEVRKEIVRLQPDIVLLCER-KDGSGVQLLPYLSKEVPDAIT 77
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKEL---LERAGYEVEtaasGEEALALLREEPPDLVLLDLRmPGMDGLELLRELRALDPDLPV 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1223536500  78 IYLTNRRDPVRTRDVNRAGAFDILFLPDEINALEDVLNRAVKALQTKLDSRDEVE 132
Cdd:COG2204    78 ILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG 132
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
143-359 3.38e-07

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 50.81  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 143 IAFYSGKGGCGQSLVASTLAQTI---GLDssssVLLVDL-----NMQYGGIETILNVDnPRNLYDLVPvinelNDNHIRS 214
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALarrGLR----VLLIDLdpqsnNSSVEGLEGDIAPA-LQALAEGLK-----GRVNLDP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 215 VTSVEEYSQ--IEVLSSPVDAETAENIT-----EEHVERLIRTARLYYDYILIDlptemTPM-----TYTVLEEADHISY 282
Cdd:pfam01656  71 ILLKEKSDEggLDLIPGNIDLEKFEKELlgprkEERLREALEALKEDYDYVIID-----GAPglgelLRNALIAADYVII 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 283 VMVPDMLSLRVLSNVLDLFSKL----NIDPTDRLHLLLNRV-SRDTELMPKDVNR--HFSFPVVASFREDyKRIQQLLNK 355
Cdd:pfam01656 146 PLEPEVILVEDAKRLGGVIAALvggyALLGLKIIGVVLNKVdGDNHGKLLKEALEelLRGLPVLGVIPRD-EAVAEAPAR 224

                  ....
gi 1223536500 356 GKLI 359
Cdd:pfam01656 225 GLPV 228
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
139-298 4.65e-05

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 44.07  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 139 QGKVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLvdLNM-QYGGIETILNVDNPRNLYDLVPVINELNDNHIRSVTS 217
Cdd:cd17869     2 ATSVITFHSPCGGSGKSTVAAACAYTLA-EKGKKTLY--LNMeRLQSTDVFFGASGRYLMSDHLYTLKSRKANLADKLES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 218 V--EEYSQIEVLSSPVDAETAENITEEHVERLIRTARLY--YDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRV 293
Cdd:cd17869    79 CvkQHESGVYYFSPFKSALDILEIKKDDILHMITKLVEAhaYDYIIMDLSFEFSSTVCKLLQASHNNVVIALQDANSSYK 158

                  ....*
gi 1223536500 294 LSNVL 298
Cdd:cd17869   159 LNKFL 163
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
138-263 5.77e-05

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 45.10  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 138 AQGKVIAFYSGKGGCGQSLVASTLAQTIGLdSSSSVLLVDLNMQYGGIETILNVDNPRNLYDLVpvineLNDNHIRSVTS 217
Cdd:TIGR01005 551 AENNLIAIAGALPDEGKSFIAANFAALIAA-GGKRTLLIDADIRKGGLHQMFGKAPKPGLLDLL-----AGEASIEAGIH 624
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1223536500 218 VEEYSQIEVLSSPVDAETAENITE----EHVERLIRTARLYYDYILIDLP 263
Cdd:TIGR01005 625 RDQRPGLAFIAAGGASHFPHNPNEllanPAMAELIDNARNAFDLVLVDLA 674
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-132 8.30e-05

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 43.02  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   1 MRNKeKLLIVSEDPSQAEDIVEQIGSL--YPQHHHIEPDEVRKEIVRLQPDIVLL-CERKDGSGVQLLPYLSKEVPDAIt 77
Cdd:COG3707     1 MRGL-RVLVVDDEPLRRADLREGLREAgyEVVAEAADGEDAVELVRELKPDLVIVdIDMPDRDGLEAARQISEERPAPV- 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1223536500  78 IYLTNRRDPVRTRDVNRAGAFDILFLP----DEINALEDVLNRA---------VKALQTKLDSRDEVE 132
Cdd:COG3707    79 ILLTAYSDPELIERALEAGVSAYLVKPldpeDLLPALELALARFrelralrreLAKLREALEERKLIE 146
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
133-263 2.19e-04

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 42.04  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 133 VNFAWAQGKVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLVDLNMQYGGIETILNVDNPRN-LYDLVpvINELNDNH 211
Cdd:TIGR01007  10 IQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFA-QAGYKTLLIDGDMRNSVMSGTFKSQNKITgLTNFL--SGTTDLSD 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1223536500 212 IRSVTSVEEYSQIEvlSSPVDAETAENITEEHVERLIRTARLYYDYILIDLP 263
Cdd:TIGR01007  87 AICDTNIENLDVIT--AGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTP 136
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
141-206 1.08e-03

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 40.18  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQT---IGLDssssVLLVDLNMqYG-GIETILNVDNpRNLYD----LVPVINE 206
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALAlakKGYK----VGLLDADI-YGpSIPRLLGVEG-KPLHQseegIVPVEVG 68
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
6-116 1.10e-03

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 38.38  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   6 KLLIVSEDPSQAE---DIVEQIgslyPQHHHI----EPDEVRKEIVRLQPDIVLLCER-KDGSGVQLLPYLSKEVPDAIT 77
Cdd:cd19925     2 NVLIVEDDPMVAEihrAYVEQV----PGFTVIgtagTGEEALKLLKERQPDLILLDIYlPDGNGLDLLRELRAAGHDVDV 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1223536500  78 IYLTNRRDPVRTRDVNRAGAFDILFLPDEINALEDVLNR 116
Cdd:cd19925    78 IVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
minD CHL00175
septum-site determining protein; Validated
141-345 1.49e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.14  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 141 KVIAFYSGKGGCGQSLVASTLAQTIGlDSSSSVLLVDLNMQYGGIETILNVDNpRNLYDLVPVIN---ELNDNHIRSvts 217
Cdd:CHL00175   16 RIIVITSGKGGVGKTTTTANLGMSIA-RLGYRVALIDADIGLRNLDLLLGLEN-RVLYTAMDVLEgecRLDQALIRD--- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500 218 vEEYSQIEVLSSPVDAETaENITEEHVERLIRTAR-LYYDYILIDLPTEMTPMTYTVLEEADHISYVMVPDMLSLRVLSN 296
Cdd:CHL00175   91 -KRWKNLSLLAISKNRQR-YNVTRKNMNMLVDSLKnRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADR 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1223536500 297 VLDLFSKLNIdptDRLHLLLNRVSRD----TELMP-KDVNRHFSFPVVASFRED 345
Cdd:CHL00175  169 VAGLLEANGI---YNVKLLVNRVRPDmiqaNDMMSvRDVQEMLGIPLLGAIPED 219
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
6-124 2.18e-03

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 39.41  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1223536500   6 KLLIVSEDPSQAEDIVEQIGSlYPQHHHIE----PDEVRKEIVRLQPDIVLL-CERKDGSGVQLLPYLSKEVPDAITIYL 80
Cdd:COG3279     3 KILIVDDEPLARERLERLLEK-YPDLEVVGeasnGEEALELLEEHKPDLVFLdIQMPGLDGFELARQLRELDPPPPIIFT 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1223536500  81 TNRRDP-VRTRDVNragAFDILFLPDEINALEDVLNRAVKALQTK 124
Cdd:COG3279    82 TAYDEYaLEAFEVN---AVDYLLKPIDEERLAKALEKAKERLEAK 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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