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Conserved domains on  [gi|86358433|ref|YP_470325|]
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methyl-accepting chemotaxis protein [Rhizobium etli CFN 42]

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List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
378-577 2.22e-52

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 180.12  E-value: 2.22e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 378 EQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQT 457
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 458 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEH 537
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86358433 538 VKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETN 577
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
219-257 3.32e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 36.07  E-value: 3.32e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 86358433 219 IRRGIGAVRQSMQRIMNGDLASDVPEkTRGDEIGEMARA 257
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARA 38
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
351-598 3.28e-69

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


:

Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 227.94  E-value: 3.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    351 DIAINSSSIEANSRQMRAAADDLAKRTEQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAM 430
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    431 AAMERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGK----- 505
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    506 ---------SGEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEET 576
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 86358433    577 NAASHTLAIDAENLTQLIKQFK 598
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
378-577 2.22e-52

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 180.12  E-value: 2.22e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 378 EQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQT 457
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 458 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEH 537
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86358433 538 VKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETN 577
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
219-257 3.32e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 36.07  E-value: 3.32e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 86358433 219 IRRGIGAVRQSMQRIMNGDLASDVPEkTRGDEIGEMARA 257
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARA 38
HAMP pfam00672
HAMP domain;
198-257 8.77e-04

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 37.98  E-value: 8.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   198 IGLGVLAILTMGVLQYVHGGSIRRGIGAVRQSMQRIMNGDLASDVPEKtRGDEIGEMARA 257
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVS-GPDEIGELARA 60
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
351-598 3.28e-69

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 227.94  E-value: 3.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    351 DIAINSSSIEANSRQMRAAADDLAKRTEQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAM 430
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    431 AAMERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGK----- 505
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    506 ---------SGEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEET 576
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 86358433    577 NAASHTLAIDAENLTQLIKQFK 598
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
225-599 8.76e-69

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 231.80  E-value: 8.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 225 AVRQSMQRIMNGDLASDVPE-KTRGDEIGEMARAADSFRLAAIEKRDLETQTETDRQRSDAEHRAREAAKLAD--AEALG 301
Cdd:COG0840   6 PLNLELIELAAGEADAGLLKlKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAIllLRAIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 302 AAVTALGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANSRQMRAAADDLAKRTEQQA 381
Cdd:COG0840  86 EPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 382 ASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGA-----------SREIGKIINVI 450
Cdd:COG0840 166 ESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsesSQEIEEITSVI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 451 DEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGK--------------SGEEVKIGGEL 516
Cdd:COG0840 246 NSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKL 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 517 VTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQ 596
Cdd:COG0840 326 VEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAK 405

                ...
gi 86358433 597 FKT 599
Cdd:COG0840 406 FKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
299-654 2.38e-63

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 220.98  E-value: 2.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  299 ALGAAVTALGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANSRQMRAAADDLAKRTE 378
Cdd:PRK15041 217 SLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTE 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  379 QQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQTN 458
Cdd:PRK15041 297 QQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTN 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  459 LLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEHV 538
Cdd:PRK15041 377 ILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIM 456
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  539 KSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQFKTgegMSARQTPREATAASHS 618
Cdd:PRK15041 457 GEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI---QQQQQQQRETSAVVKT 533
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 86358433  619 rPSPArnligkvagafnggAAAKVIASPAGDNWEEF 654
Cdd:PRK15041 534 -VTPA--------------TPRKMAVADSGENWETF 554
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
417-598 6.46e-46

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 162.23  E-value: 6.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   417 ENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAA 496
Cdd:pfam00015  16 DEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   497 KDIKTLIGKS--------------GEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQM 562
Cdd:pfam00015  96 KEIEALIEEIvkqtndstasiqqtRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARI 175
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 86358433   563 DQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQFK 598
Cdd:pfam00015 176 DQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
43-280 2.50e-05

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072) [Signal transduction, Two-component systems].


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 46.31  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    43 ASLRRAGDIQtsvnHIDDMRvanlTMVLAAMDIIVDKDDKVVEPTRIKLIGDSLAALTSGSKEMRLLADEMNDgnllksy 122
Cdd:TIGR02956 218 DDTKTSQDLA----HINQLD----EEFNRLVMILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQI------- 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   123 DADVAAMGKAIQTDLVALVQQgapdaefdkIDDAIDGAGDELTATLDKLAadgtifaqqhvelaNAVSREALILqIGLGV 202
Cdd:TIGR02956 283 LQKQQRLQQANLEQFTQLNTT---------VSQLVNAQNQRTEAAVSDLL--------------MTLSVAQFGL-LITGM 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   203 LAILTMG--VLQYVHGGSIRRgIGAVRQSMQRIMNGDLasDVPEKTRGD-EIGEMARAADSFRLAAIEKRDLETQTETDR 279
Cdd:TIGR02956 339 LGLVILVfiMWRVVYRSVILR-LNQHTQALLRLALGDL--DISLDARGDdELAHMGRAIEAFRDTAAHNLKLQADERQVA 415

                  .
gi 86358433   280 Q 280
Cdd:TIGR02956 416 Q 416
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
297-352 1.02e-04

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 43.85  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86358433  297 AEALGAAVTALGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKA-------MSDI 352
Cdd:PRK10549 185 ARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTLEKNeqmrrdfMADI 247
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
288-536 2.59e-04

TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length [Hypothetical proteins, Conserved].


Pssm-ID: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 42.87  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    288 AREAAKLADAEALGAAVTALGAGLTRLsagdvtvtidqpfRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANS--RQ 365
Cdd:TIGR02680  735 ARERARLRRIAELDARLAAVDDELAEL-------------ARELRALGARQRALADELAGAPSDRSLRAAHRRAAEaeRQ 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    366 MRAAADDLAKRTEQQAASLEETSAALDQITATVRNAT-----NRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGAS 440
Cdd:TIGR02680  802 AESAERELARAARKAAAAAAAWKQARRELERDAADLDlptdpDALEAVGLALKRFGDHLHTLEVAVRELRHAATRAAEQR 881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    441 REIGKIINVIDEIAFQTNllalNAGVEAARAGEAGKGF-AVVAQEVRELAGRAAgaakDIKTLIGKSGEEVKIGGELVTA 519
Cdd:TIGR02680  882 ARAARAESDAREAAEDAA----EARAEAEEASLRLRTLeESVGAMVDEIRARLA----ETRAALASGGRELPRLAEALAT 953
                          250
                   ....*....|....*..
gi 86358433    520 AGEALRQIGEDVLRIDE 536
Cdd:TIGR02680  954 AEEARGRAEEKRAEADA 970
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
378-577 2.22e-52

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 180.12  E-value: 2.22e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 378 EQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQT 457
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 458 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEH 537
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86358433 538 VKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETN 577
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
219-257 3.32e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 36.07  E-value: 3.32e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 86358433 219 IRRGIGAVRQSMQRIMNGDLASDVPEkTRGDEIGEMARA 257
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPV-TGRDEIGELARA 38
HAMP pfam00672
HAMP domain;
198-257 8.77e-04

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 37.98  E-value: 8.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   198 IGLGVLAILTMGVLQYVHGGSIRRGIGAVRQSMQRIMNGDLASDVPEKtRGDEIGEMARA 257
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVS-GPDEIGELARA 60
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
351-598 3.28e-69

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 227.94  E-value: 3.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    351 DIAINSSSIEANSRQMRAAADDLAKRTEQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAM 430
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    431 AAMERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGK----- 505
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    506 ---------SGEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEET 576
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 86358433    577 NAASHTLAIDAENLTQLIKQFK 598
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
225-599 8.76e-69

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 231.80  E-value: 8.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 225 AVRQSMQRIMNGDLASDVPE-KTRGDEIGEMARAADSFRLAAIEKRDLETQTETDRQRSDAEHRAREAAKLAD--AEALG 301
Cdd:COG0840   6 PLNLELIELAAGEADAGLLKlKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAIllLRAIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 302 AAVTALGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANSRQMRAAADDLAKRTEQQA 381
Cdd:COG0840  86 EPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 382 ASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGA-----------SREIGKIINVI 450
Cdd:COG0840 166 ESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEElaevvkklsesSQEIEEITSVI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 451 DEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGK--------------SGEEVKIGGEL 516
Cdd:COG0840 246 NSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEiqneaadavehmeeSASEVSEGVKL 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433 517 VTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQ 596
Cdd:COG0840 326 VEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAK 405

                ...
gi 86358433 597 FKT 599
Cdd:COG0840 406 FKL 408
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
299-654 2.38e-63

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 220.98  E-value: 2.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  299 ALGAAVTALGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANSRQMRAAADDLAKRTE 378
Cdd:PRK15041 217 SLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTE 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  379 QQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQTN 458
Cdd:PRK15041 297 QQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTN 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  459 LLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEHV 538
Cdd:PRK15041 377 ILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIM 456
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  539 KSIVTSAREQSVGLNEINTSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQFKTgegMSARQTPREATAASHS 618
Cdd:PRK15041 457 GEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI---QQQQQQQRETSAVVKT 533
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 86358433  619 rPSPArnligkvagafnggAAAKVIASPAGDNWEEF 654
Cdd:PRK15041 534 -VTPA--------------TPRKMAVADSGENWETF 554
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
314-627 4.07e-63

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 220.26  E-value: 4.07e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  314 LSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANSRQMRAAADDLAKRTEQQAASLEETSAALDQ 393
Cdd:PRK15048 230 IAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQ 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  394 ITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGE 473
Cdd:PRK15048 310 LTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGE 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  474 AGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLN 553
Cdd:PRK15048 390 QGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGID 469
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86358433  554 EINTSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQFKTGEGMSARQTPREATAASHSRPSPARNLI 627
Cdd:PRK15048 470 QVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPPAQPRLRI 543
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
307-607 7.17e-59

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 208.00  E-value: 7.17e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  307 LGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANSRQMRAAADDLAKRTEQQAASLEE 386
Cdd:PRK09793 221 IGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQ 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  387 TSAALDQITATVRNATNRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQTNLLALNAGV 466
Cdd:PRK09793 301 TAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAV 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  467 EAARAGEAGKGFAVVAQEVRELAGRAAGAAKDIKTLIGKSGEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAR 546
Cdd:PRK09793 381 EAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASE 460
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86358433  547 EQSVGLNEINTSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQFKTGEGMSARQ 607
Cdd:PRK09793 461 EQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARH 521
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
417-598 6.46e-46

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 162.23  E-value: 6.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   417 ENTAKSDIVVGDAMAAMERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAGRAAGAA 496
Cdd:pfam00015  16 DEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   497 KDIKTLIGKS--------------GEEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEINTSISQM 562
Cdd:pfam00015  96 KEIEALIEEIvkqtndstasiqqtRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARI 175
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 86358433   563 DQVTQKNAAMVEETNAASHTLAIDAENLTQLIKQFK 598
Cdd:pfam00015 176 DQVTQQNAALVEESAAAAETLEEQAEELTASVAQFR 211
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
43-280 2.50e-05

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072) [Signal transduction, Two-component systems].


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 46.31  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    43 ASLRRAGDIQtsvnHIDDMRvanlTMVLAAMDIIVDKDDKVVEPTRIKLIGDSLAALTSGSKEMRLLADEMNDgnllksy 122
Cdd:TIGR02956 218 DDTKTSQDLA----HINQLD----EEFNRLVMILSRRVQSIEDPTRSNQLKDLLVTLNKTPKLFKLLRQLSQI------- 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   123 DADVAAMGKAIQTDLVALVQQgapdaefdkIDDAIDGAGDELTATLDKLAadgtifaqqhvelaNAVSREALILqIGLGV 202
Cdd:TIGR02956 283 LQKQQRLQQANLEQFTQLNTT---------VSQLVNAQNQRTEAAVSDLL--------------MTLSVAQFGL-LITGM 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   203 LAILTMG--VLQYVHGGSIRRgIGAVRQSMQRIMNGDLasDVPEKTRGD-EIGEMARAADSFRLAAIEKRDLETQTETDR 279
Cdd:TIGR02956 339 LGLVILVfiMWRVVYRSVILR-LNQHTQALLRLALGDL--DISLDARGDdELAHMGRAIEAFRDTAAHNLKLQADERQVA 415

                  .
gi 86358433   280 Q 280
Cdd:TIGR02956 416 Q 416
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
297-352 1.02e-04

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 43.85  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86358433  297 AEALGAAVTALGAGLTRLSAGDVTVTIDQPFRDELERLRLDFNQTTATLRKA-------MSDI 352
Cdd:PRK10549 185 ARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTLEKNeqmrrdfMADI 247
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
288-536 2.59e-04

TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length [Hypothetical proteins, Conserved].


Pssm-ID: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 42.87  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    288 AREAAKLADAEALGAAVTALGAGLTRLsagdvtvtidqpfRDELERLRLDFNQTTATLRKAMSDIAINSSSIEANS--RQ 365
Cdd:TIGR02680  735 ARERARLRRIAELDARLAAVDDELAEL-------------ARELRALGARQRALADELAGAPSDRSLRAAHRRAAEaeRQ 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    366 MRAAADDLAKRTEQQAASLEETSAALDQITATVRNAT-----NRAEEVGHMVSHTRENTAKSDIVVGDAMAAMERIEGAS 440
Cdd:TIGR02680  802 AESAERELARAARKAAAAAAAWKQARRELERDAADLDlptdpDALEAVGLALKRFGDHLHTLEVAVRELRHAATRAAEQR 881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    441 REIGKIINVIDEIAFQTNllalNAGVEAARAGEAGKGF-AVVAQEVRELAGRAAgaakDIKTLIGKSGEEVKIGGELVTA 519
Cdd:TIGR02680  882 ARAARAESDAREAAEDAA----EARAEAEEASLRLRTLeESVGAMVDEIRARLA----ETRAALASGGRELPRLAEALAT 953
                          250
                   ....*....|....*..
gi 86358433    520 AGEALRQIGEDVLRIDE 536
Cdd:TIGR02680  954 AEEARGRAEEKRAEADA 970
EspB pfam05802
Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of ...
347-470 6.56e-03

Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of enteropathogenic Escherichia coli (EPEC) which is essential for EPEC pathogenesis. EspB is also found in Citrobacter rodentium.


Pssm-ID: 114524 [Multi-domain]  Cd Length: 317  Bit Score: 37.74  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433   347 KAMSDIAINSSSieANSRQMRAAAD----DLAKRTEQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHTREntaKS 422
Cdd:pfam05802 124 KGASDIAQKATS--ASSKAVNAASEvatkALVKATESVADAAEEASSTMQQAMATATKAASRTSGVADDVATSAQ---KA 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 86358433   423 DIVVGDAMAAMERiegASReIGKIINVIDEIAFQTNLLALNAGVEAAR 470
Cdd:pfam05802 199 SQVAEEAADAAQK---ASR-LSRFTAAVDKITGSTAFVAVTSLAEGTK 242
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
256-439 8.69e-03

TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length [Hypothetical proteins, Conserved].


Pssm-ID: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 37.87  E-value: 8.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    256 RAADSFRLAAIEKRDLETQTETDRQRSDAEHRAREAAKLADAEALGAAVTAlgagltrlsagdvtvtidqpfRDELERLR 335
Cdd:TIGR02680  858 DHLHTLEVAVRELRHAATRAAEQRARAARAESDAREAAEDAAEARAEAEEA---------------------SLRLRTLE 916
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    336 LDFNQTTATLRKAMSDIAinsSSIEANSRQMRAAADDLAkRTEQQAASLEETSAALDQITATVRNATNRAEEVGHMVSHT 415
Cdd:TIGR02680  917 ESVGAMVDEIRARLAETR---AALASGGRELPRLAEALA-TAEEARGRAEEKRAEADATLDERAEARDHAIGQLREFALT 992
                          170       180
                   ....*....|....*....|....
gi 86358433    416 RENTAKSDIVVGDAMAAMERIEGA 439
Cdd:TIGR02680  993 GLLEDALPDTEVPELDAKWTIEAA 1016
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
328-592 8.94e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 37.73  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    328 RDELERLRLDFNQTTATLRKAmsDIAINSSSIEAnsRQMRAAADDLAKRTEQQAASLEETSAALDQITATVRNATNRAEE 407
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAEL--EKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    408 VGHMVSHTRENTAKSDIVVGDAMAAM-----------ERIEGASREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGK 476
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELaeaeaeieeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433    477 GFAVVAQEVRELAGRAAGAAKDIKTLIGksgeEVKIGGELVTAAGEALRQIGEDVLRIDEHVKSIVTSAREQSVGLNEIN 556
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 86358433    557 TSISQMDQVTQKNAAMVEETNAASHTLAIDAENLTQ 592
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
253-496 9.79e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 37.62  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  253 EMARAADSFRLAAIEKRDLEtqtetdrqRSDAEHRAREAAKLADAEALGAAVTALGAGLTRLSAGDVTVTIDQPFRDELE 332
Cdd:PRK05035 449 EEAKARFEARQARLEREKAA--------REARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVI 520
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  333 RLRldfnQTTATLRKAMSDIAINSSSIEANSRQMRAA-ADDLAKRTEQQAASLEETSAALD---QITATVRNATNRAEEV 408
Cdd:PRK05035 521 AAR----EARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAAQQAANAEAEEEVDPkkaAVAAAIARAKAKKAAQ 596
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86358433  409 GHMVSHTRENTAKSDIVVGDAMAAMERIEGasREIGKIINVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVREL 488
Cdd:PRK05035 597 QAASAEPEEQVAEVDPKKAAVAAAIARAKA--KKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAED 674

                 ....*...
gi 86358433  489 AGRAAGAA 496
Cdd:PRK05035 675 PKKAAVAA 682
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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