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Conserved domains on  [gi|30018612|ref|NP_830243|]
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methyl-accepting chemotaxis protein [Bacillus cereus ATCC 14579]

Protein Classification

methyl-accepting chemotaxis protein (domain architecture ID 11435591)

methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
15-415 7.31e-51

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


:

Pssm-ID: 223910  Cd Length: 408  Bit Score: 179.42  E-value: 7.31e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  15 QLMLFTTVLAFITYSTSIFFIYVIYDYFQSYVSQTVYNIIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIR 94
Cdd:COG0840  25 KLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  95 EDVPLPKtDDEIKSLSVAFNMMLGNLRGMVKNIDTTFSYTNNQVQQIrkqtgeatrqaqgvSETLAEISSGAEQSAASIQ 174
Cdd:COG0840 105 KRIDESS-NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEI--------------AASATELSARADQQAESLE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 175 AIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGHSTRVFTSLIQGIQTLAKENEdsmQNVQKLEERMKQVEHIVSVVS 254
Cdd:COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLSESSQEIEEITSVIN 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 255 AIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEEAKRG 334
Cdd:COG0840 247 SIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLV 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 335 EATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSAGSQEVARVTLQQSKNMIVIDQLLKDL 414
Cdd:COG0840 327 EETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKF 406

                .
gi 30018612 415 E 415
Cdd:COG0840 407 K 407
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
15-415 7.31e-51

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 179.42  E-value: 7.31e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  15 QLMLFTTVLAFITYSTSIFFIYVIYDYFQSYVSQTVYNIIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIR 94
Cdd:COG0840  25 KLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  95 EDVPLPKtDDEIKSLSVAFNMMLGNLRGMVKNIDTTFSYTNNQVQQIrkqtgeatrqaqgvSETLAEISSGAEQSAASIQ 174
Cdd:COG0840 105 KRIDESS-NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEI--------------AASATELSARADQQAESLE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 175 AIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGHSTRVFTSLIQGIQTLAKENEdsmQNVQKLEERMKQVEHIVSVVS 254
Cdd:COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLSESSQEIEEITSVIN 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 255 AIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEEAKRG 334
Cdd:COG0840 247 SIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLV 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 335 EATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSAGSQEVARVTLQQSKNMIVIDQLLKDL 414
Cdd:COG0840 327 EETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKF 406

                .
gi 30018612 415 E 415
Cdd:COG0840 407 K 407
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
149-429 2.23e-48

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  Cd Length: 262  Bit Score: 168.62  E-value: 2.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    149 TRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGhstrvftSLIQGIQTLAKE 228
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVE-------DAITAMDQIREV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    229 NEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRN 308
Cdd:smart00283  76 VEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    309 MQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSA 388
Cdd:smart00283 156 IQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAA 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 30018612    389 GSQEVARVTlqqsknmividqllKDLEKQATDLKQTIERFS 429
Cdd:smart00283 236 MSEEISAAA--------------EELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
167-394 4.66e-39

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: 141.22  E-value: 4.66e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 167 EQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEAlghstrvftsliqgIQTLAKENEDSMQNVQKLEERMKQV 246
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQ--------------MNQIDESVDEAVSAVEELEESSAEI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 247 EHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKI 326
Cdd:cd11386  67 GEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEE 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30018612 327 AKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQvshihqtgaqtkavAAIAEETSAGSQEVA 394
Cdd:cd11386 147 VEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ--------------SASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
226-428 2.92e-32

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: 278444  Cd Length: 207  Bit Score: 122.56  E-value: 2.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   226 AKENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQL 305
Cdd:pfam00015  19 GQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEAL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   306 LRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEE 385
Cdd:pfam00015  99 IEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQ 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 30018612   386 TSAGSQEVARVTLQqsknmividqllkdLEKQATDLKQTIERF 428
Cdd:pfam00015 179 NAALVEESAAAAET--------------LEEQAEELTASVAQF 207
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
53-428 5.08e-26

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 110.04  E-value: 5.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   53 IIVMLLGVVWSGILA--YGAAVFLIKPLRKLEEAARKAAEGDIredvplpktddeIKSLSVAFNMMLGNLRGMVKNIDTT 130
Cdd:PRK15041 195 ILVGVMIVVLAVIFAvwFGIKASLVAPMNRLIDSIRHIAGGDL------------VKPIEVDGSNEMGQLAESLRHMQGE 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  131 FSYTnnqVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGH 210
Cdd:PRK15041 263 LMRT---VGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQR 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  211 STRVFTSLIQGIQTLAKENEdsmqnvqkleermkQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRK 290
Cdd:PRK15041 340 GGKVVDNVVQTMRDISTSSQ--------------KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRN 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  291 LADESDHSARNISQLLrnmQDEVQQVAMKMTeQVKIAKEeakrgeatelILKEMSSSVMEVADATQQISSYMNEQVSHIH 370
Cdd:PRK15041 406 LAQRSAQAAREIKSLI---EDSVGKVDVGST-LVESAGE----------TMAEIVSAVTRVTDIMGEIASASDEQSRGID 471
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30018612  371 QTGAqtkAVAaiaeetsagsqEVARVTLQQSKNMIVIDQLLKDLEKQATDLKQTIERF 428
Cdd:PRK15041 472 QVGL---AVA-----------EMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
35-120 1.16e-04

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593  Cd Length: 457  Bit Score: 43.92  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    35 IYVIYD--YFQSYVSQTVYNIIV-MLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLPKTDDEIKSLSV 111
Cdd:TIGR01386 146 ITVALDinAHTHLLDALRKWLILiAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPESLDQRLDPSRAPAELRELAQ 225

                  ....*....
gi 30018612   112 AFNMMLGNL 120
Cdd:TIGR01386 226 SFNAMLGRL 234
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
15-415 7.31e-51

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910  Cd Length: 408  Bit Score: 179.42  E-value: 7.31e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  15 QLMLFTTVLAFITYSTSIFFIYVIYDYFQSYVSQTVYNIIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIR 94
Cdd:COG0840  25 KLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  95 EDVPLPKtDDEIKSLSVAFNMMLGNLRGMVKNIDTTFSYTNNQVQQIrkqtgeatrqaqgvSETLAEISSGAEQSAASIQ 174
Cdd:COG0840 105 KRIDESS-NDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEI--------------AASATELSARADQQAESLE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 175 AIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGHSTRVFTSLIQGIQTLAKENEdsmQNVQKLEERMKQVEHIVSVVS 254
Cdd:COG0840 170 EVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELA---EVVKKLSESSQEIEEITSVIN 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 255 AIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEEAKRG 334
Cdd:COG0840 247 SIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLV 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 335 EATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSAGSQEVARVTLQQSKNMIVIDQLLKDL 414
Cdd:COG0840 327 EETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKF 406

                .
gi 30018612 415 E 415
Cdd:COG0840 407 K 407
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
149-429 2.23e-48

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  Cd Length: 262  Bit Score: 168.62  E-value: 2.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    149 TRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGhstrvftSLIQGIQTLAKE 228
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVE-------DAITAMDQIREV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    229 NEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRN 308
Cdd:smart00283  76 VEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    309 MQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSA 388
Cdd:smart00283 156 IQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAA 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 30018612    389 GSQEVARVTlqqsknmividqllKDLEKQATDLKQTIERFS 429
Cdd:smart00283 236 MSEEISAAA--------------EELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
167-394 4.66e-39

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: 141.22  E-value: 4.66e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 167 EQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEAlghstrvftsliqgIQTLAKENEDSMQNVQKLEERMKQV 246
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQ--------------MNQIDESVDEAVSAVEELEESSAEI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612 247 EHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKI 326
Cdd:cd11386  67 GEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEE 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30018612 327 AKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQvshihqtgaqtkavAAIAEETSAGSQEVA 394
Cdd:cd11386 147 VEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ--------------SASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
226-428 2.92e-32

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: 278444  Cd Length: 207  Bit Score: 122.56  E-value: 2.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   226 AKENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQL 305
Cdd:pfam00015  19 GQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEAL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   306 LRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEE 385
Cdd:pfam00015  99 IEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQ 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 30018612   386 TSAGSQEVARVTLQqsknmividqllkdLEKQATDLKQTIERF 428
Cdd:pfam00015 179 NAALVEESAAAAET--------------LEEQAEELTASVAQF 207
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
53-428 5.08e-26

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 110.04  E-value: 5.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   53 IIVMLLGVVWSGILA--YGAAVFLIKPLRKLEEAARKAAEGDIredvplpktddeIKSLSVAFNMMLGNLRGMVKNIDTT 130
Cdd:PRK15041 195 ILVGVMIVVLAVIFAvwFGIKASLVAPMNRLIDSIRHIAGGDL------------VKPIEVDGSNEMGQLAESLRHMQGE 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  131 FSYTnnqVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGH 210
Cdd:PRK15041 263 LMRT---VGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQR 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  211 STRVFTSLIQGIQTLAKENEdsmqnvqkleermkQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRK 290
Cdd:PRK15041 340 GGKVVDNVVQTMRDISTSSQ--------------KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRN 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  291 LADESDHSARNISQLLrnmQDEVQQVAMKMTeQVKIAKEeakrgeatelILKEMSSSVMEVADATQQISSYMNEQVSHIH 370
Cdd:PRK15041 406 LAQRSAQAAREIKSLI---EDSVGKVDVGST-LVESAGE----------TMAEIVSAVTRVTDIMGEIASASDEQSRGID 471
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30018612  371 QTGAqtkAVAaiaeetsagsqEVARVTLQQSKNMIVIDQLLKDLEKQATDLKQTIERF 428
Cdd:PRK15041 472 QVGL---AVA-----------EMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
53-430 3.86e-24

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 104.70  E-value: 3.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   53 IIVMLLGVVWsgilaYGAAVFLIKPLRKLEEAARKAAEGDIredvplpktddeIKSLSVAFNMMLGNLRGMVKNIDTTFS 132
Cdd:PRK15048 200 VVVLILLVAW-----YGIRRMLLTPLAKIIAHIREIAGGNL------------ANTLTIDGRSEMGDLAQSVSHMQRSLT 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  133 YTnnqVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVEALGHST 212
Cdd:PRK15048 263 DT---VTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGG 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  213 RVFTSLIQGIQTLAKENedsmqnvqkleermKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLA 292
Cdd:PRK15048 340 KVVDGVVKTMHEIADSS--------------KKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLA 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  293 DESDHSARNISQLLrnmQDEVQQVAmkmTEQVKIakeeakrgEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQT 372
Cdd:PRK15048 406 SRSAQAAKEIKALI---EDSVSRVD---TGSVLV--------ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQV 471
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30018612  373 GAQTKAVAAIAEETSAGSQEVARVTLQqsknmividqllkdLEKQATDLKQTIERFSM 430
Cdd:PRK15048 472 ALAVSEMDRVTQQNASLVQESAAAAAA--------------LEEQASRLTQAVSAFRL 515
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
44-394 2.51e-22

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 98.99  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   44 SYVSQTVYNIIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGM 123
Cdd:PRK09793 184 NYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAV-YGRNEITAIFASLKTMQQALRGT 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  124 VKNIdttfsytnnqvqqirKQTGEATRQaqGVSETLA---EISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTL 200
Cdd:PRK09793 263 VSDV---------------RKGSQEMHI--GIAEIVAgnnDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASEL 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  201 SSEMVEalghstrvfTSLIQGIQtlAKENEDSMQNVQKLEERmkqVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRG 280
Cdd:PRK09793 326 AKNAAT---------TAQAGGVQ--VSTMTHTMQEIATSSQK---IGDIISVIDGIAFQTNILALNAAVEAARAGEQGRG 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  281 FAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAmkmteqvKIAKEEAKrgeatelILKEMSSSVMEVADATQQISS 360
Cdd:PRK09793 392 FAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGS-------KLVNNAAA-------TMTDIVSSVTRVNDIMGEIAS 457
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 30018612  361 YMNEQVSHIHQTGAQ-------TKAVAAIAEETSAGSQEVA 394
Cdd:PRK09793 458 ASEEQRRGIEQVAQAvsqmdqvTQQNASLVEEAAVATEQLA 498
HAMP pfam00672
HAMP domain;
53-121 8.88e-11

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 58.74  E-value: 8.88e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30018612    53 IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIreDVPLPKTDDEIKSLSVAFNMMLGNLR 121
Cdd:pfam00672   2 LLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDL--DVPLESGRDEIGELARAFNQMAERLR 68
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
57-121 9.14e-10

Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 227333  Cd Length: 712  Bit Score: 60.55  E-value: 9.14e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30018612  57 LLGVVWSGILAygaAVFLIKPLRKLEEAARKAAEGDIREDVPLPKTDDEIKSLSVAFNMMLGNLR 121
Cdd:COG5000 291 LLAAIWTAIAF---ARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKAFNKMTEQLS 352
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
74-121 9.35e-08

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: 49.94  E-value: 9.35e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 30018612  74 LIKPLRKLEEAARKAAEGDIREDVPlPKTDDEIKSLSVAFNMMLGNLR 121
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLP-VTGRDEIGELARAFNQMAERLR 47
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
74-124 2.35e-07

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640  Cd Length: 53  Bit Score: 48.78  E-value: 2.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 30018612     74 LIKPLRKLEEAARKAAEGDIREDVPlPKTDDEIKSLSVAFNMMLGNLRGMV 124
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGDLTVRLP-VDGRDEIGELARAFNEMADRLEETI 52
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
35-120 1.16e-04

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593  Cd Length: 457  Bit Score: 43.92  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    35 IYVIYD--YFQSYVSQTVYNIIV-MLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLPKTDDEIKSLSV 111
Cdd:TIGR01386 146 ITVALDinAHTHLLDALRKWLILiAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPESLDQRLDPSRAPAELRELAQ 225

                  ....*....
gi 30018612   112 AFNMMLGNL 120
Cdd:TIGR01386 226 SFNAMLGRL 234
PTZ00121 PTZ00121
MAEBL; Provisional
73-426 1.64e-03

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 40.89  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    73 FLIKPLRKLEEAARKAAEGDIREDVPLPKtdDEIKSLSVAFNMMLGNLRGMVKnidttfSYTNNQVQQIRKQTG-EATRQ 151
Cdd:PTZ00121 1024 FNIEKIEELTEYGNNDDVLKEKDIIDEDI--DGNHEGKAEAKAHVGQDEGLKP------SYKDFDFDAKEDNRAdEATEE 1095
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   152 AQGVSETLAEISSG-AEQSAASIQAIVSAVDtttsiASEVEEKAKQSDTLSSEMVEALGHSTRVftsliqgiqTLAKENE 230
Cdd:PTZ00121 1096 AFGKAEEAKKTETGkAEEARKAEEAKKKAED-----ARKAEEARKAEDARKAEEARKAEDAKRV---------EIARKAE 1161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   231 DSmqnvQKLEERMKQVEhivsvvsaiasqtnllalNASIEAARAGEHGRGfavvAEEVRKLAD----ESDHSARNISQL- 305
Cdd:PTZ00121 1162 DA----RKAEEARKAED------------------AKKAEAARKAEEVRK----AEELRKAEDarkaEAARKAEEERKAe 1215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612   306 -LRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATElilkemsssvmevadATQQISSYMNEQVSHIHQTGAQTKAVAAIAE 384
Cdd:PTZ00121 1216 eARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER---------------NNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 30018612   385 ETSAGSQEVARV-TLQQSKNMIVIDQLLKDLE--KQATDLKQTIE 426
Cdd:PTZ00121 1281 DELKKAEEKKKAdEAKKAEEKKKADEAKKKAEeaKKADEAKKKAE 1325
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
57-116 2.20e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 37.36  E-value: 2.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612  57 LLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLPKTdDEIKSLSVAFNMM 116
Cdd:COG2770  13 LALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPML-DEIGELAKAFNRM 71
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
231-427 2.41e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 314924  Cd Length: 1201  Bit Score: 40.07  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    231 DSMQNVQKLEERMKQVE-HIVSVVSAIASQ-TNLLALNASIEAARAGE--HGRGFAVVAEEVRKLADESDHSARNISQLL 306
Cdd:pfam12128  598 DYAASEEELRARLQVAEeALQSARAKQKQAeEQLVQANAELEEAQRAEteARTALKNARLTLGRLQNEQQSLKDKLELAI 677
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018612    307 RNMQDEVQQVAMKMTEQVKIAKEEAKrgEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQT--GAQTKAVAAIAE 384
Cdd:pfam12128  678 AERKQQAETQLRQLDAQLKQLLEQQK--AMLEALKDDFRELRTERKAKWQVVEGELDNQLALLKAAieAARTQAKARLKA 755
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 30018612    385 ETSAGSQEVarvtlqqsKNMIVIDQLLKDLEKQATDLKQTIER 427
Cdd:pfam12128  756 LKEAYDREL--------ASLGVDPETVKELKRKIEELERTIER 790
PRK10604 PRK10604
sensor protein RstB; Provisional
66-124 4.89e-03

sensor protein RstB; Provisional


Pssm-ID: 236724  Cd Length: 433  Bit Score: 38.82  E-value: 4.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30018612   66 LAYGAAVFL-IKP----LRKLEEAARKAAEGDIREDVPLPKTdDEIKSLSVAFNMMLGNLRGMV 124
Cdd:PRK10604 147 LSLAFPVFLwMRPhwqdMLKLEAAAQRLGDGHLAERIHFDEG-SSLERLGVAFNQMADNINALI 209
envZ PRK09467
osmolarity sensor protein; Provisional
49-116 5.54e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531  Cd Length: 435  Bit Score: 38.74  E-value: 5.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30018612   49 TVYNIIVMLLGVVwsgilayGAAVF---LIKPLRKLEEAARKAAEGDIREdvPLP-KTDDEIKSLSVAFNMM 116
Cdd:PRK09467 156 FRYTLAIGLLSVA-------GGWLFiriQNRPLVALEHAALQVGKGEIPP--PLReYGASEVRSVTRAFNQM 218
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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