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Conserved domains on  [gi|966195281|gb|KTF17767|]
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chemotaxis protein [Pseudoalteromonas sp. H103]

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

CATH:  1.10.287.950
Gene Ontology:  GO:0006935
PubMed:  18165013|20738376
SCOP:  4003862

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
53-555 1.34e-91

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 290.77  E-value: 1.34e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  53 QTLLRTEIEIASKVVRYQLANGSQEDAKKALRDLTFGQGGYFFIYDTNGVSVFHALLGDAIEGQNKIGMTDPNGKKIIVG 132
Cdd:COG0840   33 LALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAAL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 133 LLEQARKGGGAFNYHFQKPGTAGLIEKMGYAAMIPGTNWMIGTGEYMDDIDAELAKYRNTMTQHMNDKVTTLLLIALFWL 212
Cdd:COG0840  113 LALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 213 VLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHGIIVNVVDVTHDVKTASG 292
Cdd:COG0840  193 ALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 293 DINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAA 372
Cdd:COG0840  271 ELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETA 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 373 EQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLV 452
Cdd:COG0840  351 ETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSET 430

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 453 SAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTT 532
Cdd:COG0840  431 EEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEV 510

                        490       500
                 ....*....|....*....|...
gi 966195281 533 SSVGLHLAGRGENLGQLVGQFKI 555
Cdd:COG0840  511 AAAAEELAELAEELQELVSRFKL 533
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
53-555 1.34e-91

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 290.77  E-value: 1.34e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  53 QTLLRTEIEIASKVVRYQLANGSQEDAKKALRDLTFGQGGYFFIYDTNGVSVFHALLGDAIEGQNKIGMTDPNGKKIIVG 132
Cdd:COG0840   33 LALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAAL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 133 LLEQARKGGGAFNYHFQKPGTAGLIEKMGYAAMIPGTNWMIGTGEYMDDIDAELAKYRNTMTQHMNDKVTTLLLIALFWL 212
Cdd:COG0840  113 LALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 213 VLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHGIIVNVVDVTHDVKTASG 292
Cdd:COG0840  193 ALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 293 DINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAA 372
Cdd:COG0840  271 ELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETA 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 373 EQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLV 452
Cdd:COG0840  351 ETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSET 430

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 453 SAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTT 532
Cdd:COG0840  431 EEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEV 510

                        490       500
                 ....*....|....*....|...
gi 966195281 533 SSVGLHLAGRGENLGQLVGQFKI 555
Cdd:COG0840  511 AAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 293-554 8.95e-62

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: 204.06  E-value: 8.95e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   293 DINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAA 372
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   373 EQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLV 452
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   453 SAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTT 532
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 966195281   533 SSVGLHLAGRGENLGQLVGQFK 554
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 320-515 5.93e-53

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 [Multi-domain]  Cd Length: 200  Bit Score: 178.58  E-value: 5.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 320 TEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAAEQVDSLSDQSKKINSVLSVIGGIAEQT 399
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 400 NLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLVSAAVEAMQASQQSCNRSVESSRAISES 479
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 966195281 480 LGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNV 515
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 367-522 2.92e-36

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: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 132.94  E-value: 2.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  367 EINVAAEQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLS 446
Cdd:pfam00015  17 EVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALII 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966195281  447 ELHNLVSAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIV 522
Cdd:pfam00015  97 EIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQVT 172
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
177-555 4.08e-35

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 138.93  E-value: 4.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 177 EYMDDIDA--ELAKYRNTMTQHMNDKVTTLLLIALfwLVLTIACALIAANTMVKPIQRMVQSLDDIAKGegDLTKRLDID 254
Cdd:PRK15041 169 AYMEQNDRlyDIAVSDNNASYSQAMWILVGVMIVV--LAVIFAVWFGIKASLVAPMNRLIDSIRHIAGG--DLVKPIEVD 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 255 TNDEIGQLGEAFNMFVSKLHGIIVNVVDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTT 334
Cdd:PRK15041 245 GSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENAR 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 335 QVAESTQAATQEVAKAQECVDislsevshlmgeiNVAAEQVDsLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAG 414
Cdd:PRK15041 325 QASHLALSASETAQRGGKVVD-------------NVVQTMRD-ISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAG 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 415 EQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLVSAAveamqasqqscNRSVESSraiSESLGAVTSSVRSINDMS 494
Cdd:PRK15041 391 EQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVG-----------STLVESA---GETMAEIVSAVTRVTDIM 456

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966195281 495 TQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTTSSVGLHLAGRGENLGQLVGQFKI 555
Cdd:PRK15041 457 GEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
53-555 1.34e-91

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 290.77  E-value: 1.34e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  53 QTLLRTEIEIASKVVRYQLANGSQEDAKKALRDLTFGQGGYFFIYDTNGVSVFHALLGDAIEGQNKIGMTDPNGKKIIVG 132
Cdd:COG0840   33 LALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAAL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 133 LLEQARKGGGAFNYHFQKPGTAGLIEKMGYAAMIPGTNWMIGTGEYMDDIDAELAKYRNTMTQHMNDKVTTLLLIALFWL 212
Cdd:COG0840  113 LALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 213 VLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHGIIVNVVDVTHDVKTASG 292
Cdd:COG0840  193 ALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 293 DINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAA 372
Cdd:COG0840  271 ELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETA 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 373 EQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLV 452
Cdd:COG0840  351 ETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSET 430

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 453 SAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTT 532
Cdd:COG0840  431 EEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEV 510

                        490       500
                 ....*....|....*....|...
gi 966195281 533 SSVGLHLAGRGENLGQLVGQFKI 555
Cdd:COG0840  511 AAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 293-554 8.95e-62

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: 204.06  E-value: 8.95e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   293 DINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAA 372
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   373 EQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLV 452
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   453 SAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTT 532
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 966195281   533 SSVGLHLAGRGENLGQLVGQFK 554
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 320-515 5.93e-53

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 [Multi-domain]  Cd Length: 200  Bit Score: 178.58  E-value: 5.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 320 TEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAAEQVDSLSDQSKKINSVLSVIGGIAEQT 399
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 400 NLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLVSAAVEAMQASQQSCNRSVESSRAISES 479
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 966195281 480 LGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNV 515
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms];
43-529 6.18e-37

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 443621 [Multi-domain]  Cd Length: 510  Bit Score: 143.63  E-value: 6.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  43 AFKTKLISDKQTLLRTEIEIASKVVRYQLANGS------QEDAKKALRDLTFGQGGYFFIYDTNGVSVFHALLGDaIEGQ 116
Cdd:COG4564   21 TLRQALLEERKAELRALVELAVSIIAALYAAGElseeeaKEQALAALRALRFGGDGYFFVYDYDGTMLAHPINPE-LVGK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 117 NKIGMTDPNGKKIIVGLLEQARKGGGAF-NYHFQKPGTAGLIEKMGYAAMIPGTNWMIGTGEYMDDIDAELAKYRntMTQ 195
Cdd:COG4564  100 NLLDLKDANGKYLIRELIEAAKKKGGGFvEYLWPKPGSGKPEPKLSYVKKFPPWDWVIGTGVYLDDIEAAFAAAA--LEL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 196 HMNDKVTTLLLIALFWLVLTIACALIAANTMVKPIQRMVQSLDDIAKGEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHG 275
Cdd:COG4564  178 LLLLALLLALALALLLLVLAALAGLLLASALEGELNLAGALAALLLAAAAELLAALLLIGAAAGALLALAEAVAAVLAEA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 276 IIVNVVDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVD 355
Cdd:COG4564  258 LAAAAAAAAASAAASSAALAAAAAEAEAALAASEASAAAALAAAAAAAAAAAAAAAAAEAAAAAAAAAAAAAAAAASVAD 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 356 ISLSEVSHLMGEINVAAEQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQ 435
Cdd:COG4564  338 VAALAAAAAAAAAIAALAAAAAAAAAAAAAAAAIAAAAAAAAAAAAAAAAAAAEAAAAAAAAATAAAALEAVAAAAAAAA 417

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 436 VSTLEISEMLSElhNLVSAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNV 515
Cdd:COG4564  418 AAAAAEAAAAEV--EAAAAITAIILEAAAAAAAAIEAEEAAAVAAAAALAAEAAAAAAAAAEAAAAAAAAEAASAVVSAA 495

                        490
                 ....*....|....
gi 966195281 516 FAIQEIVNELTISS 529
Cdd:COG4564  496 AAAAAAGAAAALAL 509
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 367-522 2.92e-36

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: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 132.94  E-value: 2.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  367 EINVAAEQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLS 446
Cdd:pfam00015  17 EVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALII 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966195281  447 ELHNLVSAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQEIV 522
Cdd:pfam00015  97 EIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQVT 172
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
177-555 4.08e-35

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 138.93  E-value: 4.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 177 EYMDDIDA--ELAKYRNTMTQHMNDKVTTLLLIALfwLVLTIACALIAANTMVKPIQRMVQSLDDIAKGegDLTKRLDID 254
Cdd:PRK15041 169 AYMEQNDRlyDIAVSDNNASYSQAMWILVGVMIVV--LAVIFAVWFGIKASLVAPMNRLIDSIRHIAGG--DLVKPIEVD 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 255 TNDEIGQLGEAFNMFVSKLHGIIVNVVDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTT 334
Cdd:PRK15041 245 GSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENAR 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 335 QVAESTQAATQEVAKAQECVDislsevshlmgeiNVAAEQVDsLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAG 414
Cdd:PRK15041 325 QASHLALSASETAQRGGKVVD-------------NVVQTMRD-ISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAG 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 415 EQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLVSAAveamqasqqscNRSVESSraiSESLGAVTSSVRSINDMS 494
Cdd:PRK15041 391 EQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVG-----------STLVESA---GETMAEIVSAVTRVTDIM 456

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966195281 495 TQIATAAMEQSSVTEEINRNVFAIQEIVNELTISSKTTSSVGLHLAGRGENLGQLVGQFKI 555
Cdd:PRK15041 457 GEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 189-520 2.90e-33

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 133.59  E-value: 2.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 189 YRNTMTQHMNDKVTTLLLIALFWLVLTIAcaLIAA-----NTMVKPIQRMVQSLDDIAKGegDLTKRLDIDTNDEIGQLG 263
Cdd:PRK15048 176 YRDIVTDNADDYRFAQWQLAVIALVVVLI--LLVAwygirRMLLTPLAKIIAHIREIAGG--NLANTLTIDGRSEMGDLA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 264 EAFNMFVSKLHGIIVNVVDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAA 343
Cdd:PRK15048 252 QSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSA 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 344 TQEVAKAQECVDislsEVSHLMGEInvaaeqvdslSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVV 423
Cdd:PRK15048 332 SDTAQHGGKVVD----GVVKTMHEI----------ADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVV 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 424 ADEVRSLASRTQVSTLEISEMLSELHNLVSAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAME 503
Cdd:PRK15048 398 AGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSE 477

                        330
                 ....*....|....*..
gi 966195281 504 QSSVTEEinrNVFAIQE 520
Cdd:PRK15048 478 MDRVTQQ---NASLVQE 491
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
185-555 8.39e-30

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 123.26  E-value: 8.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 185 ELAKYRNTMTQHMNDKV-TTLLLIALfwlVLTIACALIAANTMVKPIQRMVQSLDDIAKGegDLTKRLDIDTNDEIGQLG 263
Cdd:PRK09793 175 EAASAQSQRNYQISALVfISMIIVAA---IYISSALWWTRKMIVQPLAIIGSHFDSIAAG--NLARPIAVYGRNEITAIF 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 264 EAFNMFVSKLHGIIVNVVDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATsheVAQNTTQVAESTQAA 343
Cdd:PRK09793 250 ASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTAT---VGQNADNARQASELA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 344 TQEVAKAQECVDiSLSEVSHLMGEInvaaeqvdslSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVV 423
Cdd:PRK09793 327 KNAATTAQAGGV-QVSTMTHTMQEI----------ATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVV 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 424 ADEVRSLASRTQVSTLEISEMLSELHNLVsaaveamqasQQSCNRSVESSRAISEslgaVTSSVRSINDMSTQIATAAME 503
Cdd:PRK09793 396 AGEVRNLASRSAQAAKEIKGLIEESVNRV----------QQGSKLVNNAAATMTD----IVSSVTRVNDIMGEIASASEE 461

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966195281 504 QSSVTEEINRNVFAIQEIVNELTISSKTTSSVGLHLAGRGENLGQLVGQFKI 555
Cdd:PRK09793 462 QRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
sCache_2 pfam17200
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ...
 48-190 3.71e-27

Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain. This domain recognizes pyruvate, acetate, propionate, glycolate, L-lactate, acetoacetate, urea and hydroxyurea, acetamide, formamide, L-malate and citromalate, malonate, methyl and bromosuccinate and citraconic acid (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435780 [Multi-domain]  Cd Length: 153  Bit Score: 107.05  E-value: 3.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   48 LISDKQTLLRTEIEIAS---KVVRYQLANG--SQEDAKK----ALRDLTFGQG-GYFFIYDTNGVSVFHALlGDAIEGQN 117
Cdd:pfam17200   1 LIDQGKAQLKNLVNGAIsliEAVYAQVESGkiTLEEAQElakeLILGPRYGDGdGYFWVYDEDGNMLVHPF-NPQLEGQN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966195281  118 KIGMTDPNGKKIIVGLLEQARKGGGAF-NYHFQKPGTAGLIEKMGYAAMIPGTNWMIGTGEYMDDIDAELAKYR 190
Cdd:pfam17200  80 RSNLKDANGKYFIRELIATAKKAGGGFvTYLWKNPGEKAVEPKLAYVKYFPPWDWVIGTGSYMDDINAAAEKIL 153
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
 42-186 1.09e-24

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


Pssm-ID: 462414 [Multi-domain]  Cd Length: 298  Bit Score: 104.38  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   42 DAFKTKLISDKQTLLRTEIEIASKVVR--YQLANGS------QEDAKKALRDLTFGQG-GYFFIYDTNGVSVFHALLGDa 112
Cdd:pfam08269  36 NYYKNSLEESLKESLKSRVNEAYSIAEsiYEKYKNKlseeeiKKLIKEALRSIRFNDGtGYYFIIDKKGTVILHPDNPS- 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966195281  113 IEGQNKIGMTDPNGKKIIVGLLEQARKGGGAF-NYHFQKP-GTAGLIEKMGYAAMIPGTNWMIGTGEYMDDIDAEL 186
Cdd:pfam08269 115 LEGKNLLDLKDKDGRYIIREMIKLAKKKGEGFvDYLWPKPnGSDKPYKKISYVKYFEPLDWIIGTGEYLDDIEEEI 190
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
 76-183 4.03e-24

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


Pssm-ID: 462414 [Multi-domain]  Cd Length: 298  Bit Score: 102.45  E-value: 4.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   76 QEDAKKALRDLTFGQGGYFFIYDTNGVSVFHALlGDAIEGQNKIGMTDPNGKKIIVGLLEQARKGGGAF-NYHFQKPGTA 154
Cdd:pfam08269 191 KQELLKTLASIRYGNNGYIFIYDTDGNMILHPL-KPELNGKDLTENKDDKGQELFQELLEAAKKKGEGFvTYKWPKPGGD 269

                          90       100
                  ....*....|....*....|....*....
gi 966195281  155 GLIEKMGYAAMIPGTNWMIGTGEYMDDID 183
Cdd:pfam08269 270 KPRPKISYVRYFPPWDWIIGTGVYLDEIE 298
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
 48-130 2.13e-18

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995 [Multi-domain]  Cd Length: 91  Bit Score: 79.99  E-value: 2.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281    48 LISDKQTLLRTEIEIASKVVRYQLANGS---------QEDAKKALRDLTFGQGGYFFIYDTNGVSVFHALLgDAIEGQNK 118
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAagklteeeaQAQAKAALRALRYGGDGYFFVYDSDGVMLMHPAK-PELEGKNL 79

                           90
                   ....*....|..
gi 966195281   119 IGMTDPNGKKII 130
Cdd:smart01049  80 SDLKDPNGKYLF 91
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 227-273 1.72e-12

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 Af1503 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: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 61.69  E-value: 1.72e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 966195281 227 VKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKL 273
Cdd:cd06225    1 TRPLRRLTEAARRIA--EGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
224-277 4.73e-11

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 58.03  E-value: 4.73e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 966195281   224 NTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHGII 277
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 203-273 9.30e-11

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 63.83  E-value: 9.30e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966195281 203 TLLLIALFWLVLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKL 273
Cdd:COG5000   10 LLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVA--AGDLSVRLPVTGDDEIGELARAFNRMTDQL 78
HAMP pfam00672
HAMP domain;
221-274 2.21e-10

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 56.09  E-value: 2.21e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966195281  221 IAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLH 274
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIA--SGDLDVRLPVSGRDEIGELARAFNQMAERLR 52
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
 75-192 7.20e-08

Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of sCache_3 and sCache_2 domains.


Pssm-ID: 465378 [Multi-domain]  Cd Length: 298  Bit Score: 54.28  E-value: 7.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281   75 SQEDAKKALRDLTFGQGGYFFIYDTNGVS----VFHALLgdaiEGQNKIGMTDPNGKKIIVGLLEQARkggGAFNYHFQK 150
Cdd:pfam17201 186 ALASLRKAIKKVKIGKTGYLYVLDGKGDQkgkfIVHPTL----EGKNILDAKDADGEPFVKKLLQKKV---GSLEYPWKA 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 966195281  151 PGTAGliEKMGYAAMIPGTNWMIGTGEYMDDIDAELAKYRNT 192
Cdd:pfam17201 259 DAAGR--DKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLNQ 298
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
190-280 2.15e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.48  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 190 RNTMTQHMNDKVTTLLLIALFWLVLTIACALIAANTMVKPIQRMVQSLDDIAKGEGdltKRLDIDTNDEIGQLGEAFNMF 269
Cdd:COG2972  145 KSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDL---VRLEVSGNDEIGILARSFNEM 221

                         90
                 ....*....|.
gi 966195281 270 VSKLHGIIVNV 280
Cdd:COG2972  222 VERIKELIEEV 232
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 171-499 7.39e-06

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 48.73  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 171 WMIGTGEYMDDIDAELAKYRNTMTQHMNDKVTTLLLIALFwLVLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKR 250
Cdd:COG3850   88 ALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLA-LLLALLLAYLLRRRIVRPLRRLTQAAERIA--RGDFDAR 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 251 LDIDTNDEIGQLGEAFNMFVSKLHGIIVNVVDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVA 330
Cdd:COG3850  165 VPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLL 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 331 QNTTQVAESTQAATQEVAKAQECVDISLSEVSHLMGEINVAAEQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEA 410
Cdd:COG3850  245 QDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIA 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 411 ARAGEQGRGFAVVADEVRSLASRTQVSTLEISEMLSELHNLVSAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSI 490
Cdd:COG3850  325 NASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLV 404


                 ....*....
gi 966195281 491 NDMSTQIAT 499
Cdd:COG3850  405 DVEGGVAGE 413
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
201-550 9.20e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 45.49  E-value: 9.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 201 VTTLLLIALFWLVLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHGIIVNV 280
Cdd:COG2770  211 LLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIA--AGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEA 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 281 VDVTHDVKTASGDINTQTQLIESKLLNHNHETDLVATAITEMSATSHEVAQNTTQVAESTQAATQEVAKAQECVDISLSE 360
Cdd:COG2770  289 EEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 361 VSHLMGEINVAAEQVDSLSDQSKKINSVLSVIGGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLASRTQVSTLE 440
Cdd:COG2770  369 LEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAA 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 441 ISEMLSELHNLVSAAVEAMQASQQSCNRSVESSRAISESLGAVTSSVRSINDMSTQIATAAMEQSSVTEEINRNVFAIQE 520
Cdd:COG2770  449 AAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEV 528

                        330       340       350
                 ....*....|....*....|....*....|
gi 966195281 521 IVNELTISSKTTSSVGLHLAGRGENLGQLV 550
Cdd:COG2770  529 AEELLELEEAALLLAAAAELAALLALLLAL 558
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 81-175 1.34e-04

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 40.83  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  81 KALRDLTFGQGGYFFIYDTNGVSVFHallgdaiEGQNKIGMTDPNGKKIIVGLLEQARKGG-GAFNYHFQKpgtaglIEK 159
Cdd:cd12912    4 EIISSIKIGETGYAFLVDKDGTIIAH-------PDKELVGKKISDDEAAEEELAKKMLAGKsGSVEYTFNG------EKK 70

                         90
                 ....*....|....*.
gi 966195281 160 MGYAAMIPGTNWMIGT 175
Cdd:cd12912   71 YVAYAPIPGTGWSLVV 86
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
206-289 1.75e-04

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 44.24  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281 206 LIALFWLVLTIACALIAANTMVKPIQRMVQSLDDIAkgEGDLTKRLDIDTNDEIGQLGEAFNMFVSKLHGiivN------ 279
Cdd:PRK10549 168 LIVALSTLLAALATFLLARGLLAPVKRLVEGTHKLA--AGDFTTRVTPTSRDELGRLAQDFNQLASTLEK---Neqmrrd 242

                         90
                 ....*....|.
gi 966195281 280 -VVDVTHDVKT 289
Cdd:PRK10549 243 fMADISHELRT 253
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 83-176 3.35e-03

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 37.04  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966195281  83 LRDLTFGQGGYFFIYDTNGVSVFHAllGDAIEGQNKIGMTDPNGKKIIvglleqARKGGGAFNYHFQKpGtaglIEKMGY 162
Cdd:cd18774    6 LSSIKLGETGYAFLVDSDGTILAHP--PKELVGKGKSLDDLALLAALL------LAGESGTFEYTSDD-G----VERLVA 72

                         90
                 ....*....|....
gi 966195281 163 AAMIPGTNWMIGTG 176
Cdd:cd18774   73 YRPVPGTPWVVVVG 86
 
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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