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Conserved domains on  [gi|446786488|ref|WP_000863744|]
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methyl-accepting chemotaxis protein [Vibrio cholerae]

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];
13-543 1.95e-92

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 292.69  E-value: 1.95e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  13 IAVAFGVIALINLAFGGYLYNSLHTIKSDVLNLTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEAEIAEDIRWMNDH 92
Cdd:COG0840    9 ALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  93 YQQIAQDLSRYERSIWTDHERSIFMPVKNLWNEYLRQLGSFNNDILQKEMIKAQQDLQRSLPTFEKLETAIDELLKLNLS 172
Cdd:COG0840   89 LLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 173 YVDNNRSELTELIDNIsefsVASIVALLAFMSAVTWLLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELAD 252
Cdd:COG0840  169 AAALALAAAALALALL----AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVD--SKDEIGQLAD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 253 ACSKMQNNLRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSS 332
Cdd:COG0840  243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 333 QHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVA 412
Cdd:COG0840  323 ELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 413 DEVRSLAGKTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQ 492
Cdd:COG0840  403 DEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446786488 493 DSVSEELSRNIERINESAKQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:COG0840  483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
13-543 1.95e-92

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 292.69  E-value: 1.95e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  13 IAVAFGVIALINLAFGGYLYNSLHTIKSDVLNLTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEAEIAEDIRWMNDH 92
Cdd:COG0840    9 ALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  93 YQQIAQDLSRYERSIWTDHERSIFMPVKNLWNEYLRQLGSFNNDILQKEMIKAQQDLQRSLPTFEKLETAIDELLKLNLS 172
Cdd:COG0840   89 LLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 173 YVDNNRSELTELIDNIsefsVASIVALLAFMSAVTWLLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELAD 252
Cdd:COG0840  169 AAALALAAAALALALL----AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVD--SKDEIGQLAD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 253 ACSKMQNNLRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSS 332
Cdd:COG0840  243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 333 QHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVA 412
Cdd:COG0840  323 ELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 413 DEVRSLAGKTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQ 492
Cdd:COG0840  403 DEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446786488 493 DSVSEELSRNIERINESAKQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:COG0840  483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 281-542 1.84e-66

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: 216.00  E-value: 1.84e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   281 EVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTE 360
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   361 QRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVEIIQNLQACA 440
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   441 QKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERINESAKQVAQGSSSA 520
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 446786488   521 AQSCAELSQLASQLQDTVQRFR 542
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 309-507 7.05e-51

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: 172.81  E-value: 7.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 309 EMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTN 388
Cdd:cd11386    2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 389 LLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAI 468
Cdd:cd11386   82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446786488 469 EQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERIN 507
Cdd:cd11386  162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
191-543 9.26e-34

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 134.43  E-value: 9.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 191 FSVASIVALLAFMSAVTWLlTNLICRPLMQVVTQANAIAEGNLAHRLdrKTIGHDELGELADACSKMQNNLRLMVEEIIT 270
Cdd:PRK09793 192 FISMIIVAAIYISSALWWT-RKMIVQPLAIIGSHFDSIAAGNLARPI--AVYGRNEITAIFASLKTMQQALRGTVSDVRK 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 271 SATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQ 350
Cdd:PRK09793 269 GSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQ 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 351 hvnqeigrteqrvlELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIV 430
Cdd:PRK09793 349 --------------EIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIK 414

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 431 EIIQNLQACAQKARETTNNSrelinhcveqsqetQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERINESA 510
Cdd:PRK09793 415 GLIEESVNRVQQGSKLVNNA--------------AATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVT 480

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446786488 511 KQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:PRK09793 481 QQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 346-507 1.23e-33

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: 125.62  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  346 NDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQS 425
Cdd:pfam00015   8 SEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  426 TGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIER 505
Cdd:pfam00015  88 AKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVAR 167


                  ..
gi 446786488  506 IN 507
Cdd:pfam00015 168 MD 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-536 9.73e-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: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 9.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   286 SEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLE 365
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   366 LESQAQQINmvvDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVE---IIQNLQACAQK 442
Cdd:TIGR02168  745 LEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   443 ARETTNNSRELINHCVEQSQETQQAIEQIrhqSSQIADMTIQIASACGEQDSVSEELSRNIERINESAKQVAQGSSSAAQ 522
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250
                   ....*....|....
gi 446786488   523 SCAELSQLASQLQD 536
Cdd:TIGR02168  899 LSEELRELESKRSE 912
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
13-543 1.95e-92

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 292.69  E-value: 1.95e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  13 IAVAFGVIALINLAFGGYLYNSLHTIKSDVLNLTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEAEIAEDIRWMNDH 92
Cdd:COG0840    9 ALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  93 YQQIAQDLSRYERSIWTDHERSIFMPVKNLWNEYLRQLGSFNNDILQKEMIKAQQDLQRSLPTFEKLETAIDELLKLNLS 172
Cdd:COG0840   89 LLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 173 YVDNNRSELTELIDNIsefsVASIVALLAFMSAVTWLLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELAD 252
Cdd:COG0840  169 AAALALAAAALALALL----AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVD--SKDEIGQLAD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 253 ACSKMQNNLRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSS 332
Cdd:COG0840  243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 333 QHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVA 412
Cdd:COG0840  323 ELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 413 DEVRSLAGKTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQ 492
Cdd:COG0840  403 DEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446786488 493 DSVSEELSRNIERINESAKQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:COG0840  483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 281-542 1.84e-66

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: 216.00  E-value: 1.84e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   281 EVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTE 360
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   361 QRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVEIIQNLQACA 440
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   441 QKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERINESAKQVAQGSSSA 520
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 446786488   521 AQSCAELSQLASQLQDTVQRFR 542
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 309-507 7.05e-51

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: 172.81  E-value: 7.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 309 EMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTN 388
Cdd:cd11386    2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 389 LLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAI 468
Cdd:cd11386   82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446786488 469 EQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERIN 507
Cdd:cd11386  162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
191-543 9.26e-34

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 134.43  E-value: 9.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 191 FSVASIVALLAFMSAVTWLlTNLICRPLMQVVTQANAIAEGNLAHRLdrKTIGHDELGELADACSKMQNNLRLMVEEIIT 270
Cdd:PRK09793 192 FISMIIVAAIYISSALWWT-RKMIVQPLAIIGSHFDSIAAGNLARPI--AVYGRNEITAIFASLKTMQQALRGTVSDVRK 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 271 SATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQ 350
Cdd:PRK09793 269 GSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQ 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 351 hvnqeigrteqrvlELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIV 430
Cdd:PRK09793 349 --------------EIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIK 414

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 431 EIIQNLQACAQKARETTNNSrelinhcveqsqetQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERINESA 510
Cdd:PRK09793 415 GLIEESVNRVQQGSKLVNNA--------------AATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVT 480

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446786488 511 KQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:PRK09793 481 QQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 346-507 1.23e-33

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: 125.62  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  346 NDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQS 425
Cdd:pfam00015   8 SEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  426 TGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIER 505
Cdd:pfam00015  88 AKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVAR 167


                  ..
gi 446786488  506 IN 507
Cdd:pfam00015 168 MD 169
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
4-543 1.23e-33

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 134.31  E-value: 1.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   4 FKNLAIGKKIAVAFGVIALINLAFGGYLYNSLhtiKSDVLNLTddtlpsmmLVNGIKYNMSSVRRAQISLLSSTDEAEIA 83
Cdd:PRK15041   2 LKRIKIVTSLLLVLAVFGLLQLTSGGLFFNAL---KNDKENFT--------VLQTIRQQQSTLNGSWVALLQTRNTLNRA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  84 eDIRWMNDH-----------YQQIAQDLSRYERSIWTDHE---------RSIFMPVKNLWNEYLRQLGSFNNdILQKEMI 143
Cdd:PRK15041  71 -GIRYMMDQnnigsgstvaeLMQSASISLKQAEKNWADYEalprdprqsTAAAAEIKRNYDIYHNALAELIQ-LLGAGKI 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 144 KA--QQDLQRSLPTFEKLETAIDEllklnlsyvDNNRSELTELIDNISEFSVAS------IVALLAFMSAVTWLLTNLIC 215
Cdd:PRK15041 149 NEffDQPTQGYQDGFEKQYVAYME---------QNDRLYDIAVSDNNASYSQAMwilvgvMIVVLAVIFAVWFGIKASLV 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 216 RPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELADACSKMQNNLRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQI 295
Cdd:PRK15041 220 APMNRLIDSIRHIAGGDLVKPIEVD--GSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQ 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 296 QQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSqqmRAVNDSIQHVNqeigrteqrvlELESQAQQINM 375
Cdd:PRK15041 298 QAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGG---KVVDNVVQTMR-----------DISTSSQKIAD 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 376 VVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVEIIqnlqacaqkarETTNNSRELIN 455
Cdd:PRK15041 364 IISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLI-----------EDSVGKVDVGS 432

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 456 HCVEQSQETqqaIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERINESAKQVAQGSSSAAQSCAELSQLASQLQ 535
Cdd:PRK15041 433 TLVESAGET---MAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLT 509


                 ....*...
gi 446786488 536 DTVQRFRL 543
Cdd:PRK15041 510 EAVAVFRI 517
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 17-543 1.10e-32

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 131.67  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  17 FGVIALINLAFGGYLYNSLHT-----IKSDVLNLTDDTLPS---MMLVNGIKYNMSSVRraqisLLSSTDEAEIAEDIRW 88
Cdd:PRK15048  15 LGVFALLQLISGSLFFSSLHHsqksfVVSNQLREQQGELTStwdLMLQTRINLSRSAVR-----MMMDSSNQQSNAKVEL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  89 MNDHYQQIAQDLSRYERSIWTDHERSIFMPVKNLWNEYLRQLGSFNNdiLQKEMIKAQQDLQRSLPTfEKLETAIDELL- 167
Cdd:PRK15048  90 LDSARKTLAQAATHYKKFKSMAPLPEMVATSRNIDEKYKNYYTALTE--LIDYLDYGNTGAYFAQPT-QGMQNAMGEAFa 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 168 KLNLSYVDNNRSELTELIDN--ISEFSVASIVALLAFMSAVTWL-LTNLICRPLMQVVTQANAIAEGNLAHRLdrkTI-G 243
Cdd:PRK15048 167 QYALSSEKLYRDIVTDNADDyrFAQWQLAVIALVVVLILLVAWYgIRRMLLTPLAKIIAHIREIAGGNLANTL---TIdG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 244 HDELGELADACSKMQNNLRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEV 323
Cdd:PRK15048 244 RSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQ 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 324 ASDASRDSSQHANVGSQQMRAVNDSIQhvnqeigrteqrvlELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGE 403
Cdd:PRK15048 324 ASQLAQSASDTAQHGGKVVDGVVKTMH--------------EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGE 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 404 QGRGFAVVADEVRSLAGKTQQSTGDIVEIIQNlqacaQKARETTNNSrelinhCVEQSQETqqaIEQIRHQSSQIADMTI 483
Cdd:PRK15048 390 QGRGFAVVAGEVRNLASRSAQAAKEIKALIED-----SVSRVDTGSV------LVESAGET---MNNIVNAVTRVTDIMG 455

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 484 QIASACGEQDSVSEELSRNIERINESAKQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:PRK15048 456 EIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
 6-172 1.20e-11

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 432749 [Multi-domain]  Cd Length: 181  Bit Score: 63.42  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488    6 NLAIGKKIAVAFGVIALINLAFGGYLYNSLHTIKSDVLNLTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEAEIAED 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGVVGLYSLKQINDNLDTMYEDRLLPIKWLGDIRANLLELRANLLELILTTDPAERDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   86 IRWMNDHYQQIAQDLSRYERSIWTDHERSIFMPVKNLWNEYLRQLGSFNNDILQKEMIKAQQDL-QRSLPTFEKLETAID 164
Cdd:pfam12729  81 LKDIEELRAEIDKLLEKYEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKAGNKDEAYQLYkTEGRPAREAMIEALE 160


                  ....*...
gi 446786488  165 ELLKLNLS 172
Cdd:pfam12729 161 ELVDYNLK 168
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 193-284 2.00e-07

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: 53.43  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 193 VASIVALLAFMSAV--TWLLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELADACSKMQNNLRLMVEEIIT 270
Cdd:COG5000   10 LLLLIALLLLLLALwlALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVT--GDDEIGELARAFNRMTDQLKEQREELEE 87

                         90
                 ....*....|....
gi 446786488 271 SATQLAHAVDEVSA 284
Cdd:COG5000   88 RRRYLETILENLPA 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 261-543 4.97e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 261 LRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQ 340
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 341 QMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINmvvDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAG 420
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELE---EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 421 KTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELS 500
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446786488 501 RNIERINESAKQVAQGSSSAAQSCAELSQLASQLQDTVQRFRL 543
Cdd:COG1196  453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 216-261 9.11e-07

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: 45.51  E-value: 9.11e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446786488 216 RPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELADACSKMQNNL 261
Cdd:cd06225    2 RPLRRLTEAARRIAEGDLDVRVPVR--SKDEIGELARAFNQMAERL 45
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
7-534 8.85e-06

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 48.57  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   7 LAIGKKIAVAFGVIALINLAFGGYLYNSLHTIKSDVLNLTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEAEIAEDI 86
Cdd:COG2770   29 ALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  87 RWMNDHYQQIAQDLSRYERSIWTDHERSIFMPVKNLWNEYLRQLGSFNNDILQKEMIKAQQDLQRSLPTFEKLETAIDEL 166
Cdd:COG2770  109 LLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 167 LKLNLSYVDNNRSELTELIDNISEFSVASIVALLAFMSAVTWLLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDE 246
Cdd:COG2770  189 ALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVS--RKDE 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 247 LGELADACSKMQNNLRLMVEEIITSATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASD 326
Cdd:COG2770  267 IGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLL 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 327 ASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGR 406
Cdd:COG2770  347 AADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAA 426

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 407 GFAVVADEVRSLAGKTQQSTGDIVEIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIA 486
Cdd:COG2770  427 AAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELA 506

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 446786488 487 SACGEQDSVSEELSRNIERINESAKQVAQGSSSAAQSCAELSQLASQL 534
Cdd:COG2770  507 EELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLAL 554
HAMP pfam00672
HAMP domain;
209-262 3.54e-05

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 41.46  E-value: 3.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446786488  209 LLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELADACSKMQNNLR 262
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVS--GRDEIGELARAFNQMAERLR 52
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 282-522 7.64e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 282 VSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTEQ 361
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 362 RVLELE----SQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVEIIQNLQ 437
Cdd:COG4942   91 EIAELRaeleAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 438 ACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADmtiQIASACGEQDSVSEELSRNIERINESAKQVAQGS 517
Cdd:COG4942  171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247


                 ....*
gi 446786488 518 SSAAQ 522
Cdd:COG4942  248 FAALK 252
MCP2201-like_sensor cd19411
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
 45-170 1.83e-04

ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.


Pssm-ID: 438629 [Multi-domain]  Cd Length: 138  Bit Score: 41.85  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488  45 LTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEAEIAEDIRWMNDHYQQIAQDLSRYERSIWTDHERSIFMPVKNLWN 124
Cdd:cd19411    1 IVEDRYPKVRLANEWKDNVNANARRTRNLLLSTDPAERAKELARIAAARARITELLKKLEKLITSPEGKALLAAIAEARA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446786488 125 EYLRQLGSFNNDILQKEMIKAQQDLQRSL-PTFEKLETAIDELLKLN 170
Cdd:cd19411   81 AYLAARDKVLELKKAGDREEARALLLGELrPAQAAYLAALDALVDYQ 127
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
216-266 3.84e-04

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 38.38  E-value: 3.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 446786488   216 RPLMQVVTQANAIAEGNLAHRLDrkTIGHDELGELADACSKMQNNLRLMVE 266
Cdd:smart00304   5 RPLRRLAEAAQRIADGDLTVRLP--VDGRDEIGELARAFNEMADRLEETIA 53
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 127-394 3.89e-04

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 43.14  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 127 LRQLGSFNNDILQ--KEMIKAQQDLQRSLPTFEKLETAIDELLKlnlSYVDNNRSELTELIDNISEF-----SVASIVAL 199
Cdd:COG4192  257 LLAIGSGEGGLPSlrRDELAAQATLEALAEENNSILEQLRTQIS---GLVGNSREQLVALNQETAQLvqqsgILLLAIAL 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 200 LAFMSAV--TWLL--TNLICRpLMQVVTQANAIAEGNLAHRLdrKTIGHDELGELAdacskmqNNLRLMVEEIITSATQL 275
Cdd:COG4192  334 LSLLLAVliNYFYvrRRLVKR-LNALSDAMAAIAAGDLDVPI--PVDGNDEIGRIA-------RLLRVFRDQAIEKTQEL 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 276 AhavDEVSAvSEQTSQGMQIQQEEVMQiATAMAEMKSTVAEVARNTEVASDASRD--SSQHANVGSQQMRAVNDSIQHVN 353
Cdd:COG4192  404 E---TEIEE-RKRIEKNLRQTQDELIQ-AAKMAVVGQTMTSLAHELNQPLNAMSMylFSAKKALEQENYAQLPTSLDKIE 478

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446786488 354 QEIGRTEQRVLELESQAQQIN---MVVDVISNIAEQTNLLALNA 394
Cdd:COG4192  479 GLIERMDKIIKSLRQFSRKSDtplQPVDLRQVIEQAWELVESRA 522
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 191-506 5.20e-04

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 42.56  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 191 FSVASIVALLAFMSAVTWLLTNLICRPLMQVVTQANAIAEGNLAHRLDRKtiGHDELGELADACSKMQNNLRLMVEEIIT 270
Cdd:COG3850  119 LALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVS--GRDELGTLARAFNRMADELQELYAELEE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 271 SATQLAHAVDEVSAVSEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQ 350
Cdd:COG3850  197 EEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLAS 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 351 HVNQEIGRTEQRVLELESQAQQINMVVDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIV 430
Cdd:COG3850  277 ALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAA 356

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446786488 431 EIIQNLQACAQKARETTNNSRELINHCVEQSQETQQAIEQIRHQSSQIADMTIQIASACGEQDSVSEELSRNIERI 506
Cdd:COG3850  357 AAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIAR 432
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
178-278 7.50e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 41.93  E-value: 7.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488 178 RSELTELIDNISEFSVASIVALLAFMSAVTWLLTNLICRPLMQVVTQANAIAEGNLAHrldRKTIGHDELGELADACSKM 257
Cdd:COG2972  145 KSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVR---LEVSGNDEIGILARSFNEM 221

                         90       100
                 ....*....|....*....|.
gi 446786488 258 QNNLRLMVEEIITSATQLAHA 278
Cdd:COG2972  222 VERIKELIEEVYELELEKKEA 242
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 1-107 6.27e-03

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 39.28  E-value: 6.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   1 MAFFKNLAIGKKIAVAFGVIALINLAFGGYLYNSLHTIKSDVLNLTDDTLPSMMLVNGIKYNMSSVRRAQISLLSSTDEA 80
Cdd:COG4192    2 KKLLKRLGIGARLLLAFALSALLTLVASLVALFSWNSLSNQIRYILDDSLPKLQASLKLEENSNELVAALPEFAAATNTT 81

                         90       100
                 ....*....|....*....|....*..
gi 446786488  81 EIAEdirwmndHYQQIAQDLSRYERSI 107
Cdd:COG4192   82 ERSQ-------LRNQLNTQLADIEELL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-536 9.73e-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: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 9.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   286 SEQTSQGMQIQQEEVMQIATAMAEMKSTVAEVARNTEVASDASRDSSQHANVGSQQMRAVNDSIQHVNQEIGRTEQRVLE 365
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   366 LESQAQQINmvvDVISNIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRSLAGKTQQSTGDIVE---IIQNLQACAQK 442
Cdd:TIGR02168  745 LEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786488   443 ARETTNNSRELINHCVEQSQETQQAIEQIrhqSSQIADMTIQIASACGEQDSVSEELSRNIERINESAKQVAQGSSSAAQ 522
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250
                   ....*....|....
gi 446786488   523 SCAELSQLASQLQD 536
Cdd:TIGR02168  899 LSEELRELESKRSE 912
 
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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