|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
35-562 |
1.54e-87 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 280.75 E-value: 1.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 35 SGAQTVESFATQMENDRKAEVSNYQKIAMSSIAHLIAQDDGSNTEQLQSQAKSILRNLRFDDAGDTGYVFVYDVKGVNIA 114
Cdd:COG0840 8 LALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 115 HGVNASLEGKNLYDFKDPNGVYLIRELIDAAKKGGGYVQYSWKNTNGSVNPKLGYAALVPKWNWVLGTGFWISGLEQQVA 194
Cdd:COG0840 88 LLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 195 VTEQRVNEGIDNAFINTVIASIFAVAITAAIAVVVSRSITSPLHTTVLAMNDISqgDGDLTQRLMVKRDDELGKLGSSFN 274
Cdd:COG0840 168 EAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDVDSKDEIGQLADAFN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 275 RFADDVGKMVIDIRQSSQSMNQASHKLNELLANMHSGINRQHEESEQVATAINEMSAASMEVARSAQEASTAAEHADHLV 354
Cdd:COG0840 246 RMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 355 KQANNQLLIAIKVINGLAKQVDEGANAVDQLNQQSSQIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEV 434
Cdd:COG0840 326 EEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 435 RTLAKRTQDSTHEIEAMIEQVQQGTTTVNSIMQSIKSGSATSVNEAGEVEKALNEVLLSVNTITSQNAQIATAAEEQTSV 514
Cdd:COG0840 406 RKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAG 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1859350790 515 SEAINQNMTTIVDIANKTANDTDVATSYMHELTDTATQLEQNVSRYKT 562
Cdd:COG0840 486 TEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
310-561 |
7.07e-61 |
|
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: 202.13 E-value: 7.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 310 SGINRQHEESEQVATAINEMSAASMEVARSAQEASTAAEHADHLVKQANNQLLIAIKVINGLAKQVDEGANAVDQLNQQS 389
Cdd:smart00283 11 AGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 390 SQIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMIEQVQQGTTTVNSIMQSI 469
Cdd:smart00283 91 DEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 470 KSGSATSVNEAGEVEKALNEVLLSVNTITSQNAQIATAAEEQTSVSEAINQNMTTIVDIANKTANDTDVATSYMHELTDT 549
Cdd:smart00283 171 SSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGL 250
|
250
....*....|..
gi 1859350790 550 ATQLEQNVSRYK 561
Cdd:smart00283 251 AEELDELVERFK 262
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
327-525 |
2.91e-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: 179.74 E-value: 2.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 327 NEMSAASMEVARSAQEASTAAEHADHLVKQANNQLLIAIKVINGLAKQVDEGANAVDQLNQQSSQIGSVLDVIRNIAEQT 406
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 407 NLLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMIEQVQQGTTTVNSIMQSIKSGSATSVNEAGEVEKA 486
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1859350790 487 LNEVLLSVNTITSQNAQIATAAEEQTSVSEAINQNMTTI 525
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
|
|
| COG4564 |
COG4564 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
39-533 |
1.36e-41 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 443621 [Multi-domain] Cd Length: 510 Bit Score: 157.12 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 39 TVESFATQMENDRKAEVSNYQKIAMSSIAHLIAQDDGSNtEQLQSQAKSILRNLRFddaGDTGYVFVYDVKGVNIAHGVN 118
Cdd:COG4564 18 SLETLRQALLEERKAELRALVELAVSIIAALYAAGELSE-EEAKEQALAALRALRF---GGDGYFFVYDYDGTMLAHPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 119 ASLEGKNLYDFKDPNGVYLIRELIDAAKK-GGGYVQYSWKN-TNGSVNPKLGYAALVPKWNWVLGTGFWISGLEQQVAVT 196
Cdd:COG4564 94 PELVGKNLLDLKDANGKYLIRELIEAAKKkGGGFVEYLWPKpGSGKPEPKLSYVKKFPPWDWVIGTGVYLDDIEAAFAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 197 EQRVNEGIdnAFINTVIASIFAVAITAAIAVVVSRSITSPLHTTVLAMNDISQGDGDLTQRLMVKRDDELGKLGSSFNRF 276
Cdd:COG4564 174 ALELLLLL--ALLLALALALLLLVLAALAGLLLASALEGELNLAGALAALLLAAAAELLAALLLIGAAAGALLALAEAVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 277 ADDVGKMVIDIRQSSQSMNQASHKLNELLANMHSGINRQHEESEQVATAINEMSAASMEVARSAQEASTAAEHADHLVKQ 356
Cdd:COG4564 252 AVLAEALAAAAAAAAASAAASSAALAAAAAEAEAALAASEASAAAALAAAAAAAAAAAAAAAAAEAAAAAAAAAAAAAAA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 357 ANNQLLIAIKVINGLAKQVDEGANAVDQLNQQSSQIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRT 436
Cdd:COG4564 332 AASVADVAALAAAAAAAAAIAALAAAAAAAAAAAAAAAAIAAAAAAAAAAAAAAAAAAAEAAAAAAAAATAAAALEAVAA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 437 LAKRTQDSTHEIEAMIEQVQQGTTTVNSIMQSIKSGSATSVNEAGEVEKALNEVLLSVNTITSQNAQIATAAEEQTSVSE 516
Cdd:COG4564 412 AAAAAAAAAAAEAAAAEVEAAAAITAIILEAAAAAAAAIEAEEAAAVAAAAALAAEAAAAAAAAAEAAAAAAAAEAASAV 491
|
490
....*....|....*..
gi 1859350790 517 AINQNMTTIVDIANKTA 533
Cdd:COG4564 492 VSAAAAAAAAGAAAALA 508
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
373-528 |
1.04e-39 |
|
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: 142.57 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 373 KQVDEGANAVDQLNQQSSQIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMI 452
Cdd:pfam00015 16 KEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALI 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859350790 453 EQVQQGTTTVNSIMQSIKSGSATSVNEAGEVEKALNEVLLSVNTITSQNAQIATAAEEQTSVSEAINQNMTTIVDI 528
Cdd:pfam00015 96 IEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQV 171
|
|
| sCache_2 |
pfam17200 |
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ... |
47-194 |
6.43e-36 |
|
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: 131.32 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 47 MENDRKAEVSNYQKIAMSSIAHLIAQ-DDGSNT-EQLQSQAKSILRNLRFDDaGDtGYVFVYDVKGVNIAHGVNASLEGK 124
Cdd:pfam17200 1 LIDQGKAQLKNLVNGAISLIEAVYAQvESGKITlEEAQELAKELILGPRYGD-GD-GYFWVYDEDGNMLVHPFNPQLEGQ 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859350790 125 NLYDFKDPNGVYLIRELIDAAKK-GGGYVQYSWKNTN-GSVNPKLGYAALVPKWNWVLGTGFWISGLEQQVA 194
Cdd:pfam17200 79 NRSNLKDANGKYFIRELIATAKKaGGGFVTYLWKNPGeKAVEPKLAYVKYFPPWDWVIGTGSYMDDINAAAE 150
|
|
| dCache_2 |
pfam08269 |
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ... |
26-212 |
3.85e-34 |
|
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: 131.34 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 26 LYNYVqskHSGAQTVESFATQMENDRKAEVSNyQKIAMSSIAHLIAQDDGSN--TEQLQSQAKSILRNLRFDDagDTGYV 103
Cdd:pfam08269 24 LKSEV---DSAIDYINYYKNSLEESLKESLKS-RVNEAYSIAESIYEKYKNKlsEEEIKKLIKEALRSIRFND--GTGYY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 104 FVYDVKGVNIAHGVNASLEGKNLYDFKDPNGVYLIRELIDAA-KKGGGYVQYSWKNTNGSVNP--KLGYAALVPKWNWVL 180
Cdd:pfam08269 98 FIIDKKGTVILHPDNPSLEGKNLLDLKDKDGRYIIREMIKLAkKKGEGFVDYLWPKPNGSDKPykKISYVKYFEPLDWII 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1859350790 181 GTGFWISGLEQQV------AVTEQRVNEGiDNAFINTV 212
Cdd:pfam08269 178 GTGEYLDDIEEEIkqellkTLASIRYGNN-GYIFIYDT 214
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
231-561 |
1.07e-30 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 126.27 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 231 RSITSPLHTTVLAMNDISQGDgdLTQRLMVKRDDELGKLGSSFNRFADDVGKMVIDIRQSSQSMNQAShklnellANMHS 310
Cdd:PRK15048 214 RMLLTPLAKIIAHIREIAGGN--LANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGT-------REIAA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 311 GINRQHEESEQVATAINEMSAASMEVARSAQEASTAAEHADHLVKQANNQLLIAIKVINGLAKQVDEGANAvdqlnqqSS 390
Cdd:PRK15048 285 GNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS-------SK 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 391 QIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMIEQVqqgtttvnsiMQSIK 470
Cdd:PRK15048 358 KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDS----------VSRVD 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 471 SGSATsVNEAGEvekALNEVLLSVNTITSQNAQIATAAEEQtsvSEAINQNMTTIVDIANKTANDtdvaTSYMHELTDTA 550
Cdd:PRK15048 428 TGSVL-VESAGE---TMNNIVNAVTRVTDIMGEIASASDEQ---SRGIDQVALAVSEMDRVTQQN----ASLVQESAAAA 496
|
330
....*....|.
gi 1859350790 551 TQLEQNVSRYK 561
Cdd:PRK15048 497 AALEEQASRLT 507
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
248-561 |
4.59e-29 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 120.95 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 248 SQGDGDLTQRLMVKRDDELGKLGSSFNRFADDVGKMVIDIRQSSQSMNQASHKLNELLANMHSGINRQHEESEQVATAIN 327
Cdd:PRK09793 227 SIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASME 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 328 EMSAASMEVARSAQEASTAAEHADHLVKQANNQlliaikvinglakqVDEGANAVDQLNQQSSQIGSVLDVIRNIAEQTN 407
Cdd:PRK09793 307 QLTATVGQNADNARQASELAKNAATTAQAGGVQ--------------VSTMTHTMQEIATSSQKIGDIISVIDGIAFQTN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 408 LLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMIEQ----VQQGTTTVNSimqsiksgsatsvneageV 483
Cdd:PRK09793 373 ILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEEsvnrVQQGSKLVNN------------------A 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1859350790 484 EKALNEVLLSVNTITSQNAQIATAAEEQTSVSEAINQNMTTIVDIANKTANDTDVATSYMHELTDTATQLEQNVSRYK 561
Cdd:PRK09793 435 AATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFT 512
|
|
| dCache_2 |
pfam08269 |
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ... |
78-190 |
5.18e-29 |
|
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: 116.70 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 78 TEQLQSQAKSILRNLRFddaGDTGYVFVYDVKGVNIAHGVNASLEGKNLYDFKDPNGVYLIRELIDAAKKGG-GYVQYSW 156
Cdd:pfam08269 187 EEEIKQELLKTLASIRY---GNNGYIFIYDTDGNMILHPLKPELNGKDLTENKDDKGQELFQELLEAAKKKGeGFVTYKW 263
|
90 100 110
....*....|....*....|....*....|....*
gi 1859350790 157 KNTNGSVN-PKLGYAALVPKWNWVLGTGFWISGLE 190
Cdd:pfam08269 264 PKPGGDKPrPKISYVRYFPPWDWIIGTGVYLDEIE 298
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
232-559 |
1.03e-28 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 120.06 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 232 SITSPLHTTVLAMNDISqgDGDLTQRLMVKRDDELGKLGSSFNRFADDVGKMVIDIRQSSQSMNQASHKLNellanmhSG 311
Cdd:PRK15041 217 SLVAPMNRLIDSIRHIA--GGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIA-------TG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 312 INRQHEESEQVATAINEmSAASMEvarsaQEASTAAEHADHlVKQANNQLLIAIKVINGLAKQVDEGANAVDQLNQQSSQ 391
Cdd:PRK15041 288 NNDLSSRTEQQAASLEE-TAASME-----QLTATVKQNAEN-ARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 392 IGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMIE----QVQQGTTTVNSimq 467
Cdd:PRK15041 361 IADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEdsvgKVDVGSTLVES--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 468 siksgsatsvneAGEvekALNEVLLSVNTITSQNAQIATAAEEQtsvSEAINQNMTTIVDIANKTANDtdvaTSYMHELT 547
Cdd:PRK15041 438 ------------AGE---TMAEIVSAVTRVTDIMGEIASASDEQ---SRGIDQVGLAVAEMDRVTQQN----AALVEESA 495
|
330
....*....|..
gi 1859350790 548 DTATQLEQNVSR 559
Cdd:PRK15041 496 AAAAALEEQASR 507
|
|
| Cache_2 |
smart01049 |
Cache is an extracellular domain that is predicted to have a role in small-molecule ... |
47-138 |
2.84e-24 |
|
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: 96.94 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 47 MENDRKAEVSNYQKIAMSSIAHLIAQ-DDGSNT-EQLQSQAKSILRNLRFddaGDTGYVFVYDVKGVNIAHGVNASLEGK 124
Cdd:smart01049 1 LLEERKAELKNLVEIAVSIVEAYYAQaAAGKLTeEEAQAQAKAALRALRY---GGDGYFFVYDSDGVMLMHPAKPELEGK 77
|
90
....*....|....
gi 1859350790 125 NLYDFKDPNGVYLI 138
Cdd:smart01049 78 NLSDLKDPNGKYLF 91
|
|
| Cache_3-Cache_2 |
pfam17201 |
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ... |
73-187 |
3.99e-10 |
|
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: 61.21 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 73 DDGSNTEQLQSQaksiLRNLRFddaGDTGYVFVYD----VKGVNIAHgvnASLEGKNLYDFKDPNGVYLIRELIDAAKkg 148
Cdd:pfam17201 182 PQDEALASLRKA----IKKVKI---GKTGYLYVLDgkgdQKGKFIVH---PTLEGKNILDAKDADGEPFVKKLLQKKV-- 249
|
90 100 110
....*....|....*....|....*....|....*....
gi 1859350790 149 gGYVQYSWKNTNGSVNpKLGYAALVPKWNWVLGTGFWIS 187
Cdd:pfam17201 250 -GSLEYPWKADAAGRD-KLAAFTYFEPWDWVIVASVYED 286
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
230-312 |
8.15e-09 |
|
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: 58.05 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 230 SRSITSPLHTTVLAMNDISQGDgdLTQRLMVKRDDELGKLGSSFNRfaddvgkMVIDIRQSSQSMNQASHKLNELLANMH 309
Cdd:COG5000 30 ARRLTRPLRRLAEATRAVAAGD--LSVRLPVTGDDEIGELARAFNR-------MTDQLKEQREELEERRRYLETILENLP 100
|
...
gi 1859350790 310 SGI 312
Cdd:COG5000 101 AGV 103
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
234-278 |
8.89e-09 |
|
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: 51.29 E-value: 8.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1859350790 234 TSPLHTTVLAMNDISQGDgdLTQRLMVKRDDELGKLGSSFNRFAD 278
Cdd:cd06225 1 TRPLRRLTEAARRIAEGD--LDVRVPVRSKDEIGELARAFNQMAE 43
|
|
| HAMP |
pfam00672 |
HAMP domain; |
230-278 |
1.50e-08 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 51.09 E-value: 1.50e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1859350790 230 SRSITSPLHTTVLAMNDISqgDGDLTQRLMVKRDDELGKLGSSFNRFAD 278
Cdd:pfam00672 3 ARRILRPLRRLAEAARRIA--SGDLDVRLPVSGRDEIGELARAFNQMAE 49
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
231-284 |
1.76e-07 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 48.01 E-value: 1.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1859350790 231 RSITSPLHTTVLAMNDISqgDGDLTQRLMVKRDDELGKLGSSFNRFADDVGKMV 284
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52
|
|
| PDC2_MCP_like |
cd12912 |
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ... |
87-182 |
6.62e-07 |
|
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: 47.38 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 87 SILRNLRFddaGDTGYVFVYDVKGVNIAHGvNASLEGKNLYDFKDPNGvyliRELIDAAKKGGGYVQYSWKNTNgsvnpK 166
Cdd:cd12912 4 EIISSIKI---GETGYAFLVDKDGTIIAHP-DKELVGKKISDDEAAEE----ELAKKMLAGKSGSVEYTFNGEK-----K 70
|
90
....*....|....*.
gi 1859350790 167 LGYAALVPKWNWVLGT 182
Cdd:cd12912 71 YVAYAPIPGTGWSLVV 86
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
230-437 |
8.35e-06 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 48.34 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 230 SRSITSPLHTTVLAMNDISQGDgdLTQRLMVKRDDELGKLGSSFNRFADDVGKMVIDIRQSSQSMNQASHKLNELLANMH 309
Cdd:COG3850 139 RRRIVRPLRRLTQAAERIARGD--FDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 310 SGINRQHEESEQVATAINEMSAASMEVARSAQEASTAAEHADHLVKQANNQLLIAIKVINGLAKQVDEGANAVDQLNQQS 389
Cdd:COG3850 217 AALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELL 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1859350790 390 SQIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRTL 437
Cdd:COG3850 297 ALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELA 344
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
55-314 |
3.96e-05 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 46.16 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 55 VSNYQKIAMSSIAHLIAQDDGSNTEQLQSQAKSILRNLRFDDAGDTGYVFVYDVKGVNIAHG--VNASLEGKNLYDFKDP 132
Cdd:COG2972 1 LSKSLSLLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLllLLLLLLLLLLLLLALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 133 NGVYLIRELIDAAKKGGGYVQYSWKNTNGSVNPKLGYAALVPKWNWVLGTGFWISGLEQQVAVTEQRVNEGIDNAFINTV 212
Cdd:COG2972 81 LILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 213 IASIFAVAITAAIAVVVSRSITSPLHTTVLAMNDISQGDGdltQRLMVKRDDELGKLGSSFNRFADDVGKMVIDIRQSSQ 292
Cdd:COG2972 161 LIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDL---VRLEVSGNDEIGILARSFNEMVERIKELIEEVYELEL 237
|
250 260
....*....|....*....|..
gi 1859350790 293 SMNQAshklnELLAnMHSGINR 314
Cdd:COG2972 238 EKKEA-----ELKA-LQAQINP 253
|
|
| PDC2_HK_sensor |
cd18774 |
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ... |
87-183 |
5.24e-04 |
|
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: 39.35 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 87 SILRNLRFddaGDTGYVFVYDVKGVNIAHgVNASLEGKNLYDFKDPNGVYLIrelidaAKKGGGYVQYSWKntNGsvNPK 166
Cdd:cd18774 4 DLLSSIKL---GETGYAFLVDSDGTILAH-PPKELVGKGKSLDDLALLAALL------LAGESGTFEYTSD--DG--VER 69
|
90
....*....|....*..
gi 1859350790 167 LGYAALVPKWNWVLGTG 183
Cdd:cd18774 70 LVAYRPVPGTPWVVVVG 86
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
230-557 |
3.24e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 40.48 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 230 SRSITSPLHTTVLAMNDISQGDgdLTQRLMVKRDDELGKLGSSFNRFADDVGKMVIDIRQSSQSMNQASHKLNELLANMH 309
Cdd:COG2770 233 ARRITRPLRRLAEAARRIAAGD--LDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 310 SGINRQHEESEQVATAINEMSAASMEVARSAQEASTAAEHADHLVKQANNQLLIAIKVINGLAKQVDEGANAVDQLNQQS 389
Cdd:COG2770 311 LALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 390 SQIGSVLDVIRNIAEQTNLLALNAAIESARAGEAGRGFAVVADEVRTLAKRTQDSTHEIEAMIEQVQQGTTTVNSIMQSI 469
Cdd:COG2770 391 VLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350790 470 KSGSATSVNEAGEVEKALNEVLLSVNTITSQNAQIATAAEEQTSVSEAINQNMTTIVDIANKTANDTDVATSYMHELTDT 549
Cdd:COG2770 471 ALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAA 550
|
....*...
gi 1859350790 550 ATQLEQNV 557
Cdd:COG2770 551 LLALLLAL 558
|
|
| PRK10935 |
PRK10935 |
nitrate/nitrite two-component system sensor histidine kinase NarQ; |
231-307 |
4.70e-03 |
|
nitrate/nitrite two-component system sensor histidine kinase NarQ;
Pssm-ID: 236800 [Multi-domain] Cd Length: 565 Bit Score: 39.84 E-value: 4.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859350790 231 RSITSPLHTTVLAMNDISQGDGDlTQRLMVKRDDELGKLGSSFNRFADDVGKMVidiRQSSQSMNQASHKLNEllAN 307
Cdd:PRK10935 174 RQVVAPLNQLVTASQQIEKGQFD-HIPLDTTLPNELGLLAKAFNQMSSELHKLY---RSLEASVEEKTRKLTQ--AN 244
|
|
| |
