|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
180-640 |
2.30e-73 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 245.32 E-value: 2.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 180 NELAAYYSLLNLKEQAGVERALLSNIFSMDRFDDGQFSMFSDVVGQQDAWLTAARSFSTPVQAAELDKSLQSAEATRALE 259
Cdd:COG0840 44 ALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 260 LRETAFNKAAEGGFGVNPTDWFNLQTQRIETLQKVENRAVDALQEHAALLAHNARVDWQSFLVISLVALLIAIAFAVMVA 339
Cdd:COG0840 124 LAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 340 RSIQQQLNGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKSGAVVLRSASSDIAAGNQDLAQRT 418
Cdd:COG0840 204 RSITRPLRELLEVLERIaEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 419 DEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRV--------------SNEASQSMAEIRSSSEQI 484
Cdd:COG0840 284 EEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVveeavegieeiresVEETAETIEELGESSQEI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 485 SQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELIN--------------QNMDK 550
Cdd:COG0840 364 GEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEeiqseteeaveameEGSEE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 551 IGEGVARVTASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEA 630
Cdd:COG0840 444 VEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEE 523
|
490
....*....|
gi 1995340955 631 MSTLVDRFIV 640
Cdd:COG0840 524 LQELVSRFKL 533
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
321-638 |
5.67e-64 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 220.98 E-value: 5.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 321 LVISLVALLIAIAFAVMVarSIQQQLNGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKSGAVV 399
Cdd:PRK15041 199 VMIVVLAVIFAVWFGIKA--SLVAPMNRLIDSIRHIaGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 400 LRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMAEIRS 479
Cdd:PRK15041 277 IYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIST 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 480 SSEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGVARVT 559
Cdd:PRK15041 357 SSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVE 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1995340955 560 ASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEAMSTLVDRF 638
Cdd:PRK15041 437 SAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
392-638 |
9.62e-53 |
|
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: 182.10 E-value: 9.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 392 EIKSGAVVLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEAS 471
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 472 QSMAEIRSSSEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELIN------ 545
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 546 --------QNMDKIGEGVARVTASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQA 617
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|.
gi 1995340955 618 ASASQMLDGQSEAMSTLVDRF 638
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
419-618 |
4.02e-44 |
|
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: 156.63 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 419 DEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMAEIRSSSEQISQIVASIDEISFQT 498
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 499 NLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGVARVTASGTALKAAAENTGRMKQY 578
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1995340955 579 VSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAA 618
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
|
|
| NIT |
pfam08376 |
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ... |
59-303 |
2.65e-40 |
|
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.
Pssm-ID: 462453 [Multi-domain] Cd Length: 227 Bit Score: 146.87 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 59 VHQLQSERGMSAGFIGARGQKfrddlKFRDDLAAQRQLTDKVLATFKRLLTDTNkdlLQGNIAAPLKTFNESIQFLDSTR 138
Cdd:pfam08376 1 VHALQKERGLSAGYLASGGGG-----RFAAELAAQRAATDAALAALRAALAELA---LPARLADRLAALLRALDQLPALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 139 TAISELTIDSPKASQFYTQTISDVLKFVGGMGHLSTSGSMVNELAAYYSLLNLKEQAGVERALLSNIFSMDRFDDGQFSM 218
Cdd:pfam08376 73 RQVDAGALSALEALAAYTELIAALLDLVDELAAGSPDPELARQLRALAALLRAKEAAGQERALLAAALAAGRFTAAEYRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 219 FSDVVGQQDAWLTAARSFSTPVQAAELDKSLQSAEATRALELRETAfnkaaeggfgVNPTDWFNLQTQRIETLQKVENRA 298
Cdd:pfam08376 153 FLSLVAAQRAALAEFRAAATPEQRALYDATVTGPAVAAAERLRDRL----------VDAAAWFAASTARIDLLREVEDRL 222
|
....*
gi 1995340955 299 VDALQ 303
Cdd:pfam08376 223 ADDLA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-632 |
7.76e-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: 39.65 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 370 DELSALNRAYNQAIENIQHIVQEIKSGAVVLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEA 449
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 450 ERLIHSMERDVLEANrvsneasqsmaeirsssEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNL 529
Cdd:TIGR02168 781 EAEIEELEAQIEQLK-----------------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 530 SQRcAREASQIRELINQNMDKIGEGVARVTAsgtALKAAAENTGRMKQYVSDIARAANEQSLGV----SQVHQALNQLEQ 605
Cdd:TIGR02168 844 EEQ-IEELSEDIESLAAEIEELEELIEELES---ELEALLNERASLEEALALLRSELEELSEELreleSKRSELRRELEE 919
|
250 260
....*....|....*....|....*..
gi 1995340955 606 VTQQNAALVSQAASASQMLDGQSEAMS 632
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
180-640 |
2.30e-73 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 245.32 E-value: 2.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 180 NELAAYYSLLNLKEQAGVERALLSNIFSMDRFDDGQFSMFSDVVGQQDAWLTAARSFSTPVQAAELDKSLQSAEATRALE 259
Cdd:COG0840 44 ALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 260 LRETAFNKAAEGGFGVNPTDWFNLQTQRIETLQKVENRAVDALQEHAALLAHNARVDWQSFLVISLVALLIAIAFAVMVA 339
Cdd:COG0840 124 LAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 340 RSIQQQLNGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKSGAVVLRSASSDIAAGNQDLAQRT 418
Cdd:COG0840 204 RSITRPLRELLEVLERIaEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 419 DEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRV--------------SNEASQSMAEIRSSSEQI 484
Cdd:COG0840 284 EEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVveeavegieeiresVEETAETIEELGESSQEI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 485 SQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELIN--------------QNMDK 550
Cdd:COG0840 364 GEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEeiqseteeaveameEGSEE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 551 IGEGVARVTASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEA 630
Cdd:COG0840 444 VEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEE 523
|
490
....*....|
gi 1995340955 631 MSTLVDRFIV 640
Cdd:COG0840 524 LQELVSRFKL 533
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
321-638 |
5.67e-64 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 220.98 E-value: 5.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 321 LVISLVALLIAIAFAVMVarSIQQQLNGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKSGAVV 399
Cdd:PRK15041 199 VMIVVLAVIFAVWFGIKA--SLVAPMNRLIDSIRHIaGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 400 LRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMAEIRS 479
Cdd:PRK15041 277 IYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDIST 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 480 SSEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGVARVT 559
Cdd:PRK15041 357 SSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVE 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1995340955 560 ASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEAMSTLVDRF 638
Cdd:PRK15041 437 SAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
317-638 |
7.35e-64 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 220.65 E-value: 7.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 317 WQsFLVISLVALLIAIAFAVMVARSIQQQLNGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKS 395
Cdd:PRK15048 192 WQ-LAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIaGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVRE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 396 GAVVLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMA 475
Cdd:PRK15048 271 GSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMH 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 476 EIRSSSEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGV 555
Cdd:PRK15048 351 EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 556 ARVTASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEAMSTLV 635
Cdd:PRK15048 431 VLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAV 510
|
...
gi 1995340955 636 DRF 638
Cdd:PRK15048 511 SAF 513
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
263-640 |
6.99e-62 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 214.55 E-value: 6.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 263 TAFNKAAEGGFGVNPTDWfnlqtqrietlQKVENRAVDALQEHAALLAHNARVdwqSFLVISLVALLIAIAFAVMVARSI 342
Cdd:PRK09793 149 TAPVQGSQNAFDVNFEAW-----------QLEINHVLEAASAQSQRNYQISAL---VFISMIIVAAIYISSALWWTRKMI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 343 QQQL---NGTLKTIAemDGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKSGAVVLRSASSDIAAGNQDLAQRTD 419
Cdd:PRK09793 215 VQPLaiiGSHFDSIA--AGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 420 EQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMAEIRSSSEQISQIVASIDEISFQTN 499
Cdd:PRK09793 293 QQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTN 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 500 LLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGVARVTASGTALKAAAENTGRMKQYV 579
Cdd:PRK09793 373 ILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIM 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1995340955 580 SDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEAMSTLVDRFIV 640
Cdd:PRK09793 453 GEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
392-638 |
9.62e-53 |
|
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: 182.10 E-value: 9.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 392 EIKSGAVVLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEAS 471
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 472 QSMAEIRSSSEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELIN------ 545
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 546 --------QNMDKIGEGVARVTASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQA 617
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|.
gi 1995340955 618 ASASQMLDGQSEAMSTLVDRF 638
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
419-618 |
4.02e-44 |
|
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: 156.63 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 419 DEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMAEIRSSSEQISQIVASIDEISFQT 498
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 499 NLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGVARVTASGTALKAAAENTGRMKQY 578
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1995340955 579 VSDIARAANEQSLGVSQVHQALNQLEQVTQQNAALVSQAA 618
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
|
|
| NIT |
pfam08376 |
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ... |
59-303 |
2.65e-40 |
|
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.
Pssm-ID: 462453 [Multi-domain] Cd Length: 227 Bit Score: 146.87 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 59 VHQLQSERGMSAGFIGARGQKfrddlKFRDDLAAQRQLTDKVLATFKRLLTDTNkdlLQGNIAAPLKTFNESIQFLDSTR 138
Cdd:pfam08376 1 VHALQKERGLSAGYLASGGGG-----RFAAELAAQRAATDAALAALRAALAELA---LPARLADRLAALLRALDQLPALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 139 TAISELTIDSPKASQFYTQTISDVLKFVGGMGHLSTSGSMVNELAAYYSLLNLKEQAGVERALLSNIFSMDRFDDGQFSM 218
Cdd:pfam08376 73 RQVDAGALSALEALAAYTELIAALLDLVDELAAGSPDPELARQLRALAALLRAKEAAGQERALLAAALAAGRFTAAEYRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 219 FSDVVGQQDAWLTAARSFSTPVQAAELDKSLQSAEATRALELRETAfnkaaeggfgVNPTDWFNLQTQRIETLQKVENRA 298
Cdd:pfam08376 153 FLSLVAAQRAALAEFRAAATPEQRALYDATVTGPAVAAAERLRDRL----------VDAAAWFAASTARIDLLREVEDRL 222
|
....*
gi 1995340955 299 VDALQ 303
Cdd:pfam08376 223 ADDLA 227
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
461-607 |
3.51e-32 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 122.54 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 461 LEANRVSNEASQSMAEIRSSSEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNLSQRCAREASQI 540
Cdd:pfam00015 12 QDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 541 RELIN--------------QNMDKIGEGVARVTASGTALKAAAENTGRMKQYVSDIARAANEQSLGVSQVHQALNQLEQV 606
Cdd:pfam00015 92 EALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQV 171
|
.
gi 1995340955 607 T 607
Cdd:pfam00015 172 T 172
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
319-557 |
2.46e-10 |
|
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: 63.06 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 319 SFLVISLVALLIAIAFAVMVARSIQQQLNGTLKTIAE-----MDGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEI 393
Cdd:COG5000 6 LFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEatravAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 394 KSGAV----VLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNE 469
Cdd:COG5000 86 EERRRyletILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQEEIELTRD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 470 ASQSMAeIRSSSEQISQIVASIDEISfqtnllalnAAVEAARAGELGKGFAVVATEVRN-----------LSQRCAREAS 538
Cdd:COG5000 166 GRRTLL-VRASPLRDDGYVIVFDDIT---------ELLRAERLAAWGELARRIAHEIKNpltpiqlsaerLRRKLADKLE 235
|
250
....*....|....*....
gi 1995340955 539 QIRELINQNMDKIGEGVAR 557
Cdd:COG5000 236 EDREDLERALDTIIRQVDR 254
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
107-640 |
5.58e-05 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 46.26 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 107 LLTDTNKDLLQGNIAAPLKTFNESIQFLDSTRTAISELTIDSPKASQFYTQTISDVLKFVGGMGHLSTSGSMVNELAAYY 186
Cdd:COG2770 1 LLLLLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 187 SLLNLKEQAGVERALLSNIFSMDRFDDGQFSMFSDVVGQQDAWLTAARSFSTPVQAAELDKSLQSAEATRALELRETAFN 266
Cdd:COG2770 81 LLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 267 KAAEGGFGVNPTDWFNLQTQRIETLQKVENRAVDALQEHAALLAHNARVDWQSFLVISLVALLIAIAFAVMVARSIQQQL 346
Cdd:COG2770 161 AAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 347 NGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQEIKSGAVVLRSASSDIAAGNQDLAQRTDEQAASI 425
Cdd:COG2770 241 RRLAEAARRIaAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 426 VETAASMEQISTAITQTADNASEAERLIHSMERDVLEANRVSNEASQSMAEIRSSSEQISQIVASIDEISFQTNLLALNA 505
Cdd:COG2770 321 LLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 506 AVEAARAGELGKGFAVVATEVRNLSQRCAREASQIRELINQNMDKIGEGVARVTASGTALKAAAENTGRMKQYVSDIARA 585
Cdd:COG2770 401 ALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLL 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1995340955 586 ANEQSLGVSQVHQALNQLEQVTQQNAALVSQAASASQMLDGQSEAMSTLVDRFIV 640
Cdd:COG2770 481 LAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLEL 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
319-546 |
6.98e-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: 45.53 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 319 SFLVISLVALLIAIAFAVmVARSIQQQLNGTLKTIAEMDGDLTRRLDVPGS--DELSALNRAYNQAIENIQHIVQEIKSG 396
Cdd:COG4942 3 KLLLLALLLALAAAAQAD-AAAEAEAELEQLQQEIAELEKELAALKKEEKAllKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 397 AVVLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEAERLIHSMerdvleaNRVSNEASQSMAE 476
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL-------KYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 477 IRSSSEQISQIVASIDEIsfQTNLLALNAAVEAARAgELGKGFAVVATEVRNLSQRCAREASQIRELINQ 546
Cdd:COG4942 155 LRADLAELAALRAELEAE--RAELEALLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| HAMP |
pfam00672 |
HAMP domain; |
337-388 |
2.43e-04 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 39.14 E-value: 2.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1995340955 337 MVARSIQQQLNGTLKTIAEM-DGDLTRRLDVPGSDELSALNRAYNQAIENIQH 388
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIaSGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
344-391 |
2.77e-04 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 39.15 E-value: 2.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1995340955 344 QQLNGTLKTIAemDGDLTRRLDVPGSDELSALNRAYNQAIENIQHIVQ 391
Cdd:smart00304 8 RRLAEAAQRIA--DGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
344-386 |
1.88e-03 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the 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: 36.27 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1995340955 344 QQLNGTLKTIAEmdGDLTRRLDVPGSDELSALNRAYNQAIENI 386
Cdd:cd06225 5 RRLTEAARRIAE--GDLDVRVPVRSKDEIGELARAFNQMAERL 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-632 |
7.76e-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: 39.65 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 370 DELSALNRAYNQAIENIQHIVQEIKSGAVVLRSASSDIAAGNQDLAQRTDEQAASIVETAASMEQISTAITQTADNASEA 449
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 450 ERLIHSMERDVLEANrvsneasqsmaeirsssEQISQIVASIDEISFQTNLLALNAAVEAARAGELGKGFAVVATEVRNL 529
Cdd:TIGR02168 781 EAEIEELEAQIEQLK-----------------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995340955 530 SQRcAREASQIRELINQNMDKIGEGVARVTAsgtALKAAAENTGRMKQYVSDIARAANEQSLGV----SQVHQALNQLEQ 605
Cdd:TIGR02168 844 EEQ-IEELSEDIESLAAEIEELEELIEELES---ELEALLNERASLEEALALLRSELEELSEELreleSKRSELRRELEE 919
|
250 260
....*....|....*....|....*..
gi 1995340955 606 VTQQNAALVSQAASASQMLDGQSEAMS 632
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
|