|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
299-641 |
1.28e-84 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 275.36 E-value: 1.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 299 IVGEVDKSVLLSSVTAMRDRFLLAGVVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLID 378
Cdd:COG0840 163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 379 AINGIGGGLQKIVLQVREAAGEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETS 458
Cdd:COG0840 243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 459 LAVHQGGETVTHAVSTMDDIR--------------EASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVA 524
Cdd:COG0840 323 ELAEEGGEVVEEAVEGIEEIResveetaetieelgESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 525 QEVRALAGRSANAVKEIEQLIGD--------------TLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQ 590
Cdd:COG0840 403 DEVRKLAERSAEATKEIEELIEEiqseteeaveameeGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2728967322 591 SAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSLFQL 641
Cdd:COG0840 483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
|
|
| Cache_3-Cache_2 |
pfam17201 |
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ... |
34-317 |
2.52e-78 |
|
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: 251.11 E-value: 2.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 34 SQKASQQLEALAVEDLHNQSTGMVDMVQMFNTSLSEEVESYTRLFTTFLPQPLNSDPSQPQTINGLSVPLLKGGDTGL-- 111
Cdd:pfam17201 1 SRSAKGEVRALAESDLEEQVQDLADMLETQDESLRESVDSDLNVFRKLLPGSWRAVNQFTVDVGGVSLPVLYLGGTWLgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 112 ----HENNTLSDDFLNRTGAISTLFVRSGNDFVRVATSLRKENGERAMGTVLDASSPAFAAVNKGEVYRGLALLFGKRYI 187
Cdd:pfam17201 81 nrdpNKNFPLVDEFTELTGGTATVFQRMNDDLLRVATSVKKEDGSRAIGTYIPASSPVYKAVLAGETYVGRAKVFGKWYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 188 TQYQPVKNAEGQVIAIVFVGVDITHSWNVMREKILNRRLGESGHFFVLDrSNGKTRGQYLFHAGEEGQ---LPKWDDATQ 264
Cdd:pfam17201 161 TAYEPIRDADGKVIGILYVGVPQDEALASLRKAIKKVKIGKTGYLYVLD-GKGDQKGKFIVHPTLEGKnilDAKDADGEP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2728967322 265 --QQLLGDKPGTLE---RVSDDGRTLKMAYTPLQGWNWTIVGEVDKSVLLSSVTAMRD 317
Cdd:pfam17201 240 fvKKLLQKKVGSLEypwKADAAGRDKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLN 297
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
320-641 |
4.62e-78 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 258.40 E-value: 4.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 320 LLAGVVLSILFAGLFVvlIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVREAAG 399
Cdd:PRK15048 196 VIALVVVLILLVAWYG--IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSD 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 400 EIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIR 479
Cdd:PRK15048 274 AIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 480 EASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALS 559
Cdd:PRK15048 354 DSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 560 EKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSLF 639
Cdd:PRK15048 434 ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAF 513
|
..
gi 2728967322 640 QL 641
Cdd:PRK15048 514 RL 515
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
393-640 |
7.96e-65 |
|
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: 214.07 E-value: 7.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 393 QVREAAGEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAV 472
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 473 STMDDIREASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGD----- 547
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 548 ---------TLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRS 618
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|..
gi 2728967322 619 EQTAQTLREKGSHLAQLVSLFQ 640
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
422-613 |
1.54e-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: 182.05 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 422 QASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIREASKRIEDITRVIESIAFQTNI 501
Cdd:cd11386 3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 502 LALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVT 581
Cdd:cd11386 83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162
|
170 180 190
....*....|....*....|....*....|..
gi 2728967322 582 EINHASREQSAGIGQVNLAMTHIGEASHINAD 613
Cdd:cd11386 163 EIVASVEEVADGIQEISAATQEQSASTQEIAA 194
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
463-604 |
1.65e-43 |
|
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: 153.74 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 463 QGGETVTHAVSTMDDIREASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIE 542
Cdd:pfam00015 13 DGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2728967322 543 QLIG--------------DTLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHI 604
Cdd:pfam00015 93 ALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARM 168
|
|
| PDC2_MCP_like |
cd12912 |
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ... |
219-306 |
5.27e-09 |
|
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: 53.54 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 219 EKILNRRLGESGHFFVLDRSngktrGQYLFHAGEE------GQLPKWDDATQQQLLGDKPGTLErVSDDGRTLKMAYTPL 292
Cdd:cd12912 4 EIISSIKIGETGYAFLVDKD-----GTIIAHPDKElvgkkiSDDEAAEEELAKKMLAGKSGSVE-YTFNGEKKYVAYAPI 77
|
90
....*....|....
gi 2728967322 293 QGWNWTIVGEVDKS 306
Cdd:cd12912 78 PGTGWSLVVVVPES 91
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
299-641 |
1.28e-84 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 275.36 E-value: 1.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 299 IVGEVDKSVLLSSVTAMRDRFLLAGVVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLID 378
Cdd:COG0840 163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 379 AINGIGGGLQKIVLQVREAAGEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETS 458
Cdd:COG0840 243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 459 LAVHQGGETVTHAVSTMDDIR--------------EASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVA 524
Cdd:COG0840 323 ELAEEGGEVVEEAVEGIEEIResveetaetieelgESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 525 QEVRALAGRSANAVKEIEQLIGD--------------TLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQ 590
Cdd:COG0840 403 DEVRKLAERSAEATKEIEELIEEiqseteeaveameeGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2728967322 591 SAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSLFQL 641
Cdd:COG0840 483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
|
|
| Cache_3-Cache_2 |
pfam17201 |
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ... |
34-317 |
2.52e-78 |
|
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: 251.11 E-value: 2.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 34 SQKASQQLEALAVEDLHNQSTGMVDMVQMFNTSLSEEVESYTRLFTTFLPQPLNSDPSQPQTINGLSVPLLKGGDTGL-- 111
Cdd:pfam17201 1 SRSAKGEVRALAESDLEEQVQDLADMLETQDESLRESVDSDLNVFRKLLPGSWRAVNQFTVDVGGVSLPVLYLGGTWLgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 112 ----HENNTLSDDFLNRTGAISTLFVRSGNDFVRVATSLRKENGERAMGTVLDASSPAFAAVNKGEVYRGLALLFGKRYI 187
Cdd:pfam17201 81 nrdpNKNFPLVDEFTELTGGTATVFQRMNDDLLRVATSVKKEDGSRAIGTYIPASSPVYKAVLAGETYVGRAKVFGKWYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 188 TQYQPVKNAEGQVIAIVFVGVDITHSWNVMREKILNRRLGESGHFFVLDrSNGKTRGQYLFHAGEEGQ---LPKWDDATQ 264
Cdd:pfam17201 161 TAYEPIRDADGKVIGILYVGVPQDEALASLRKAIKKVKIGKTGYLYVLD-GKGDQKGKFIVHPTLEGKnilDAKDADGEP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2728967322 265 --QQLLGDKPGTLE---RVSDDGRTLKMAYTPLQGWNWTIVGEVDKSVLLSSVTAMRD 317
Cdd:pfam17201 240 fvKKLLQKKVGSLEypwKADAAGRDKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLN 297
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
320-641 |
4.62e-78 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 258.40 E-value: 4.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 320 LLAGVVLSILFAGLFVvlIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVREAAG 399
Cdd:PRK15048 196 VIALVVVLILLVAWYG--IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSD 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 400 EIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIR 479
Cdd:PRK15048 274 AIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 480 EASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALS 559
Cdd:PRK15048 354 DSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 560 EKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSLF 639
Cdd:PRK15048 434 ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAF 513
|
..
gi 2728967322 640 QL 641
Cdd:PRK15048 514 RL 515
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
324-642 |
6.39e-72 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 242.17 E-value: 6.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 324 VVLSILFAGLFVVL-----IRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVREAA 398
Cdd:PRK15041 195 ILVGVMIVVLAVIFavwfgIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 399 GEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDI 478
Cdd:PRK15041 275 NAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 479 REASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHAL 558
Cdd:PRK15041 355 STSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 559 SEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSL 638
Cdd:PRK15041 435 VESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAV 514
|
....
gi 2728967322 639 FQLK 642
Cdd:PRK15041 515 FRIQ 518
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
324-642 |
4.41e-66 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 226.11 E-value: 4.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 324 VVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVREAAGEIHL 403
Cdd:PRK09793 196 IIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 404 GTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIREASK 483
Cdd:PRK09793 276 GIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 484 RIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALSEKTR 563
Cdd:PRK09793 356 KIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAA 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2728967322 564 LAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSLFQLK 642
Cdd:PRK09793 436 ATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLE 514
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
393-640 |
7.96e-65 |
|
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: 214.07 E-value: 7.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 393 QVREAAGEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAV 472
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 473 STMDDIREASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGD----- 547
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 548 ---------TLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRS 618
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|..
gi 2728967322 619 EQTAQTLREKGSHLAQLVSLFQ 640
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
422-613 |
1.54e-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: 182.05 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 422 QASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIREASKRIEDITRVIESIAFQTNI 501
Cdd:cd11386 3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 502 LALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVT 581
Cdd:cd11386 83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162
|
170 180 190
....*....|....*....|....*....|..
gi 2728967322 582 EINHASREQSAGIGQVNLAMTHIGEASHINAD 613
Cdd:cd11386 163 EIVASVEEVADGIQEISAATQEQSASTQEIAA 194
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
463-604 |
1.65e-43 |
|
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: 153.74 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 463 QGGETVTHAVSTMDDIREASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIE 542
Cdd:pfam00015 13 DGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2728967322 543 QLIG--------------DTLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHI 604
Cdd:pfam00015 93 ALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARM 168
|
|
| sCache_3_3 |
pfam17202 |
Single cache domain 3; |
111-211 |
9.98e-31 |
|
Single cache domain 3;
Pssm-ID: 465379 [Multi-domain] Cd Length: 104 Bit Score: 115.72 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 111 LHENNTLSDDFLNRTGAISTLFVrsgnDFVRVATSLRKENGERAMGTVLDASsPAFAAVNKGEVYRGLALLFGKRYITQY 190
Cdd:pfam17202 3 INGNFELVDKIKELTGGTATIFL----GDTRIATTVKDEDGKRAVGTKLSDE-VAEAVLKKGETYRGRADILGKWYYTAY 77
|
90 100
....*....|....*....|.
gi 2728967322 191 QPVKNAEGQVIAIVFVGVDIT 211
Cdd:pfam17202 78 EPLKDADGKVIGMLFVGIPEE 98
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
320-496 |
1.14e-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: 63.83 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 320 LLAGVVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVREAAG 399
Cdd:COG5000 11 LLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 400 EI-----HLGTNALAADTGEISEQINKQASSVEETSAS------------MEQLAATVQQNAANMEQTQ---QLVGETSL 459
Cdd:COG5000 91 YLetileNLPAGVIVLDADGRITLANPAAERLLGIPLEeligkpleellpELDLAELLREALERGWQEEielTRDGRRTL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 2728967322 460 AVHQGGETVTHAVSTMDDIRE--ASKRIEDITRVIESIA 496
Cdd:COG5000 171 LVRASPLRDDGYVIVFDDITEllRAERLAAWGELARRIA 209
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
259-396 |
2.17e-09 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 60.03 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 259 WDDATQQQLLGDKPGTLERVSDDGRTLKMAYTPLQGWNWTIVGEVDKSVLLSSVTAMRdRFLLAGVVLSILFAGLFVVLI 338
Cdd:COG2972 99 LLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSLR-RLILLIILLLLLLALLLSYLL 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2728967322 339 RRVLTRPLRNVIHLARQYAAGDLrSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVRE 396
Cdd:COG2972 178 SRSITRPIKRLKKAMKKVEKGDL-VRLEVSGNDEIGILARSFNEMVERIKELIEEVYE 234
|
|
| dCache_1 |
pfam02743 |
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ... |
111-302 |
3.87e-09 |
|
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460673 [Multi-domain] Cd Length: 237 Bit Score: 57.73 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 111 LHENNTLSDDFLNRTGAISTLFVRSGNDFVRVAtslrkeNGERAMGTVLDAS-SPAFAAVNKGE-----VYRGLALLF-- 182
Cdd:pfam02743 50 AEEELAKLESLLRSNPGISSIYLVDADGRVLAS------SDESPSYPGLDVSeRPWYKEALKGGggiiwVFSSPYPSSes 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 183 GKRYITQYQPVKNAEGQVIAIVFVGVDIthswNVMREKILNRRLGESGHFFVLDRsngktRGQYLFHAGEE---GQLPKW 259
Cdd:pfam02743 124 GEPVLTIARPIYDDDGEVIGVLVADLDL----DTLQELLSQIKLGEGGYVFIVDS-----DGRILAHPLGKnlrSLLAPF 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2728967322 260 DDATQQQLLGDKPGTLERVSDDGRTLKMAYTPLQGWNWTIVGE 302
Cdd:pfam02743 195 LGKSLADALPGSGITEIAVDLDGEDYLVAYAPIPGTGWTLVVV 237
|
|
| PDC2_MCP_like |
cd12912 |
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ... |
219-306 |
5.27e-09 |
|
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: 53.54 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 219 EKILNRRLGESGHFFVLDRSngktrGQYLFHAGEE------GQLPKWDDATQQQLLGDKPGTLErVSDDGRTLKMAYTPL 292
Cdd:cd12912 4 EIISSIKIGETGYAFLVDKD-----GTIIAHPDKElvgkkiSDDEAAEEELAKKMLAGKSGSVE-YTFNGEKKYVAYAPI 77
|
90
....*....|....
gi 2728967322 293 QGWNWTIVGEVDKS 306
Cdd:cd12912 78 PGTGWSLVVVVPES 91
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
343-381 |
1.01e-08 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the 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: 1.01e-08
10 20 30
....*....|....*....|....*....|....*....
gi 2728967322 343 TRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAIN 381
Cdd:cd06225 1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFN 39
|
|
| PDC2_HK_sensor |
cd18774 |
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ... |
217-305 |
1.80e-08 |
|
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: 52.06 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 217 MREKILNRRLGESGHFFVLDRSngktrGQYLFHAGEE----GQLPKWDDATQQQLLGDKPGTLERVSDDGRTLKMAYTPL 292
Cdd:cd18774 2 LSDLLSSIKLGETGYAFLVDSD-----GTILAHPPKElvgkGKSLDDLALLAALLLAGESGTFEYTSDDGVERLVAYRPV 76
|
90
....*....|...
gi 2728967322 293 QGWNWTIVGEVDK 305
Cdd:cd18774 77 PGTPWVVVVGVPE 89
|
|
| COG4564 |
COG4564 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
286-623 |
2.06e-08 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 443621 [Multi-domain] Cd Length: 510 Bit Score: 56.96 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 286 KMAY-TPLQGWNWTIVGEVDKSVLLSSVTAMRDRFLLAGVVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSS 364
Cdd:COG4564 143 KLSYvKKFPPWDWVIGTGVYLDDIEAAFAAAALELLLLLALLLALALALLLLVLAALAGLLLASALEGELNLAGALAALL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 365 LPVTrhDEVGQLIDAINGIGGGLQKIVLQVREAAGEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNA 444
Cdd:COG4564 223 LAAA--AELLAALLLIGAAAGALLALAEAVAAVLAEALAAAAAAAAASAAASSAALAAAAAEAEAALAASEASAAAALAA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 445 ANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIREASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVA 524
Cdd:COG4564 301 AAAAAAAAAAAAAAAEAAAAAAAAAAAAAAAAASVADVAALAAAAAAAAAIAALAAAAAAAAAAAAAAAAIAAAAAAAAA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 525 QEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHI 604
Cdd:COG4564 381 AAAAAAAAAAEAAAAAAAAATAAAALEAVAAAAAAAAAAAAAEAAAAEVEAAAAITAIILEAAAAAAAAIEAEEAAAVAA 460
|
330
....*....|....*....
gi 2728967322 605 GEASHINADRISRSEQTAQ 623
Cdd:COG4564 461 AAALAAEAAAAAAAAAEAA 479
|
|
| HAMP |
pfam00672 |
HAMP domain; |
337-381 |
4.16e-08 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 49.93 E-value: 4.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2728967322 337 LIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAIN 381
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFN 45
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
241-641 |
1.49e-07 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 54.12 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 241 KTRGQYLFHAGEEGQLPKWDDATQQQLLGDKPGTLERVSDDGRTLKMAYTPLQGWNWTIVGEVDKSVLLSSVTAMRDRFL 320
Cdd:COG3850 41 TLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLLLLAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 321 LAGVVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIVLQVREAAGE 400
Cdd:COG3850 121 LLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 401 IHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGETVTHAVSTMDDIRE 480
Cdd:COG3850 201 EAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 481 ASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIGDTLRKVSEGHALSE 560
Cdd:COG3850 281 LELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 561 KTRLAMDDIIIHIDNISQLVTEINHASREQSAGIGQVNLAMTHIGEASHINADRISRSEQTAQTLREKGSHLAQLVSLFQ 640
Cdd:COG3850 361 ALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEALAARG 440
|
.
gi 2728967322 641 L 641
Cdd:COG3850 441 L 441
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
340-391 |
7.60e-07 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 46.47 E-value: 7.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2728967322 340 RVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKIV 391
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
307-594 |
2.59e-05 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 47.42 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 307 VLLSSVTAMRDRFLLAGVVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGG 386
Cdd:COG2770 201 VVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADS 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 387 LQKIVLQVREAAGEIHLGTNALAADTGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQTQQLVGETSLAVHQGGE 466
Cdd:COG2770 281 LRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 467 TVTHAVSTMDDIREASKRIEDITRVIESIAFQTNILALNAAVEAARAGEHGKGFAVVAQEVRALAGRSANAVKEIEQLIG 546
Cdd:COG2770 361 LLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALEL 440
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2728967322 547 DTLRKVSEGHALSEKTRLAMDDIIIHIDNISQLVTEINHASREQSAGI 594
Cdd:COG2770 441 AAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALE 488
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
371-452 |
1.00e-04 |
|
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: 44.58 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 371 DEVGQLIDAINGIGGGLQKIVLQVREAAGEIhlgtnalaadtGEISEQINKQASSVEETSASMEQLAATVQQNAANMEQT 450
Cdd:smart00283 172 SEVEEGVELVEETGDALEEIVDSVEEIADLV-----------QEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
..
gi 2728967322 451 QQ 452
Cdd:smart00283 241 SA 242
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
320-376 |
1.28e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 41.98 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2728967322 320 LLAGVVLSILFAGLFVVL-IRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQL 376
Cdd:COG4192 328 LLAIALLSLLLAVLINYFyVRRRLVKRLNALSDAMAAIAAGDLDVPIPVDGNDEIGRI 385
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
372-451 |
2.78e-03 |
|
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: 39.53 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 372 EVGQLIDAINGiggGLQKIVLQVREAAGEIHLGTnALAADTG----EISEQINKQASSVEETSASMEQLAATVQQNAANM 447
Cdd:cd11386 121 EIEELIEEIQE---QTEEAVEAMEETSEEVEEGV-ELVEETGrafeEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
|
....
gi 2728967322 448 EQTQ 451
Cdd:cd11386 197 EEIA 200
|
|
| sCache_3_2 |
pfam17203 |
Single cache domain 3; This domain is associated to sensor histidine kinases and recognizes ... |
164-212 |
3.61e-03 |
|
Single cache domain 3; This domain is associated to sensor histidine kinases and recognizes citrate and TCA cycle intermediates, Ag(II), Zn(II), Mg(II) (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435783 [Multi-domain] Cd Length: 140 Bit Score: 38.16 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2728967322 164 PAFAAVNKGEVYRGLALLFGKRYITQYQPVKNAEGQVIAIVFVGVDITH 212
Cdd:pfam17203 82 ATAPALTAGRSYTGTVTGTLGPSLDAKLPIFDADGRVIGIVSVGVKQDS 130
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
324-425 |
4.01e-03 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 40.40 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728967322 324 VVLSILFAGLFVVLIRRVLTRPLRNVIHLARQYAAGDLRSSLPVTRHDEVGQLIDAINGIGGGLQKivlQVREAAGEIHL 403
Cdd:PRK15347 303 LLILVLLTSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNE---QYDTLENKVAE 379
|
90 100
....*....|....*....|..
gi 2728967322 404 GTNALaADTGEISEQINKQASS 425
Cdd:PRK15347 380 RTQAL-AEAKQRAEQANKRKSE 400
|
|
|