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Conserved domains on  [gi|1122544240|ref|WP_074093152|]
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methyl-accepting chemotaxis protein [Paenibacillus xylanexedens]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 12036995)

methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
305-666 2.66e-89

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 288.07  E-value: 2.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVnsset 384
Cdd:COG0840   200 LLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAA----- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 tkateqvalITEESAAGLEKQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRF 464
Cdd:COG0840   275 ---------SAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRES 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGA 544
Cdd:COG0840   346 VEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEE 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIdqihaisetnad 624
Cdd:COG0840   426 IQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI------------ 493
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1122544240 625 gtENISAATEEQVASMQEISSSADSLAHLAHKLQKLVEQFKL 666
Cdd:COG0840   494 --EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
46-272 7.72e-20

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: 89.32  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  46 VEEKMYENAISSVTVLNQTIDQIIGATRKNVDFLASQLdagNVGPNQGDETDTIRTLLDAYKETHDDVELASIGTDQGVY 125
Cdd:pfam02743   3 IKEQAEEQLLSLAKQLAENIESYLDSLEEILELLASNP---DLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 126 INSPVTAVNKEGYDPRERPWYQAATQNKD--VPTIITPYLSSNTGNVVASVAQTSTDGH----GVVSVSLSLEALSKTVN 199
Cdd:pfam02743  80 LASSDESPSYPGLDVSERPWYKEALKGGGgiIWVFSSPYPSSESGEPVLTIARPIYDDDgeviGVLVADLDLDTLQELLS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1122544240 200 STKIGEKGYIYIIDNANKIIVHPTEKPGTEGTmAPYKDIF------AQKNGSLTYTLNGNQEHAFFSTNETTGWTVVGV 272
Cdd:pfam02743 160 QIKLGEGGYVFIVDSDGRILAHPLGKNLRSLL-APFLGKSladalpGSGITEIAVDLDGEDYLVAYAPIPGTGWTLVVV 237
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
305-666 2.66e-89

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 288.07  E-value: 2.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVnsset 384
Cdd:COG0840   200 LLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAA----- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 tkateqvalITEESAAGLEKQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRF 464
Cdd:COG0840   275 ---------SAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRES 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGA 544
Cdd:COG0840   346 VEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEE 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIdqihaisetnad 624
Cdd:COG0840   426 IQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI------------ 493
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1122544240 625 gtENISAATEEQVASMQEISSSADSLAHLAHKLQKLVEQFKL 666
Cdd:COG0840   494 --EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
390-665 4.60e-60

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: 4.60e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  390 QVALITEESAAGLEKQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRFVQGMA 469
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  470 DTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEI 549
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  550 SMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNAdgteni 629
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETA------ 234
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1122544240  630 saateeqvASMQEISSSADSLAHLAHKLQKLVEQFK 665
Cdd:smart00283 235 --------AMSEEISAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
418-615 6.95e-52

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: 177.81  E-value: 6.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 418 ELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRFVQGMADTAGRLEQHSTSIGEMVSVITDIAAQTN 497
Cdd:cd11386     2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 498 LLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEISMANHNVQIGQQDVSNGIRAVQFADESF 577
Cdd:cd11386    82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1122544240 578 AQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQI 615
Cdd:cd11386   162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
305-642 2.80e-40

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 155.50  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSET 384
Cdd:PRK15041  212 FGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDL 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 TKATEQVALITEESAAGLEKQTSNLKHTAlqmkelaggvgqvtNSTQQVSEAAMQASELADKGNATmqtavsemssVSRF 464
Cdd:PRK15041  292 SSRTEQQAASLEETAASMEQLTATVKQNA--------------ENARQASHLALSASETAQRGGKV----------VDNV 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRleqhSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSlsgQKIVEMVGA 544
Cdd:PRK15041  348 VQTMRDISTS----SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSA---QAAREIKSL 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISmanhnvqigqqDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNAD 624
Cdd:PRK15041  421 IEDSVG-----------KVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAA 489
                         330       340
                  ....*....|....*....|.
gi 1122544240 625 GTENISAAT---EEQVASMQE 642
Cdd:PRK15041  490 LVEESAAAAaalEEQASRLTE 510
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
434-619 3.01e-37

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: 136.79  E-value: 3.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 434 SEAAMQASELADKGNATMQTAVSEMssvsrfvqgmadtaGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEH 513
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQM--------------EQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 514 GRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLEN 593
Cdd:pfam00015  67 GRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQE 146
                         170       180
                  ....*....|....*....|....*.
gi 1122544240 594 IAAASQQMSASTAEVVQSIDQIHAIS 619
Cdd:pfam00015 147 IAAASDEQSAGIDQVNQAVARMDQVT 172
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
46-272 7.72e-20

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: 89.32  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  46 VEEKMYENAISSVTVLNQTIDQIIGATRKNVDFLASQLdagNVGPNQGDETDTIRTLLDAYKETHDDVELASIGTDQGVY 125
Cdd:pfam02743   3 IKEQAEEQLLSLAKQLAENIESYLDSLEEILELLASNP---DLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 126 INSPVTAVNKEGYDPRERPWYQAATQNKD--VPTIITPYLSSNTGNVVASVAQTSTDGH----GVVSVSLSLEALSKTVN 199
Cdd:pfam02743  80 LASSDESPSYPGLDVSERPWYKEALKGGGgiIWVFSSPYPSSESGEPVLTIARPIYDDDgeviGVLVADLDLDTLQELLS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1122544240 200 STKIGEKGYIYIIDNANKIIVHPTEKPGTEGTmAPYKDIF------AQKNGSLTYTLNGNQEHAFFSTNETTGWTVVGV 272
Cdd:pfam02743 160 QIKLGEGGYVFIVDSDGRILAHPLGKNLRSLL-APFLGKSladalpGSGITEIAVDLDGEDYLVAYAPIPGTGWTLVVV 237
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
194-274 2.12e-17

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: 77.42  E-value: 2.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 194 LSKTVNSTKIGEKGYIYIIDNANKIIVHPTEK-------PGTEGTMAPYKDIFAQKNGSLTYTLNGNQEHAFFSTNETTG 266
Cdd:cd12912     2 LSEIISSIKIGETGYAFLVDKDGTIIAHPDKElvgkkisDDEAAEEELAKKMLAGKSGSVEYTFNGEKKYVAYAPIPGTG 81

                  ....*...
gi 1122544240 267 WTVVGVID 274
Cdd:cd12912    82 WSLVVVVP 89
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
305-666 2.66e-89

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 288.07  E-value: 2.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVnsset 384
Cdd:COG0840   200 LLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAA----- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 tkateqvalITEESAAGLEKQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRF 464
Cdd:COG0840   275 ---------SAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRES 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGA 544
Cdd:COG0840   346 VEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEE 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIdqihaisetnad 624
Cdd:COG0840   426 IQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI------------ 493
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1122544240 625 gtENISAATEEQVASMQEISSSADSLAHLAHKLQKLVEQFKL 666
Cdd:COG0840   494 --EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
390-665 4.60e-60

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: 4.60e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  390 QVALITEESAAGLEKQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRFVQGMA 469
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  470 DTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEI 549
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  550 SMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNAdgteni 629
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETA------ 234
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1122544240  630 saateeqvASMQEISSSADSLAHLAHKLQKLVEQFK 665
Cdd:smart00283 235 --------AMSEEISAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
418-615 6.95e-52

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: 177.81  E-value: 6.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 418 ELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRFVQGMADTAGRLEQHSTSIGEMVSVITDIAAQTN 497
Cdd:cd11386     2 ELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 498 LLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEISMANHNVQIGQQDVSNGIRAVQFADESF 577
Cdd:cd11386    82 LLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1122544240 578 AQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQI 615
Cdd:cd11386   162 EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
305-642 2.80e-40

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 155.50  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSET 384
Cdd:PRK15041  212 FGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDL 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 TKATEQVALITEESAAGLEKQTSNLKHTAlqmkelaggvgqvtNSTQQVSEAAMQASELADKGNATmqtavsemssVSRF 464
Cdd:PRK15041  292 SSRTEQQAASLEETAASMEQLTATVKQNA--------------ENARQASHLALSASETAQRGGKV----------VDNV 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRleqhSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSlsgQKIVEMVGA 544
Cdd:PRK15041  348 VQTMRDISTS----SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSA---QAAREIKSL 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISmanhnvqigqqDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNAD 624
Cdd:PRK15041  421 IEDSVG-----------KVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAA 489
                         330       340
                  ....*....|....*....|.
gi 1122544240 625 GTENISAAT---EEQVASMQE 642
Cdd:PRK15041  490 LVEESAAAAaalEEQASRLTE 510
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
305-645 3.78e-40

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 154.84  E-value: 3.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSET 384
Cdd:PRK09793  208 WWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDL 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 TKATEQvaliteesaaglekQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNatmqtavsemSSVSRF 464
Cdd:PRK09793  288 SSRTEQ--------------QAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGG----------VQVSTM 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRleqhSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAeqsSLSGQKIVEMVGA 544
Cdd:PRK09793  344 THTMQEIATS----SQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLA---SRSAQAAKEIKGL 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISmanhNVQIGQQDVSNgiravqfADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNAD 624
Cdd:PRK09793  417 IEESVN----RVQQGSKLVNN-------AAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNAS 485
                         330       340
                  ....*....|....*....|.
gi 1122544240 625 GTENISAATEEQVASMQEISS 645
Cdd:PRK09793  486 LVEEAAVATEQLANQADHLSS 506
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
305-666 4.30e-38

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 149.00  E-value: 4.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSET 384
Cdd:PRK15048  210 YGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDL 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 TKATEQVALITEESAAGLEKQTSNLKHTAlqmkelaggvgqvtNSTQQVSEAAMQASELADKGnatmqtavsemssvSRF 464
Cdd:PRK15048  290 SSRTEQQASALEETAASMEQLTATVKQNA--------------DNARQASQLAQSASDTAQHG--------------GKV 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMvga 544
Cdd:PRK15048  342 VDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKAL--- 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISManhnvqigqqdVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSastaevvQSIDQIH-AISEtna 623
Cdd:PRK15048  419 IEDSVSR-----------VDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQS-------RGIDQVAlAVSE--- 477
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1122544240 624 dgtenISAATEEQVASMQEISSSADSLAHLAHKLQKLVEQFKL 666
Cdd:PRK15048  478 -----MDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
434-619 3.01e-37

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: 136.79  E-value: 3.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 434 SEAAMQASELADKGNATMQTAVSEMssvsrfvqgmadtaGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEH 513
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQM--------------EQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 514 GRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLEN 593
Cdd:pfam00015  67 GRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQE 146
                         170       180
                  ....*....|....*....|....*.
gi 1122544240 594 IAAASQQMSASTAEVVQSIDQIHAIS 619
Cdd:pfam00015 147 IAAASDEQSAGIDQVNQAVARMDQVT 172
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
46-272 7.72e-20

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: 89.32  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  46 VEEKMYENAISSVTVLNQTIDQIIGATRKNVDFLASQLdagNVGPNQGDETDTIRTLLDAYKETHDDVELASIGTDQGVY 125
Cdd:pfam02743   3 IKEQAEEQLLSLAKQLAENIESYLDSLEEILELLASNP---DLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 126 INSPVTAVNKEGYDPRERPWYQAATQNKD--VPTIITPYLSSNTGNVVASVAQTSTDGH----GVVSVSLSLEALSKTVN 199
Cdd:pfam02743  80 LASSDESPSYPGLDVSERPWYKEALKGGGgiIWVFSSPYPSSESGEPVLTIARPIYDDDgeviGVLVADLDLDTLQELLS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1122544240 200 STKIGEKGYIYIIDNANKIIVHPTEKPGTEGTmAPYKDIF------AQKNGSLTYTLNGNQEHAFFSTNETTGWTVVGV 272
Cdd:pfam02743 160 QIKLGEGGYVFIVDSDGRILAHPLGKNLRSLL-APFLGKSladalpGSGITEIAVDLDGEDYLVAYAPIPGTGWTLVVV 237
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
194-274 2.12e-17

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: 77.42  E-value: 2.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 194 LSKTVNSTKIGEKGYIYIIDNANKIIVHPTEK-------PGTEGTMAPYKDIFAQKNGSLTYTLNGNQEHAFFSTNETTG 266
Cdd:cd12912     2 LSEIISSIKIGETGYAFLVDKDGTIIAHPDKElvgkkisDDEAAEEELAKKMLAGKSGSVEYTFNGEKKYVAYAPIPGTG 81

                  ....*...
gi 1122544240 267 WTVVGVID 274
Cdd:cd12912    82 WSLVVVVP 89
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
312-356 3.49e-13

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: 64.00  E-value: 3.49e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1122544240 312 TKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESL 356
Cdd:cd06225     1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
194-274 5.37e-13

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: 64.77  E-value: 5.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 194 LSKTVNSTKIGEKGYIYIIDNANKIIVHPTEKPGTEGTMAP-----YKDIFAQKNGSLTYTLNGNQEH-AFFSTNETTGW 267
Cdd:cd18774     2 LSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVGKGKSLDdlallAALLLAGESGTFEYTSDDGVERlVAYRPVPGTPW 81

                  ....*..
gi 1122544240 268 TVVGVID 274
Cdd:cd18774    82 VVVVGVP 88
HAMP pfam00672
HAMP domain;
306-358 9.71e-13

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 63.03  E-value: 9.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1122544240 306 WIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRT 358
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
183-364 2.49e-12

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 69.28  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 183 GVVSVSLSLEALSKTVNSTKIGEKGYIYIIDNANKIIVHPTEKPGTEGTMAPYKDIFAQKNGSLTYTLNGNQEHAFFSTN 262
Cdd:COG2972    53 LLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 263 ETTGWTVVGVIDSGEVTASVRPILYTTLIVVAIAIAVSSIIIFWIVQSITKPLNRLVKASDEISNGNLTIeVAVLGQDEF 342
Cdd:COG2972   133 SLLGWTLVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVR-LEVSGNDEI 211
                         170       180
                  ....*....|....*....|..
gi 1122544240 343 GKLSTSFNKMSESLRTVIQDVR 364
Cdd:COG2972   212 GILARSFNEMVERIKELIEEVY 233
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
310-361 5.39e-12

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 60.72  E-value: 5.39e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1122544240  310 SITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQ 361
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
305-608 2.53e-11

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 66.45  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSET 384
Cdd:COG3850   136 YLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 TKATEQVALITEESAAGLEKQTSNLKHTALQMkelaggvgQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRF 464
Cdd:COG3850   216 LAALLLLLALLLALLLAALLAALLLLLLLQDA--------LAESELLALNILAGLLELLLALLLLLLASALLLLELELLA 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGA 544
Cdd:COG3850   288 LLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAA 367
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1122544240 545 IQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEV 608
Cdd:COG3850   368 AAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIA 431
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
118-286 5.52e-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: 60.82  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 118 IGTdqgvYI--NSPVTAVNKEGYDPRERpwyqAATQNKDVPTIITPYLSSNtGNVVasvaqtstdghGVVSV----SLSL 191
Cdd:pfam17201 128 IGT----YIpaSSPVYKAVLAGETYVGR----AKVFGKWYVTAYEPIRDAD-GKVI-----------GILYVgvpqDEAL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 192 EALSKTVNSTKIGEKGYIYIIDNA----NKIIVHPT------EKPGTEGTMAPYKDIFAQKNGSLTYTLNGNQEH----A 257
Cdd:pfam17201 188 ASLRKAIKKVKIGKTGYLYVLDGKgdqkGKFIVHPTlegkniLDAKDADGEPFVKKLLQKKVGSLEYPWKADAAGrdklA 267
                         170       180
                  ....*....|....*....|....*....
gi 1122544240 258 FFSTNETTGWTVVGVIDSGEVTASVRPIL 286
Cdd:pfam17201 268 AFTYFEPWDWVIVASVYEDEFLAATNRLL 296
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
305-364 6.60e-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: 61.52  E-value: 6.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVR 364
Cdd:COG5000    27 LLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELE 86
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
69-191 2.12e-08

first 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: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 52.95  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  69 IGATRKNVDFLASQLDAGNVGPNQGDETdtIRTLLDAYKETHDDVELASIGTDQGVYI-NSPVTAVNKEGYDPRERPWYQ 147
Cdd:cd18773     1 LEEADLLLRSLASALEALAALGSADREE--LQALLRRLLERNPEISGIYVVDADGRVVaSSDRDPGGGDDDDDRDRFWYQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1122544240 148 AATQNKDvPTIITPYLSSNTGNVVASVAQ--TSTDGH--GVVSVSLSL 191
Cdd:cd18773    79 AAKATGK-LVISEPYISRVTGKPVITLSRpiRDADGRfiGVVGADIDL 125
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
305-654 2.83e-07

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 53.96  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 305 FWIVQSITKPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSET 384
Cdd:COG2770   230 LLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLEL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 385 TKATEQVALITEESAAGLEKQTSNLKHTALQMKELAGGVGQVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRF 464
Cdd:COG2770   310 LLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELA 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 465 VQGMADTAGRLEQHSTSIGEMVSVITDIAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGA 544
Cdd:COG2770   390 AVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAA 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 545 IQQEISMANHNVQIGQQDVSNGIRAVQFADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNAD 624
Cdd:COG2770   470 EALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELA 549
                         330       340       350
                  ....*....|....*....|....*....|
gi 1122544240 625 GTENISAATEEQVASMQEISSSADSLAHLA 654
Cdd:COG2770   550 ALLALLLALAAVEAAALLLAALLLAAVAAL 579
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms];
192-644 2.95e-07

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 443621 [Multi-domain]  Cd Length: 510  Bit Score: 53.50  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 192 EALSKTVNSTKIGEKGYIYIIDNANKIIVHPTeKPGTEGT-MAPYKDIF-------------AQKNGSLTYT---LNGNQ 254
Cdd:COG4564    61 EQALAALRALRFGGDGYFFVYDYDGTMLAHPI-NPELVGKnLLDLKDANgkylirelieaakKKGGGFVEYLwpkPGSGK 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 255 EH---AFFSTNETTGWTVVGVIDSGEVTASVRPILYTTLIVVAIAIAVSSIIIFWIVQSITKPLNRLVKASDEISNGNLT 331
Cdd:COG4564   140 PEpklSYVKKFPPWDWVIGTGVYLDDIEAAFAAAALELLLLLALLLALALALLLLVLAALAGLLLASALEGELNLAGALA 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 332 IEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQLAVNSSETTKATEQVALITEESAAGLEkqtsnlkh 411
Cdd:COG4564   220 ALLLAAAAELLAALLLIGAAAGALLALAEAVAAVLAEALAAAAAAAAASAAASSAALAAAAAEAEAALAASE-------- 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 412 talqmkelaggvgqVTNSTQQVSEAAMQASELADKGNATMQTAVSEMSSVSRFVQGMADTAGRLEQHSTSIGEMVSVITD 491
Cdd:COG4564   292 --------------ASAAAALAAAAAAAAAAAAAAAAAEAAAAAAAAAAAAAAAAASVADVAALAAAAAAAAAIAALAAA 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 492 IAAQTNLLALNASIEAARAGEHGRGFSVVASEVRKLAEQSSLSGQKIVEMVGAIQQEISMANHNVQIGQQDVSNGIRAVQ 571
Cdd:COG4564   358 AAAAAAAAAAAAAIAAAAAAAAAAAAAAAAAAAEAAAAAAAAATAAAALEAVAAAAAAAAAAAAAEAAAAEVEAAAAITA 437
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1122544240 572 FADESFAQISEAVGVVNHQLENIAAASQQMSASTAEVVQSIDQIHAISETNADGTENISAATEEQVASMQEIS 644
Cdd:COG4564   438 IILEAAAAAAAAIEAEEAAAVAAAAALAAEAAAAAAAAAEAAAAAAAAEAASAVVSAAAAAAAAGAAAALALA 510
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
309-376 6.33e-06

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 49.47  E-value: 6.33e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1122544240 309 QSITKPLNRLVKASDEISNGNL-TIEVAVLGQDEFGKLSTSFNKMSESLRTVIQDVRHTADELTASSTQ 376
Cdd:PRK10935  174 RQVVAPLNQLVTASQQIEKGQFdHIPLDTTLPNELGLLAKAFNQMSSELHKLYRSLEASVEEKTRKLTQ 242
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
64-191 1.16e-05

first 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 first 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: 350338  Cd Length: 139  Bit Score: 45.60  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  64 TIDQIIGATRKNVDFLASQLDAGNVGPNQgdetdtIRTLLDAYKETHDDVELASIGTDQGVYI--------------NSP 129
Cdd:cd12913     1 FLEEAESIAEQLASTLESLVSSGSLDREL------LENLLKQVLESNPDILGVYVAFEPNAFSdetgrfapywyrddGGI 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1122544240 130 VTAVNKEGYDPRERPWYQAATQNKDvPTIITPYL-SSNTGNVVASVAQ-TSTDGH--GVVSVSLSL 191
Cdd:cd12913    75 IDLDEPPDYDYRTRDWYKLAKETGK-PVWTEPYIdEVGTGVLMITISVpIYDNGKfiGVVGVDISL 139
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
313-409 4.36e-05

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 46.55  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240 313 KPLNRLVKASDEISNGNLTIEVAVLGQDEFGKLSTSFNKMSESL-------RTVIQDVRHtadELtasSTQLAVNSSETT 385
Cdd:PRK10549  190 APVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTLekneqmrRDFMADISH---EL---RTPLAVLRGELE 263
                          90       100
                  ....*....|....*....|....
gi 1122544240 386 KATEQVALITEESAAGLEKQTSNL 409
Cdd:PRK10549  264 AIQDGVRKFTPESVASLQAEVGTL 287
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
69-191 4.45e-05

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase 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 first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. 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: 350339  Cd Length: 123  Bit Score: 43.53  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1122544240  69 IGATRKNVDFLASQLDAGNVGPNQGDEtdtIRTLLDAYKETHDDVELASIGTDQGVYINSPVTAVNkEGYDPRERPWYQA 148
Cdd:cd12914     1 LDEADLLLRSLADDLEARGAASADPAA---LQALLRRLLARLPEVRSIFVVDADGRVVASSGPGPA-PGLDVSDRDYFQA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1122544240 149 ATQNKDVPTIITPYLSSNTGN--VVASVAQTSTDGH--GVVSVSLSL 191
Cdd:cd12914    77 ARAGGGGLFISEPVISRVTGKpvIPLSRPIRDADGRfaGVVVASIDL 123
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
306-360 1.25e-03

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 41.84  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1122544240 306 WIVQSITKPLNRLVKASDEISNGNLTIEVAV-LGQDEFGKLSTSFNKMSESLRTVI 360
Cdd:PRK09470  185 WLAWSLAKPARKLKNAADEVAQGNLRQHPELeTGPQEFRQAGASFNQMVTALERMM 240
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
196-225 4.36e-03

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: 39.66  E-value: 4.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1122544240 196 KTVNSTKIGEKGYIYIIDNANKIIVHPTEK 225
Cdd:pfam08269 196 KTLASIRYGNNGYIFIYDTDGNMILHPLKP 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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