NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500212009|ref|WP_011882190|]
View 

methyl-accepting chemotaxis protein [Burkholderia vietnamiensis]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 12983517)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MCP_signal super family cl46910
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 277-599 6.00e-96

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.


The actual alignment was detected with superfamily member PRK15048:

Pssm-ID: 481250 [Multi-domain]  Cd Length: 553  Bit Score: 304.24  E-value: 6.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 277 ITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASE 356
Cdd:PRK15048 196 VIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGG--NLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSD 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 357 SVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGKIE 436
Cdd:PRK15048 274 AIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIA 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 437 EASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQV 516
Cdd:PRK15048 354 DSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLV 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 517 RQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVGQF 596
Cdd:PRK15048 434 ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAF 513


                 ...
gi 500212009 597 KIA 599
Cdd:PRK15048 514 RLA 516
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 14-168 4.11e-21

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: 89.51  E-value: 4.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  14 VAIVVFALVATTLINYFIARSYNDDAIDRNLTSVASGHVVGIGDWVAtksrmiasLQDAALSPDplpvfkqmaaaggfTN 93
Cdd:cd12913    4 EAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVA--------FEPNAFSDE--------------TG 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500212009  94 VYAGYADKVYHFADPTGIPSDYDPTVRPWYKQAAQAGKPVVTPPYVD-AGTGKLVVSFAVPILRDGVLKGVVGADV 168
Cdd:cd12913   62 RFAPYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDeVGTGVLMITISVPIYDNGKFIGVVGVDI 137
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 177-263 1.18e-07

Sensor domains of Histidine Kinase receptors; 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.


The actual alignment was detected with superfamily member cd12912:

Pssm-ID: 365792 [Multi-domain]  Cd Length: 92  Bit Score: 49.69  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 177 VKSIHPTPASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELGGMSAASIATATAPVEVHVGDDAKLVRAQAVPGTDWYAL 256
Cdd:cd12912    6 ISSIKIGETGYAFLVDKDGTIIAHPDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYTFNGEKKYVAYAPIPGTGWSLV 85


                 ....*..
gi 500212009 257 VLLDKAE 263
Cdd:cd12912   86 VVVPESE 92
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 277-599 6.00e-96

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 304.24  E-value: 6.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 277 ITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASE 356
Cdd:PRK15048 196 VIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGG--NLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSD 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 357 SVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGKIE 436
Cdd:PRK15048 274 AIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIA 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 437 EASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQV 516
Cdd:PRK15048 354 DSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLV 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 517 RQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVGQF 596
Cdd:PRK15048 434 ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAF 513


                 ...
gi 500212009 597 KIA 599
Cdd:PRK15048 514 RLA 516
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
238-598 8.05e-91

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 290.38  E-value: 8.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 238 DDAKLVRAQAVPGTDWYALVLLDKAEATAGMRSLLTASLITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgD 317
Cdd:COG0840  147 LLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEG--D 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 318 LTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATV 397
Cdd:COG0840  225 LTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATV 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 398 GQSAAAATQADERAASASRIASHGGVVVSDVVA--------------TMGKIEEASGRIGDIIGVIDGIAFQTNILALNA 463
Cdd:COG0840  305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNA 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 464 AVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSA--------------GSGQVRQAGDTMREIVAN 529
Cdd:COG0840  385 AIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEaveameegseeveeGVELVEEAGEALEEIVEA 464

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500212009 530 VANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVGQFKI 598
Cdd:COG0840  465 VEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 350-597 2.25e-70

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: 227.94  E-value: 2.25e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   350 QIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVV 429
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   430 ATMGKIEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLV------- 502
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   503 -------ESTVASVSAGSGQVRQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQS 575
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 500212009   576 TAAATALQTQANALATTVGQFK 597
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 377-575 4.95e-58

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: 193.22  E-value: 4.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 377 ESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGKIEEASGRIGDIIGVIDGIAFQT 456
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 457 NILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQVRQAGDTMREIVANVANVTTI 536
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 500212009 537 ISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQS 575
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 409-565 1.34e-51

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: 174.93  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  409 ERAASASRIASHGGVVVSDVVATMGKIEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLA 488
Cdd:pfam00015   2 DLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  489 QRSAQAAREVKVLV--------------ESTVASVSAGSGQVRQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEV 554
Cdd:pfam00015  82 ERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 161

                         170
                  ....*....|.
gi 500212009  555 NRAVTQLDEMV 565
Cdd:pfam00015 162 NQAVARMDQVT 172
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 14-168 4.11e-21

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: 89.51  E-value: 4.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  14 VAIVVFALVATTLINYFIARSYNDDAIDRNLTSVASGHVVGIGDWVAtksrmiasLQDAALSPDplpvfkqmaaaggfTN 93
Cdd:cd12913    4 EAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVA--------FEPNAFSDE--------------TG 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500212009  94 VYAGYADKVYHFADPTGIPSDYDPTVRPWYKQAAQAGKPVVTPPYVD-AGTGKLVVSFAVPILRDGVLKGVVGADV 168
Cdd:cd12913   62 RFAPYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDeVGTGVLMITISVPIYDNGKFIGVVGVDI 137
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 38-257 1.28e-15

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: 76.61  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   38 DAIDRNLTSVASGHVVGIGDWVATK---SRMIAS---LQDAALSPDPLPVFKQMAAAGGFTNVYAGY----ADKVYHFAD 107
Cdd:pfam02743   5 EQAEEQLLSLAKQLAENIESYLDSLeeiLELLASnpdLQDLLSAPAEEELAKLESLLRSNPGISSIYlvdaDGRVLASSD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  108 PTGIPSDYDPTVRPWYKQAAQAGKPVVTP---PYVDAGTGKLVVSFAVPIL-RDGVLKGVVGADVGMDSVIANVKSIHPT 183
Cdd:pfam02743  85 ESPSYPGLDVSERPWYKEALKGGGGIIWVfssPYPSSESGEPVLTIARPIYdDDGEVIGVLVADLDLDTLQELLSQIKLG 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500212009  184 PASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELGGMSAASIATATAPVEvhVGDDAKLVRAQAVPGTDWYALV 257
Cdd:pfam02743 165 EGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD--LDGEDYLVAYAPIPGTGWTLVV 236
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 177-263 1.18e-07

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 49.69  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 177 VKSIHPTPASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELGGMSAASIATATAPVEVHVGDDAKLVRAQAVPGTDWYAL 256
Cdd:cd12912    6 ISSIKIGETGYAFLVDKDGTIIAHPDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYTFNGEKKYVAYAPIPGTGWSLV 85


                 ....*..
gi 500212009 257 VLLDKAE 263
Cdd:cd12912   86 VVVPESE 92
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 277-599 6.00e-96

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 304.24  E-value: 6.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 277 ITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASE 356
Cdd:PRK15048 196 VIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGG--NLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSD 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 357 SVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGKIE 436
Cdd:PRK15048 274 AIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIA 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 437 EASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQV 516
Cdd:PRK15048 354 DSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLV 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 517 RQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVGQF 596
Cdd:PRK15048 434 ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAF 513


                 ...
gi 500212009 597 KIA 599
Cdd:PRK15048 514 RLA 516
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
265-598 3.45e-93

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 297.25  E-value: 3.45e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 265 TAGMRSLLTASLITLVVIVGIASVIIGAITTTAFRRLSQVRQAmasigsGTGDLTQRLPAEGRDEVSDIARSFNSFVDKL 344
Cdd:PRK15041 190 SQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHI------AGGDLVKPIEVDGSNEMGQLAESLRHMQGEL 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 345 NDVMRQIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVV 424
Cdd:PRK15041 264 MRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKV 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 425 VSDVVATMGKIEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVES 504
Cdd:PRK15041 344 VDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIED 423

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 505 TVASVSAGSGQVRQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQT 584
Cdd:PRK15041 424 SVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEE 503

                        330
                 ....*....|....
gi 500212009 585 QANALATTVGQFKI 598
Cdd:PRK15041 504 QASRLTEAVAVFRI 517
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
238-598 8.05e-91

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 290.38  E-value: 8.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 238 DDAKLVRAQAVPGTDWYALVLLDKAEATAGMRSLLTASLITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgD 317
Cdd:COG0840  147 LLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEG--D 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 318 LTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATV 397
Cdd:COG0840  225 LTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATV 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 398 GQSAAAATQADERAASASRIASHGGVVVSDVVA--------------TMGKIEEASGRIGDIIGVIDGIAFQTNILALNA 463
Cdd:COG0840  305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNA 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 464 AVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSA--------------GSGQVRQAGDTMREIVAN 529
Cdd:COG0840  385 AIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEaveameegseeveeGVELVEEAGEALEEIVEA 464

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500212009 530 VANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVGQFKI 598
Cdd:COG0840  465 VEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
282-598 3.94e-89

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 285.81  E-value: 3.94e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 282 IVGIASVIIGAITTTA--FRRLSQVRQAMASIGS-----GTGDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDA 354
Cdd:PRK09793 190 LVFISMIIVAAIYISSalWWTRKMIVQPLAIIGShfdsiAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKG 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 355 SESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGK 434
Cdd:PRK09793 270 SQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQE 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 435 IEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSG 514
Cdd:PRK09793 350 IATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSK 429

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 515 QVRQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVG 594
Cdd:PRK09793 430 LVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVA 509


                 ....
gi 500212009 595 QFKI 598
Cdd:PRK09793 510 VFTL 513
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 350-597 2.25e-70

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: 227.94  E-value: 2.25e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   350 QIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVV 429
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   430 ATMGKIEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLV------- 502
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   503 -------ESTVASVSAGSGQVRQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQS 575
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 500212009   576 TAAATALQTQANALATTVGQFK 597
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 377-575 4.95e-58

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: 193.22  E-value: 4.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 377 ESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGKIEEASGRIGDIIGVIDGIAFQT 456
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 457 NILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQVRQAGDTMREIVANVANVTTI 536
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 500212009 537 ISEITHAANEQTRGIQEVNRAVTQLDEMVQQNAALVEQS 575
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 409-565 1.34e-51

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: 174.93  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  409 ERAASASRIASHGGVVVSDVVATMGKIEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLA 488
Cdd:pfam00015   2 DLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  489 QRSAQAAREVKVLV--------------ESTVASVSAGSGQVRQAGDTMREIVANVANVTTIISEITHAANEQTRGIQEV 554
Cdd:pfam00015  82 ERSAQAAKEIEALIieiqkqtndstasiESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 161

                         170
                  ....*....|.
gi 500212009  555 NRAVTQLDEMV 565
Cdd:pfam00015 162 NQAVARMDQVT 172
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 14-168 4.11e-21

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: 89.51  E-value: 4.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  14 VAIVVFALVATTLINYFIARSYNDDAIDRNLTSVASGHVVGIGDWVAtksrmiasLQDAALSPDplpvfkqmaaaggfTN 93
Cdd:cd12913    4 EAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVA--------FEPNAFSDE--------------TG 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500212009  94 VYAGYADKVYHFADPTGIPSDYDPTVRPWYKQAAQAGKPVVTPPYVD-AGTGKLVVSFAVPILRDGVLKGVVGADV 168
Cdd:cd12913   62 RFAPYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDeVGTGVLMITISVPIYDNGKFIGVVGVDI 137
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 38-257 1.28e-15

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: 76.61  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   38 DAIDRNLTSVASGHVVGIGDWVATK---SRMIAS---LQDAALSPDPLPVFKQMAAAGGFTNVYAGY----ADKVYHFAD 107
Cdd:pfam02743   5 EQAEEQLLSLAKQLAENIESYLDSLeeiLELLASnpdLQDLLSAPAEEELAKLESLLRSNPGISSIYlvdaDGRVLASSD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  108 PTGIPSDYDPTVRPWYKQAAQAGKPVVTP---PYVDAGTGKLVVSFAVPIL-RDGVLKGVVGADVGMDSVIANVKSIHPT 183
Cdd:pfam02743  85 ESPSYPGLDVSERPWYKEALKGGGGIIWVfssPYPSSESGEPVLTIARPIYdDDGEVIGVLVADLDLDTLQELLSQIKLG 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500212009  184 PASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELGGMSAASIATATAPVEvhVGDDAKLVRAQAVPGTDWYALV 257
Cdd:pfam02743 165 EGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD--LDGEDYLVAYAPIPGTGWTLVV 236
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
 38-168 4.38e-13

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: 66.43  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  38 DAIDRNLTSVASGHVVGIGDWVATKSRMIASLQDAAlspdplpvfkqmAAAGGFTNVYAGYADK--VYHFADPTGIPSDY 115
Cdd:cd18773    2 EEADLLLRSLASALEALAALGSADREELQALLRRLL------------ERNPEISGIYVVDADGrvVASSDRDPGGGDDD 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500212009 116 DPTVRPWYKQAAQAGKPVVTPPYVDAGTGKLVVSFAVPILR-DGVLKGVVGADV 168
Cdd:cd18773   70 DDRDRFWYQAAKATGKLVISEPYISRVTGKPVITLSRPIRDaDGRFIGVVGADI 123
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
241-367 1.06e-09

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 60.80  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 241 KLVRAQAVPGTDWYALVLLDKAEATAGMRSLLTASLITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgDLTq 320
Cdd:COG2972  125 LLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKG--DLV- 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 500212009 321 RLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASESVRTAanEIAA 367
Cdd:COG2972  202 RLEVSGNDEIGILARSFNEMVERIKELIEEVYELELEKKEA--ELKA 246
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
299-349 2.23e-09

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 53.41  E-value: 2.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 500212009   299 RRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMR 349
Cdd:smart00304   5 RPLRRLAEAAQRIADG--DLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 299-344 7.86e-09

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 51.68  E-value: 7.86e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 500212009 299 RRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKL 344
Cdd:cd06225    2 RPLRRLTEAARRIAEG--DLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP pfam00672
HAMP domain;
299-346 1.84e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 50.70  E-value: 1.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 500212009  299 RRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLND 346
Cdd:pfam00672   8 RPLRRLAEAARRIASG--DLDVRLPVSGRDEIGELARAFNQMAERLRE 53
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 271-368 3.08e-08

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: 56.12  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 271 LLTASLITLVVIVGIASVIIGAITttafRRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQ 350
Cdd:COG5000   11 LLLIALLLLLLALWLALLLARRLT----RPLRRLAEATRAVAAG--DLSVRLPVTGDDEIGELARAFNRMTDQLKEQREE 84

                         90
                 ....*....|....*...
gi 500212009 351 IRDASESVRTAANEIAAG 368
Cdd:COG5000   85 LEERRRYLETILENLPAG 102
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 177-263 1.18e-07

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 49.69  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 177 VKSIHPTPASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELGGMSAASIATATAPVEVHVGDDAKLVRAQAVPGTDWYAL 256
Cdd:cd12912    6 ISSIKIGETGYAFLVDKDGTIIAHPDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYTFNGEKKYVAYAPIPGTGWSLV 85


                 ....*..
gi 500212009 257 VLLDKAE 263
Cdd:cd12912   86 VVVPESE 92
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
 120-168 3.05e-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: 43.91  E-value: 3.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500212009 120 RPWYKQA-AQAGKPVVTPPYVDAGTGKLVVSFAVPILR-DGVLKGVVGADV 168
Cdd:cd12914   71 RDYFQAArAGGGGLFISEPVISRVTGKPVIPLSRPIRDaDGRFAGVVVASI 121
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 177-261 1.20e-04

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 41.28  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 177 VKSIHPTPASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELGGMSAASIATATAPVEVHVGDDaKLVRAQAVPGTDWYAL 256
Cdd:cd18774    6 LSSIKLGETGYAFLVDSDGTILAHPPKELVGKGKSLDDLALLAALLLAGESGTFEYTSDDGVE-RLVAYRPVPGTPWVVV 84


                 ....*
gi 500212009 257 VLLDK 261
Cdd:cd18774   85 VGVPE 89
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 275-507 1.25e-04

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 44.87  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 275 SLITLVVIVGIASVIIGAITTTAFRRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDA 354
Cdd:COG3850  120 ALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARG--DFDARVPVSGRDELGTLARAFNRMADELQELYAELEEE 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 355 SESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGK 434
Cdd:COG3850  198 EELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASA 277

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500212009 435 IEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVA 507
Cdd:COG3850  278 LLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQ 350
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
232-595 1.64e-04

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 44.72  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 232 VEVHVGDDAKLVRAQAVPGTDWYALVLLDKAEATAGMRSLLTASLITLVVIVGIASVIIGAITttafRRLSQVRQAMASI 311
Cdd:COG2770  175 LLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRIT----RPLRRLAEAARRI 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 312 GSGtgDLTQRLPAEGRDEVSDIARSFNSFVDKLNDVMRQIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASME 391
Cdd:COG2770  251 AAG--DLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAAL 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 392 EITATVGQSAAAATQADERAASASRIASHGGVVVSDVVATMGKIEEASGRIGDIIGVIDGIAFQTNILALNAAVEAARAG 471
Cdd:COG2770  329 LLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELA 408

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 472 EQGRGFAVVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQVRQAGDTMREIVANVANVTTIISEITHAANEQTRGI 551
Cdd:COG2770  409 LEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALE 488

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 500212009 552 QEVNRAVTQLDEMVQQNAALVEQSTAAATALQTQANALATTVGQ 595
Cdd:COG2770  489 LLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEEL 532
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 265-446 2.30e-04

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 44.29  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 265 TAGMRSLLTASLITLVVIVGIASVIIG-AITttafRRLSQVRQAMASIGSGtgDLTQRLPAEGRDEVSDIARSFNSFVDK 343
Cdd:COG4192  322 QQSGILLLAIALLSLLLAVLINYFYVRrRLV----KRLNALSDAMAAIAAG--DLDVPIPVDGNDEIGRIARLLRVFRDQ 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 344 LNdvmrqirdasESVRTAANEIAAGNQdlssrtesAAASLEET------AASMEEITATVGQSAAAATQADERAA----S 413
Cdd:COG4192  396 AI----------EKTQELETEIEERKR--------IEKNLRQTqdeliqAAKMAVVGQTMTSLAHELNQPLNAMSmylfS 457

                        170       180       190
                 ....*....|....*....|....*....|...
gi 500212009 414 ASRIASHGGvvVSDVVATMGKIEEASGRIGDII 446
Cdd:COG4192  458 AKKALEQEN--YAQLPTSLDKIEGLIERMDKII 488
PRK15347 PRK15347
two component system sensor kinase;
34-345 1.11e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 41.94  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  34 SYNDDAIDRNLTSVASGHVVGIGDWVatkSRMIaSLQDAalSPDPLPVFKQmaaAGGFTNVYaGYADKVYH--------- 104
Cdd:PRK15347  67 ERDAKNLMYRCQSATEIDHNDIKPEV---SRYI-PFNPK--NCDPTLNGKK---DRWFIQAY-GIAGQSYYldsfilkpk 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 105 ----FADPTGIPSDYDP----TVRPWYKQAAQA----GKPVVTPpyvdagTGKLVVSFAVpILRDGVLKGVVgadVGMDS 172
Cdd:PRK15347 137 egisLFSPDKSSSDYLTlrplELKQLPLQPTHNgiywGKPEYIP------GGGWHVSVAV-ADKQGVLVGFT---VKLND 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 173 VIANVksiHPTP-ASFGMLVDSSGHVVAHPDTKLTLKPVAEVSSELggmsaasiatatAPVEVHVG----DDAKLVRAQa 247
Cdd:PRK15347 207 LISYN---HPVLdDDINLWLDQNGELLPFSTIPLSSNQLQKILNQL------------ENVKLHDGwqqiPDYLVLRTQ- 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009 248 VPGTDWYALVLLDKA----EATAGMRSLLTASLITLVVIVGIASVIIG---AITTTAFrrlsqvrqaMASIGS-GTGDLT 319
Cdd:PRK15347 271 LKGPGWQQVTLYPRRnlanEALKPALQQLPFALLILVLLTSVLFLLLRrylAKPLWRF---------VDIINKtGPAALE 341

                        330       340
                 ....*....|....*....|....*.
gi 500212009 320 QRLPAEGRDEVSDIARSFNSFVDKLN 345
Cdd:PRK15347 342 PRLPENRLDELGSIAKAYNQLLDTLN 367
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 324-409 5.69e-03

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: 38.81  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009   324 AEGRDEVSDIARSFNSFVDklndVMRQIRDASESVRTAANEIAAGNQDLSSRTESAAASLEETAASMEEITATVGQSAAA 403
Cdd:smart00283 175 EEGVELVEETGDALEEIVD----SVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGL 250


                   ....*.
gi 500212009   404 ATQADE 409
Cdd:smart00283 251 AEELDE 256
PHA03332 PHA03332
membrane glycoprotein; Provisional
 443-574 8.42e-03

membrane glycoprotein; Provisional


Pssm-ID: 223047 [Multi-domain]  Cd Length: 1328  Bit Score: 39.18  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500212009  443 GDIIGVIDGiAFQTNILALNAAVEAARageqgrgfavVAQEVRSLAQRSAQAAREVKVLVESTVASVSAGSGQVRQAGDT 522
Cdd:PHA03332  852 GDAIGLSAA-AFTMASAALNAATQALA----------VATLYVNQLLQATAATAEMASKIGGLNARVDKTSDVITKLGDT 920

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 500212009  523 MREIVA----NVANVTTIISEITHAANEQTRGIQ-EVNRAVTQLDEMVQQ-NAALVEQ 574
Cdd:PHA03332  921 IAKISAtldnNIRAVNGRVSDLEDQVNLRFLAVAtNFNTLATQLKELGTTtNERIEEV 978
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH