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Conserved domains on  [gi|506321803|ref|WP_015841578|]
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MULTISPECIES: methyl-accepting chemotaxis protein [Pectobacterium]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 12182752)

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

CATH:  1.10.287.950
Gene Ontology:  GO:0006935
PubMed:  18165013|20738376
SCOP:  4003862

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];
315-646 1.93e-86

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 279.98  E-value: 1.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 315 AEINHTRNLFLGGGIILVLLFAAFFVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTT 394
Cdd:COG0840  174 LAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRE 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 395 IVSQVRNASEEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVT 474
Cdd:COG0840  254 LVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 475 DSVS--------------TMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSS 540
Cdd:COG0840  334 EAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSA 413

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 541 TAVKEIETLIDES--------------LEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAI 606
Cdd:COG0840  414 EATKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI 493

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 506321803 607 VQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:COG0840  494 EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
 35-322 7.96e-81

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: 257.66  E-value: 7.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   35 TRSAGNQLKSLTLNDMQSQVNGVTDMINMYDTSLQAEVSNYTRLLASFLPTQFSLDTVNRTPFGNASQPTLKAGDTVL-- 112
Cdd:pfam17201   1 SRSAKGEVRALAESDLEEQVQDLADMLETQDESLRESVDSDLNVFRKLLPGSWRAVNQFTVDVGGVSLPVLYLGGTWLgq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  113 ----NLNTEVPDDFLSRTHAISTIFVRDGEDFTRVTTSLKKEDGSRAMGTKLDRESPAYALVMKGETYSGLATLFGKQYI 188
Cdd:pfam17201  81 nrdpNKNFPLVDEFTELTGGTATVFQRMNDDLLRVATSVKKEDGSRAIGTYIPASSPVYKAVLAGETYVGRAKVFGKWYV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  189 TQYQPIRDSASKVIGILFVGVDITKQFTEMQQTILNKKMGETGHFFVLNTkKGKDAGNYLYHQSNANQRPDWSEGA---- 264
Cdd:pfam17201 161 TAYEPIRDADGKVIGILYVGVPQDEALASLRKAIKKVKIGKTGYLYVLDG-KGDQKGKFIVHPTLEGKNILDAKDAdgep 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 506321803  265 -LEKVLATGNGTIEYDNNTmTGEEKTRIMVYRSIPQWNWIVAGTVSKESLMAEINHTRN 322
Cdd:pfam17201 240 fVKKLLQKKVGSLEYPWKA-DAAGRDKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLN 297
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
315-646 1.93e-86

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 279.98  E-value: 1.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 315 AEINHTRNLFLGGGIILVLLFAAFFVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTT 394
Cdd:COG0840  174 LAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRE 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 395 IVSQVRNASEEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVT 474
Cdd:COG0840  254 LVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 475 DSVS--------------TMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSS 540
Cdd:COG0840  334 EAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSA 413

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 541 TAVKEIETLIDES--------------LEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAI 606
Cdd:COG0840  414 EATKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI 493

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 506321803 607 VQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:COG0840  494 EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 329-646 1.09e-81

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 268.41  E-value: 1.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 329 IILVLLFAAFFVVltRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNASEEISA 408
Cdd:PRK15048 200 VVVLILLVAWYGI--RRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYA 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 409 STDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQ 488
Cdd:PRK15048 278 GTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSK 357

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 489 RIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQ 568
Cdd:PRK15048 358 KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAG 437

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506321803 569 AVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:PRK15048 438 ETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
 35-322 7.96e-81

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: 257.66  E-value: 7.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   35 TRSAGNQLKSLTLNDMQSQVNGVTDMINMYDTSLQAEVSNYTRLLASFLPTQFSLDTVNRTPFGNASQPTLKAGDTVL-- 112
Cdd:pfam17201   1 SRSAKGEVRALAESDLEEQVQDLADMLETQDESLRESVDSDLNVFRKLLPGSWRAVNQFTVDVGGVSLPVLYLGGTWLgq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  113 ----NLNTEVPDDFLSRTHAISTIFVRDGEDFTRVTTSLKKEDGSRAMGTKLDRESPAYALVMKGETYSGLATLFGKQYI 188
Cdd:pfam17201  81 nrdpNKNFPLVDEFTELTGGTATVFQRMNDDLLRVATSVKKEDGSRAIGTYIPASSPVYKAVLAGETYVGRAKVFGKWYV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  189 TQYQPIRDSASKVIGILFVGVDITKQFTEMQQTILNKKMGETGHFFVLNTkKGKDAGNYLYHQSNANQRPDWSEGA---- 264
Cdd:pfam17201 161 TAYEPIRDADGKVIGILYVGVPQDEALASLRKAIKKVKIGKTGYLYVLDG-KGDQKGKFIVHPTLEGKNILDAKDAdgep 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 506321803  265 -LEKVLATGNGTIEYDNNTmTGEEKTRIMVYRSIPQWNWIVAGTVSKESLMAEINHTRN 322
Cdd:pfam17201 240 fVKKLLQKKVGSLEYPWKA-DAAGRDKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLN 297
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 398-645 6.03e-64

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: 212.15  E-value: 6.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   398 QVRNASEEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSV 477
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   478 STMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLI------- 550
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   551 -------DESLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNS 623
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 506321803   624 EDTAQGLRQKGHHLSELVSVFR 645
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 427-623 2.22e-53

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 181.67  E-value: 2.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 427 QASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRIADITTVIESIAFQTNI 506
Cdd:cd11386    3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 507 LALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVN 586
Cdd:cd11386   83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 506321803 587 DIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNS 623
Cdd:cd11386  163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 457-613 1.73e-43

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 153.74  E-value: 1.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  457 DLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALA 536
Cdd:pfam00015   2 DLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  537 QRSSTAVKEIETLIDE--------------SLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQV 602
Cdd:pfam00015  82 ERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 161

                         170
                  ....*....|.
gi 506321803  603 NIAIVQIGQAT 613
Cdd:pfam00015 162 NQAVARMDQVT 172
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 217-311 3.05e-11

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: 60.09  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 217 EMQQTILNKKMGETGHFFVLNTKkgkdaGNYLYHQ------SNANQRPDWSEGALEKVLATGNGTIEYDNNtmtGEEKtr 290
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKD-----GTIIAHPdkelvgKKISDDEAAEEELAKKMLAGKSGSVEYTFN---GEKK-- 70

                         90       100
                 ....*....|....*....|.
gi 506321803 291 IMVYRSIPQWNWIVAGTVSKE 311
Cdd:cd12912   71 YVAYAPIPGTGWSLVVVVPES 91
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
315-646 1.93e-86

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 279.98  E-value: 1.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 315 AEINHTRNLFLGGGIILVLLFAAFFVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTT 394
Cdd:COG0840  174 LAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRE 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 395 IVSQVRNASEEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVT 474
Cdd:COG0840  254 LVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 475 DSVS--------------TMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSS 540
Cdd:COG0840  334 EAVEgieeiresveetaeTIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSA 413

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 541 TAVKEIETLIDES--------------LEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAI 606
Cdd:COG0840  414 EATKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI 493

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 506321803 607 VQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:COG0840  494 EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 329-646 1.09e-81

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 268.41  E-value: 1.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 329 IILVLLFAAFFVVltRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNASEEISA 408
Cdd:PRK15048 200 VVVLILLVAWYGI--RRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYA 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 409 STDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQ 488
Cdd:PRK15048 278 GTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSK 357

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 489 RIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQ 568
Cdd:PRK15048 358 KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAG 437

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506321803 569 AVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:PRK15048 438 ETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
 35-322 7.96e-81

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: 257.66  E-value: 7.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   35 TRSAGNQLKSLTLNDMQSQVNGVTDMINMYDTSLQAEVSNYTRLLASFLPTQFSLDTVNRTPFGNASQPTLKAGDTVL-- 112
Cdd:pfam17201   1 SRSAKGEVRALAESDLEEQVQDLADMLETQDESLRESVDSDLNVFRKLLPGSWRAVNQFTVDVGGVSLPVLYLGGTWLgq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  113 ----NLNTEVPDDFLSRTHAISTIFVRDGEDFTRVTTSLKKEDGSRAMGTKLDRESPAYALVMKGETYSGLATLFGKQYI 188
Cdd:pfam17201  81 nrdpNKNFPLVDEFTELTGGTATVFQRMNDDLLRVATSVKKEDGSRAIGTYIPASSPVYKAVLAGETYVGRAKVFGKWYV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  189 TQYQPIRDSASKVIGILFVGVDITKQFTEMQQTILNKKMGETGHFFVLNTkKGKDAGNYLYHQSNANQRPDWSEGA---- 264
Cdd:pfam17201 161 TAYEPIRDADGKVIGILYVGVPQDEALASLRKAIKKVKIGKTGYLYVLDG-KGDQKGKFIVHPTLEGKNILDAKDAdgep 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 506321803  265 -LEKVLATGNGTIEYDNNTmTGEEKTRIMVYRSIPQWNWIVAGTVSKESLMAEINHTRN 322
Cdd:pfam17201 240 fVKKLLQKKVGSLEYPWKA-DAAGRDKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLN 297
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
330-646 7.55e-77

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 255.26  E-value: 7.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 330 ILVLLFAAFFVVLTRKW------LSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNAS 403
Cdd:PRK15041 195 ILVGVMIVVLAVIFAVWfgikasLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGA 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 404 EEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDI 483
Cdd:PRK15041 275 NAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDI 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 484 KNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHF 563
Cdd:PRK15041 355 STSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTL 434

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 564 SEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSV 643
Cdd:PRK15041 435 VESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAV 514


                 ...
gi 506321803 644 FRI 646
Cdd:PRK15041 515 FRI 517
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
329-646 5.84e-74

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 247.29  E-value: 5.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 329 IILVLLFAAFFVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNASEEISA 408
Cdd:PRK09793 196 IIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHI 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 409 STDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQ 488
Cdd:PRK09793 276 GIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQ 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 489 RIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQ 568
Cdd:PRK09793 356 KIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAA 435

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506321803 569 AVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:PRK09793 436 ATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 398-645 6.03e-64

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: 212.15  E-value: 6.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   398 QVRNASEEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSV 477
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   478 STMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLI------- 550
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   551 -------DESLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNS 623
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 506321803   624 EDTAQGLRQKGHHLSELVSVFR 645
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 427-623 2.22e-53

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 181.67  E-value: 2.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 427 QASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRIADITTVIESIAFQTNI 506
Cdd:cd11386    3 LSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 507 LALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVN 586
Cdd:cd11386   83 LALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFE 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 506321803 587 DIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNS 623
Cdd:cd11386  163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 457-613 1.73e-43

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 153.74  E-value: 1.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  457 DLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALA 536
Cdd:pfam00015   2 DLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  537 QRSSTAVKEIETLIDE--------------SLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIASREQSAGIGQV 602
Cdd:pfam00015  82 ERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 161

                         170
                  ....*....|.
gi 506321803  603 NIAIVQIGQAT 613
Cdd:pfam00015 162 NQAVARMDQVT 172
sCache_3_3 pfam17202
Single cache domain 3;
110-212 2.00e-34

Single cache domain 3;


Pssm-ID: 465379 [Multi-domain]  Cd Length: 104  Bit Score: 126.12  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  110 TVLNLNTEVPDDFLSRTHAISTIFVrdgeDFTRVTTSLKKEDGSRAMGTKLDREsPAYALVMKGETYSGLATLFGKQYIT 189
Cdd:pfam17202   1 TLINGNFELVDKIKELTGGTATIFL----GDTRIATTVKDEDGKRAVGTKLSDE-VAEAVLKKGETYRGRADILGKWYYT 75

                          90       100
                  ....*....|....*....|...
gi 506321803  190 QYQPIRDSASKVIGILFVGVDIT 212
Cdd:pfam17202  76 AYEPLKDADGKVIGMLFVGIPEE 98
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms];
265-646 3.13e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 443621 [Multi-domain]  Cd Length: 510  Bit Score: 69.29  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 265 LEKVLATGNGTIEYD-NNTMTGEEKTRIMVYRSIPQWNWIVAGTVSKESLMAEINHTRN-----LFLGGGIILVLLFAAF 338
Cdd:COG4564  117 IEAAKKKGGGFVEYLwPKPGSGKPEPKLSYVKKFPPWDWVIGTGVYLDDIEAAFAAAALellllLALLLALALALLLLVL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 339 FVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNASEEISASTDALAADSE 418
Cdd:COG4564  197 AALAGLLLASALEGELNLAGALAALLLAAAAELLAALLLIGAAAGALLALAEAVAAVLAEALAAAAAAAAASAAASSAAL 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 419 NISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRIADITTVIE 498
Cdd:COG4564  277 AAAAAEAEAALAASEASAAAALAAAAAAAAAAAAAAAAAEAAAAAAAAAAAAAAAAASVADVAALAAAAAAAAAIAALAA 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 499 SIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQAVMDDLRNRI 578
Cdd:COG4564  357 AAAAAAAAAAAAAAIAAAAAAAAAAAAAAAAAAAEAAAAAAAAATAAAALEAVAAAAAAAAAAAAAEAAAAEVEAAAAIT 436

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506321803 579 LQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTILVNNSEDTAQGLRQKGHHLSELVSVFRI 646
Cdd:COG4564  437 AIILEAAAAAAAAIEAEEAAAVAAAAALAAEAAAAAAAAAEAAAAAAAAEAASAVVSAAAAAAAAGAA 504
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 217-311 3.05e-11

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: 60.09  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 217 EMQQTILNKKMGETGHFFVLNTKkgkdaGNYLYHQ------SNANQRPDWSEGALEKVLATGNGTIEYDNNtmtGEEKtr 290
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKD-----GTIIAHPdkelvgKKISDDEAAEEELAKKMLAGKSGSVEYTFN---GEKK-- 70

                         90       100
                 ....*....|....*....|.
gi 506321803 291 IMVYRSIPQWNWIVAGTVSKE 311
Cdd:cd12912   71 YVAYAPIPGTGWSLVVVVPES 91
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 217-310 1.99e-08

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


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 52.06  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 217 EMQQTILNKKMGETGHFFVLNTKkgkdaGNYLYH----QSNANQRPDWSEGALEKVLATGNGTIEYDNNTmtGEEktRIM 292
Cdd:cd18774    1 YLSDLLSSIKLGETGYAFLVDSD-----GTILAHppkeLVGKGKSLDDLALLAALLLAGESGTFEYTSDD--GVE--RLV 71

                         90
                 ....*....|....*...
gi 506321803 293 VYRSIPQWNWIVAGTVSK 310
Cdd:cd18774   72 AYRPVPGTPWVVVVGVPE 89
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
 201-313 6.00e-08

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: 54.68  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  201 VIGilfVGVDITKQFTEMQQTILNK----KMGETGHFFVLNTKkgkdaGNYLYH------QSNANQRPDWSEGA------ 264
Cdd:pfam08269 176 IIG---TGEYLDDIEEEIKQELLKTlasiRYGNNGYIFIYDTD-----GNMILHplkpelNGKDLTENKDDKGQelfqel 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 506321803  265 LEKVLATGNGTIEYDNNTMTGEEKTRIMVY-RSIPQWNWIVAGTVSKESL 313
Cdd:pfam08269 248 LEAAKKKGEGFVTYKWPKPGGDKPRPKISYvRYFPPWDWIIGTGVYLDEI 297
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 323-421 2.74e-07

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: 53.43  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 323 LFLGGGIILVLLFAAFFVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINgigqgltTIVSQVRNA 402
Cdd:COG5000    9 LLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFN-------RMTDQLKEQ 81

                         90
                 ....*....|....*....
gi 506321803 403 SEEISASTDALAADSENIS 421
Cdd:COG5000   82 REELEERRRYLETILENLP 100
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 329-618 1.15e-06

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 51.42  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 329 IILVLLFAAFFVVLTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNASEEISA 408
Cdd:COG3850  124 LLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAE 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 409 STDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQ 488
Cdd:COG3850  204 LELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLEL 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 489 RIADITTVIESIAFQTNILALNAAVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQ 568
Cdd:COG3850  284 ELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGAALA 363

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 506321803 569 AVMDDLRNRILQVSTIVNDIDIASREQSAGIGQVNIAIVQIGQATQENTI 618
Cdd:COG3850  364 AAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGE 413
sCache_3_2 pfam17203
Single cache domain 3; This domain is associated to sensor histidine kinases and recognizes ...
 123-213 5.31e-06

Single cache domain 3; This domain is associated to sensor histidine kinases and recognizes citrate and TCA cycle intermediates, Ag(II), Zn(II), Mg(II) (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435783 [Multi-domain]  Cd Length: 140  Bit Score: 46.25  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  123 LSRTHAISTIFVRDGEDfTRVTTSLKKEDGSRAMGtkldreSPAYALVMKGETYSGLATLFGKQYITQYQPIRDSASKVI 202
Cdd:pfam17203  47 VRRITGADYVVIADRRG-RVLAHPDPERVGRRLSG------PATAPALTAGRSYTGTVTGTLGPSLDAKLPIFDADGRVI 119

                          90
                  ....*....|.
gi 506321803  203 GILFVGVDITK 213
Cdd:pfam17203 120 GIVSVGVKQDS 130
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 376-461 1.03e-05

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: 47.67  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   376 DEVGRLIDAINGIGQGLTTIVSQVRNAS---EEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNV 452
Cdd:smart00283 172 SEVEEGVELVEETGDALEEIVDSVEEIAdlvQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLA 251


                   ....*....
gi 506321803   453 SAAKDLAEQ 461
Cdd:smart00283 252 EELDELVER 260
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 120-307 1.80e-05

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: 46.56  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  120 DDFLSRTHAISTIFVRDGEDFTRVTTSLKKEDGSRAMgtkldRESPAYALVMKGE-------TYSGLATLFGKQYITQYQ 192
Cdd:pfam02743  58 ESLLRSNPGISSIYLVDADGRVLASSDESPSYPGLDV-----SERPWYKEALKGGggiiwvfSSPYPSSESGEPVLTIAR 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803  193 PIRDSASKVIGILFVGVDItkqfTEMQQTILNKKMGETGHFFVLNtkkgkDAGNYLYHQSNANQRPDWSEGALEKVLATG 272
Cdd:pfam02743 133 PIYDDDGEVIGVLVADLDL----DTLQELLSQIKLGEGGYVFIVD-----SDGRILAHPLGKNLRSLLAPFLGKSLADAL 203

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 506321803  273 NGTIEYDNNTmTGEEKTRIMVYRSIPQWNWIVAGT 307
Cdd:pfam02743 204 PGSGITEIAV-DLDGEDYLVAYAPIPGTGWTLVVV 237
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
112-612 2.75e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 47.42  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 112 LNLNTEVPDDFLSRTHAISTIFVRDGEDFTRVTTSLKKEDGSRAMGTKLDRESPAYALVMKGETYSGLATLFGKQYITQY 191
Cdd:COG2770    3 LLLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 192 QPIRDSASKVIGILFVGVDITKQFTEMQQTILNKKMGETGHFFVLNTKKGKDAGNYLYHQSNANQRPDWSEGALEKVLAT 271
Cdd:COG2770   83 SLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 272 GNGTIEYDNNTMTGEEKTRIMVYRSIPQWNWIVAGTVSKESLMAEINHTRNLFLGGGIILvlLFAAFFVVLTRKWLSQPL 351
Cdd:COG2770  163 ALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLAL--LLALLLALLLARRITRPL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 352 VEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVSQVRNASEEISASTDALAADSENISEQIARQASSV 431
Cdd:COG2770  241 RRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 432 EETSASMEQLSASVKQNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRIADITTVIESIAFQTNILALNA 511
Cdd:COG2770  321 LLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803 512 AVEAARAGEHGRGFAVVAAEVRALAQRSSTAVKEIETLIDESLEKIEAGYHFSEKTQAVMDDLRNRILQVSTIVNDIDIA 591
Cdd:COG2770  401 ALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLL 480

                        490       500
                 ....*....|....*....|.
gi 506321803 592 SREQSAGIGQVNIAIVQIGQA 612
Cdd:COG2770  481 LAALGALELLLLEEEEEAGAA 501
HAMP pfam00672
HAMP domain;
342-386 4.70e-05

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 41.07  E-value: 4.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 506321803  342 LTRKWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAIN 386
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFN 45
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 348-386 1.07e-04

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: 40.12  E-value: 1.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 506321803 348 SQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAIN 386
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFN 39
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
345-397 4.40e-04

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 38.38  E-value: 4.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 506321803   345 KWLSQPLVEIVKVAEQFSAGNLTATLSSNRYDEVGRLIDAINGIGQGLTTIVS 397
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 377-452 1.82e-03

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 39.91  E-value: 1.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506321803 377 EVGRLIDAINGIGQGLTTIVSQVRNASEEISASTDALAADSENISEQIARQASSVEETSASMEQLSASVKQNADNV 452
Cdd:cd11386  121 EIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 371-490 2.12e-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: 40.35  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506321803   371 SSNRYDEVGRLIDAI----NGIGQGLTTIVSQVRNASEEISASTDALaadsENISEQIARQASSVEETSASMEQLSASVK 446
Cdd:smart00283 142 SAESAKEIESLIKEIqeetNEAVAAMEESSSEVEEGVELVEETGDAL----EEIVDSVEEIADLVQEIAAATDEQAAGSE 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 506321803   447 QNADNVSAAKDLAEQSAAAARSGSQTVTDSVSTMSDIKNSSQRI 490
Cdd:smart00283 218 EVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERF 261
 
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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