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Conserved domains on  [gi|1490893222|gb|RLE28182|]
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hypothetical protein DRJ65_00490 [Acidobacteria bacterium]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 12798465)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
115-408 1.29e-54

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 192.93  E-value: 1.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 115 IAASVEAAVRALSGLVQQIQSVSVEVAGTANTVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAA 194
Cdd:COG0840   240 LADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 195 QSEAAGRNGAEAIEAAVTGIESVREGMGIIASRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFS 274
Cdd:COG0840   320 EASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 275 VVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLAT 354
Cdd:COG0840   400 VVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAAS 479
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490893222 355 QEQQTASQEVLLAVREESDVITEIAEGLEEFTGAAIRLNQLALSIQLLSQSFRL 408
Cdd:COG0840   480 EEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
414-540 3.48e-10

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: 57.96  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 414 LKHLVFQVAQSLESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAFAVNRDLVGEDLekgvaavgqSYSDRPWFQ 493
Cdd:cd18773     8 LRSLASALEALAALGSADREELQALLRRLLERNPEISGIYVVDADGRVVASSDRDPGGGDDD---------DDRDRFWYQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1490893222 494 AAGRDNLTSVTPVYQSLLTGDQCFSVVVPVKRRDGTQEATLGVDVNV 540
Cdd:cd18773    79 AAKATGKLVISEPYISRVTGKPVITLSRPIRDADGRFIGVVGADIDL 125
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
115-408 1.29e-54

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 192.93  E-value: 1.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 115 IAASVEAAVRALSGLVQQIQSVSVEVAGTANTVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAA 194
Cdd:COG0840   240 LADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 195 QSEAAGRNGAEAIEAAVTGIESVREGMGIIASRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFS 274
Cdd:COG0840   320 EASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 275 VVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLAT 354
Cdd:COG0840   400 VVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAAS 479
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490893222 355 QEQQTASQEVLLAVREESDVITEIAEGLEEFTGAAIRLNQLALSIQLLSQSFRL 408
Cdd:COG0840   480 EEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
146-407 9.75e-47

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: 164.00  E-value: 9.75e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  146 TVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAAQSEAAGRNGAEAIEAAVTGIESVREGMGIIA 225
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  226 SRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAAI 305
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  306 HAVVISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVREESDVITEIAEGLEEF 385
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 1490893222  386 TGAAIRLNQLALSIQLLSQSFR 407
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
173-370 1.98e-37

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: 136.98  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 173 EELARTAAQIATNASSQADLAAQSEAAGRNGAEAIEAAVTGIESVREGMGIIASRAEILDSRSREIYQVLDLITDISQET 252
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 253 HILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGKKTDLVAEQARATATA 332
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1490893222 333 VEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVRE 370
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
115-411 5.76e-25

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 108.56  E-value: 5.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 115 IAASVEAAVRALSGLVQQIQSVSVEVAGTANTVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAA 194
Cdd:PRK15048  250 LAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQ 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 195 QSEAAGRNGAEAIEaavtgiesvregmGIIASRAEILDSrSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFS 274
Cdd:PRK15048  330 SASDTAQHGGKVVD-------------GVVKTMHEIADS-SKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 275 VVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGkktdlvaEQARATATAVEQLSAALGntaqaarEISLAT 354
Cdd:PRK15048  396 VVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAG-------ETMNNIVNAVTRVTDIMG-------EIASAS 461
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490893222 355 QEQQTASQEVLLAVREESDVITEIAEGLEEFTGAAIRLNQLALSIQLLSQSFRLESS 411
Cdd:PRK15048  462 DEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAAS 518
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
229-375 4.12e-23

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: 96.35  E-value: 4.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 229 EILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAAIHAV 308
Cdd:pfam00015  26 EQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDS 105
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490893222 309 VISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVREESDVI 375
Cdd:pfam00015 106 TASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQVT 172
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
414-540 3.48e-10

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: 57.96  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 414 LKHLVFQVAQSLESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAFAVNRDLVGEDLekgvaavgqSYSDRPWFQ 493
Cdd:cd18773     8 LRSLASALEALAALGSADREELQALLRRLLERNPEISGIYVVDADGRVVASSDRDPGGGDDD---------DDRDRFWYQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1490893222 494 AAGRDNLTSVTPVYQSLLTGDQCFSVVVPVKRRDGTQEATLGVDVNV 540
Cdd:cd18773    79 AAKATGKLVISEPYISRVTGKPVITLSRPIRDADGRFIGVVGADIDL 125
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
425-542 7.94e-04

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: 41.17  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 425 LESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAFAVNRDlvgedlekgvAAVGQSYSDRPWFQAA---GRDNLT 501
Cdd:pfam02743  43 QDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSDESP----------SYPGLDVSERPWYKEAlkgGGGIIW 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1490893222 502 SVTPVYQSLLTGDQCFSVVVPVKRRDGTQEATLGVDVNVGN 542
Cdd:pfam02743 113 VFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDT 153
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
115-408 1.29e-54

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 192.93  E-value: 1.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 115 IAASVEAAVRALSGLVQQIQSVSVEVAGTANTVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAA 194
Cdd:COG0840   240 LADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 195 QSEAAGRNGAEAIEAAVTGIESVREGMGIIASRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFS 274
Cdd:COG0840   320 EASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFA 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 275 VVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLAT 354
Cdd:COG0840   400 VVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAAS 479
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490893222 355 QEQQTASQEVLLAVREESDVITEIAEGLEEFTGAAIRLNQLALSIQLLSQSFRL 408
Cdd:COG0840   480 EEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
146-407 9.75e-47

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: 164.00  E-value: 9.75e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  146 TVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAAQSEAAGRNGAEAIEAAVTGIESVREGMGIIA 225
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  226 SRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAAI 305
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  306 HAVVISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVREESDVITEIAEGLEEF 385
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 1490893222  386 TGAAIRLNQLALSIQLLSQSFR 407
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
173-370 1.98e-37

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: 136.98  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 173 EELARTAAQIATNASSQADLAAQSEAAGRNGAEAIEAAVTGIESVREGMGIIASRAEILDSRSREIYQVLDLITDISQET 252
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 253 HILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGKKTDLVAEQARATATA 332
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1490893222 333 VEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVRE 370
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEE 198
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
115-411 5.76e-25

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 108.56  E-value: 5.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 115 IAASVEAAVRALSGLVQQIQSVSVEVAGTANTVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAA 194
Cdd:PRK15048  250 LAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQ 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 195 QSEAAGRNGAEAIEaavtgiesvregmGIIASRAEILDSrSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFS 274
Cdd:PRK15048  330 SASDTAQHGGKVVD-------------GVVKTMHEIADS-SKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 275 VVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGkktdlvaEQARATATAVEQLSAALGntaqaarEISLAT 354
Cdd:PRK15048  396 VVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAG-------ETMNNIVNAVTRVTDIMG-------EIASAS 461
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490893222 355 QEQQTASQEVLLAVREESDVITEIAEGLEEFTGAAIRLNQLALSIQLLSQSFRLESS 411
Cdd:PRK15048  462 DEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAAS 518
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
115-396 2.00e-24

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 107.08  E-value: 2.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 115 IAASVEAAVRALSGLVQQIQSVSVEVAGTANTVRDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAA 194
Cdd:PRK09793  248 IFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAK 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 195 QSEAAGRNGAEAIEAavtgiesvregmgiIASRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFS 274
Cdd:PRK09793  328 NAATTAQAGGVQVST--------------MTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 275 VVAREVRRLAERSRESVESVRNILHEFTAAIHavvisteEGGKKTDLVAEQARATATAVEQLSAALGntaqaarEISLAT 354
Cdd:PRK09793  394 VVAGEVRNLASRSAQAAKEIKGLIEESVNRVQ-------QGSKLVNNAAATMTDIVSSVTRVNDIMG-------EIASAS 459
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1490893222 355 QEQQTASQEVLLAVREESDVITEIAEGLEEftgAAIRLNQLA 396
Cdd:PRK09793  460 EEQRRGIEQVAQAVSQMDQVTQQNASLVEE---AAVATEQLA 498
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
229-375 4.12e-23

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: 96.35  E-value: 4.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 229 EILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAAIHAV 308
Cdd:pfam00015  26 EQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDS 105
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490893222 309 VISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVREESDVI 375
Cdd:pfam00015 106 TASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQVT 172
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
129-410 4.25e-21

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 96.95  E-value: 4.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 129 LVQQIQSVSVEVAGTANTVRDTSAQLASGSSE--------------QAASVVEITATMEELARTAAQIATNASSQADLA- 193
Cdd:PRK15041  252 LAESLRHMQGELMRTVGDVRNGANAIYSGASEiatgnndlssrteqQAASLEETAASMEQLTATVKQNAENARQASHLAl 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 194 AQSEAAGRNGAEaieaavtgIESVREGMGIIASRaeildsrSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERF 273
Cdd:PRK15041  332 SASETAQRGGKV--------VDNVVQTMRDISTS-------SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGF 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 274 SVVAREVRRLAERSRESVESVRNILHEFTAAIHAVVISTEEGGKKTDLVaeqaratATAVEQLSAALGntaqaarEISLA 353
Cdd:PRK15041  397 AVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEI-------VSAVTRVTDIMG-------EIASA 462
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490893222 354 TQEQQTASQEVLLAVREESDVITEIAEGLEEFTGAAIRLNQLALSIQLLSQSFRLES 410
Cdd:PRK15041  463 SDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQ 519
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
414-540 3.48e-10

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: 57.96  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 414 LKHLVFQVAQSLESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAFAVNRDLVGEDLekgvaavgqSYSDRPWFQ 493
Cdd:cd18773     8 LRSLASALEALAALGSADREELQALLRRLLERNPEISGIYVVDADGRVVASSDRDPGGGDDD---------DDRDRFWYQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1490893222 494 AAGRDNLTSVTPVYQSLLTGDQCFSVVVPVKRRDGTQEATLGVDVNV 540
Cdd:cd18773    79 AAKATGKLVISEPYISRVTGKPVITLSRPIRDADGRFIGVVGADIDL 125
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
412-529 3.68e-07

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: 48.92  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 412 HSLKHLVFQVAQSlESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAFAVnrdlvgedlekGVAAVGQSYSDRPW 491
Cdd:cd12914     6 LLLRSLADDLEAR-GAASADPAALQALLRRLLARLPEVRSIFVVDADGRVVASSG-----------PGPAPGLDVSDRDY 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490893222 492 FQAA-GRDNLTSVTPVYQSLLTGDQCFSVVVPVKRRDGT 529
Cdd:cd12914    74 FQAArAGGGGLFISEPVISRVTGKPVIPLSRPIRDADGR 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
148-481 1.36e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 148 RDTSAQLASGSSEQAASVVEITATMEELARTAAQIATNASSQADLAAQSEAAG---RNGAEAIEAAVTGIESVREGmgiI 224
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEER---R 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 225 ASRAEILDSRSREIYQVLDLITDISQETHILSLNAAIEASTAGEYGERFSVVAREVRRLAERSRESVESVRNILHEFTAA 304
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 305 IHAVVISTEEGGKKTDLVAEQARATATAVEQLSAALGNTAQAAREISLATQEQQTASQEVLLAVREESDVITEIAEGLEE 384
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 385 FTGAAIRLNQLALSIQLLSQSFRLESSHSLKHLVFQVAQSLESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAF 464
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
                         330
                  ....*....|....*..
gi 1490893222 465 AVNRDLVGEDLEKGVAA 481
Cdd:COG1196   552 VVEDDEVAAAAIEYLKA 568
PHA03247 PHA03247
large tegument protein UL36; Provisional
116-221 7.54e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 7.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222  116 AASVEAAVRALSGLVQQiqsvsveVAGTANTVRDTSAQLA--SGSSEQAASVVEITATMEELARTAAQIATNASSQADLA 193
Cdd:PHA03247  1149 ESTVDAAVRAHGVLADA-------VAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARLGALGAAAADLA 1221
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1490893222  194 AQ--SEAAGRNG--AEAIEAAVTGIESVREGM 221
Cdd:PHA03247  1222 VAvrRENPQAEGdrAALLEAAARAVTAAREGL 1253
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
425-542 7.94e-04

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: 41.17  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893222 425 LESVSGNLEATDRILHGVFTDLPYLEMAYLVDTEGGMVAFAVNRDlvgedlekgvAAVGQSYSDRPWFQAA---GRDNLT 501
Cdd:pfam02743  43 QDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSDESP----------SYPGLDVSERPWYKEAlkgGGGIIW 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1490893222 502 SVTPVYQSLLTGDQCFSVVVPVKRRDGTQEATLGVDVNVGN 542
Cdd:pfam02743 113 VFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDT 153
 
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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