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Conserved domains on  [gi|446332381|ref|WP_000410236|]
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MULTISPECIES: methyl-accepting chemotaxis protein [Bacillus]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 11435591)

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];
53-428 1.45e-66

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 221.43  E-value: 1.45e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGMVknidttfs 132
Cdd:COG0840  185 AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDV-DSKDEIGQLADAFNRMIENLRELV-------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 133 ytnnqvQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGHST 212
Cdd:COG0840  256 ------GQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 213 RVFTSLIQGIQTLAKENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLA 292
Cdd:COG0840  330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLA 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 293 DESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQT 372
Cdd:COG0840  410 ERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEV 489

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446332381 373 GAQTKAVAAIAEETSAGSQEVARVTlqqsknmvvidqllKDLEKQATDLKQTIERF 428
Cdd:COG0840  490 NQAIEQIAAAAQENAASVEEVAAAA--------------EELAELAEELQELVSRF 531
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
53-428 1.45e-66

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 221.43  E-value: 1.45e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGMVknidttfs 132
Cdd:COG0840  185 AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDV-DSKDEIGQLADAFNRMIENLRELV-------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 133 ytnnqvQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGHST 212
Cdd:COG0840  256 ------GQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 213 RVFTSLIQGIQTLAKENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLA 292
Cdd:COG0840  330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLA 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 293 DESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQT 372
Cdd:COG0840  410 ERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEV 489

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446332381 373 GAQTKAVAAIAEETSAGSQEVARVTlqqsknmvvidqllKDLEKQATDLKQTIERF 428
Cdd:COG0840  490 NQAIEQIAAAAQENAASVEEVAAAA--------------EELAELAEELQELVSRF 531
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 149-429 2.45e-49

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: 168.23  E-value: 2.45e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   149 TRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGhstrvftSLIQGIQTLAKE 228
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVE-------DAITAMDQIREV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   229 NEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRN 308
Cdd:smart00283  76 VEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   309 MQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSA 388
Cdd:smart00283 156 IQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAA 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 446332381   389 GSQEVARVTlqqsknmvvidqllKDLEKQATDLKQTIERFS 429
Cdd:smart00283 236 MSEEISAAA--------------EELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 167-394 6.63e-40

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: 141.61  E-value: 6.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 167 EQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQAlghstrvftsliqgIQTLAKENEDSMQNVQKLEERMKQV 246
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQ--------------MNQIDESVDEAVSAVEELEESSAEI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 247 EHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKI 326
Cdd:cd11386   67 GEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEE 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446332381 327 AKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQvshihqtgaqtkavAAIAEETSAGSQEVA 394
Cdd:cd11386  147 VEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ--------------SASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 227-382 3.65e-30

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: 114.84  E-value: 3.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  227 KENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLL 306
Cdd:pfam00015  16 KEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALI 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446332381  307 RNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAI 382
Cdd:pfam00015  96 IEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQV 171
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
53-428 1.82e-25

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 108.89  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILA--YGAAVFLIKPLRKLEEAARKAAEGDIredvplpktddeIKSLSVAFNMMLGNLRGMVKNIDTT 130
Cdd:PRK15041 195 ILVGVMIVVLAVIFAvwFGIKASLVAPMNRLIDSIRHIAGGDL------------VKPIEVDGSNEMGQLAESLRHMQGE 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 131 FSYTnnqVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGH 210
Cdd:PRK15041 263 LMRT---VGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQR 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 211 STRVFTSLIQGIQTLAKENEdsmqnvqkleermkQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRK 290
Cdd:PRK15041 340 GGKVVDNVVQTMRDISTSSQ--------------KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRN 405

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 291 LADESDHSARNISQLLrnmQDEVQQVAMKMTeQVKIAKEeakrgeatelILKEMSSSVMEVADATQQISSYMNEQVSHIH 370
Cdd:PRK15041 406 LAQRSAQAAREIKSLI---EDSVGKVDVGST-LVESAGE----------TMAEIVSAVTRVTDIMGEIASASDEQSRGID 471

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446332381 371 QTGAqtkAVAaiaeetsagsqEVARVTLQQSKNMVVIDQLLKDLEKQATDLKQTIERF 428
Cdd:PRK15041 472 QVGL---AVA-----------EMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
 35-120 1.32e-04

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 43.92  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   35 IYVIYD--YFQSYVSQTVYNIIV-MLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLPKTDDEIKSLSV 111
Cdd:TIGR01386 146 ITVALDinAHTHLLDALRKWLILiAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPESLDQRLDPSRAPAELRELAQ 225


                  ....*....
gi 446332381  112 AFNMMLGNL 120
Cdd:TIGR01386 226 SFNAMLGRL 234
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
53-428 1.45e-66

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 221.43  E-value: 1.45e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGMVknidttfs 132
Cdd:COG0840  185 AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDV-DSKDEIGQLADAFNRMIENLRELV-------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 133 ytnnqvQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGHST 212
Cdd:COG0840  256 ------GQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 213 RVFTSLIQGIQTLAKENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLA 292
Cdd:COG0840  330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLA 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 293 DESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQT 372
Cdd:COG0840  410 ERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEV 489

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446332381 373 GAQTKAVAAIAEETSAGSQEVARVTlqqsknmvvidqllKDLEKQATDLKQTIERF 428
Cdd:COG0840  490 NQAIEQIAAAAQENAASVEEVAAAA--------------EELAELAEELQELVSRF 531
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 149-429 2.45e-49

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: 168.23  E-value: 2.45e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   149 TRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGhstrvftSLIQGIQTLAKE 228
Cdd:smart00283   3 SEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVE-------DAITAMDQIREV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   229 NEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRN 308
Cdd:smart00283  76 VEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   309 MQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSA 388
Cdd:smart00283 156 IQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAA 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 446332381   389 GSQEVARVTlqqsknmvvidqllKDLEKQATDLKQTIERFS 429
Cdd:smart00283 236 MSEEISAAA--------------EELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 167-394 6.63e-40

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: 141.61  E-value: 6.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 167 EQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQAlghstrvftsliqgIQTLAKENEDSMQNVQKLEERMKQV 246
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQ--------------MNQIDESVDEAVSAVEELEESSAEI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 247 EHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKI 326
Cdd:cd11386   67 GEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEE 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446332381 327 AKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQvshihqtgaqtkavAAIAEETSAGSQEVA 394
Cdd:cd11386  147 VEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ--------------SASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 227-382 3.65e-30

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: 114.84  E-value: 3.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  227 KENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLL 306
Cdd:pfam00015  16 KEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALI 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446332381  307 RNMQDEVQQVAMKMTEQVKIAKEEAKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAI 382
Cdd:pfam00015  96 IEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARMDQV 171
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
53-428 1.82e-25

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 108.89  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILA--YGAAVFLIKPLRKLEEAARKAAEGDIredvplpktddeIKSLSVAFNMMLGNLRGMVKNIDTT 130
Cdd:PRK15041 195 ILVGVMIVVLAVIFAvwFGIKASLVAPMNRLIDSIRHIAGGDL------------VKPIEVDGSNEMGQLAESLRHMQGE 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 131 FSYTnnqVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGH 210
Cdd:PRK15041 263 LMRT---VGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQR 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 211 STRVFTSLIQGIQTLAKENEdsmqnvqkleermkQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRK 290
Cdd:PRK15041 340 GGKVVDNVVQTMRDISTSSQ--------------KIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRN 405

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 291 LADESDHSARNISQLLrnmQDEVQQVAMKMTeQVKIAKEeakrgeatelILKEMSSSVMEVADATQQISSYMNEQVSHIH 370
Cdd:PRK15041 406 LAQRSAQAAREIKSLI---EDSVGKVDVGST-LVESAGE----------TMAEIVSAVTRVTDIMGEIASASDEQSRGID 471

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446332381 371 QTGAqtkAVAaiaeetsagsqEVARVTLQQSKNMVVIDQLLKDLEKQATDLKQTIERF 428
Cdd:PRK15041 472 QVGL---AVA-----------EMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVF 515
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 53-430 1.49e-23

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 103.16  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWsgilaYGAAVFLIKPLRKLEEAARKAAEGDIredvplpktddeIKSLSVAFNMMLGNLRGMVKNIDTTFS 132
Cdd:PRK15048 200 VVVLILLVAW-----YGIRRMLLTPLAKIIAHIREIAGGNL------------ANTLTIDGRSEMGDLAQSVSHMQRSLT 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 133 YTnnqVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGHST 212
Cdd:PRK15048 263 DT---VTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGG 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 213 RVFTSLIQGIQTLAKENedsmqnvqkleermKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLA 292
Cdd:PRK15048 340 KVVDGVVKTMHEIADSS--------------KKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLA 405

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 293 DESDHSARNISQLLrnmQDEVQQVAmkmTEQVKIakeeakrgEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQT 372
Cdd:PRK15048 406 SRSAQAAKEIKALI---EDSVSRVD---TGSVLV--------ESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQV 471

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446332381 373 GAQTKAVAAIAEETSAGSQEVARVTLQqsknmvvidqllkdLEKQATDLKQTIERFSM 430
Cdd:PRK15048 472 ALAVSEMDRVTQQNASLVQESAAAAAA--------------LEEQASRLTQAVSAFRL 515
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
44-394 2.63e-22

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 98.99  E-value: 2.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  44 SYVSQTVYNIIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGM 123
Cdd:PRK09793 184 NYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAV-YGRNEITAIFASLKTMQQALRGT 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 124 VKNIdttfsytnnqvqqirKQTGEATRQaqGVSETLA---EISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTL 200
Cdd:PRK09793 263 VSDV---------------RKGSQEMHI--GIAEIVAgnnDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASEL 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 201 S---SEMVQALGHSTRVFTSLIQGIQTLAKENEDsmqnvqkleermkqvehIVSVVSAIASQTNLLALNASIEAARAGEH 277
Cdd:PRK09793 326 AknaATTAQAGGVQVSTMTHTMQEIATSSQKIGD-----------------IISVIDGIAFQTNILALNAAVEAARAGEQ 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 278 GRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAmkmteqvKIAKEEAKrgeatelILKEMSSSVMEVADATQQ 357
Cdd:PRK09793 389 GRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGS-------KLVNNAAA-------TMTDIVSSVTRVNDIMGE 454

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446332381 358 ISSYMNEQVSHIHQTGAQ-------TKAVAAIAEETSAGSQEVA 394
Cdd:PRK09793 455 IASASEEQRRGIEQVAQAvsqmdqvTQQNASLVEEAAVATEQLA 498
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 75-120 1.44e-08

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


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 50.52  E-value: 1.44e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446332381  75 IKPLRKLEEAARKAAEGDIREDVPlPKTDDEIKSLSVAFNMMLGNL 120
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVP-VRSKDEIGELARAFNQMAERL 45
HAMP pfam00672
HAMP domain;
74-121 2.46e-08

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 49.93  E-value: 2.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446332381   74 LIKPLRKLEEAARKAAEGDIREDVPlPKTDDEIKSLSVAFNMMLGNLR 121
Cdd:pfam00672   6 ILRPLRRLAEAARRIASGDLDVRLP-VSGRDEIGELARAFNQMAERLR 52
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 53-141 3.79e-08

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 54.97  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGMVKNIDTTFS 132
Cdd:COG5000   12 LLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPV-TGDDEIGELARAFNRMTDQLKEQREELEERRR 90


                 ....*....
gi 446332381 133 YTNNQVQQI 141
Cdd:COG5000   91 YLETILENL 99
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
74-124 6.57e-08

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 48.78  E-value: 6.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 446332381    74 LIKPLRKLEEAARKAAEGDIREDVPlPKTDDEIKSLSVAFNMMLGNLRGMV 124
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGDLTVRLP-VDGRDEIGELARAFNEMADRLEETI 52
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
11-426 3.93e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 45.87  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  11 GLRTQLMLFTTVLAFITYSTSIFFIYVIYDYFQSYVSQTVYNIIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAE 90
Cdd:COG2770  173 LLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAA 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  91 GDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGMVKNIDTTFSYTNNQVQQIRKQTGEATRQAQGVSETLAEISSGAEQSA 170
Cdd:COG2770  253 GDLDVRIPV-SRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 171 ASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGHSTRVFTSLIQGIQTLAKENEDSMQNVQKLEERMKQVEHIV 250
Cdd:COG2770  332 LLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEE 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 251 SVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLADESDHSARNISQLLRNMQDEVQQVAMKMTEQVKIAKEE 330
Cdd:COG2770  412 LVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLL 491

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 331 AKRGEATELILKEMSSSVMEVADATQQISSYMNEQVSHIHQTGAQTKAVAAIAEETSAGSQEVARVTLQQSKNMVVIDQL 410
Cdd:COG2770  492 LEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAAL 571

                        410
                 ....*....|....*.
gi 446332381 411 LKDLEKQATDLKQTIE 426
Cdd:COG2770  572 LLAAVAALLELAALLL 587
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
 35-120 1.32e-04

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 43.92  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   35 IYVIYD--YFQSYVSQTVYNIIV-MLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLPKTDDEIKSLSV 111
Cdd:TIGR01386 146 ITVALDinAHTHLLDALRKWLILiAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPESLDQRLDPSRAPAELRELAQ 225


                  ....*....
gi 446332381  112 AFNMMLGNL 120
Cdd:TIGR01386 226 SFNAMLGRL 234
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
11-127 8.36e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 41.54  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  11 GLRTQLMLFTTVLAFITYSTSIFFIYVIYDYFQSYVSQTVYN-----IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAA 85
Cdd:COG2972  113 LLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSlrrliLLIILLLLLLALLLSYLLSRSITRPIKRLKKAM 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446332381  86 RKAAEGDIREdvPLPKTDDEIKSLSVAFNMMLGNLRGMVKNI 127
Cdd:COG2972  193 KKVEKGDLVR--LEVSGNDEIGILARSFNEMVERIKELIEEV 232
PTZ00121 PTZ00121
MAEBL; Provisional
 73-426 1.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381   73 FLIKPLRKLEEAARKAAEGDIREDVPLPKtdDEIKSLSVAFNMMLGNLRGMVKnidttfSYTNNQVQQIRKQTG-EATRQ 151
Cdd:PTZ00121 1024 FNIEKIEELTEYGNNDDVLKEKDIIDEDI--DGNHEGKAEAKAHVGQDEGLKP------SYKDFDFDAKEDNRAdEATEE 1095

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  152 AQGVSETLAEISSG-AEQSAASIQAIVSAVDtttsiASEVEEKAKQSDTLSSEMVQALGHSTRVftsliqgiqTLAKENE 230
Cdd:PTZ00121 1096 AFGKAEEAKKTETGkAEEARKAEEAKKKAED-----ARKAEEARKAEDARKAEEARKAEDAKRV---------EIARKAE 1161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  231 DSmqnvQKLEERMKQVEhivsvvsaiasqtnllalNASIEAARAGEHGRGfavvAEEVRKLAD----ESDHSARNISQL- 305
Cdd:PTZ00121 1162 DA----RKAEEARKAED------------------AKKAEAARKAEEVRK----AEELRKAEDarkaEAARKAEEERKAe 1215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  306 -LRNMQDEVQQVAMKMTEQVKIAKEEAKRGEATElilkemsssvmevadATQQISSYMNEQVSHIHQTGAQTKAVAAIAE 384
Cdd:PTZ00121 1216 eARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER---------------NNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 446332381  385 ETSAGSQEVARV-TLQQSKNMVVIDQLLKDLE--KQATDLKQTIE 426
Cdd:PTZ00121 1281 DELKKAEEKKKAdEAKKAEEKKKADEAKKKAEeaKKADEAKKKAE 1325
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 53-296 2.43e-03

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 40.25  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381  53 IIVMLLGVVWSGILAYGAAVFLIKPLRKLEEAARKAAEGDIREDVPLpKTDDEIKSLSVAFNMMLGNLRGMVKNIDTTFS 132
Cdd:COG3850  121 LLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPV-SGRDELGTLARAFNRMADELQELYAELEEEEE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 133 YTNNQVQQIRKQTGEATRQAQGVSETLAEISSGAEQSAASIQAIVSAVDTTTSIASEVEEKAKQSDTLSSEMVQALGHST 212
Cdd:COG3850  200 LEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALL 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446332381 213 RVFTSLIQGIQTLAKENEDSMQNVQKLEERMKQVEHIVSVVSAIASQTNLLALNASIEAARAGEHGRGFAVVAEEVRKLA 292
Cdd:COG3850  280 LLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAG 359


                 ....
gi 446332381 293 DESD 296
Cdd:COG3850  360 AALA 363
PRK10604 PRK10604
sensor protein RstB; Provisional
 66-124 5.73e-03

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 38.82  E-value: 5.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446332381  66 LAYGAAVFL-IKP----LRKLEEAARKAAEGDIREDVPLPKTdDEIKSLSVAFNMMLGNLRGMV 124
Cdd:PRK10604 147 LSLAFPVFLwMRPhwqdMLKLEAAAQRLGDGHLAERIHFDEG-SSLERLGVAFNQMADNINALI 209
envZ PRK09467
osmolarity sensor protein; Provisional
 49-116 6.33e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 38.74  E-value: 6.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446332381  49 TVYNIIVMLLGVVwsgilayGAAVF---LIKPLRKLEEAARKAAEGDIREdvPLP-KTDDEIKSLSVAFNMM 116
Cdd:PRK09467 156 FRYTLAIGLLSVA-------GGWLFiriQNRPLVALEHAALQVGKGEIPP--PLReYGASEVRSVTRAFNQM 218
 
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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