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Conserved domains on  [gi|1956494107|ref|WP_200374649|]
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methyl-accepting chemotaxis protein [Thiocystis violacea]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MCP_signal super family cl46910
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 563-892 5.53e-85

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


The actual alignment was detected with superfamily member PRK15048:

Pssm-ID: 481250 [Multi-domain]  Cd Length: 553  Bit Score: 283.44  E-value: 5.53e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 563 LTDLARVM---NAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSERTESQ 639
Cdd:PRK15048  217 LTPLAKIIahiREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQ 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 640 ASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNIL 719
Cdd:PRK15048  297 ASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNIL 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 720 ALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSE 799
Cdd:PRK15048  377 ALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGE 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 800 IADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQARELKRAVSLFKLdTSGLRNQDWTGAERRGPDRA 879
Cdd:PRK15048  457 IASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL-AASPLTNKPQTPSRPASEQP 535

                         330
                  ....*....|...
gi 1956494107 880 TNVTRLAPEPADT 892
Cdd:PRK15048  536 PAQPRLRIAEQDP 548
NIT pfam08376
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ...
 57-295 5.16e-47

Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.


:

Pssm-ID: 462453 [Multi-domain]  Cd Length: 227  Bit Score: 167.67  E-value: 5.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  57 AHELQKERGMSAGFLSS-KGVKFADRLPGQRQASDTGIAGLESALSGVDLAtmaPEYQRLLGQSREGLSQLPDFRQRIDQ 135
Cdd:pfam08376   1 VHALQKERGLSAGYLASgGGGRFAAELAAQRAATDAALAALRAALAELALP---ARLADRLAALLRALDQLPALRRQVDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 136 LQVPPPASFQEYSRLIADLLEVATRSSNELPDAAIARLANAKTALLYLKERNGQERAILSGAFSAGRITPANYDILLTLL 215
Cdd:pfam08376  78 GALSALEALAAYTELIAALLDLVDELAAGSPDPELARQLRALAALLRAKEAAGQERALLAAALAAGRFTAAEYRRFLSLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 216 SDQANFLRLTKSFALPEQTALLESKLSQPVVKdvgEVERMvketgadREIFYPPEVWFDQITQKIDLLRDVEQQFSQDIA 295
Cdd:pfam08376 158 AAQRAALAEFRAAATPEQRALYDATVTGPAVA---AAERL-------RDRLVDAAAWFAASTARIDLLREVEDRLADDLA 227
NtrY super family cl34858
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 346-498 6.58e-07

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


The actual alignment was detected with superfamily member COG5000:

Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 52.66  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 346 VQVAHDIAKGRLDNEIPVKSGDSVSLLA-SMKHMQQQLHERietERRLAAESRRIQSALDKASTNMMVADNDGRIIYMNA 424
Cdd:COG5000    41 AEATRAVAAGDLSVRLPVTGDDEIGELArAFNRMTDQLKEQ---REELEERRRYLETILENLPAGVIVLDADGRITLANP 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956494107 425 AVTRMMRDSEpdmrkdlpnfqaERLLGANFDDFHRHPARQKNMLGSLTQEHVAQIRI--GGRLYKLVSNPVMNDQG 498
Cdd:COG5000   118 AAERLLGIPL------------EELIGKPLEELLPELDLAELLREALERGWQEEIELtrDGRRTLLVRASPLRDDG 181
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 563-892 5.53e-85

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 283.44  E-value: 5.53e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 563 LTDLARVM---NAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSERTESQ 639
Cdd:PRK15048  217 LTPLAKIIahiREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQ 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 640 ASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNIL 719
Cdd:PRK15048  297 ASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNIL 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 720 ALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSE 799
Cdd:PRK15048  377 ALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGE 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 800 IADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQARELKRAVSLFKLdTSGLRNQDWTGAERRGPDRA 879
Cdd:PRK15048  457 IASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL-AASPLTNKPQTPSRPASEQP 535

                         330
                  ....*....|...
gi 1956494107 880 TNVTRLAPEPADT 892
Cdd:PRK15048  536 PAQPRLRIAEQDP 548
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
555-858 7.53e-82

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 274.59  E-value: 7.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 555 LMEIVSAGLTDLARVMNAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSE 634
Cdd:COG0840   202 LSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAA 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 635 RTESQASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVV--------------GTMDGIQDSSR 700
Cdd:COG0840   282 GAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQ 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 701 RIADIIGVIDSIAFQTNILALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLI----------VDSMAK-- 768
Cdd:COG0840   362 EIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIeeiqseteeaVEAMEEgs 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 769 --VDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQA 846
Cdd:COG0840   442 eeVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELA 521

                         330
                  ....*....|..
gi 1956494107 847 RELKRAVSLFKL 858
Cdd:COG0840   522 EELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 611-857 4.89e-63

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: 213.69  E-value: 4.89e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  611 ILESTESINSAAQEISAGNSDLSERTESQASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVG 690
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  691 TMDGIQDSSRRIADIIGVIDSIAFQTNILALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLI-------- 762
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeetn 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  763 ------VDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAA 836
Cdd:smart00283 162 eavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241

                          250       260
                   ....*....|....*....|.
gi 1956494107  837 AATESLEDQARELKRAVSLFK 857
Cdd:smart00283 242 AAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 637-828 1.35e-50

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: 176.66  E-value: 1.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 637 ESQASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQT 716
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 717 NILALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATL 796
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1956494107 797 VSEIADASREQSSGIGQVTQAVSQIDEMTQQN 828
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 670-825 5.19e-50

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


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 174.16  E-value: 5.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 670 LSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNILALNAAVEAARAGEQGKGFAVVASEVRQLAQ 749
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 750 RSAQAAKEIKGLIV--------------DSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSGIGQVT 815
Cdd:pfam00015  83 RSAQAAKEIEALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVN 162

                         170
                  ....*....|
gi 1956494107 816 QAVSQIDEMT 825
Cdd:pfam00015 163 QAVARMDQVT 172
NIT pfam08376
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ...
 57-295 5.16e-47

Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.


Pssm-ID: 462453 [Multi-domain]  Cd Length: 227  Bit Score: 167.67  E-value: 5.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  57 AHELQKERGMSAGFLSS-KGVKFADRLPGQRQASDTGIAGLESALSGVDLAtmaPEYQRLLGQSREGLSQLPDFRQRIDQ 135
Cdd:pfam08376   1 VHALQKERGLSAGYLASgGGGRFAAELAAQRAATDAALAALRAALAELALP---ARLADRLAALLRALDQLPALRRQVDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 136 LQVPPPASFQEYSRLIADLLEVATRSSNELPDAAIARLANAKTALLYLKERNGQERAILSGAFSAGRITPANYDILLTLL 215
Cdd:pfam08376  78 GALSALEALAAYTELIAALLDLVDELAAGSPDPELARQLRALAALLRAKEAAGQERALLAAALAAGRFTAAEYRRFLSLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 216 SDQANFLRLTKSFALPEQTALLESKLSQPVVKdvgEVERMvketgadREIFYPPEVWFDQITQKIDLLRDVEQQFSQDIA 295
Cdd:pfam08376 158 AAQRAALAEFRAAATPEQRALYDATVTGPAVA---AAERL-------RDRLVDAAAWFAASTARIDLLREVEDRLADDLA 227
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 346-498 6.58e-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: 52.66  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 346 VQVAHDIAKGRLDNEIPVKSGDSVSLLA-SMKHMQQQLHERietERRLAAESRRIQSALDKASTNMMVADNDGRIIYMNA 424
Cdd:COG5000    41 AEATRAVAAGDLSVRLPVTGDDEIGELArAFNRMTDQLKEQ---REELEERRRYLETILENLPAGVIVLDADGRITLANP 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956494107 425 AVTRMMRDSEpdmrkdlpnfqaERLLGANFDDFHRHPARQKNMLGSLTQEHVAQIRI--GGRLYKLVSNPVMNDQG 498
Cdd:COG5000   118 AAERLLGIPL------------EELIGKPLEELLPELDLAELLREALERGWQEEIELtrDGRRTLLVRASPLRDDG 181
HAMP_I cd17529
first HAMP domain of aerotaxis transducer Aer2 and similar domains; HAMP is a signaling domain ...
 339-382 6.47e-06

first HAMP domain of aerotaxis transducer Aer2 and similar domains; 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: 381746 [Multi-domain]  Cd Length: 44  Bit Score: 43.88  E-value: 6.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1956494107 339 GGEPAFAVQVAHDIAKGRLDNEIPVKSGDSVSLLASMKHMQQQL 382
Cdd:cd17529     1 GGEPADLAVLAKRFAAGDLDTKIGLPAPDKTSLMASMRRLQRTL 44
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 416-511 3.37e-04

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 40.52  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 416 DGRIIYMNAAVTRMMRDSEPD-MRKDLPNFQAErllganfDDFHRHPARQKNMLGSLTQEHVAQIRIGGRLY--KLVSNP 492
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREElLGKSITDLFAE-------PEDSERLREALREGKAVREFEVVLYRKDGEPFpvLVSLAP 73

                          90
                  ....*....|....*....
gi 1956494107 493 VMNDQGERLGSVVEWTDRT 511
Cdd:pfam13426  74 IRDDGGELVGIIAILRDIT 92
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 397-465 2.58e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 37.38  E-value: 2.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956494107  397 RRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMrdsepdmrkdlpNFQAERLLGANFDDFHRHPARQK 465
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELL------------GYSPEELIGKSLLELIHPEDRER 57
 
Name Accession Description Interval E-value
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 563-892 5.53e-85

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 283.44  E-value: 5.53e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 563 LTDLARVM---NAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSERTESQ 639
Cdd:PRK15048  217 LTPLAKIIahiREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQ 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 640 ASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNIL 719
Cdd:PRK15048  297 ASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNIL 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 720 ALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSE 799
Cdd:PRK15048  377 ALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGE 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 800 IADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQARELKRAVSLFKLdTSGLRNQDWTGAERRGPDRA 879
Cdd:PRK15048  457 IASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL-AASPLTNKPQTPSRPASEQP 535

                         330
                  ....*....|...
gi 1956494107 880 TNVTRLAPEPADT 892
Cdd:PRK15048  536 PAQPRLRIAEQDP 548
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
561-928 3.85e-82

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 275.68  E-value: 3.85e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 561 AGLTDLARVMNAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSERTESQA 640
Cdd:PRK15041  220 APMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQA 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 641 SSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNILA 720
Cdd:PRK15041  300 ASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILA 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 721 LNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSEI 800
Cdd:PRK15041  380 LNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEI 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 801 ADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQARELKRAVSLFKLdtsglrnqdwtgaeRRGPDRAT 880
Cdd:PRK15041  460 ASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI--------------QQQQQQQR 525

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1956494107 881 NVTRLAPEPADTSgPKKPAAASlaaksdrprnpstakpspSEDEWEEF 928
Cdd:PRK15041  526 ETSAVVKTVTPAT-PRKMAVAD------------------SGENWETF 554
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
555-858 7.53e-82

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 274.59  E-value: 7.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 555 LMEIVSAGLTDLARVMNAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSE 634
Cdd:COG0840   202 LSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAA 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 635 RTESQASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVV--------------GTMDGIQDSSR 700
Cdd:COG0840   282 GAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQ 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 701 RIADIIGVIDSIAFQTNILALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLI----------VDSMAK-- 768
Cdd:COG0840   362 EIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIeeiqseteeaVEAMEEgs 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 769 --VDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQA 846
Cdd:COG0840   442 eeVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELA 521

                         330
                  ....*....|..
gi 1956494107 847 RELKRAVSLFKL 858
Cdd:COG0840   522 EELQELVSRFKL 533
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
571-859 2.05e-73

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 251.53  E-value: 2.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 571 NAIAQGDLTQGITADYEGTFGQMKTDTNATLEQLREVVGRILESTESINSAAQEISAGNSDLSERTESQASSLEQTASSM 650
Cdd:PRK09793  226 DSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASM 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 651 EELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNILALNAAVEAARA 730
Cdd:PRK09793  306 EQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 731 GEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSG 810
Cdd:PRK09793  386 GEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRG 465

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1956494107 811 IGQVTQAVSQIDEMTQQNAALVEEAAAATESLEDQARELKRAVSLFKLD 859
Cdd:PRK09793  466 IEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLE 514
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 611-857 4.89e-63

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: 213.69  E-value: 4.89e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  611 ILESTESINSAAQEISAGNSDLSERTESQASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVG 690
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  691 TMDGIQDSSRRIADIIGVIDSIAFQTNILALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLI-------- 762
Cdd:smart00283  82 AVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeetn 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  763 ------VDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSGIGQVTQAVSQIDEMTQQNAALVEEAA 836
Cdd:smart00283 162 eavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEIS 241

                          250       260
                   ....*....|....*....|.
gi 1956494107  837 AATESLEDQARELKRAVSLFK 857
Cdd:smart00283 242 AAAEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 637-828 1.35e-50

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: 176.66  E-value: 1.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 637 ESQASSLEQTASSMEELNATVQQNAQNAQQANQLSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQT 716
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 717 NILALNAAVEAARAGEQGKGFAVVASEVRQLAQRSAQAAKEIKGLIVDSMAKVDGGAKLARQAGGEMDEVVAGFQQVATL 796
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1956494107 797 VSEIADASREQSSGIGQVTQAVSQIDEMTQQN 828
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEI 192
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 670-825 5.19e-50

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


Pssm-ID: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 174.16  E-value: 5.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 670 LSVTANERIQRGGETVKAVVGTMDGIQDSSRRIADIIGVIDSIAFQTNILALNAAVEAARAGEQGKGFAVVASEVRQLAQ 749
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 750 RSAQAAKEIKGLIV--------------DSMAKVDGGAKLARQAGGEMDEVVAGFQQVATLVSEIADASREQSSGIGQVT 815
Cdd:pfam00015  83 RSAQAAKEIEALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVN 162

                         170
                  ....*....|
gi 1956494107 816 QAVSQIDEMT 825
Cdd:pfam00015 163 QAVARMDQVT 172
NIT pfam08376
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ...
 57-295 5.16e-47

Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.


Pssm-ID: 462453 [Multi-domain]  Cd Length: 227  Bit Score: 167.67  E-value: 5.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107  57 AHELQKERGMSAGFLSS-KGVKFADRLPGQRQASDTGIAGLESALSGVDLAtmaPEYQRLLGQSREGLSQLPDFRQRIDQ 135
Cdd:pfam08376   1 VHALQKERGLSAGYLASgGGGRFAAELAAQRAATDAALAALRAALAELALP---ARLADRLAALLRALDQLPALRRQVDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 136 LQVPPPASFQEYSRLIADLLEVATRSSNELPDAAIARLANAKTALLYLKERNGQERAILSGAFSAGRITPANYDILLTLL 215
Cdd:pfam08376  78 GALSALEALAAYTELIAALLDLVDELAAGSPDPELARQLRALAALLRAKEAAGQERALLAAALAAGRFTAAEYRRFLSLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 216 SDQANFLRLTKSFALPEQTALLESKLSQPVVKdvgEVERMvketgadREIFYPPEVWFDQITQKIDLLRDVEQQFSQDIA 295
Cdd:pfam08376 158 AAQRAALAEFRAAATPEQRALYDATVTGPAVA---AAERL-------RDRLVDAAAWFAASTARIDLLREVEDRLADDLA 227
HAMP_2 pfam18947
HAMP domain;
542-599 4.36e-11

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 59.04  E-value: 4.36e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1956494107 542 TGFFQQMTDGLNRLMEIVSAGLTDLARVMNAIAQGDLTQGITADYEGTFGQMKTDTNA 599
Cdd:pfam18947   3 QGDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNA 60
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 346-498 6.58e-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: 52.66  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 346 VQVAHDIAKGRLDNEIPVKSGDSVSLLA-SMKHMQQQLHERietERRLAAESRRIQSALDKASTNMMVADNDGRIIYMNA 424
Cdd:COG5000    41 AEATRAVAAGDLSVRLPVTGDDEIGELArAFNRMTDQLKEQ---REELEERRRYLETILENLPAGVIVLDADGRITLANP 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956494107 425 AVTRMMRDSEpdmrkdlpnfqaERLLGANFDDFHRHPARQKNMLGSLTQEHVAQIRI--GGRLYKLVSNPVMNDQG 498
Cdd:COG5000   118 AAERLLGIPL------------EELIGKPLEELLPELDLAELLREALERGWQEEIELtrDGRRTLLVRASPLRDDG 181
HAMP_I cd17529
first HAMP domain of aerotaxis transducer Aer2 and similar domains; HAMP is a signaling domain ...
 339-382 6.47e-06

first HAMP domain of aerotaxis transducer Aer2 and similar domains; 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: 381746 [Multi-domain]  Cd Length: 44  Bit Score: 43.88  E-value: 6.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1956494107 339 GGEPAFAVQVAHDIAKGRLDNEIPVKSGDSVSLLASMKHMQQQL 382
Cdd:cd17529     1 GGEPADLAVLAKRFAAGDLDTKIGLPAPDKTSLMASMRRLQRTL 44
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
391-519 6.72e-06

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.46  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 391 RLAAESRRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMRDSepdmrkdlpnfqAERLLGANFDDFHRHPARQKNML-- 468
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLS------------AEELLGRPLAELFPEDSPLRELLer 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1956494107 469 -----GSLTQEHVAQIRIGG--RLYKLVSNPVMNDQGERlGSVVEWTDRTNEAKVEQE 519
Cdd:COG3852    69 alaegQPVTEREVTLRRKDGeeRPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERE 125
PAS COG2202
PAS domain [Signal transduction mechanisms];
387-519 2.85e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 43.86  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 387 ETERRLAAESRRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMRDSEPDMRKDLPNFqaerLLGANFDDFHRHPARQKN 466
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRD----LLPPEDDDEFLELLRAAL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1956494107 467 MLGSLTQEHVAQIRIGGRLY--KLVSNPVMNDQGERLGSVVEWTDRTNEAKVEQE 519
Cdd:COG2202    77 AGGGVWRGELRNRRKDGSLFwvELSISPVRDEDGEITGFVGIARDITERKRAEEA 131
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 416-511 3.37e-04

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 40.52  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 416 DGRIIYMNAAVTRMMRDSEPD-MRKDLPNFQAErllganfDDFHRHPARQKNMLGSLTQEHVAQIRIGGRLY--KLVSNP 492
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREElLGKSITDLFAE-------PEDSERLREALREGKAVREFEVVLYRKDGEPFpvLVSLAP 73

                          90
                  ....*....|....*....
gi 1956494107 493 VMNDQGERLGSVVEWTDRT 511
Cdd:pfam13426  74 IRDDGGELVGIIAILRDIT 92
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 397-448 3.62e-04

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 39.45  E-value: 3.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1956494107 397 RRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMRDSEPD--MRKDLPNFQAER 448
Cdd:pfam13188   1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGelLGELLDLLDPLL 54
PAS COG2202
PAS domain [Signal transduction mechanisms];
384-519 7.77e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 42.32  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 384 ERIETERRLAAESRRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMRDSepdmrkdlpnfqAERLLGANFDDFHRHPAR 463
Cdd:COG2202   124 ERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYS------------PEELLGKSLLDLLHPEDR 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956494107 464 QKNML--------GSLTQEHVAQIRIGGRLYKLVSNPV--MNDQGERLGSVVEWTDRTNEAKVEQE 519
Cdd:COG2202   192 ERLLEllrrllegGRESYELELRLKDGDGRWVWVEASAvpLRDGGEVIGVLGIVRDITERKRAEEA 257
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 389-530 1.24e-03

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 42.45  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 389 ERRLAAESRRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMrdsepdmrkdlpNFQAERLLGANFDDFHRHPARQKnML 468
Cdd:COG3829     3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERIL------------GLPREEVIGKNVTELIPNSPLLE-VL 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956494107 469 GSLTQEHVAQIRIGGRLYKLVSN--PVMNDqGERLGSVVEWTDRTNEAKVEQELAALLAAAVRG 530
Cdd:COG3829    70 KTGKPVTGVIQKTGGKGKTVIVTaiPIFED-GEVIGAVETFRDITELKRLERKLREEELERGLS 132
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 397-465 2.58e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 37.38  E-value: 2.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956494107  397 RRIQSALDKASTNMMVADNDGRIIYMNAAVTRMMrdsepdmrkdlpNFQAERLLGANFDDFHRHPARQK 465
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELL------------GYSPEELIGKSLLELIHPEDRER 57
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 397-510 8.30e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 37.01  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956494107 397 RRIQSALDKAstnMMVADNDGRIIYMNAAVTRMMRDSEPD-MRKDLPNFQAErllganfDDFHRHPARQKNMLGSLTQEH 475
Cdd:pfam00989   4 RAILESLPDG---IFVVDEDGRILYVNAAAEELLGLSREEvIGKSLLDLIPE-------EDDAEVAELLRQALLQGEESR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1956494107 476 VAQIRIG---GRLYKLVSN--PVMNDQGERLGSVVEWTDR 510
Cdd:pfam00989  74 GFEVSFRvpdGRPRHVEVRasPVRDAGGEILGFLGVLRDI 113
 
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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