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Conserved domains on  [gi|1859350792|ref|WP_175082859|]
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MULTISPECIES: PAS domain-containing methyl-accepting chemotaxis protein [Pseudoalteromonas]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 11451354)

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:  3.30.450.20|1.10.287.950
Gene Ontology:  GO:0098561|GO:0007165|GO:0006935|GO:0016020|GO:0004888
PubMed:  28409190|15009198|9382818|18165013|20738376
SCOP:  3000471|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];
264-436 4.40e-48

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 172.51  E-value: 4.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 264 STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLAL 343
Cdd:COG0840   303 TVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLAL 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 344 NAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIK 423
Cdd:COG0840   383 NAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIV 462

                         170
                  ....*....|...
gi 1859350792 424 TGADKVVDQISEV 436
Cdd:COG0840   463 EAVEEVSDLIQEI 475
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-267 8.36e-24

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 99.71  E-value: 8.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  18 ALQHDVDRSQQYLAGIRENI--AYIEFTPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYSSSkEYQTFWQDIAKG 95
Cdd:COG2202     1 TAEEALEESERRLRALVESSpdAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  96 QAKSGVFSRINGAGENIWLRATYFPVRGDDGKVRCAIKFASEIT--KEVE-KLDEMSAIYDAVNKST--AMIRFTPDGHI 170
Cdd:COG2202    80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITerKRAEeALRESEERLRLLVENApdGIFVLDLDGRI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 171 ISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNPNFWQELANG--RIFSGQFSRKKRDGSPLYLEATYNPIFNkQGKV 248
Cdd:COG2202   160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGgrESYELELRLKDGDGRWVWVEASAVPLRD-GGEV 238

                         250
                  ....*....|....*....
gi 1859350792 249 TQIIKFASDVTARVNSTEE 267
Cdd:COG2202   239 IGVLGIVRDITERKRAEEA 257
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
264-436 4.40e-48

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 172.51  E-value: 4.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 264 STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLAL 343
Cdd:COG0840   303 TVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLAL 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 344 NAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIK 423
Cdd:COG0840   383 NAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIV 462

                         170
                  ....*....|...
gi 1859350792 424 TGADKVVDQISEV 436
Cdd:COG0840   463 EAVEEVSDLIQEI 475
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 264-436 7.17e-46

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: 157.40  E-value: 7.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 264 STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLAL 343
Cdd:cd11386     6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 344 NAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIK 423
Cdd:cd11386    86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIV 165

                         170
                  ....*....|...
gi 1859350792 424 TGADKVVDQISEV 436
Cdd:cd11386   166 ASVEEVADGIQEI 178
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 248-436 2.63e-43

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: 152.83  E-value: 2.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  248 VTQIIKFASDVTARVN----STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQ 323
Cdd:smart00283  13 AEEQAEELEELAERMEelsaSIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  324 IGEIVTTINSIAEQTNLLALNAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEA 403
Cdd:smart00283  93 IGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSS 172

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1859350792  404 LSGESQQNVEEVSMIMEDIKTGADKVVDQISEV 436
Cdd:smart00283 173 EVEEGVELVEETGDALEEIVDSVEEIADLVQEI 205
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 306-436 1.92e-34

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: 126.39  E-value: 1.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 306 QVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLALNAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIG 385
Cdd:pfam00015  17 EVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALII 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1859350792 386 KTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIKTGADKVVDQISEV 436
Cdd:pfam00015  97 EIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
265-441 1.33e-24

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 106.31  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 265 TEEVKHAAENAGHTSEETSQVVTNGQQrilssvesskKVSEQVHQTRELSDVlAQQSSQIGEIVTTINSIAEQTNLLALN 344
Cdd:PRK09793  309 TATVGQNADNARQASELAKNAATTAQA----------GGVQVSTMTHTMQEI-ATSSQKIGDIISVIDGIAFQTNILALN 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 345 AAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIKT 424
Cdd:PRK09793  378 AAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIAS 457

                         170       180
                  ....*....|....*....|
gi 1859350792 425 GAD---KVVDQISEVIIRYD 441
Cdd:PRK09793  458 ASEeqrRGIEQVAQAVSQMD 477
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-267 8.36e-24

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 99.71  E-value: 8.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  18 ALQHDVDRSQQYLAGIRENI--AYIEFTPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYSSSkEYQTFWQDIAKG 95
Cdd:COG2202     1 TAEEALEESERRLRALVESSpdAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  96 QAKSGVFSRINGAGENIWLRATYFPVRGDDGKVRCAIKFASEIT--KEVE-KLDEMSAIYDAVNKST--AMIRFTPDGHI 170
Cdd:COG2202    80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITerKRAEeALRESEERLRLLVENApdGIFVLDLDGRI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 171 ISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNPNFWQELANG--RIFSGQFSRKKRDGSPLYLEATYNPIFNkQGKV 248
Cdd:COG2202   160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGgrESYELELRLKDGDGRWVWVEASAVPLRD-GGEV 238

                         250
                  ....*....|....*....
gi 1859350792 249 TQIIKFASDVTARVNSTEE 267
Cdd:COG2202   239 IGVLGIVRDITERKRAEEA 257
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 170-255 6.02e-14

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 66.98  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 170 IISANDNFLNVVGYSLAEIQGQHHKLFCY---DDFYQKNPNFWQELANGRIFSGQFSRKKRDGSPLYLEATYNPIFNKQG 246
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhpDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                  ....*....
gi 1859350792 247 KVTQIIKFA 255
Cdd:pfam08447  81 KPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 158-258 6.29e-10

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. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 56.10  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 158 STAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHHKLFC-YDDFYQKNPNFWQELANGRIFSGQFSRKKRDGSPLYLEA 236
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIhPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81

                          90       100
                  ....*....|....*....|..
gi 1859350792 237 TYNPIFNKQGKVTQIIKFASDV 258
Cdd:cd00130    82 SLTPIRDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 160-267 1.54e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 52.68  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 160 AMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNP-NFWQELAN-GRIFSGQFSRKKRDGSPLYLEAT 237
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVReRIERRLEGePEPVSEERRVRRKDGSEIWVEVS 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 1859350792 238 YNPIFnKQGKVTQIIKFASDVTARVNSTEE 267
Cdd:TIGR00229  95 VSPIR-TNGGELGVVGIVRDITERKEAEEA 123
PRK13560 PRK13560
hypothetical protein; Provisional
 23-271 3.79e-06

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 49.29  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  23 VDRSQQYLAGIRENIAYIEF--TPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFcAPEYSSsKEYQTFwqDIAKGQAKSg 100
Cdd:PRK13560  199 IDEALHFLQQLLDNIADPAFwkDEDAKVFGCNDAACLACGFRREEIIGMSIHDF-APAQPA-DDYQEA--DAAKFDADG- 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 101 vfSRI------NGAGENIWLRATYFPVRGDDGKVRCA--IKFASEITKE-------VEKLDEMSAIYDAVnkSTAMIRFT 165
Cdd:PRK13560  274 --SQIieaefqNKDGRTRPVDVIFNHAEFDDKENHCAglVGAITDISGRraaerelLEKEDMLRAIIEAA--PIAAIGLD 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 166 PDGHIISANDNFL-NVVGYSLAEIQG--------QHHKLFCYDDFYQKNPN----------FWQELANGRIFSGQFSRKK 226
Cdd:PRK13560  350 ADGNICFVNNNAAeRMLGWSAAEVMGkplpgmdpELNEEFWCGDFQEWYPDgrpmafdacpMAKTIKGGKIFDGQEVLIE 429

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1859350792 227 R-DGSPLYLEATYNPIFNKQGKVTQIIKFASDVTARVNSTEEVKHA 271
Cdd:PRK13560  430 ReDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLA 475
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 219-261 2.66e-04

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 38.32  E-value: 2.66e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1859350792  219 SGQFSRKKRDGSPLYLEATYNPIFNKQGKVTQIIKFASDVTAR 261
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
264-436 4.40e-48

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 172.51  E-value: 4.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 264 STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLAL 343
Cdd:COG0840   303 TVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLAL 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 344 NAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIK 423
Cdd:COG0840   383 NAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIV 462

                         170
                  ....*....|...
gi 1859350792 424 TGADKVVDQISEV 436
Cdd:COG0840   463 EAVEEVSDLIQEI 475
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 264-436 7.17e-46

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: 157.40  E-value: 7.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 264 STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLAL 343
Cdd:cd11386     6 SIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 344 NAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIK 423
Cdd:cd11386    86 NAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIV 165

                         170
                  ....*....|...
gi 1859350792 424 TGADKVVDQISEV 436
Cdd:cd11386   166 ASVEEVADGIQEI 178
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 248-436 2.63e-43

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: 152.83  E-value: 2.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  248 VTQIIKFASDVTARVN----STEEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELSDVLAQQSSQ 323
Cdd:smart00283  13 AEEQAEELEELAERMEelsaSIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  324 IGEIVTTINSIAEQTNLLALNAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEA 403
Cdd:smart00283  93 IGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSS 172

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1859350792  404 LSGESQQNVEEVSMIMEDIKTGADKVVDQISEV 436
Cdd:smart00283 173 EVEEGVELVEETGDALEEIVDSVEEIADLVQEI 205
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 306-436 1.92e-34

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: 126.39  E-value: 1.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 306 QVHQTRELSDVLAQQSSQIGEIVTTINSIAEQTNLLALNAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIG 385
Cdd:pfam00015  17 EVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALII 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1859350792 386 KTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIKTGADKVVDQISEV 436
Cdd:pfam00015  97 EIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEI 147
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
265-441 1.33e-24

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 106.31  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 265 TEEVKHAAENAGHTSEETSQVVTNGQQrilssvesskKVSEQVHQTRELSDVlAQQSSQIGEIVTTINSIAEQTNLLALN 344
Cdd:PRK09793  309 TATVGQNADNARQASELAKNAATTAQA----------GGVQVSTMTHTMQEI-ATSSQKIGDIISVIDGIAFQTNILALN 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 345 AAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEEVSMIMEDIKT 424
Cdd:PRK09793  378 AAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIAS 457

                         170       180
                  ....*....|....*....|
gi 1859350792 425 GAD---KVVDQISEVIIRYD 441
Cdd:PRK09793  458 ASEeqrRGIEQVAQAVSQMD 477
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-267 8.36e-24

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 99.71  E-value: 8.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  18 ALQHDVDRSQQYLAGIRENI--AYIEFTPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYSSSkEYQTFWQDIAKG 95
Cdd:COG2202     1 TAEEALEESERRLRALVESSpdAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  96 QAKSGVFSRINGAGENIWLRATYFPVRGDDGKVRCAIKFASEIT--KEVE-KLDEMSAIYDAVNKST--AMIRFTPDGHI 170
Cdd:COG2202    80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITerKRAEeALRESEERLRLLVENApdGIFVLDLDGRI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 171 ISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNPNFWQELANG--RIFSGQFSRKKRDGSPLYLEATYNPIFNkQGKV 248
Cdd:COG2202   160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGgrESYELELRLKDGDGRWVWVEASAVPLRD-GGEV 238

                         250
                  ....*....|....*....
gi 1859350792 249 TQIIKFASDVTARVNSTEE 267
Cdd:COG2202   239 IGVLGIVRDITERKRAEEA 257
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
265-436 1.04e-22

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 100.80  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 265 TEEVKHAAENAGHTSE------ETSQ----VVTNgqqrilssvesskkvseqVHQTreLSDVlAQQSSQIGEIVTTINSI 334
Cdd:PRK15041  313 TATVKQNAENARQASHlalsasETAQrggkVVDN------------------VVQT--MRDI-STSSQKIADIISVIDGI 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 335 AEQTNLLALNAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTALIEEIEALSGESQQNVEE 414
Cdd:PRK15041  372 AFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTR 451

                         170       180
                  ....*....|....*....|..
gi 1859350792 415 VSMIMEDIKTGADKVVDQISEV 436
Cdd:PRK15041  452 VTDIMGEIASASDEQSRGIDQV 473
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 317-441 4.60e-22

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 98.54  E-value: 4.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 317 LAQQSSQIGEIVTTINSIAEQTNLLALNAAIEAARAGEHGRGFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAKMTA 396
Cdd:PRK15048  352 IADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSV 431

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1859350792 397 LIEEiealSGESQQN----VEEVSMIMEDIKTGAD---KVVDQISEVIIRYD 441
Cdd:PRK15048  432 LVES----AGETMNNivnaVTRVTDIMGEIASASDeqsRGIDQVALAVSEMD 479
PAS COG2202
PAS domain [Signal transduction mechanisms];
143-294 2.97e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.22  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 143 EKLDEMSAIYDAVnkSTAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHHK-LFCYDDFYQKNPNFWQELANGRIFSGQ 221
Cdd:COG2202     8 ESERRLRALVESS--PDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRdLLPPEDDDEFLELLRAALAGGGVWRGE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859350792 222 FSRKKRDGSPLYLEATYNPIFNKQGKVTQIIKFASDVTARVNSTEEVKHAAENAGHTSEETSQ--VVTNGQQRIL 294
Cdd:COG2202    86 LRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDgiFVLDLDGRIL 160
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 25-273 4.13e-17

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 83.49  E-value: 4.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  25 RSQQYLAGIRENI--AYIEFTPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYSssKEYQTFWQDIAKGQAKSGV- 101
Cdd:COG5809    12 KSEQRFRSLFENApdAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDE--KELREILKLLKEGESRDELe 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 102 FSRINGAGENIWLRATYFPVRGDDGKVRCAIKFASEIT--KEVEKLDEMS-----AIYDAVnkSTAMIRFTPDGHIISAN 174
Cdd:COG5809    90 FELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITerKRMEEALRESeekfrLIFNHS--PDGIIVTDLDGRIIYAN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 175 DNFLNVVGYSLAEIQGQHHK-LFCYDDFYQKNPNFWQELANGRIFSGQFSRKKRDGSPLYLEATYNPIfNKQGKVTQIIK 253
Cdd:COG5809   168 PAACKLLGISIEELIGKSILeLIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVI 246

                         250       260
                  ....*....|....*....|
gi 1859350792 254 FASDVTARVnSTEEVKHAAE 273
Cdd:COG5809   247 IFRDITERK-KLEELLRKSE 265
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 170-255 6.02e-14

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 66.98  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 170 IISANDNFLNVVGYSLAEIQGQHHKLFCY---DDFYQKNPNFWQELANGRIFSGQFSRKKRDGSPLYLEATYNPIFNKQG 246
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLvhpDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                  ....*....
gi 1859350792 247 KVTQIIKFA 255
Cdd:pfam08447  81 KPVRVIGVA 89
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 143-269 2.83e-10

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 61.91  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 143 EKLDEMSAIYDAV--NKSTAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNPNFWQELANGRIFSG 220
Cdd:COG5809     8 LQLRKSEQRFRSLfeNAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDE 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1859350792 221 -QFSRKKRDGSPLYLEATYNPIFNKQGKVTQIIKFASDVTARVNSTEEVK 269
Cdd:COG5809    88 lEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALR 137
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 158-258 6.29e-10

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. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 56.10  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 158 STAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHHKLFC-YDDFYQKNPNFWQELANGRIFSGQFSRKKRDGSPLYLEA 236
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIhPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81

                          90       100
                  ....*....|....*....|..
gi 1859350792 237 TYNPIFNKQGKVTQIIKFASDV 258
Cdd:cd00130    82 SLTPIRDEGGEVIGLLGVVRDI 103
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 167-260 1.19e-09

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: 55.16  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 167 DGHIISANDNFLNVVGYSLAEIQGQH-HKLFCYDDFYQKNPNFWQELANGRIFSGQFSRKkrDGSPLYLEATYNPIFNKQ 245
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPEDSERLREALREGKAVREFEVVLYRK--DGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|....*
gi 1859350792 246 GKVTQIIKFASDVTA 260
Cdd:pfam13426  79 GELVGIIAILRDITE 93
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 48-135 1.43e-08

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 51.96  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  48 VLEANDLFCKTMKVQAGDIIG--QHHRKFCAPEYSSsKEYQTFWQDIAKGQAKSGVFSRINGAGENIWLRATYFPVRGDD 125
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 1859350792 126 GKVRCAIKFA 135
Cdd:pfam08447  80 GKPVRVIGVA 89
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 160-267 1.54e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 52.68  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 160 AMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNP-NFWQELAN-GRIFSGQFSRKKRDGSPLYLEAT 237
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVReRIERRLEGePEPVSEERRVRRKDGSEIWVEVS 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 1859350792 238 YNPIFnKQGKVTQIIKFASDVTARVNSTEE 267
Cdd:TIGR00229  95 VSPIR-TNGGELGVVGIVRDITERKEAEEA 123
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
144-272 3.03e-08

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 55.24  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 144 KLDEMSAIYDAV--NKSTAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQH-HKLFCYDDFYQKnpNFWQELANGR-IFS 219
Cdd:COG3852     1 ALRESEELLRAIldSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPEDSPLRE--LLERALAEGQpVTE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1859350792 220 GQFSRKKRDGSPLYLEATYNPIFNKQGKvTQIIKFASDVTARVNSTEEVKHAA 272
Cdd:COG3852    79 REVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAE 130
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 45-140 3.39e-07

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: 48.23  E-value: 3.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  45 DGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYSSSKEYQtFWQDIAKGQAKSGVFSRINgaGENIWLRATYFPVRGD 124
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLRE-ALREGKAVREFEVVLYRKD--GEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1859350792 125 DGKVRCAIKFASEITK 140
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 164-262 3.23e-06

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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 45.87  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 164 FTPDGHIISANDNFLNVVGYSLAEIQGQHHKLFCYDDFYQKNPNFWQELANGRIFSGQFSRKKRDGSPLYLEATYNPIFN 243
Cdd:pfam08448  11 LDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPLRD 90

                          90
                  ....*....|....*....
gi 1859350792 244 KQGKVTQIIKFASDVTARV 262
Cdd:pfam08448  91 PDGEVIGVLVISRDITERR 109
PRK13560 PRK13560
hypothetical protein; Provisional
 23-271 3.79e-06

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 49.29  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  23 VDRSQQYLAGIRENIAYIEF--TPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFcAPEYSSsKEYQTFwqDIAKGQAKSg 100
Cdd:PRK13560  199 IDEALHFLQQLLDNIADPAFwkDEDAKVFGCNDAACLACGFRREEIIGMSIHDF-APAQPA-DDYQEA--DAAKFDADG- 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 101 vfSRI------NGAGENIWLRATYFPVRGDDGKVRCA--IKFASEITKE-------VEKLDEMSAIYDAVnkSTAMIRFT 165
Cdd:PRK13560  274 --SQIieaefqNKDGRTRPVDVIFNHAEFDDKENHCAglVGAITDISGRraaerelLEKEDMLRAIIEAA--PIAAIGLD 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 166 PDGHIISANDNFL-NVVGYSLAEIQG--------QHHKLFCYDDFYQKNPN----------FWQELANGRIFSGQFSRKK 226
Cdd:PRK13560  350 ADGNICFVNNNAAeRMLGWSAAEVMGkplpgmdpELNEEFWCGDFQEWYPDgrpmafdacpMAKTIKGGKIFDGQEVLIE 429

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1859350792 227 R-DGSPLYLEATYNPIFNKQGKVTQIIKFASDVTARVNSTEEVKHA 271
Cdd:PRK13560  430 ReDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLA 475
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 147-258 1.05e-05

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: 44.33  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 147 EMSAIYDAVNksTAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQH-HKLFCYDDFYQKNPNFWQELANGRIF-SGQFSR 224
Cdd:pfam00989   2 DLRAILESLP--DGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSlLDLIPEEDDAEVAELLRQALLQGEESrGFEVSF 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1859350792 225 KKRDGSPLYLEATYNPIFNKQGKVTQIIKFASDV 258
Cdd:pfam00989  80 RVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 116-269 1.09e-05

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 47.91  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 116 ATYFPVRGDDGKVRCAIKFASEITKEVEKLDEMSAIYDAVNKST----------AMIRFT------PDGHIISANDNFLN 179
Cdd:PRK13558  103 AAYVPAVSDDATAAIAERIESAVPEHSRDTEARMPISDLTVESDrrlkeraldeAPVGITiadatlPDEPLIYINDAFER 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 180 VVGYSLAEIQGQHHKlfcyddFYQ---KNP----NFWQELANGRIFSGQFSRKKRDGSPLYLEATYNPIFNKQGKVTQII 252
Cdd:PRK13558  183 ITGYSPDEVLGRNCR------FLQgedTNEervaELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYV 256

                         170
                  ....*....|....*..
gi 1859350792 253 KFASDVTARVNSTEEVK 269
Cdd:PRK13558  257 GFQTDVTERKEAELALQ 273
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 36-138 1.34e-05

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. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 43.78  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  36 NIAYIEFTPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYsSSKEYQTFWQDIAKGQAKSGVFSRINGAGENIWLR 115
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|...
gi 1859350792 116 ATYFPVRGDDGKVRCAIKFASEI 138
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 136-282 2.53e-05

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: 46.30  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 136 SEITKEVEKLDEMSAIYDAVNKstAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQHhklfCYDDFyqKNPNFWQELANG 215
Cdd:COG3829     1 AEELELKELEEELEAILDSLDD--GIIVVDADGRITYVNRAAERILGLPREEVIGKN----VTELI--PNSPLLEVLKTG 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859350792 216 RIFSGQFSRKKRDGSplYLEATYNPIFnKQGKVTQIIKFASDVTARVNSTEEVKHAAENAGHTSEET 282
Cdd:COG3829    73 KPVTGVIQKTGGKGK--TVIVTAIPIF-EDGEVIGAVETFRDITELKRLERKLREEELERGLSAKYT 136
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 40-143 7.15e-05

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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 42.02  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  40 IEFTPDGTVLEANDLFCKTMKVQAGDIIGQHHRKFCAPEYSSskEYQTFWQDIAKGQAKSGVFSRINGAGENIWLRATYF 119
Cdd:pfam08448   9 AVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAA--RLERALRRALEGEEPIDFLEELLLNGEERHYELRLT 86

                          90       100
                  ....*....|....*....|....
gi 1859350792 120 PVRGDDGKVRCAIKFASEITKEVE 143
Cdd:pfam08448  87 PLRDPDGEVIGVLVISRDITERRR 110
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 219-261 2.66e-04

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 38.32  E-value: 2.66e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1859350792  219 SGQFSRKKRDGSPLYLEATYNPIFNKQGKVTQIIKFASDVTAR 261
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 266-393 8.72e-04

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 40.73  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792  266 EEVKHAAENAGHTSEETSQVVTNGQQRILSSVESSKKVSEQVHQTRELS----DVLAQQSSQIGEIVTTINSIAEQTNLL 341
Cdd:smart00283 133 DEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVeetgDALEEIVDSVEEIADLVQEIAAATDEQ 212

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1859350792  342 AlNAAIEAARAGEHgrgFAVVADEVRNLSQRTSVSTSEISGLIGKTQEIAAK 393
Cdd:smart00283 213 A-AGSEEVNAAIDE---IAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 158-192 5.15e-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: 35.45  E-value: 5.15e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1859350792  158 STAMIRFTPDGHIISANDNFLNVVGYSLAEIQGQH 192
Cdd:smart00091  11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
312-435 5.84e-03

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 38.85  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350792 312 ELSDVLAQQSSQIGEIVTTINSIAEQTNLLA--LNAAIEAARAGehgrgfavvADEVRNLSQRTSVSTSEISGLIGKTQE 389
Cdd:COG0840   239 QLADAFNRMIENLRELVGQVRESAEQVASASeeLAASAEELAAG---------AEEQAASLEETAAAMEELSATVQEVAE 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1859350792 390 IAAKMTALIEEIEALSGESQQNVEEVSMIMEDIKTGADKVVDQISE 435
Cdd:COG0840   310 NAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEE 355
 
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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