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Conserved domains on  [gi|1521279972|gb|RPR03513|]
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biofilm dispersion protein BdlA [Pseudomonas aeruginosa]

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];
242-412 1.81e-61

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 207.57  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:COG0840   308 AENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIE 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:COG0840   388 AARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEE 467

                         170
                  ....*....|.
gi 1521279972 402 VVEAVQQFSRT 412
Cdd:COG0840   468 VSDLIQEIAAA 478
PAS COG2202
PAS domain [Signal transduction mechanisms];
11-240 1.55e-29

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 115.51  E-value: 1.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  11 VEFDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYN 90
Cdd:COG2202    25 IITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  91 PVRDGQGRLLKVVKYASDI-------DAIVHQEHEMQSKLDALsrSMAMIEFDLDGNVLAANDNFLATMGYGRAELASAN 163
Cdd:COG2202   104 PVRDEDGEITGFVGIARDIterkraeEALRESEERLRLLVENA--PDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1521279972 164 HRQFCEPgyRDGPQYADLWRRLNRGEYVTG--QFRRVHRNGQPVWLEASYNPVYDADGKLYkVVKFASDVSDRMRRYQA 240
Cdd:COG2202   182 LLDLLHP--EDRERLLELLRRLLEGGRESYelELRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEA 257
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
242-412 1.81e-61

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 207.57  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:COG0840   308 AENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIE 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:COG0840   388 AARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEE 467

                         170
                  ....*....|.
gi 1521279972 402 VVEAVQQFSRT 412
Cdd:COG0840   468 VSDLIQEIAAA 478
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 242-414 1.55e-53

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: 179.02  E-value: 1.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:smart00283  38 AANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIE 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:smart00283 118 AARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEE 197

                          170
                   ....*....|...
gi 1521279972  402 VVEAVQQFSRTLN 414
Cdd:smart00283 198 IADLVQEIAAATD 210
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 242-414 2.36e-53

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


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 176.27  E-value: 2.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:cd11386    11 AASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:cd11386    91 AARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEE 170

                         170
                  ....*....|...
gi 1521279972 402 VVEAVQQFSRTLN 414
Cdd:cd11386   171 VADGIQEISAATQ 183
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 251-412 5.61e-39

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: 137.95  E-value: 5.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 251 LSTETRTVAEHGALIIQSAVEEMlkiantldasslniGELSQHSQQITSIVNTIREIAEQTNLLALNAAIEAARAGDQGR 330
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQM--------------EQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 331 GFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHKVVEAVQQFS 410
Cdd:pfam00015  69 GFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIA 148


                  ..
gi 1521279972 411 RT 412
Cdd:pfam00015 149 AA 150
PAS COG2202
PAS domain [Signal transduction mechanisms];
11-240 1.55e-29

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 115.51  E-value: 1.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  11 VEFDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYN 90
Cdd:COG2202    25 IITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  91 PVRDGQGRLLKVVKYASDI-------DAIVHQEHEMQSKLDALsrSMAMIEFDLDGNVLAANDNFLATMGYGRAELASAN 163
Cdd:COG2202   104 PVRDEDGEITGFVGIARDIterkraeEALRESEERLRLLVENA--PDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1521279972 164 HRQFCEPgyRDGPQYADLWRRLNRGEYVTG--QFRRVHRNGQPVWLEASYNPVYDADGKLYkVVKFASDVSDRMRRYQA 240
Cdd:COG2202   182 LLDLLHP--EDRERLLELLRRLLEGGRESYelELRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEA 257
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 242-364 3.37e-25

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 107.78  E-value: 3.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTldasslnigelsqhSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:PRK15048  318 ADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAVE 383

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKE----IADMIGRIQTGT 364
Cdd:PRK15048  384 AARAGEQGRGFAVVAGEVRNLASRSAQAAKEikalIEDSVSRVDTGS 430
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 141-228 4.88e-17

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: 75.84  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 141 VLAANDNFLATMGYGRAELAS--ANHRQFCEPGYRDgPQYADLWRRLNRGEYVTGQFRRVHRNGQPVWLEASYNPVYDAD 218
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 1521279972 219 GKLYKVVKFA 228
Cdd:pfam08447  80 GKPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-109 2.04e-12

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: 63.04  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPVR 93
Cdd:cd00130     9 DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87

                          90
                  ....*....|....*.
gi 1521279972  94 DGQGRLLKVVKYASDI 109
Cdd:cd00130    88 DEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 131-234 4.12e-10

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: 57.30  E-value: 4.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 131 AMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPGYRDgPQYADLWRRLNRGEYVTGQFRRV-HRNGQPVWLEA 209
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE-EVRERIERRLEGEPEPVSEERRVrRKDGSEIWVEV 93

                          90       100
                  ....*....|....*....|....*
gi 1521279972 210 SYNPVYDADGKLYkVVKFASDVSDR 234
Cdd:TIGR00229  94 SVSPIRTNGGELG-VVGIVRDITER 117
PRK13560 PRK13560
hypothetical protein; Provisional
 14-234 8.62e-09

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 57.76  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLcDGAYaQSEDYRRF-WERLRRGEHFSGRCKRITREGRPLWLEATYNPV 92
Cdd:PRK13560  221 DEDAKVFGCNDAACLACGFRREEIIGMSIHDF-APAQ-PADDYQEAdAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  93 R--DGQGRLLKVVKYASDIDAIVHQEHEMQSKLDALSRSM-----AMIEFDLDGNVLAANDNFLATMGYG---------- 155
Cdd:PRK13560  299 EfdDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIeaapiAAIGLDADGNICFVNNNAAERMLGWsaaevmgkpl 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 156 -------RAELASANHRQFCEPGYRDGPQYADLWRRLNRGEYVTGQFRRVHR-NGQPVWLEASYNPVYDADGKLYKVVKF 227
Cdd:PRK13560  379 pgmdpelNEEFWCGDFQEWYPDGRPMAFDACPMAKTIKGGKIFDGQEVLIEReDDGPADCSAYAEPLHDADGNIIGAIAL 458


                  ....*..
gi 1521279972 228 ASDVSDR 234
Cdd:PRK13560  459 LVDITER 465
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 192-234 9.96e-06

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: 42.17  E-value: 9.96e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1521279972  192 TGQFRRVHRNGQPVWLEASYNPVYDADGKLYKVVKFASDVSDR 234
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
242-412 1.81e-61

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 207.57  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:COG0840   308 AENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIE 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:COG0840   388 AARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEE 467

                         170
                  ....*....|.
gi 1521279972 402 VVEAVQQFSRT 412
Cdd:COG0840   468 VSDLIQEIAAA 478
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 242-414 1.55e-53

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: 179.02  E-value: 1.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:smart00283  38 AANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIE 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:smart00283 118 AARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEE 197

                          170
                   ....*....|...
gi 1521279972  402 VVEAVQQFSRTLN 414
Cdd:smart00283 198 IADLVQEIAAATD 210
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 242-414 2.36e-53

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


Pssm-ID: 206779 [Multi-domain]  Cd Length: 200  Bit Score: 176.27  E-value: 2.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:cd11386    11 AASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHK 401
Cdd:cd11386    91 AARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEE 170

                         170
                  ....*....|...
gi 1521279972 402 VVEAVQQFSRTLN 414
Cdd:cd11386   171 VADGIQEISAATQ 183
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 251-412 5.61e-39

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: 137.95  E-value: 5.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 251 LSTETRTVAEHGALIIQSAVEEMlkiantldasslniGELSQHSQQITSIVNTIREIAEQTNLLALNAAIEAARAGDQGR 330
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQM--------------EQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 331 GFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHKVVEAVQQFS 410
Cdd:pfam00015  69 GFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIA 148


                  ..
gi 1521279972 411 RT 412
Cdd:pfam00015 149 AA 150
PAS COG2202
PAS domain [Signal transduction mechanisms];
11-240 1.55e-29

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 115.51  E-value: 1.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  11 VEFDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYN 90
Cdd:COG2202    25 IITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  91 PVRDGQGRLLKVVKYASDI-------DAIVHQEHEMQSKLDALsrSMAMIEFDLDGNVLAANDNFLATMGYGRAELASAN 163
Cdd:COG2202   104 PVRDEDGEITGFVGIARDIterkraeEALRESEERLRLLVENA--PDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKS 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1521279972 164 HRQFCEPgyRDGPQYADLWRRLNRGEYVTG--QFRRVHRNGQPVWLEASYNPVYDADGKLYkVVKFASDVSDRMRRYQA 240
Cdd:COG2202   182 LLDLLHP--EDRERLLELLRRLLEGGRESYelELRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEA 257
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 242-364 3.37e-25

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 107.78  E-value: 3.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTldasslnigelsqhSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:PRK15048  318 ADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAVE 383

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKE----IADMIGRIQTGT 364
Cdd:PRK15048  384 AARAGEQGRGFAVVAGEVRNLASRSAQAAKEikalIEDSVSRVDTGS 430
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
242-404 5.26e-24

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 104.00  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTldasslnigelsqhSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:PRK09793  316 ADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATS--------------SQKIGDIISVIDGIAFQTNILALNAAVE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMI----GRIQTGTRSV----------------IDDMQ----HSQEQ 377
Cdd:PRK09793  382 AARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIeesvNRVQQGSKLVnnaaatmtdivssvtrVNDIMgeiaSASEE 461

                         170       180
                  ....*....|....*....|....*..
gi 1521279972 378 ARRGVELANEAGAAILGIRESTHKVVE 404
Cdd:PRK09793  462 QRRGIEQVAQAVSQMDQVTQQNASLVE 488
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
242-367 1.11e-23

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 103.11  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 242 ADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTldasslnigelsqhSQQITSIVNTIREIAEQTNLLALNAAIE 321
Cdd:PRK15041  320 AENARQASHLALSASETAQRGGKVVDNVVQTMRDISTS--------------SQKIADIISVIDGIAFQTNILALNAAVE 385

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1521279972 322 AARAGDQGRGFAVVADEVRQLAERTSKSTKEIA----DMIGRIQTGTRSV 367
Cdd:PRK15041  386 AARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKslieDSVGKVDVGSTLV 435
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 13-236 1.59e-22

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: 99.28  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  13 FDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAY-AQSEDYRRFWE--RLRRGEHFsgrcKRITREGRPLWLEATY 89
Cdd:COG5809    31 LDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDeKELREILKLLKegESRDELEF----ELRHKNGKRLEFSSKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  90 NPVRDGQGRLLKVVKYASDIDAIVHQE---HEMQSKLDALSR--SMAMIEFDLDGNVLAANDNFLATMGYGRAELASANH 164
Cdd:COG5809   107 SPIFDQNGDIEGMLAISRDITERKRMEealRESEEKFRLIFNhsPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSI 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1521279972 165 RQFCEPGYRDGPQyADLWRRLNRGEYVTGQFRRVHRNGQPVWLEASYNPVyDADGKLYKVVKFASDVSDRMR 236
Cdd:COG5809   187 LELIHSDDQENVA-AFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKK 256
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 141-228 4.88e-17

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: 75.84  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 141 VLAANDNFLATMGYGRAELAS--ANHRQFCEPGYRDgPQYADLWRRLNRGEYVTGQFRRVHRNGQPVWLEASYNPVYDAD 218
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRE-RVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 1521279972 219 GKLYKVVKFA 228
Cdd:pfam08447  80 GKPVRVIGVA 89
PAS COG2202
PAS domain [Signal transduction mechanisms];
115-240 1.24e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 73.52  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 115 QEHEMQSKLDALSRSMAMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPGYRDgPQYADLWRRLNRGEYVTGQ 194
Cdd:COG2202     7 EESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-EFLELLRAALAGGGVWRGE 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1521279972 195 FRRVHRNGQPVWLEASYNPVYDADGKLYKVVKFASDVSDRMRRYQA 240
Cdd:COG2202    86 LRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEA 131
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 16-109 2.54e-14

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: 68.26  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  16 DGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCkrITREGRPLWLEATYNPVRDG 95
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDS-ERLREALREGKAVREFEVVL--YRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....
gi 1521279972  96 QGRLLKVVKYASDI 109
Cdd:pfam13426  78 GGELVGIIAILRDI 91
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 19-106 5.60e-13

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: 64.28  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  19 ITDANENFLTLLGYRRDEILGKP--HRQLC---DGAYAqsedYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPVR 93
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGesWLDLVhpdDRERV----REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76

                          90
                  ....*....|...
gi 1521279972  94 DGQGRLLKVVKYA 106
Cdd:pfam08447  77 DENGKPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-109 2.04e-12

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: 63.04  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPVR 93
Cdd:cd00130     9 DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87

                          90
                  ....*....|....*.
gi 1521279972  94 DGQGRLLKVVKYASDI 109
Cdd:cd00130    88 DEGGEVIGLLGVVRDI 103
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 13-109 2.15e-11

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: 60.51  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  13 FDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQseDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPV 92
Cdd:pfam08448  11 LDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAA--RLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPL 88

                          90
                  ....*....|....*..
gi 1521279972  93 RDGQGRLLKVVKYASDI 109
Cdd:pfam08448  89 RDPDGEVIGVLVISRDI 105
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 129-231 2.18e-11

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: 60.34  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 129 SMAMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPGYRDGPQyADLWRRLNRGEYVTGQFRRVHRNGQPVWLE 208
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELR-ERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|...
gi 1521279972 209 ASYNPVYDADGKLYKVVKFASDV 231
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
13-133 8.84e-11

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 62.94  E-value: 8.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  13 FDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAyaqSEDYRRFWERLRRGEHFSGRCKRI-TREGRPLWLEATYNP 91
Cdd:COG3852    23 LDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED---SPLRELLERALAEGQPVTEREVTLrRKDGEERPVDVSVSP 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1521279972  92 VRDGQGRLLkVVKYASDIDAIVHQEHEMQ--SKLDALSRSMAMI 133
Cdd:COG3852   100 LRDAEGEGG-VLLVLRDITERKRLERELRraEKLAAVGELAAGL 142
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 14-109 1.14e-10

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: 58.58  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYaQSEDYRRFWERLRRGEHFSGRCKRITRE-GRPLWLEATYNPV 92
Cdd:pfam00989  18 DEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEED-DAEVAELLRQALLQGEESRGFEVSFRVPdGRPRHVEVRASPV 96

                          90
                  ....*....|....*..
gi 1521279972  93 RDGQGRLLKVVKYASDI 109
Cdd:pfam00989  97 RDAGGEILGFLGVLRDI 113
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 138-233 2.82e-10

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: 56.70  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 138 DGNVLAANDNFLATMGYGRAELASANHRQFCEPGYRDGPqYADLWRRLNRGEYVTGQFRRvhRNGQPVWLEASYNPVYDA 217
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSER-LREALREGKAVREFEVVLYR--KDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1521279972 218 DGKLYKVVKFASDVSD 233
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 131-234 4.12e-10

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: 57.30  E-value: 4.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 131 AMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPGYRDgPQYADLWRRLNRGEYVTGQFRRV-HRNGQPVWLEA 209
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE-EVRERIERRLEGEPEPVSEERRVrRKDGSEIWVEV 93

                          90       100
                  ....*....|....*....|....*
gi 1521279972 210 SYNPVYDADGKLYkVVKFASDVSDR 234
Cdd:TIGR00229  94 SVSPIRTNGGELG-VVGIVRDITER 117
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 127-234 1.21e-09

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: 55.50  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 127 SRSMAMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPGyrDGPQYADLWRRLNRGEYVTGQFRRVHRNGQPVW 206
Cdd:pfam08448   3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPE--DAARLERALRRALEGEEPIDFLEELLLNGEERH 80

                          90       100
                  ....*....|....*....|....*...
gi 1521279972 207 LEASYNPVYDADGKLYKVVKFASDVSDR 234
Cdd:pfam08448  81 YELRLTPLRDPDGEVIGVLVISRDITER 108
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 13-127 1.23e-09

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 59.75  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  13 FDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPV 92
Cdd:COG5805   173 IDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKE-EFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPL 251

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1521279972  93 RDGQGRLLKVVKYASDIDAIVHQEHEMqSKLDALS 127
Cdd:COG5805   252 IDTDGSVKGILVILRDITEKKEAEELM-ARSEKLS 285
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 11-116 2.63e-09

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: 54.99  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  11 VEFDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQsEDYRRFWERLRRGEHFSGRCKRITRE-GRPLWLEATY 89
Cdd:TIGR00229  17 IVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE-EVRERIERRLEGEPEPVSEERRVRRKdGSEIWVEVSV 95

                          90       100
                  ....*....|....*....|....*..
gi 1521279972  90 NPVRDGQGRLLkVVKYASDIDAIVHQE 116
Cdd:TIGR00229  96 SPIRTNGGELG-VVGIVRDITERKEAE 121
PRK13560 PRK13560
hypothetical protein; Provisional
 14-234 8.62e-09

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 57.76  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLcDGAYaQSEDYRRF-WERLRRGEHFSGRCKRITREGRPLWLEATYNPV 92
Cdd:PRK13560  221 DEDAKVFGCNDAACLACGFRREEIIGMSIHDF-APAQ-PADDYQEAdAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  93 R--DGQGRLLKVVKYASDIDAIVHQEHEMQSKLDALSRSM-----AMIEFDLDGNVLAANDNFLATMGYG---------- 155
Cdd:PRK13560  299 EfdDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIeaapiAAIGLDADGNICFVNNNAAERMLGWsaaevmgkpl 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 156 -------RAELASANHRQFCEPGYRDGPQYADLWRRLNRGEYVTGQFRRVHR-NGQPVWLEASYNPVYDADGKLYKVVKF 227
Cdd:PRK13560  379 pgmdpelNEEFWCGDFQEWYPDGRPMAFDACPMAKTIKGGKIFDGQEVLIEReDDGPADCSAYAEPLHDADGNIIGAIAL 458


                  ....*..
gi 1521279972 228 ASDVSDR 234
Cdd:PRK13560  459 LVDITER 465
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 13-133 3.71e-08

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: 55.37  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  13 FDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQSEDyRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPV 92
Cdd:COG5809   157 TDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVA-AFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI 235

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1521279972  93 RD--GQGRLLKVVKyasDIDAIVHQEHEMQS--KLDALSRSMAMI 133
Cdd:COG5809   236 KKngEVDGIVIIFR---DITERKKLEELLRKseKLSVVGELAAGI 277
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
123-353 2.35e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.07  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 123 LDALSrsMAMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPgyrDGPQYADLWRRLNRGEYVT-GQFRRVHRN 201
Cdd:COG3852    13 LDSLP--DAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPE---DSPLRELLERALAEGQPVTeREVTLRRKD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 202 GQPVWLEASYNPVYDADGKLYkVVKFASDVSDRmRRYQAEADNAHQAHTLSTETRTVAeH----------GALiiqsave 271
Cdd:COG3852    88 GEERPVDVSVSPLRDAEGEGG-VLLVLRDITER-KRLERELRRAEKLAAVGELAAGLA-HeirnpltgirGAA------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 272 EMLkiantldASSLNIGELSQHSQQITSIVNTIREIAEQtnLLALnaaieaARAGDQGRGF---AVVADEVRQLAERTSK 348
Cdd:COG3852   158 QLL-------ERELPDDELREYTQLIIEEADRLNNLVDR--LLSF------SRPRPPEREPvnlHEVLERVLELLRAEAP 222


                  ....*
gi 1521279972 349 STKEI 353
Cdd:COG3852   223 KNIRI 227
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 145-240 4.03e-06

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 49.07  E-value: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 145 NDNFLATMGYGRAELASANHRqFCEPGYRDGPQYADLWRRLNRGEYVTGQFRRVHRNGQPVWLEASYNPVYDADGKLYKV 224
Cdd:PRK13558  177 NDAFERITGYSPDEVLGRNCR-FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHY 255

                          90
                  ....*....|....*.
gi 1521279972 225 VKFASDVSDRMRRYQA 240
Cdd:PRK13558  256 VGFQTDVTERKEAELA 271
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 14-134 4.59e-06

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 48.68  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLcDGAYAQSEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPVR 93
Cdd:PRK13558  168 LPDEPLIYINDAFERITGYSPDEVLGRNCRFL-QGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIR 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1521279972  94 DGQGRLLKVVKYASDIDAIVHQEHEMQSKLDALSRSMAMIE 134
Cdd:PRK13558  247 DEDGTVTHYVGFQTDVTERKEAELALQRERRKLQRLLERVE 287
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 192-234 9.96e-06

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: 42.17  E-value: 9.96e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1521279972  192 TGQFRRVHRNGQPVWLEASYNPVYDADGKLYKVVKFASDVSDR 234
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-68 1.10e-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.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.77  E-value: 1.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1521279972   14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGayaqsEDYRRFWERLRRGEH 68
Cdd:smart00091  18 DLDGRILYANPAAEELLGYSPEELIGKSLLELIHP-----EDRERVQEALQRLLS 67
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 14-136 5.74e-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: 45.15  E-value: 5.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPhrqlCDGAYAQSedyrRFWERLRRGEHFSGRCKRITREGRPlwLEATYNPVR 93
Cdd:COG3829    28 DADGRITYVNRAAERILGLPREEVIGKN----VTELIPNS----PLLEVLKTGKPVTGVIQKTGGKGKT--VIVTAIPIF 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1521279972  94 DgQGRLLKVVKYASDIDAIVHQEHEMQSKLDALSRSmAMIEFD 136
Cdd:COG3829    98 E-DGEVIGAVETFRDITELKRLERKLREEELERGLS-AKYTFD 138
PRK13559 PRK13559
hypothetical protein; Provisional
 130-313 1.36e-04

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 43.65  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 130 MAMIEFDL---DGNVLAANDNFLATMGYGRAELASANHRqFCEPGYRDGPQYADLWRRLNRGEYVTGQFRRVHRNGQPVW 206
Cdd:PRK13559   54 MAMCITDPhqpDLPIVLANQAFLDLTGYAAEEVVGRNCR-FLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFW 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 207 LEASYNPVYDADGKLYKVVKFASDVSDRMRryqAEADNAHQaHTLSTETRtvaeHGALIIQSAVEEMLKIANTLDASSLN 286
Cdd:PRK13559  133 NALHLGPVYGEDGRLLYFFGSQWDVTDIRA---VRALEAHE-RRLAREVD----HRSKNVFAVVDSIVRLTGRADDPSLY 204

                         170       180
                  ....*....|....*....|....*..
gi 1521279972 287 IGELSQHSQQITSIVNTIREIAEQTNL 313
Cdd:PRK13559  205 AAAIQERVQALARAHETLLDERGWETV 231
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
266-415 1.56e-04

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 43.86  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 266 IQSAVEEMLKIAN-----TLDASSLN-IGELSQH----SQQITSIVNTIREIAEQtnllaLNAAIEAARAGdqgrgfavv 335
Cdd:COG0840   210 LRELLEVLERIAEgdltvRIDVDSKDeIGQLADAfnrmIENLRELVGQVRESAEQ-----VASASEELAAS--------- 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 336 ADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHKVVEAVQQFSRTLNA 415
Cdd:COG0840   276 AEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEE 355
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
14-131 7.75e-04

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 41.88  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  14 DPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQSEDYRRfweRLRRGEHFSGRCKRITREGRPLWLEATYNPVR 93
Cdd:PRK11360  279 DRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLD---TLEHGTEHVDLEISFPGRDRTIELSVSTSLLH 355

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1521279972  94 DGQGRLLKVVKYASDIDAIVHQEHEM--QSKLDALSRSMA 131
Cdd:PRK11360  356 NTHGEMIGALVIFSDLTERKRLQRRVarQERLAALGELVA 395
PRK13559 PRK13559
hypothetical protein; Provisional
 15-165 1.28e-03

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 40.57  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  15 PDGNITDANENFLTLLGYRRDEILGKPHRQLcDGAYAQSEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPVRD 94
Cdd:PRK13559   64 PDLPIVLANQAFLDLTGYAAEEVVGRNCRFL-QGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYG 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1521279972  95 GQGRLLKVvkYASDIDaiVHQEHEMQSkLDALSRSMAMiefDLD---GNVLAANDNFLATMGYGR--AELASA-NHR 165
Cdd:PRK13559  143 EDGRLLYF--FGSQWD--VTDIRAVRA-LEAHERRLAR---EVDhrsKNVFAVVDSIVRLTGRADdpSLYAAAiQER 211
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 131-231 1.53e-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: 38.17  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 131 AMIEFDLDGNVLAANDNFLATMGYGRAELASAN-HRQFCEPGYRDGPQyADLWRRLNRGEYVTGQFRRVHRNGQPVWLEA 209
Cdd:pfam00989  13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSlLDLIPEEDDAEVAE-LLRQALLQGEESRGFEVSFRVPDGRPRHVEV 91

                          90       100
                  ....*....|....*....|..
gi 1521279972 210 SYNPVYDADGKLYKVVKFASDV 231
Cdd:pfam00989  92 RASPVRDAGGEILGFLGVLRDI 113
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 3-243 1.74e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 40.52  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972   3 ALDRS-MARVEFDPDGNITDANENFLTLLGYRRDEILGKPHRQL----CDGAYAqseDYRRFwERLRRGEHFSGRCKRIT 77
Cdd:PRK11359   17 ALEQNmMGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLiprdLRPAHP---EYIRH-NREGGKARVEGMSRELQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972  78 RE---GRPLWLEATYNPVrDGQGRL--LKVVKYASDIDAIVHQEHEMQSKLDALSRsmAMIEFDLDGNVLAANDNFLATM 152
Cdd:PRK11359   93 LEkkdGSKIWTRFALSKV-SAEGKVyyLALVRDASVEMAQKEQTRQLIIAVDHLDR--PVIVLDPERRIVQCNRAFTEMF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 153 GYGRAELASanhRQFcePGYRDGPQYAD---------LWRRlnrgEYVTGQFRRVHRNGQPVWLEASYNPVYDADGKLYK 223
Cdd:PRK11359  170 GYCISEASG---MQP--DTLLNIPEFPAdnrirlqqlLWKT----ARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQN 240

                         250       260
                  ....*....|....*....|
gi 1521279972 224 VVKFASDVSDRMRRYQAEAD 243
Cdd:PRK11359  241 LVMTFSDITEERQIRQLEGN 260
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
131-236 6.72e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 38.80  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521279972 131 AMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPgyrDGPQYADLWRRLNRGEYVTGQFRRVHRNGQPVWLEAS 210
Cdd:PRK11360  274 GVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPP---NTPFASPLLDTLEHGTEHVDLEISFPGRDRTIELSVS 350

                          90       100
                  ....*....|....*....|....*.
gi 1521279972 211 YNPVYDADGKLYKVVKFASDVSDRMR 236
Cdd:PRK11360  351 TSLLHNTHGEMIGALVIFSDLTERKR 376
 
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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