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Conserved domains on  [gi|1635438957|ref|WP_137156342|]
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PAS domain-containing methyl-accepting chemotaxis protein [Rhizobium sp. FKL33]

Protein Classification

PAS domain-containing methyl-accepting chemotaxis protein( domain architecture ID 11453059)

PAS domain-containing 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, similar to BdlA, a chemotaxis regulator essential for biofilm dispersion in Pseudomonas aeruginosa

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 298-545 3.87e-84

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: 263.38  E-value: 3.87e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  298 AVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAV 377
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  378 GAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRN----- 452
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  453 ---------SSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEES 523
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 1635438957  524 NAASATLASETERLRSLISRFK 545
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
PAS COG2202
PAS domain [Signal transduction mechanisms];
123-254 2.70e-18

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 85.08  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 123 AKERLLNLDYANQMAAINRVQAVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYASSpSYTEFWTALRRGE 202
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGGG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1635438957 203 AQIAEFTRVGKGGKKVVINASYNPIKDGQGRVIKVVKYASDVTERVRAVEEI 254
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEAL 132
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 298-545 3.87e-84

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: 263.38  E-value: 3.87e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  298 AVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAV 377
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  378 GAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRN----- 452
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  453 ---------SSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEES 523
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 1635438957  524 NAASATLASETERLRSLISRFK 545
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
248-546 2.81e-83

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 270.35  E-value: 2.81e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 248 VRAVEEIGEGLGRLAEGDVSFELSKPFAPDFESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRNANDLARRTEQQ 327
Cdd:COG0840   207 TRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQ 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 328 AASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAV--------------GAMARIEASSNQISNI 393
Cdd:COG0840   287 AASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEI 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 394 IGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVS-------- 465
Cdd:COG0840   367 VDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEegseevee 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 466 ------ETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRS 539
Cdd:COG0840   447 gvelveEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQE 526


                  ....*..
gi 1635438957 540 LISRFKL 546
Cdd:COG0840   527 LVSRFKL 533
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 261-573 1.03e-78

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 258.78  E-value: 1.03e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 261 LAEGDVSFELSKPFAPDFESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEETAAALDE 340
Cdd:PRK15048  230 IAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQ 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 341 ITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGE 420
Cdd:PRK15048  310 LTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGE 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 421 AGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLS 500
Cdd:PRK15048  390 QGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGID 469

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1635438957 501 EVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRSLISRFKLSGSAMA--APRAASHASRPVASPARALTA 573
Cdd:PRK15048  470 QVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTnkPQTPSRPASEQPPAQPRLRIA 544
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 325-524 5.27e-62

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: 203.24  E-value: 5.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 325 EQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQT 404
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 405 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDH 484
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1635438957 485 MNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEESN 524
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 358-513 2.93e-49

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: 168.77  E-value: 2.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 358 AAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQ 437
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 438 RSAQAAKEIKDLIR--------------NSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVN 503
Cdd:pfam00015  83 RSAQAAKEIEALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVN 162

                         170
                  ....*....|
gi 1635438957 504 TAVNQMDQTT 513
Cdd:pfam00015 163 QAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
123-254 2.70e-18

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 85.08  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 123 AKERLLNLDYANQMAAINRVQAVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYASSpSYTEFWTALRRGE 202
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGGG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1635438957 203 AQIAEFTRVGKGGKKVVINASYNPIKDGQGRVIKVVKYASDVTERVRAVEEI 254
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEAL 132
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 143-249 1.13e-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. 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: 67.44  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 143 QAVIEFTPDGKVVSANQNFCDALGYRLEEIIGqnHSLFvdkDYASSPSYTEFWTALRR---GEAQIAEFTRVGKGGKKVV 219
Cdd:pfam08448   6 DALAVLDPDGRVRYANAAAAELFGLPPEELLG--KTLA---ELLPPEDAARLERALRRaleGEEPIDFLEELLLNGEERH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1635438957 220 INASYNPIKDGQGRVIKVVKYASDVTERVR 249
Cdd:pfam08448  81 YELRLTPLRDPDGEVIGVLVISRDITERRR 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 144-244 4.47e-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: 56.87  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYaSSPSYTEFWTALRRGEAQIAEFTRVGKGGKKVVINAS 223
Cdd:cd00130     4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVS 82

                          90       100
                  ....*....|....*....|.
gi 1635438957 224 YNPIKDGQGRVIKVVKYASDV 244
Cdd:cd00130    83 LTPIRDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 144-254 6.62e-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: 56.92  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYaSSPSYTEFWTALRRGEAQIAEFTRVG-KGGKKVVINA 222
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEED-REEVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEV 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1635438957 223 SYNPIkDGQGRVIKVVKYASDVTERVRAVEEI 254
Cdd:TIGR00229  94 SVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
125-273 8.48e-06

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 48.81  E-value: 8.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 125 ERLLNLDYANQMAAINRVQAVIEFTPDGKVVSANQNFCDALGYRLEEIIGQN-HSLF-VDKDYASSPSYTefwtaLRRGE 202
Cdd:PRK11360  255 QALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPySELFpPNTPFASPLLDT-----LEHGT 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635438957 203 AQIAEFTRVGKGGKKVVINASYNPIKDGQGRVIKVVKYASDVTERVRAVEEIGE-----GLGRLAEGdVSFELSKP 273
Cdd:PRK11360  330 EHVDLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARqerlaALGELVAG-VAHEIRNP 404
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 144-176 4.83e-04

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: 38.53  E-value: 4.83e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1635438957  144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQN 176
Cdd:smart00091  13 GIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 298-545 3.87e-84

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: 263.38  E-value: 3.87e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  298 AVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAV 377
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  378 GAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRN----- 452
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEiqeet 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  453 ---------SSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEES 523
Cdd:smart00283 161 neavaameeSSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 1635438957  524 NAASATLASETERLRSLISRFK 545
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
248-546 2.81e-83

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 270.35  E-value: 2.81e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 248 VRAVEEIGEGLGRLAEGDVSFELSKPFAPDFESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRNANDLARRTEQQ 327
Cdd:COG0840   207 TRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQ 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 328 AASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAV--------------GAMARIEASSNQISNI 393
Cdd:COG0840   287 AASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEI 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 394 IGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVS-------- 465
Cdd:COG0840   367 VDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEegseevee 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 466 ------ETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRS 539
Cdd:COG0840   447 gvelveEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQE 526


                  ....*..
gi 1635438957 540 LISRFKL 546
Cdd:COG0840   527 LVSRFKL 533
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 261-573 1.03e-78

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 258.78  E-value: 1.03e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 261 LAEGDVSFELSKPFAPDFESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEETAAALDE 340
Cdd:PRK15048  230 IAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQ 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 341 ITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGE 420
Cdd:PRK15048  310 LTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGE 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 421 AGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLS 500
Cdd:PRK15048  390 QGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGID 469

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1635438957 501 EVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRSLISRFKLSGSAMA--APRAASHASRPVASPARALTA 573
Cdd:PRK15048  470 QVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTnkPQTPSRPASEQPPAQPRLRIA 544
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
256-578 1.20e-75

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 250.64  E-value: 1.20e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 256 EGLGRLAEGDVSFELSKPFAPDFESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEETA 335
Cdd:PRK15041  227 DSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETA 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 336 AALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEA 415
Cdd:PRK15041  307 ASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEA 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 416 ARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQ 495
Cdd:PRK15041  387 ARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQ 466

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 496 SVGLSEVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRSLISRFKLSGSAMAAPRAAshASRPVASPARALTAKV 575
Cdd:PRK15041  467 SRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETS--AVVKTVTPATPRKMAV 544


                  ...
gi 1635438957 576 AKS 578
Cdd:PRK15041  545 ADS 547
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
254-566 2.97e-73

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 243.83  E-value: 2.97e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 254 IGEGLGRLAEGDVSFELSKPFAPDFESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRNANDLARRTEQQAASLEE 333
Cdd:PRK09793  221 IGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQ 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 334 TAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGV 413
Cdd:PRK09793  301 TAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAV 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 414 EAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASR 493
Cdd:PRK09793  381 EAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASE 460

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1635438957 494 EQSVGLSEVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRSLISRFKLSGSAMAAPRAASHASRPVAS 566
Cdd:PRK09793  461 EQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARHESAQLQIAPVVS 533
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 325-524 5.27e-62

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: 203.24  E-value: 5.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 325 EQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQT 404
Cdd:cd11386     1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 405 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDH 484
Cdd:cd11386    81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1635438957 485 MNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEESN 524
Cdd:cd11386   161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 358-513 2.93e-49

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: 168.77  E-value: 2.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 358 AAGEANDSAARSGKVVADAVGAMARIEASSNQISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQ 437
Cdd:pfam00015   3 LAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 438 RSAQAAKEIKDLIR--------------NSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVN 503
Cdd:pfam00015  83 RSAQAAKEIEALIIeiqkqtndstasieSTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVN 162

                         170
                  ....*....|
gi 1635438957 504 TAVNQMDQTT 513
Cdd:pfam00015 163 QAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
123-254 2.70e-18

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 85.08  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 123 AKERLLNLDYANQMAAINRVQAVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYASSpSYTEFWTALRRGE 202
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGGG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1635438957 203 AQIAEFTRVGKGGKKVVINASYNPIKDGQGRVIKVVKYASDVTERVRAVEEI 254
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEAL 132
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 143-249 1.13e-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. 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: 67.44  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 143 QAVIEFTPDGKVVSANQNFCDALGYRLEEIIGqnHSLFvdkDYASSPSYTEFWTALRR---GEAQIAEFTRVGKGGKKVV 219
Cdd:pfam08448   6 DALAVLDPDGRVRYANAAAAELFGLPPEELLG--KTLA---ELLPPEDAARLERALRRaleGEEPIDFLEELLLNGEERH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1635438957 220 INASYNPIKDGQGRVIKVVKYASDVTERVR 249
Cdd:pfam08448  81 YELRLTPLRDPDGEVIGVLVISRDITERRR 110
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 151-246 6.95e-12

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: 61.71  E-value: 6.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 151 DGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYASSPsYTEFWTALRRGEAQIAEFTRvgKGGKKVVINASYNPIKDG 230
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSER-LREALREGKAVREFEVVLYR--KDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1635438957 231 QGRVIKVVKYASDVTE 246
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
PAS COG2202
PAS domain [Signal transduction mechanisms];
24-254 3.10e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 63.89  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  24 VMLADAQLNITYMNDSVRELLQEAESDLKKELPRFAMSTligssidvfHKNPSHQRNMLAALK--KPHNATIWV-----G 96
Cdd:COG2202    24 IIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP---------EDDDEFLELLRAALAggGVWRGELRNrrkdgS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957  97 KHAFDLKVAPLID-GGKTFGFVV------EWANAKERLLNLDYANQMAAINRVQAVIEFTPDGKVVSANQNFCDALGYRL 169
Cdd:COG2202    95 LFWVELSISPVRDeDGEITGFVGiarditERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 170 EEIIGQNHSLFVDKDYAssPSYTEFWTALRRGEAQI--AEFTRVGKGGKKVVINASYNPIKDGqGRVIKVVKYASDVTER 247
Cdd:COG2202   175 EELLGKSLLDLLHPEDR--ERLLELLRRLLEGGRESyeLELRLKDGDGRWVWVEASAVPLRDG-GEVIGVLGIVRDITER 251


                  ....*..
gi 1635438957 248 VRAVEEI 254
Cdd:COG2202   252 KRAEEAL 258
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 144-244 4.47e-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: 56.87  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYaSSPSYTEFWTALRRGEAQIAEFTRVGKGGKKVVINAS 223
Cdd:cd00130     4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVS 82

                          90       100
                  ....*....|....*....|.
gi 1635438957 224 YNPIKDGQGRVIKVVKYASDV 244
Cdd:cd00130    83 LTPIRDEGGEVIGLLGVVRDI 103
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 154-241 5.38e-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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 56.19  E-value: 5.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 154 VVSANQNFCDALGYRLEEIIGQNHSLF-----VDKDYAsspsYTEFWTALRRGEAQIAEFTRVGKGGKKVVINASYNPIK 228
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLdlvhpDDRERV----REALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76

                          90
                  ....*....|...
gi 1635438957 229 DGQGRVIKVVKYA 241
Cdd:pfam08447  77 DENGKPVRVIGVA 89
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 144-254 6.62e-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: 56.92  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYaSSPSYTEFWTALRRGEAQIAEFTRVG-KGGKKVVINA 222
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEED-REEVRERIERRLEGEPEPVSEERRVRrKDGSEIWVEV 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1635438957 223 SYNPIkDGQGRVIKVVKYASDVTERVRAVEEI 254
Cdd:TIGR00229  94 SVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 140-269 1.44e-09

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: 60.56  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 140 NRVQAVIEFTPD--------GKVVSANQNFCDALGYRLEEIIGQNhslfVDKDYASSPSYtefwTALRRGEAQIAEFTRV 211
Cdd:COG3829    11 EELEAILDSLDDgiivvdadGRITYVNRAAERILGLPREEVIGKN----VTELIPNSPLL----EVLKTGKPVTGVIQKT 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1635438957 212 GKGGKKVVINASynPIKDgQGRVIKVVKYASDVTERVRAVEEI-GEGLGRLAEGDVSFE 269
Cdd:COG3829    83 GGKGKTVIVTAI--PIFE-DGEVIGAVETFRDITELKRLERKLrEEELERGLSAKYTFD 138
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
144-264 3.77e-09

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 58.70  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQN-HSLFVDkdyaSSPSYTEFWTALRRGEAQIA-EFTRVGKGGKKVVIN 221
Cdd:COG3852    19 AVIVLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPE----DSPLRELLERALAEGQPVTErEVTLRRKDGEERPVD 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1635438957 222 ASYNPIKDGQGRvIKVVKYASDVTERVRAVEEIG-----EGLGRLAEG 264
Cdd:COG3852    95 VSVSPLRDAEGE-GGVLLVLRDITERKRLERELRraeklAAVGELAAG 141
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 144-254 1.58e-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: 57.29  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYasSPSYTEFWTALRRGEAQIA-EFTRVGKGGKKVVINA 222
Cdd:COG5809    27 AILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDD--EKELREILKLLKEGESRDElEFELRHKNGKRLEFSS 104

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1635438957 223 SYNPIKDGQGRVIKVVKYASDVTERVRAVEEI 254
Cdd:COG5809   105 KLSPIFDQNGDIEGMLAISRDITERKRMEEAL 136
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 318-587 1.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 318 NDLARRTEQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGAMARIE-----------AS 386
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarleerrrEL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 387 SNQISNIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAQAAKEIKDLIRNSSEEVKTGVRLVSE 466
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 467 TGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAAMVEESNAASATLASETERLRSLISRFKL 546
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1635438957 547 SGSAMAAPRAASHASRPVASPARALTAKVAKSIGGGAAQQQ 587
Cdd:COG1196   475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 144-238 3.84e-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 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: 45.87  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYaSSPSYTEFWTALR-RGEAQIAEFTRVGKGGKKVVINA 222
Cdd:pfam00989  13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEED-DAEVAELLRQALLqGEESRGFEVSFRVPDGRPRHVEV 91

                          90
                  ....*....|....*.
gi 1635438957 223 SYNPIKDGQGRVIKVV 238
Cdd:pfam00989  92 RASPVRDAGGEILGFL 107
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
125-273 8.48e-06

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 48.81  E-value: 8.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 125 ERLLNLDYANQMAAINRVQAVIEFTPDGKVVSANQNFCDALGYRLEEIIGQN-HSLF-VDKDYASSPSYTefwtaLRRGE 202
Cdd:PRK11360  255 QALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPySELFpPNTPFASPLLDT-----LEHGT 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635438957 203 AQIAEFTRVGKGGKKVVINASYNPIKDGQGRVIKVVKYASDVTERVRAVEEIGE-----GLGRLAEGdVSFELSKP 273
Cdd:PRK11360  330 EHVDLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARqerlaALGELVAG-VAHEIRNP 404
PRK13560 PRK13560
hypothetical protein; Provisional
 115-261 4.82e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 46.59  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 115 GFVVEWANAKERLLNLDyanqmAAINRVQAVIEFTP--------DGKVVSANQNFCDALGYRLEEIIGQN-HSL---FVD 182
Cdd:PRK13560  184 GFAEDITERKRAEERID-----EALHFLQQLLDNIAdpafwkdeDAKVFGCNDAACLACGFRREEIIGMSiHDFapaQPA 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 183 KDYASSPsytefWTALRRGEAQIAEFTRVGKGGKKVVINASYNPIK--DGQGRVIKVVKYASDVTERVRAVEEIGEGLGR 260
Cdd:PRK13560  259 DDYQEAD-----AAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAERELLEKEDM 333


                  .
gi 1635438957 261 L 261
Cdd:PRK13560  334 L 334
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 150-263 1.16e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 150 PDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYASSPSyTEFWTALRRGEAQIAEFTRVGKGGKKVVINASYNPIKD 229
Cdd:PRK13558  169 PDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERV-AELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRD 247

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1635438957 230 GQGRVIKVVKYASDVTERVRA---VEEIGEGLGRLAE 263
Cdd:PRK13558  248 EDGTVTHYVGFQTDVTERKEAelaLQRERRKLQRLLE 284
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 136-252 2.84e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 43.99  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 136 MAAINRV-QAVIEFTPDGKVVSANQNFCDALGYRLEEIIGQNHSLFVDKDYASSPSYTEFWTALRRGEAQIAEFTRVGKG 214
Cdd:PRK11359  139 IIAVDHLdRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRT 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1635438957 215 GKKVVINASYNPIKDGQGRVIKVVKYASDVTE--RVRAVE 252
Cdd:PRK11359  219 GEKIWIKASISPVYDVLAHLQNLVMTFSDITEerQIRQLE 258
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 144-176 4.83e-04

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: 38.53  E-value: 4.83e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1635438957  144 AVIEFTPDGKVVSANQNFCDALGYRLEEIIGQN 176
Cdd:smart00091  13 GIFVLDLDGRILYANPAAEELLGYSPEELIGKS 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 279-573 1.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 279 ESLRVNLNNALKRLSETLGAVAQSTSEIDGGTQEISRnandLARRTEQQAASLEETAAALDEITANVGNSSKRAEEARRA 358
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIAR----LEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 359 AGEANDSAARSGKVVADAVGAMARIEASSNQIsniigvideiafQTNLLALNAGVEAARAGEagkgfAVVAQEVRELAQR 438
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEA------------EEELEELAEELLEALRAA-----AELAAQLEELEEA 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 439 SAQAAKEIKDLIRNSSEEVKTGVRLVSETGEALKTIETNIVAVNDHMNAIANASREQSVGLSEVNTAVNQMDQTTQQNAA 518
Cdd:COG1196   409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1635438957 519 MVEESNAASATLASETERLRSLISRFKLSGSAMAAPRAASHASRPVASPARALTA 573
Cdd:COG1196   489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
300-439 1.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 300 AQSTSEIDGGTQEISRNANDLARRTEQQAASLEETAAALDEITANVGNSSKRAEEARRAAGEANDSAARSGKVVADAVGA 379
Cdd:PRK02224  501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1635438957 380 MARIEASSNQISNIIGVIDEIAfqtnllalNAGVEAARAGEAGKGFAVVAQEVRE-LAQRS 439
Cdd:PRK02224  581 LAELKERIESLERIRTLLAAIA--------DAEDEIERLREKREALAELNDERRErLAEKR 633
PRK13559 PRK13559
hypothetical protein; Provisional
 150-364 3.72e-03

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 39.80  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 150 PDGKVVSANQNFCDALGYRLEEIIGQNhSLFVDKDYASSPSYTEFWTALRRGEAQIAEFTRVGKGGKKVVINASYNPIKD 229
Cdd:PRK13559   64 PDLPIVLANQAFLDLTGYAAEEVVGRN-CRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635438957 230 GQGRVIKVVKYASDVTErVRAVEEIGEGLGRLAEgDVSFELSKPFApdfeslrvnLNNALKRLSETLGAVAQSTSEIDGG 309
Cdd:PRK13559  143 EDGRLLYFFGSQWDVTD-IRAVRALEAHERRLAR-EVDHRSKNVFA---------VVDSIVRLTGRADDPSLYAAAIQER 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1635438957 310 TQEISRNANDLARRTEQQAASLEETaaaldeITANVgnsSKRAEEARRAAGEAND 364
Cdd:PRK13559  212 VQALARAHETLLDERGWETVEVEEL------IRAQV---APYAPRATRVAFEGPG 257
 
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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