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Conserved domains on  [gi|1345382204|gb|AVF03159|]
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chemotaxis protein [Devosia sp. I507]

Protein Classification

PAS and Tar domain-containing protein( domain architecture ID 11451354)

PAS and Tar domain-containing protein

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];
209-504 1.03e-61

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


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 211.03  E-value: 1.03e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 209 VSALGGQLDNMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQRHA 288
Cdd:COG0840   210 LRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAAS 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 289 VENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDA--------------NKAMASISESSAKISNIIGI 354
Cdd:COG0840   290 LEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAvegieeiresveetAETIEELGESSQEIGEIVDV 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 355 IDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDA--- 431
Cdd:COG0840   370 IDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEgve 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 432 -----------LLGAIDEASRLVAEIADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIAD 500
Cdd:COG0840   450 lveeagealeeIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529


                  ....
gi 1345382204 501 IFTI 504
Cdd:COG0840   530 RFKL 533
PAS COG2202
PAS domain [Signal transduction mechanisms];
2-212 3.03e-32

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 124.37  E-value: 3.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQAYgQSAEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDVT 81
Cdd:COG2202    45 GYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDIT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  82 ERKRRDaDALGQIEAISRS------QAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsaRPEYKLFWDR 155
Cdd:COG2202   124 ERKRAE-EALRESEERLRLlvenapDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPED--RERLLELLRR 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382204 156 LRDGQFQ--QAEYLRIGKAGNDVWIQATYNPIFSPSGRIYkIVKFATDVTARKQAVSAL 212
Cdd:COG2202   201 LLEGGREsyELELRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEAL 258
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
209-504 1.03e-61

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 211.03  E-value: 1.03e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 209 VSALGGQLDNMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQRHA 288
Cdd:COG0840   210 LRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAAS 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 289 VENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDA--------------NKAMASISESSAKISNIIGI 354
Cdd:COG0840   290 LEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAvegieeiresveetAETIEELGESSQEIGEIVDV 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 355 IDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDA--- 431
Cdd:COG0840   370 IDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEgve 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 432 -----------LLGAIDEASRLVAEIADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIAD 500
Cdd:COG0840   450 lveeagealeeIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529


                  ....
gi 1345382204 501 IFTI 504
Cdd:COG0840   530 RFKL 533
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
207-516 3.26e-59

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 204.53  E-value: 3.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 207 QAVSALGGQLDNMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQR 286
Cdd:PRK09793  216 QPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 287 HAVENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLA 366
Cdd:PRK09793  296 ASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILA 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 367 LNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEI 446
Cdd:PRK09793  376 LNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEI 455

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 447 ADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIADIFTIPPHASAVPEARR 516
Cdd:PRK09793  456 ASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARHESAQ 525
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 259-503 3.64e-55

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: 185.95  E-value: 3.64e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  259 RSAQGLRRATSSIAGGARNLSERTDKQRHAVENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDANKAM 338
Cdd:smart00283   4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  339 ASISESSAKISNIIGIIDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLI---------- 408
Cdd:smart00283  84 EELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeetnea 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  409 ----EASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDA 484
Cdd:smart00283 164 vaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAA 243

                          250
                   ....*....|....*....
gi 1345382204  485 VAEADHEAMTLDHIADIFT 503
Cdd:smart00283 244 AEELSGLAEELDELVERFK 262
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 289-482 1.60e-44

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: 155.47  E-value: 1.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 289 VENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAgvvIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLALN 368
Cdd:cd11386    10 VAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDES---VDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 369 ASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIAD 448
Cdd:cd11386    87 AAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVA 166

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1345382204 449 ATRNQASTIGSVADAVDLIDQMTRHNMNLVSETN 482
Cdd:cd11386   167 SVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 314-471 2.44e-37

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: 135.25  E-value: 2.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 314 SEKTLASASIANEAGVVIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRL 393
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 394 AQSTATASSEVKSLIEA--------------SGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIADATRNQASTIGS 459
Cdd:pfam00015  81 AERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 1345382204 460 VADAVDLIDQMT 471
Cdd:pfam00015 161 VNQAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
2-212 3.03e-32

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 124.37  E-value: 3.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQAYgQSAEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDVT 81
Cdd:COG2202    45 GYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDIT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  82 ERKRRDaDALGQIEAISRS------QAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsaRPEYKLFWDR 155
Cdd:COG2202   124 ERKRAE-EALRESEERLRLlvenapDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPED--RERLLELLRR 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382204 156 LRDGQFQ--QAEYLRIGKAGNDVWIQATYNPIFSPSGRIYkIVKFATDVTARKQAVSAL 212
Cdd:COG2202   201 LLEGGREsyELELRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEAL 258
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 112-199 9.57e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 66.59  E-value: 9.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 112 ILTANENFCAALGYRIDEIVGK--HHRIFVAPEESARpEYKLFWDRLRDGQFQQAEYLRIGKAGNDVWIQATYNPIFSPS 189
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRER-VREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 1345382204 190 GRIYKIVKFA 199
Cdd:pfam08447  80 GKPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 100-202 5.02e-13

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: 65.35  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 100 SQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEESARpEYKLFWDRLRDGQFQQAEYLRIGKAGNDVWIQ 179
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREE-LRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|...
gi 1345382204 180 ATYNPIFSPSGRIYKIVKFATDV 202
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 102-212 2.08e-12

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: 64.23  E-value: 2.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 102 AVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsaRPEYKLFWDRLRDGQ--FQQAEYLRIGKAGNDVWIQ 179
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEED--REEVRERIERRLEGEpePVSEERRVRRKDGSEIWVE 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1345382204 180 ATYNPIFSPSGRIYkIVKFATDVTARKQAVSAL 212
Cdd:TIGR00229  93 VSVSPIRTNGGELG-VVGIVRDITERKEAEEAL 124
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 2-207 2.99e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 56.32  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQ----AYGQSAEY-KAFWKGLAEGRFQAAEYRRiaKGGRAVWIQATYNPIfDKTGKpTGVVKF 76
Cdd:PRK11359   46 GYKREEVIGNNIDMLIPRdlrpAHPEYIRHnREGGKARVEGMSRELQLEK--KDGSKIWTRFALSKV-SAEGK-VYYLAL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  77 ATDVT-ERKRRDADALGQIEAISRSQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVA----PEESARPEYKL 151
Cdd:PRK11359  122 VRDASvEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNipefPADNRIRLQQL 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382204 152 FWDRLRDgqfqQAEYLRIGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTARKQ 207
Cdd:PRK11359  202 LWKTARD----QDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQ 253
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 43-83 5.96e-07

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: 46.02  E-value: 5.96e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1345382204   43 EYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDVTER 83
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
209-504 1.03e-61

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 211.03  E-value: 1.03e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 209 VSALGGQLDNMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQRHA 288
Cdd:COG0840   210 LRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAAS 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 289 VENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDA--------------NKAMASISESSAKISNIIGI 354
Cdd:COG0840   290 LEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAvegieeiresveetAETIEELGESSQEIGEIVDV 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 355 IDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDA--- 431
Cdd:COG0840   370 IDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEgve 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 432 -----------LLGAIDEASRLVAEIADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIAD 500
Cdd:COG0840   450 lveeagealeeIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529


                  ....
gi 1345382204 501 IFTI 504
Cdd:COG0840   530 RFKL 533
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
207-516 3.26e-59

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 204.53  E-value: 3.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 207 QAVSALGGQLDNMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQR 286
Cdd:PRK09793  216 QPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 287 HAVENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLA 366
Cdd:PRK09793  296 ASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILA 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 367 LNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEI 446
Cdd:PRK09793  376 LNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEI 455

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 447 ADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIADIFTIPPHASAVPEARR 516
Cdd:PRK09793  456 ASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARHESAQ 525
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
218-504 3.02e-56

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 197.10  E-value: 3.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 218 NMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQRHAVENTAQAVK 297
Cdd:PRK15041  231 HIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASME 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 298 RLSGTVADNAERAKSASEKTLASASIANEAGVVIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLALNASVEAARAG 377
Cdd:PRK15041  311 QLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAG 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 378 EAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIADATRNQASTI 457
Cdd:PRK15041  391 EQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGI 470

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1345382204 458 GSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIADIFTI 504
Cdd:PRK15041  471 DQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 259-503 3.64e-55

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: 185.95  E-value: 3.64e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  259 RSAQGLRRATSSIAGGARNLSERTDKQRHAVENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDANKAM 338
Cdd:smart00283   4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  339 ASISESSAKISNIIGIIDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLI---------- 408
Cdd:smart00283  84 EELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeetnea 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  409 ----EASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIADATRNQASTIGSVADAVDLIDQMTRHNMNLVSETNDA 484
Cdd:smart00283 164 vaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAA 243

                          250
                   ....*....|....*....
gi 1345382204  485 VAEADHEAMTLDHIADIFT 503
Cdd:smart00283 244 AEELSGLAEELDELVERFK 262
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 214-518 4.66e-54

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 190.99  E-value: 4.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 214 GQLDNMANGQLADQLAARLPGEFEDIRVALKSTLAQFARFVSELKRSAQGLRRATSSIAGGARNLSERTDKQRHAVENTA 293
Cdd:PRK15048  225 AHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETA 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 294 QAVKRLSGTVADNAERAKSASEKTLASASIANEAGVVIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLALNASVEA 373
Cdd:PRK15048  305 ASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEA 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 374 ARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIADATRNQ 453
Cdd:PRK15048  385 ARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQ 464

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382204 454 ASTIGSVADAVDLIDQMTRHNMNLVSETNDAVAEADHEAMTLDHIADIF--TIPPHASAVPEARRAV 518
Cdd:PRK15048  465 SRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFrlAASPLTNKPQTPSRPA 531
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 289-482 1.60e-44

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: 155.47  E-value: 1.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 289 VENTAQAVKRLSGTVADNAERAKSASEKTLASASIANEAgvvIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLALN 368
Cdd:cd11386    10 VAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDES---VDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 369 ASVEAARAGEAGKGFAVVAVEVRRLAQSTATASSEVKSLIEASGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIAD 448
Cdd:cd11386    87 AAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVA 166

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1345382204 449 ATRNQASTIGSVADAVDLIDQMTRHNMNLVSETN 482
Cdd:cd11386   167 SVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 314-471 2.44e-37

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: 135.25  E-value: 2.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 314 SEKTLASASIANEAGVVIGDANKAMASISESSAKISNIIGIIDDIAFQTNLLALNASVEAARAGEAGKGFAVVAVEVRRL 393
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 394 AQSTATASSEVKSLIEA--------------SGKEVHKGSHLVSEAHGKVDALLGAIDEASRLVAEIADATRNQASTIGS 459
Cdd:pfam00015  81 AERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQ 160

                         170
                  ....*....|..
gi 1345382204 460 VADAVDLIDQMT 471
Cdd:pfam00015 161 VNQAVARMDQVT 172
PAS COG2202
PAS domain [Signal transduction mechanisms];
2-212 3.03e-32

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 124.37  E-value: 3.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQAYgQSAEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDVT 81
Cdd:COG2202    45 GYSAEELLGKTLRDLLPPED-DDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDIT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  82 ERKRRDaDALGQIEAISRS------QAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsaRPEYKLFWDR 155
Cdd:COG2202   124 ERKRAE-EALRESEERLRLlvenapDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPED--RERLLELLRR 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382204 156 LRDGQFQ--QAEYLRIGKAGNDVWIQATYNPIFSPSGRIYkIVKFATDVTARKQAVSAL 212
Cdd:COG2202   201 LLEGGREsyELELRLKDGDGRWVWVEASAVPLRDGGEVIG-VLGIVRDITERKRAEEAL 258
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 2-207 1.54e-23

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: 103.52  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQAY-GQSAEYKAFWKGlaEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDV 80
Cdd:COG5809    49 GYTEDELLGTNILDFLHPDDeKELREILKLLKE--GESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  81 TERKRRDAdALGQIEAISRS------QAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEESARpEYKLFWD 154
Cdd:COG5809   127 TERKRMEE-ALRESEEKFRLifnhspDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQEN-VAAFISQ 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1345382204 155 RLRDGQFQQAEYLRIGKAGNDVWIQATYNPIFsPSGRIYKIVKFATDVTARKQ 207
Cdd:COG5809   205 LLKDGGIAQGEVRFWTKDGRWRLLEASGAPIK-KNGEVDGIVIIFRDITERKK 256
PAS COG2202
PAS domain [Signal transduction mechanisms];
82-212 1.66e-21

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 93.94  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  82 ERKRRDADALGQIEAISRSQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEESARpEYKLFWDRLRDGQF 161
Cdd:COG2202     3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE-FLELLRAALAGGGV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1345382204 162 QQAEYLRIGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTARKQAVSAL 212
Cdd:COG2202    82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEAL 132
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 112-199 9.57e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 66.59  E-value: 9.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 112 ILTANENFCAALGYRIDEIVGK--HHRIFVAPEESARpEYKLFWDRLRDGQFQQAEYLRIGKAGNDVWIQATYNPIFSPS 189
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRER-VREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                          90
                  ....*....|
gi 1345382204 190 GRIYKIVKFA 199
Cdd:pfam08447  80 GKPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 100-202 5.02e-13

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: 65.35  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 100 SQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEESARpEYKLFWDRLRDGQFQQAEYLRIGKAGNDVWIQ 179
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREE-LRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                          90       100
                  ....*....|....*....|...
gi 1345382204 180 ATYNPIFSPSGRIYKIVKFATDV 202
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 1-77 8.09e-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: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGR--HHSMFV---DQAYgqsaEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVK 75
Cdd:pfam08447  12 LGYTPEELLGKgeSWLDLVhpdDRER----VREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKPVRVIG 87


                  ..
gi 1345382204  76 FA 77
Cdd:pfam08447  88 VA 89
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 109-204 1.02e-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: 64.02  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 109 DGTILTANENFCAALGYRIDEIVGKHHRIFVAPEESARPEYKLFwdrLRDGQFQQAEYLRIGKAGNDVWIQATYNPIFSP 188
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREAL---REGKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 1345382204 189 SGRIYKIVKFATDVTA 204
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 ...
 102-212 2.08e-12

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: 64.23  E-value: 2.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 102 AVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsaRPEYKLFWDRLRDGQ--FQQAEYLRIGKAGNDVWIQ 179
Cdd:TIGR00229  15 AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEED--REEVRERIERRLEGEpePVSEERRVRRKDGSEIWVE 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1345382204 180 ATYNPIFSPSGRIYkIVKFATDVTARKQAVSAL 212
Cdd:TIGR00229  93 VSVSPIRTNGGELG-VVGIVRDITERKEAEEAL 124
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 2-230 8.12e-12

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: 67.45  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQ--AYGQSAEYKAFWKGLAEGRFqaaEYRRiAKGGRAVWIQATYNPIFDKTGKpTGVVKFaTD 79
Cdd:COG5805    68 GYTSEEIIGKTIFDFLEKeyHYRVKTRIERLQKGYDVVMI---EQIY-CKDGELIYVEVKLFPIYNQNGQ-AAILAL-RD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  80 VTERKRRDAdALGQIEaiSRSQAVIE--------FDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsaRPEYKL 151
Cdd:COG5805   142 ITKKKKIEE-ILQEQE--ERLQTLIEnspdlicvIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCD--KEEFKE 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 152 FWDRLRDgQFQQAEYLR--IGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTARKQAvSALGGQLDNMAngqLADQLA 229
Cdd:COG5805   217 RIESITE-VWQEFIIEReiITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEA-EELMARSEKLS---IAGQLA 291


                  .
gi 1345382204 230 A 230
Cdd:COG5805   292 A 292
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 98-207 9.85e-12

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: 61.66  E-value: 9.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  98 SRSQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEesARPEYKLFWDRL---RDGQFQQAEYLRIGKagn 174
Cdd:pfam08448   3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPE--DAARLERALRRAlegEEPIDFLEELLLNGE--- 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1345382204 175 DVWIQATYNPIFSPSGRIYKIVKFATDVTARKQ 207
Cdd:pfam08448  78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 102-206 5.03e-11

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: 65.00  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 102 AVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPE-ESARPEYKLFWDrlRDGQFQQAEYLRIGKAGNDVWIQA 180
Cdd:COG5809    27 AILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDdEKELREILKLLK--EGESRDELEFELRHKNGKRLEFSS 104

                          90       100
                  ....*....|....*....|....*.
gi 1345382204 181 TYNPIFSPSGRIYKIVKFATDVTARK 206
Cdd:COG5809   105 KLSPIFDQNGDIEGMLAISRDITERK 130
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 102-202 8.64e-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: 56.27  E-value: 8.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 102 AVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVaPEESARPEYKLFWDRLRDGQFQQAEYLRIGKA-GNDVWIQA 180
Cdd:pfam00989  13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLI-PEEDDAEVAELLRQALLQGEESRGFEVSFRVPdGRPRHVEV 91

                          90       100
                  ....*....|....*....|..
gi 1345382204 181 TYNPIFSPSGRIYKIVKFATDV 202
Cdd:pfam00989  92 RASPVRDAGGEILGFLGVLRDI 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
102-229 1.69e-08

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 56.39  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 102 AVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsarPEYKLFWDRLRDGQ-FQQAEYLRIGKAGNDVWIQA 180
Cdd:COG3852    19 AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS---PLRELLERALAEGQpVTEREVTLRRKDGEERPVDV 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1345382204 181 TYNPIFSPSGRIYkIVKFATDVTARKQAVSALgGQLDNM-ANGQLADQLA 229
Cdd:COG3852    96 SVSPLRDAEGEGG-VLLVLRDITERKRLEREL-RRAEKLaAVGELAAGLA 143
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 2-207 2.99e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 56.32  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVDQ----AYGQSAEY-KAFWKGLAEGRFQAAEYRRiaKGGRAVWIQATYNPIfDKTGKpTGVVKF 76
Cdd:PRK11359   46 GYKREEVIGNNIDMLIPRdlrpAHPEYIRHnREGGKARVEGMSRELQLEK--KDGSKIWTRFALSKV-SAEGK-VYYLAL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  77 ATDVT-ERKRRDADALGQIEAISRSQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVA----PEESARPEYKL 151
Cdd:PRK11359  122 VRDASvEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQCNRAFTEMFGYCISEASGMQPDTLLNipefPADNRIRLQQL 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382204 152 FWDRLRDgqfqQAEYLRIGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTARKQ 207
Cdd:PRK11359  202 LWKTARD----QDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQ 253
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 107-243 5.86e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 52.15  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 107 DPDGTILTANENFCAALGYRIDEIVGKHHRiFVAPEESARPEYKLFWDRLRDGQFQQAEYLRIGKAGNDVWIQATYNPIF 186
Cdd:PRK13558  168 LPDEPLIYINDAFERITGYSPDEVLGRNCR-FLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIR 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382204 187 SPSGRIYKIVKFATDVTARKQAVSALGGQLDNMangqlaDQLAARLPGEFEDIRVAL 243
Cdd:PRK13558  247 DEDGTVTHYVGFQTDVTERKEAELALQRERRKL------QRLLERVEGLVNDVTSAL 297
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 43-83 5.96e-07

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: 46.02  E-value: 5.96e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1345382204   43 EYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDVTER 83
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 1-82 6.48e-07

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 47.46  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGRHHSMFVDQAYGQSAEYKAFWKGLAEGRFQAAEYRriaKGGRAVWIQATYNPIFDKTGKPTGVVKFATDV 80
Cdd:pfam13426  15 LGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVVLYR---KDGEPFPVLVSLAPIRDDGGELVGIIAILRDI 91


                  ..
gi 1345382204  81 TE 82
Cdd:pfam13426  92 TE 93
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 2-85 1.92e-06

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: 46.90  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFVdqAYGQSAEYKAFWKGLAEGR--FQAAEYRRIAKGGRAVWIQATYNPIFdKTGKPTGVVKFATD 79
Cdd:TIGR00229  37 GYSAEELIGRNVLELI--PEEDREEVRERIERRLEGEpePVSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRD 113


                  ....*.
gi 1345382204  80 VTERKR 85
Cdd:TIGR00229 114 ITERKE 119
PRK13560 PRK13560
hypothetical protein; Provisional
 76-212 3.36e-06

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 50.06  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  76 FATDVTERKR---RDADALGQIEAISRSQAVIEF--DPDGTILTANENFCAALGYRIDEIVGKHHRIFvAPEESARPEYK 150
Cdd:PRK13560  185 FAEDITERKRaeeRIDEALHFLQQLLDNIADPAFwkDEDAKVFGCNDAACLACGFRREEIIGMSIHDF-APAQPADDYQE 263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382204 151 LFWDRLRDGQFQQAEYLRIGKAGNDVWIQATYNPI--FSPSGRIYKIVKFATDVTARKQAVSAL 212
Cdd:PRK13560  264 ADAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAefDDKENHCAGLVGAITDISGRRAAEREL 327
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 1-85 3.82e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 45.87  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGRH-HSMFVDQAYgqsAEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATD 79
Cdd:pfam08448  28 FGLPPEELLGKTlAELLPPEDA---ARLERALRRALEGEEPIDFLEELLLNGEERHYELRLTPLRDPDGEVIGVLVISRD 104


                  ....*.
gi 1345382204  80 VTERKR 85
Cdd:pfam08448 105 ITERRR 110
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 2-105 5.60e-06

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 49.07  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   2 GYGLEEILGRHHSMFvdQAYGQSAEYKA-FWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDV 80
Cdd:PRK13558  185 GYSPDEVLGRNCRFL--QGEDTNEERVAeLREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDV 262

                          90       100
                  ....*....|....*....|....*
gi 1345382204  81 TERKRRDADALGQIEAISRSQAVIE 105
Cdd:PRK13558  263 TERKEAELALQRERRKLQRLLERVE 287
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 1-80 1.41e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 44.16  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGRHHSMFVDQAYGQsAEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDV 80
Cdd:cd00130    25 LGYSPEELIGKSLLDLIHPEDRE-ELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
1-85 2.95e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.79  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGRHHSMFVDQAYGQsaEYKAFWKGLAEGRFQA--AEYRRIAKGGRAVWIQATYNPIFDKtGKPTGVVKFAT 78
Cdd:COG2202   170 LGYSPEELLGKSLLDLLHPEDRE--RLLELLRRLLEGGRESyeLELRLKDGDGRWVWVEASAVPLRDG-GEVIGVLGIVR 246


                  ....*..
gi 1345382204  79 DVTERKR 85
Cdd:COG2202   247 DITERKR 253
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 93-212 1.99e-04

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: 43.99  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  93 QIEAI--SRSQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVapeesarPEYKLfWDRLRDGQFQQAEYLRIG 170
Cdd:COG3829    12 ELEAIldSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELI-------PNSPL-LEVLKTGKPVTGVIQKTG 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1345382204 171 KAGNDVWIQATynPIFSpSGRIYKIVKFATDVTARKQAVSAL 212
Cdd:COG3829    84 GKGKTVIVTAI--PIFE-DGEVIGAVETFRDITELKRLERKL 122
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 100-146 2.12e-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: 39.69  E-value: 2.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1345382204  100 SQAVIEFDPDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEESAR 146
Cdd:smart00091  11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRER 57
PRK13560 PRK13560
hypothetical protein; Provisional
 6-208 2.57e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 43.89  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   6 EEILGRHHSMFVDQAYGQSAEYKAFWKGLAEGR-FQAAEYRRIAKGGRAVWIQATYNPIFDKTGKPTGVVKFATDVTERK 84
Cdd:PRK13560  387 EEFWCGDFQEWYPDGRPMAFDACPMAKTIKGGKiFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERK 466

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  85 RRDaDALGQIEAISRSQAVIEF----DPDGTILTANENFcAALGYRIDE-IVGKhhRIFVA---PEESAR--PEYKLFWD 154
Cdd:PRK13560  467 QVE-EQLLLANLIVENSPLVLFrwkaEEGWPVELVSKNI-TQFGYEPDEfISGK--RMFAAiihPADLEQvaAEVAEFAA 542

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1345382204 155 RLRDgQFQQaEYLRIGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTARKQA 208
Cdd:PRK13560  543 QGVD-RFEQ-EYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHA 594
PRK13560 PRK13560
hypothetical protein; Provisional
 1-212 3.16e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 43.51  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGRHHSMFvDQAYGQSAEYKAFWKGLAEGRFQAAEYRRIAKGGRAVWIQATYNPI--FDKTGKPTGVVKFAT 78
Cdd:PRK13560  237 CGFRREEIIGMSIHDF-APAQPADDYQEADAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAefDDKENHCAGLVGAIT 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  79 DVTERKRRDADALgqiEAISRSQAVIEFDP--------DGTILTANENFC-AALGYRIDEIVGKhhrifvaPEESARPEY 149
Cdd:PRK13560  316 DISGRRAAERELL---EKEDMLRAIIEAAPiaaigldaDGNICFVNNNAAeRMLGWSAAEVMGK-------PLPGMDPEL 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 150 -KLFWDR----------------------LRDGQ-FQQAEYLRIGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTAR 205
Cdd:PRK13560  386 nEEFWCGdfqewypdgrpmafdacpmaktIKGGKiFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITER 465


                  ....*..
gi 1345382204 206 KQAVSAL 212
Cdd:PRK13560  466 KQVEEQL 472
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1-105 1.51e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 40.99  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204   1 MGYGLEEILGRHhsmFVDQAYGQSAEYKAFWKGLAEGR-FQAAEYRRIAKGGRAVWIQATYNPIFDKTGKpTGVVKFATD 79
Cdd:COG3852    40 LGLSAEELLGRP---LAELFPEDSPLRELLERALAEGQpVTEREVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRD 115

                          90       100
                  ....*....|....*....|....*.
gi 1345382204  80 VTERKRRDAdalgQIEAISRSQAVIE 105
Cdd:COG3852   116 ITERKRLER----ELRRAEKLAAVGE 137
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
71-206 2.86e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 40.34  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204  71 TGVVKFATDVTERKRRDADALGQI--------EAISRSQ------------AVIEFDPDGTILTANENFCAALGYRIDEI 130
Cdd:PRK11360  223 DGLSTLENDLSTRLPPLPGELGEIsqainnlaQALRETRslnelilesiadGVIAIDRQGKITTMNPAAEVITGLQRHEL 302

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382204 131 VGKHHRIFVAPEEsarPEYKLFWDRLRDGQFQQAEYLRIGKAGNDVWIQATYNPIFSPSGRIYKIVKFATDVTARK 206
Cdd:PRK11360  303 VGKPYSELFPPNT---PFASPLLDTLEHGTEHVDLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERK 375
PRK13557 PRK13557
histidine kinase; Provisional
 108-286 5.40e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 39.27  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 108 PDGTILTANENFCAALGYRIDEIVGKHHRIFVAPEEsarpeyklfwDR-----LRDGQFQQ----AEYLRIGKAGNDVWI 178
Cdd:PRK13557   51 PDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPET----------DRatvaeVRDAIAERreiaTEILNYRKDGSSFWN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382204 179 QATYNPIFSPSGRIykIVKFAT--DVTARKQAVSALgGQLDNM-ANGQLA-------DQLAARLPGEFEDIRVALKSTLA 248
Cdd:PRK13557  121 ALFVSPVYNDAGDL--VYFFGSqlDVSRRRDAEDAL-RQAQKMeALGQLTggiahdfNNLLQVMSGYLDVIQAALSHPDA 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1345382204 249 QFARfvseLKRSAQGLRRATSSIAGGARNLSERTDKQR 286
Cdd:PRK13557  198 DRGR----MARSVENIRAAAERAATLTQQLLAFARKQR 231
 
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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