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Conserved domains on  [gi|491647096|ref|WP_005504622|]
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sigma-54 dependent transcriptional regulator [Grimontia hollisae]

Protein Classification

sigma-54-dependent transcriptional regulator( domain architecture ID 11454220)

sigma-54 factor interaction domain-containing protein with a domain similar to that found in the response regulator FleR from Pseudomonas aeruginosa

CATH:  3.40.50.2300
Gene Ontology:  GO:0006355|GO:0005524|GO:0000160|GO:0000156|GO:0003677
PubMed:  8830233|20226724|12618438|10966457
SCOP:  4003632

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-426 1.70e-122

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


:

Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 362.36  E-value: 1.70e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVML 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRElkrqletqsapGPRILGNADAVKQLRRTLFH 160
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-----------DSGLIGRSPAMQEVRRLIEK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 161 LKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTL 240
Cdd:COG2204  150 VAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 241 FIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDD 308
Cdd:COG2204  230 FLDEIGEMPLALQAKLLRVLqerefervgGNKPIPvdvRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 309 DVITLCQNFVRTTASRFGVAPPVmNRDHKERLLQHPWKGNIRELRAYAERWVLMGE-QSLTGDDgeshekahdtLAERIQ 387
Cdd:COG2204  310 DIPLLARHFLARFAAELGKPVKL-SPEALEALLAYDWPGNVRELENVIERAVILADgEVITAED----------LPEALE 378

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 491647096 388 KVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKH 426
Cdd:COG2204  379 EVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-426 1.70e-122

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 362.36  E-value: 1.70e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVML 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRElkrqletqsapGPRILGNADAVKQLRRTLFH 160
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-----------DSGLIGRSPAMQEVRRLIEK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 161 LKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTL 240
Cdd:COG2204  150 VAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 241 FIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDD 308
Cdd:COG2204  230 FLDEIGEMPLALQAKLLRVLqerefervgGNKPIPvdvRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 309 DVITLCQNFVRTTASRFGVAPPVmNRDHKERLLQHPWKGNIRELRAYAERWVLMGE-QSLTGDDgeshekahdtLAERIQ 387
Cdd:COG2204  310 DIPLLARHFLARFAAELGKPVKL-SPEALEALLAYDWPGNVRELENVIERAVILADgEVITAED----------LPEALE 378

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 491647096 388 KVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKH 426
Cdd:COG2204  379 EVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-429 8.55e-74

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 238.21  E-value: 8.55e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTP--EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIV 78
Cdd:PRK11361   1 MTAinRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  79 MLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQLETQSAPGpRILGNADAVKQLRRTL 158
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWG-HILTNSPAMMDICKDT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 159 FHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKG 238
Cdd:PRK11361 160 AKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 239 TLFIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRER 306
Cdd:PRK11361 240 TLLLDEIGEMPLVLQAKLLRILqereferigGHQTIKvdiRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 307 DDDVITLCQNFVRTTASR-----FGVAPPVMnrdhkERLLQHPWKGNIRELRAYAERWVLMG--------------EQSL 367
Cdd:PRK11361 320 REDISLLANHFLQKFSSEnqrdiIDIDPMAM-----SLLTAWSWPGNIRELSNVIERAVVMNsgpiifsedlppqiRQPV 394

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647096 368 TGDDG-ESHEKAHDTLAERIQKVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKHHLD 429
Cdd:PRK11361 395 CNAGEvKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 7-428 5.74e-71

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 230.79  E-value: 5.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096    7 IIDDERTIRDALSQTLDieGFQSRAFASAIDALDQLSNAFEGVIISDINMP-----QMDGMTFLQKALAVDSELSIVMLT 81
Cdd:TIGR02915   3 IVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIVIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   82 GHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQLETQSAPGprILGNADAVKQLRRTLFHL 161
Cdd:TIGR02915  81 GNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG--LITSSPGMQKICRTIEKI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  162 KDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLF 241
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  242 IDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDD 309
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLqervierlgGREEIPvdvRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  310 VITLCQNFVRTTASRFGVAPPVMNRDHKERLLQHPWKGNIRELRAYAERWVLMGEQS------LTGDDGESHEKAHD-TL 382
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNqitaedLGLDARERAETPLEvNL 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 491647096  383 AERIQKVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKHHL 428
Cdd:TIGR02915 399 REVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 5-134 1.39e-67

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 211.19  E-value: 1.39e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQL 134
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
Sigma54_activat pfam00158
Sigma-54 interaction domain;
144-298 3.57e-34

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 125.21  E-value: 3.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  144 ILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAY-- 221
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFtg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  222 ASlpSYKNSKIAAAGKGTLFIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCAL 289
Cdd:pfam00158  81 AD--SDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLqegefervgGTKPIKvdvRIIAATNRDLEEAVAEGRFREDL 158


                  ....*....
gi 491647096  290 YQALSGTTL 298
Cdd:pfam00158 159 YYRLNVIPI 167
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 5-57 1.45e-08

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 50.64  E-value: 1.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 491647096     5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMP 57
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
5-105 1.06e-05

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 46.40  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDqlsnAFEGV----IISDINMPQMDGMTfLQKALAVDSELSIVML 80
Cdd:NF040689   1 ILVVDDDPALAEMLGIVLRAEGFETVFCADGAEAVE----AFREVrpdlVLLDLMLPGMDGIE-VCRQIRAESGVPIIML 75

                         90       100
                 ....*....|....*....|....*
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPF 105
Cdd:NF040689  76 TAKSDTVDVVRGLEAGADDYVVKPF 100
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-426 1.70e-122

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 362.36  E-value: 1.70e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVML 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRElkrqletqsapGPRILGNADAVKQLRRTLFH 160
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-----------DSGLIGRSPAMQEVRRLIEK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 161 LKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTL 240
Cdd:COG2204  150 VAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 241 FIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDD 308
Cdd:COG2204  230 FLDEIGEMPLALQAKLLRVLqerefervgGNKPIPvdvRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 309 DVITLCQNFVRTTASRFGVAPPVmNRDHKERLLQHPWKGNIRELRAYAERWVLMGE-QSLTGDDgeshekahdtLAERIQ 387
Cdd:COG2204  310 DIPLLARHFLARFAAELGKPVKL-SPEALEALLAYDWPGNVRELENVIERAVILADgEVITAED----------LPEALE 378

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 491647096 388 KVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKH 426
Cdd:COG2204  379 EVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-429 8.55e-74

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 238.21  E-value: 8.55e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTP--EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIV 78
Cdd:PRK11361   1 MTAinRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  79 MLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQLETQSAPGpRILGNADAVKQLRRTL 158
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWG-HILTNSPAMMDICKDT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 159 FHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKG 238
Cdd:PRK11361 160 AKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 239 TLFIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRER 306
Cdd:PRK11361 240 TLLLDEIGEMPLVLQAKLLRILqereferigGHQTIKvdiRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 307 DDDVITLCQNFVRTTASR-----FGVAPPVMnrdhkERLLQHPWKGNIRELRAYAERWVLMG--------------EQSL 367
Cdd:PRK11361 320 REDISLLANHFLQKFSSEnqrdiIDIDPMAM-----SLLTAWSWPGNIRELSNVIERAVVMNsgpiifsedlppqiRQPV 394

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647096 368 TGDDG-ESHEKAHDTLAERIQKVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKHHLD 429
Cdd:PRK11361 395 CNAGEvKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 7-428 5.74e-71

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 230.79  E-value: 5.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096    7 IIDDERTIRDALSQTLDieGFQSRAFASAIDALDQLSNAFEGVIISDINMP-----QMDGMTFLQKALAVDSELSIVMLT 81
Cdd:TIGR02915   3 IVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIVIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   82 GHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQLETQSAPGprILGNADAVKQLRRTLFHL 161
Cdd:TIGR02915  81 GNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG--LITSSPGMQKICRTIEKI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  162 KDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLF 241
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  242 IDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDD 309
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLqervierlgGREEIPvdvRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  310 VITLCQNFVRTTASRFGVAPPVMNRDHKERLLQHPWKGNIRELRAYAERWVLMGEQS------LTGDDGESHEKAHD-TL 382
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNqitaedLGLDARERAETPLEvNL 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 491647096  383 AERIQKVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKHHL 428
Cdd:TIGR02915 399 REVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 5-425 5.09e-68

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 223.59  E-value: 5.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRElkrqlETQSAPGPRILGNADAVKQLRRTLFHLKDL 164
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRN-----IQVNGPTTDIIGEAPAMQDVFRIIGRLSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 165 NDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLFIDG 244
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 245 IEALPPAVQEKLATLI--GTENR----------PRIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVIT 312
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLadGQFYRvggyapvkvdVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 313 LCQNFVRTTASRFGVAPPVMNRDHKERLLQHPWKGNIRELRAYAeRWV-LMGE------QSLTGDDGESHEKA------- 378
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTC-RWLtVMAAgqevliQDLPGELFESTVPEstsqmqp 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647096 379 -------------------HDTLAERIQKVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKK 425
Cdd:PRK10923 400 dswatllaqwadralrsghQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKE 465
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 5-134 1.39e-67

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 211.19  E-value: 1.39e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQL 134
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-425 1.38e-61

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 206.03  E-value: 1.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:PRK10365   7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEkrqlvmENRELKRQLETQSAPGPRILGNADAVKQLRRTLFHLKD 163
Cdd:PRK10365  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA------HTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 164 LNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLFID 243
Cdd:PRK10365 161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 244 GIEALPP--------AVQEKLATLIGTENR----PRIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVI 311
Cdd:PRK10365 241 EIGDISPmmqvrllrAIQEREVQRVGSNQTisvdVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 312 TLCQNFVRTTASRF-----GVAPPVMnrdhkERLLQHPWKGNIRELRAYAERWVLMgeqsLTGDDGESHEK----AHDTL 382
Cdd:PRK10365 321 LLAGHFLQRFAERNrkavkGFTPQAM-----DLLIHYDWPGNIRELENAVERAVVL----LTGEYISERELplaiASTPI 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 491647096 383 ----AERIQ---KVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKK 425
Cdd:PRK10365 392 plgqSQDIQplvEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 118-429 2.97e-60

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: 202.69  E-value: 2.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 118 VEKRQLVMENRELKRQLETQSAPGpRILGNADAVKQLRRTLfhLK----DLNddVLFQGERGTGKEMAARFLHDQGSRQD 193
Cdd:COG3829  115 LKRLERKLREEELERGLSAKYTFD-DIIGKSPAMKELLELA--KRvaksDST--VLILGESGTGKELFARAIHNASPRRD 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 194 EPFVAIKCRRIPEALIAMELFGSEQHAY--ASlpsyKNSK---IAAAGKGTLFIDGIEALPPAVQEKLATLI-------- 260
Cdd:COG3829  190 GPFVAVNCAAIPENLLESELFGYEKGAFtgAK----KGGKpglFELADGGTLFLDEIGEMPLSLQAKLLRVLqekevrrv 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 261 -GTENRP---RIIASTRVDLAASVRLGRF--DcaLYQALSGTTLLFPPLRERDDDVITLCQNFVRTTASRFGVAPPVMNR 334
Cdd:COG3829  266 gGTKPIPvdvRIIAATNRDLEEMVEEGRFreD--LYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISP 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 335 DHKERLLQHPWKGNIRELRAYAERWVLMGE----------QSLTGDDGESHEKAHDTLAERIQKVERAILFDALNRHNGM 404
Cdd:COG3829  344 EALELLLAYDWPGNVRELENVIERAVVLSEgdvitpehlpEYLLEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGN 423

                        330       340
                 ....*....|....*....|....*
gi 491647096 405 LKEVQAELGLARKTLYEKLKKHHLD 429
Cdd:COG3829  424 KSKAAKALGISRSTLYRKLKKYGIK 448
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
68-427 1.35e-53

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 188.96  E-value: 1.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  68 ALAVDSELSIVMLTghgdiSTAVAAIRQGAYDFLEKPFST------DTLLDVLR-RGVEKRQLVMEN------------- 127
Cdd:COG3284  229 LLAFDEDGRIVAAN-----RAARRLLGLADAALLGRPLEElfgldlEALPDGARrAPASPRPLRLRDgrrlgallrlrpa 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 128 -RELKRQLETQSAPG--PRILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRI 204
Cdd:COG3284  304 rRAARAAPAGAPAPAalAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAI 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 205 PEALIAMELFGSEQHAY--ASLPSYKnSKIAAAGKGTLFIDGIEALPPAVQEKLAT---------LIGTENRP---RIIA 270
Cdd:COG3284  384 PEELIESELFGYEPGAFtgARRKGRP-GKIEQADGGTLFLDEIGDMPLALQARLLRvlqerevtpLGGTKPIPvdvRLIA 462

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 271 STRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERdDDVITLCQNFVRTTASRFG---VAPPVMnrdhkERLLQHPWKG 347
Cdd:COG3284  463 ATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAGRGplrLSPEAL-----ALLAAYPWPG 536

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 348 NIRELRAYAERWVLMGEQSLTG---------DDGESHEKAHDTLAERIQKVERAILFDALNRHNGMLKEVQAELGLARKT 418
Cdd:COG3284  537 NVRELRNVLRTALALADGGVITvedlpdelrAELAAAAPAAAAPLTSLEEAERDAILRALRACGGNVSAAARALGISRST 616


                 ....*....
gi 491647096 419 LYEKLKKHH 427
Cdd:COG3284  617 LYRKLKRYG 625
PRK15115 PRK15115
response regulator GlrR; Provisional
 7-435 6.98e-52

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 180.42  E-value: 6.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDI 86
Cdd:PRK15115  10 LVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  87 STAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENReLKRQLETQSAPGPRILGNADAVKQlrrtlfhlKDLNd 166
Cdd:PRK15115  90 PDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDER-WREAIVTRSPLMLRLLEQARMVAQ--------SDVS- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 167 dVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLFIDGIE 246
Cdd:PRK15115 160 -VLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 247 ALPPAVQEKLATLIGTEN-RP-----------RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVITLC 314
Cdd:PRK15115 239 DMPAPLQVKLLRVLQERKvRPlgsnrdididvRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 315 QNFVRTTASRFGVAPPVMNRDHKERLLQHPWKGNIRELRAYAERWVLMG----------EQSLTGDdgeshEKAHDTLAE 384
Cdd:PRK15115 319 NHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTsspvisdalvEQALEGE-----NTALPTFVE 393

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491647096 385 RIQKVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKHHLDKESFKG 435
Cdd:PRK15115 394 ARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE 444
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
110-420 2.59e-39

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 147.63  E-value: 2.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 110 LLDVLRRGVEKRQLVMEnrelkrQLETQSAPGPRILGNADAVKQLRR--TLFHLKDLNddVLFQGERGTGKEMAARFLHD 187
Cdd:PRK05022 161 LIEQLESQAELPQDVAE------FLRQEALKEGEMIGQSPAMQQLKKeiEVVAASDLN--VLILGETGVGKELVARAIHA 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 188 QGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLFIDGIEALPPAVQEK-LATL------- 259
Cdd:PRK05022 233 ASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKlLRVLqygeiqr 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 260 IGtENRP-----RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVITLCQNFVRTTASRFGVAPPVMNR 334
Cdd:PRK05022 313 VG-SDRSlrvdvRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSP 391

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 335 DHKERLLQHPWKGNIREL---------RAYAE---RWVLMGEQSLTGDDGESHEKAHDTLAERIQKV----------ERA 392
Cdd:PRK05022 392 AAQAALLAYDWPGNVRELehvisraalLARARgagRIVTLEAQHLDLPAEVALPPPEAAAAPAAVVSqnlreateafQRQ 471

                        330       340
                 ....*....|....*....|....*...
gi 491647096 393 ILFDALNRHNGMLKEVQAELGLARKTLY 420
Cdd:PRK05022 472 LIRQALAQHQGNWAAAARALELDRANLH 499
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 168-435 4.10e-39

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 149.06  E-value: 4.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 168 VLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSeqhAYASLPSYKNSKIAAAGKGTLFIDGIEA 247
Cdd:PRK11388 351 VLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLGS---DRTDSENGRLSKFELAHGGTLFLEKVEY 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 248 LPPAVQEKLATLIGT-------ENR--P---RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVITLCQ 315
Cdd:PRK11388 428 LSPELQSALLQVLKTgvitrldSRRliPvdvRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVN 507

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 316 NFVRT----TASRFGVAPPVMnrdhkERLLQHPWKGNIRELRAYAERWVLMGEQSL---------------TGDDGESHE 376
Cdd:PRK11388 508 NKLRSlekrFSTRLKIDDDAL-----ARLVSYRWPGNDFELRSVIENLALSSDNGRirlsdlpehlfteqaTDDVSATRL 582

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491647096 377 KAHDTLAEriqkVERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKKHHLDKESFKG 435
Cdd:PRK11388 583 STSLSLAE----LEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQFKR 637
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 5-136 1.19e-38

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 138.31  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEK----RQLVMENRELKRQLET 136
Cdd:COG4566   82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARdrarRAERARRAELRARLAS 137
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
 144-425 3.68e-38

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 145.25  E-value: 3.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 144 ILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLH-----DQGSRQDE---PFVAIKCRRIPEALIAMELFG 215
Cdd:PRK15424 221 LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfaRHDARQGKkshPFVAVNCGAIAESLLEAELFG 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 216 SEQHAY-ASLPSYKNSKIAAAGKGTLFIDGIEALPPAVQ--------EKLATLIGTeNRP-----RIIASTRVDLAASVR 281
Cdd:PRK15424 301 YEEGAFtGSRRGGRAGLFEIAHGGTLFLDEIGEMPLPLQtrllrvleEKEVTRVGG-HQPvpvdvRVISATHCDLEEDVR 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 282 LGRFDCALYQALSGTTLLFPPLRERDDDVITLCQNFVRTTASRFGVAPPVMNR----DHKERLLQHPWKGNIRELRAYAE 357
Cdd:PRK15424 380 QGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAPFSAALRqglqQCETLLLHYDWPGNVRELRNLME 459

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647096 358 R----WVLMGEQSLTGDDGE--SHEKAHDTLAERIQKVERAILFDALNRHNGMlKEVQAE-LGLARKTLYEKLKK 425
Cdd:PRK15424 460 RlalfLSVEPTPDLTPQFLQllLPELARESAKTPAPRLLAATLQQALERFNGD-KTAAANyLGISRTTLWRRLKA 533
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 171-429 3.24e-36

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


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 135.75  E-value: 3.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 171 QGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIamelfgseqhayaslpsyknskiaaagkgtlfidgiEALpp 250
Cdd:COG3604  121 LGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLL------------------------------------ESL-- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 251 avQEKLATLIGtENRP-----RIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVITLCQNFVRTTASRF 325
Cdd:COG3604  163 --QEGEFERVG-GDETikvdvRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHFLEKFSRRL 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 326 GVAPPVMNRDHKERLLQHPWKGNIRELRAYAERWVLMGE-QSLTGDDGESHEKahdtlaERIQKVERAILFDALNRHNGM 404
Cdd:COG3604  240 GKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEgGVLDADDLAPGSR------EALEEVEREHILEALERTGGN 313

                        250       260
                 ....*....|....*....|....*
gi 491647096 405 LKEVQAELGLARKTLYEKLKKHHLD 429
Cdd:COG3604  314 IAGAARLLGLTPSTLRSRMKKLGIK 338
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 5-119 1.37e-35

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 127.23  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVE 119
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
 143-394 2.58e-34

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 133.78  E-value: 2.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 143 RILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYA 222
Cdd:COG3283  205 HIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFG 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 223 SLPSYKNSKIAAAGKGTLFIDGIEALPPAVQEKLATLI--GT-----ENRP-----RIIASTRVDLAASVRLGRFDCALY 290
Cdd:COG3283  285 NAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLqdGTfrrvgEEQEvkvdvRVICATQKDLAELVQEGEFREDLY 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 291 QALSGTTLLFPPLRERDDDVITLCQNFVRTTASRFGVAPPVMNRDHKERLLQHPWKGNIRELR-------AYAERWVLMG 363
Cdd:COG3283  365 YRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLEnalyravSLLEGDELTP 444

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 491647096 364 EQ----SLTGDDGESHEKAHDTLAERIQKVERAIL 394
Cdd:COG3283  445 EDlqlpEYAASAGLLDDLLEGSLDEIVKRFERSLL 479
Sigma54_activat pfam00158
Sigma-54 interaction domain;
144-298 3.57e-34

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 125.21  E-value: 3.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  144 ILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAY-- 221
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFtg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  222 ASlpSYKNSKIAAAGKGTLFIDGIEALPPAVQEKLATLI---------GTENRP---RIIASTRVDLAASVRLGRFDCAL 289
Cdd:pfam00158  81 AD--SDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLqegefervgGTKPIKvdvRIIAATNRDLEEAVAEGRFREDL 158


                  ....*....
gi 491647096  290 YQALSGTTL 298
Cdd:pfam00158 159 YYRLNVIPI 167
fixJ PRK09390
response regulator FixJ; Provisional
 3-122 3.79e-32

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 120.88  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:PRK09390   4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQ 122
Cdd:PRK09390  84 HGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAP 123
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 3-118 2.90e-31

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 115.83  E-value: 2.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGV 118
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 5-117 9.44e-31

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 114.23  E-value: 9.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRG 117
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQA 115
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
 144-360 8.85e-30

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 117.85  E-value: 8.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 144 ILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYAS 223
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 224 LPSYKNSKIAAAGKGTLFIDGIEALPPAVQEKLATLI--GTENR----------PRIIASTRVDLAASVRLGRFDCALYQ 291
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIeyGELERvggsqplqvnVRLVCATNADLPAMVAEGKFRADLLD 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 292 ALSGTTLLFPPLRERDDDVITLCQNFVRTTASRFGVAP-PVMNRDHKERLLQHPWKGNIRELRAYAERWV 360
Cdd:PRK11608 168 RLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPLfPGFTERARETLLNYRWPGNIRELKNVVERSV 237
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 5-115 3.77e-29

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 109.93  E-value: 3.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096    5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 491647096   85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
120-431 2.93e-28

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 117.62  E-value: 2.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 120 KRQLVMENRELKRQLETQSAPGPRILGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAI 199
Cdd:PRK15429 354 KERLVDENLALTEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKM 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 200 KCRRIPEALIAMELFGSEQHAYASLPSYKNSKIAAAGKGTLFIDGIEALPPAVQEKLA--------------TLIGTEnr 265
Cdd:PRK15429 434 NCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLrvlqeqeferlgsnKIIQTD-- 511

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 266 PRIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPPLRERDDDVITLCQNFVRTTASRFGVAPPVMNRDHKERLLQHPW 345
Cdd:PRK15429 512 VRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEW 591

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 346 KGNIRELRAYAERWVLMGEQS---LTGDDGESHEKAHDTLAERIQKV---ERAILFDALNRHNGML---KEVQAELGLAR 416
Cdd:PRK15429 592 PGNVRELENVIERAVLLTRGNvlqLSLPDITLPEPETPPAATVVAQEgedEYQLIVRVLKETNGVVagpKGAAQRLGLKR 671

                        330
                 ....*....|....*
gi 491647096 417 KTLYEKLKKHHLDKE 431
Cdd:PRK15429 672 TTLLSRMKRLGIDKS 686
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 1-135 1.05e-27

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 109.48  E-value: 1.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIV 78
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRllRADPSTRDIPVI 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491647096  79 MLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQLE 135
Cdd:COG3437   85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLK 141
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 7-104 1.04e-26

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 103.08  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDI 86
Cdd:cd00156    2 IVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADE 81

                         90
                 ....*....|....*...
gi 491647096  87 STAVAAIRQGAYDFLEKP 104
Cdd:cd00156   82 EDAVRALELGADDYLVKP 99
PRK10820 PRK10820
transcriptional regulator TyrR;
151-353 6.18e-26

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 109.78  E-value: 6.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 151 VKQLRRtlfhLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEQHAYASLPSYKNS 230
Cdd:PRK10820 217 VEQARK----LAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPNALEGKKG 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 231 KIAAAGKGTLFIDGIEALPPAVQEKLATLI--GTENRP----------RIIASTRVDLAASVRLGRFDCALYQALSGTTL 298
Cdd:PRK10820 293 FFEQANGGSVLLDEIGEMSPRMQAKLLRFLndGTFRRVgedhevhvdvRVICATQKNLVELVQKGEFREDLYYRLNVLTL 372

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491647096 299 LFPPLRERDDDVITLCQNFVRTTASRFGVAPPVMNRDHKERLLQHPWKGNIRELR 353
Cdd:PRK10820 373 NLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLK 427
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 5-122 7.63e-25

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 98.77  E-value: 7.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTG 82
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRriRALPRLPDIPIIALTA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQ 122
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 7-120 1.12e-23

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 95.10  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIE--GFQS-RAFASAIDALDQL-SNAFEgVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd17536    3 IVDDEPLIREGLKKLIDWEelGFEVvGEAENGEEALELIeEHKPD-IVITDIRMPGMDGLELIEKIRELYPDIKIIILSG 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEK 120
Cdd:cd17536   82 YDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 7-104 4.73e-23

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 92.91  E-value: 4.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLD-IEGFQSRAFA-SAIDALDQL-SNAFEgVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:COG4753    4 IVDDEPLIREGLKRILEwEAGFEVVGEAeNGEEALELLeEHKPD-LVITDINMPGMDGLELLEAIRELDPDTKIIILSGY 82

                         90       100
                 ....*....|....*....|.
gi 491647096  84 GDISTAVAAIRQGAYDFLEKP 104
Cdd:COG4753   83 SDFEYAQEAIKLGADDYLLKP 103
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 7-135 8.54e-23

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 94.60  E-value: 8.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDI 86
Cdd:COG4567    9 LVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGYASI 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491647096  87 STAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQLE 135
Cdd:COG4567   89 ATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLDRLE 137
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 5-116 1.11e-22

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 95.02  E-value: 1.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:COG0745   84 DEEDRVRGLEAGADDYLTKPFDPEELLARIRA 115
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 1-129 1.17e-22

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 93.11  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLD-IEGFQS-RAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIV 78
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLErLPGFEVvGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491647096  79 MLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRE 129
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 7-116 1.87e-22

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 93.82  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTGHG 84
Cdd:COG3706    6 VVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRrlRADPRTADIPIIFLTALD 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL---DVLRR 116
Cdd:COG3706   86 DEEDRARALEAGADDYLTKPFDPEELLarvDLVAR 120
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 7-114 3.21e-22

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 90.96  E-value: 3.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQL-SNAFEGVIIsDINMPQMDGMTFLQKALAVDSELSIVMLTGHGD 85
Cdd:cd17563    5 LVDDDEVFAERLARALERRGFEVETAHSVEEALALArEEKPDYAVL-DLRLGGDSGLDLIPPLRALQPDARIVVLTGYAS 83

                         90       100
                 ....*....|....*....|....*....
gi 491647096  86 ISTAVAAIRQGAYDFLEKPFSTDTLLDVL 114
Cdd:cd17563   84 IATAVEAIKLGADDYLAKPADADEILAAL 112
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
145-303 2.20e-21

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 89.71  E-value: 2.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  145 LGNADAVKQLRRTLFHLKDLNDDVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALiamelfgSEQhayasl 224
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLEL-------LEQ------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  225 psyknskiaaAGKGTLFIDGIEALPPAVQEKLATLIG--TENRPRIIASTRVDLAASVRLGRFDCALYQALSGTTLLFPP 302
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAkaEGYRVRLVCTSSKDLPQLAAAGLFDEQLYFELSALRLHVPP 137


                  .
gi 491647096  303 L 303
Cdd:pfam14532 138 L 138
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 5-123 3.92e-21

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 88.41  E-value: 3.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQL 123
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKL 119
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 3-119 4.94e-21

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 87.84  E-value: 4.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491647096  83 HGDISTAVAAIRQGA-YDFLEKPFSTDTLLDVLRRGVE 119
Cdd:cd17569   81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 5-105 1.81e-19

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 83.65  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTL-DIEGFQSRAFASAIDALDQL-SNAFEgVIISDINMPQMDGMTFLQ--KALAVDSELSIVML 80
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLrSAGYLEVVSFTDPREALAWCrENPPD-LILLDYMMPGMDGLEFIRrlRALPGLEDVPIVMI 81

                         90       100
                 ....*....|....*....|....*
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPF 105
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPF 106
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 5-115 3.44e-18

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 80.12  E-value: 3.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEELLARVR 111
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
 1-116 5.52e-17

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 76.76  E-value: 5.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVML 80
Cdd:COG5803    1 MMKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMM 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:COG5803   81 TAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNK 116
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 5-116 1.04e-16

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 75.80  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTG 82
Cdd:cd17562    3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKelRKLPAYKFTPILMLTT 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17562   83 ESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 3-134 1.34e-16

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 75.87  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDiEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd17596    1 PTILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491647096  83 HGDISTAVAAIRQ-GAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRELKRQL 134
Cdd:cd17596   80 YTDSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLEL 132
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 7-104 1.75e-16

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 74.37  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQL-SNAFeGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGD 85
Cdd:cd17574    2 VVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELArEEQP-DLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                         90
                 ....*....|....*....
gi 491647096  86 ISTAVAAIRQGAYDFLEKP 104
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 3-120 2.71e-16

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 74.54  E-value: 2.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFsTDtlLDVLRRGVEK 120
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPI-ED--LAVLEHAVRR 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 8-116 1.45e-15

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 72.66  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   8 IDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEG--VIISDINMPQMDGMTFLQKALAVdSELSIVMLTGHGD 85
Cdd:cd17584    4 VDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEfdLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSADGS 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  86 ISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17584   83 TSTVMKGLAHGACDYLLKPVSIEDLKNIWQH 113
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 5-114 2.30e-15

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 71.72  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQK--ALAVDSELSIVMLTG 82
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRlrELPWLANTPAIALTG 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVL 114
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 5-104 2.60e-15

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 71.32  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTGHG 84
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQR-LRQKSTLPVIFLTSKD 79

                         90       100
                 ....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKP 104
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 7-145 2.86e-15

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 74.85  E-value: 2.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTL-DIEGFQSRA-FASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:COG3279    6 IVDDEPLARERLERLLeKYPDLEVVGeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTAYD 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647096  85 DisTAVAAIRQGAYDFLEKPFSTDTLLDVLRRgvekrqlVMENRELKRQLETQSAPGPRIL 145
Cdd:COG3279   86 E--YALEAFEVNAVDYLLKPIDEERLAKALEK-------AKERLEAKAAAEASPEEKDRIF 137
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 7-116 3.35e-15

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 71.48  E-value: 3.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQsraFASAIDALDQLSNAFEG---VIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:cd17625    2 VVEDEKDLSEAITKHLKKEGYT---VDVCFDGEEGLEYALSGiydLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTAL 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:cd17625   79 DAVEDRVKGLDLGADDYLPKPFSLAELLarirALLRR 115
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 7-116 3.80e-15

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 71.39  E-value: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIE-GFQ-SRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17535    3 IVDDHPLVREGLRRLLESEpDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAHD 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17535   83 DPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 5-110 6.79e-15

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 70.83  E-value: 6.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFAS-AIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAvDSELS---IVML 80
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNNVEEAEdGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRA-DGALShlpVLMV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTL 110
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
orf27 CHL00148
Ycf27; Reviewed
 5-129 8.95e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 73.60  E-value: 8.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTGHG 84
Cdd:CHL00148   9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQE-IRKESDVPIIMLTALG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTL----LDVLRRgVEKRQLVMENRE 129
Cdd:CHL00148  88 DVSDRITGLELGADDYVVKPFSPKELeariRSVLRR-TNKKSFSSKIPN 135
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 5-136 5.00e-14

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 70.37  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFA-SAIDALDQLSNAFEGVIISDINMPQMDGMTFLqKALAVDSELSIVMLTGH 83
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVVAEAaDGEDAVELVRELKPDLVIVDIDMPDRDGLEAA-RQISEERPAPVILLTAY 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVL----RRGVEKRQLVMENRELKRQLET 136
Cdd:COG3707   85 SDPELIERALEAGVSAYLVKPLDPEDLLPALelalARFRELRALRRELAKLREALEE 141
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 3-116 1.20e-13

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 66.92  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFAS-AIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLT 81
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGEAAnGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  82 GHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEK 115
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 4-108 2.99e-13

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 66.00  E-value: 2.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQL-SNAFEGVIISDINMPQMDGMTFLQKALAVDS--ELSIVML 80
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLeQHPDIKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGI 81

                         90       100
                 ....*....|....*....|....*...
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTD 108
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKPFLPE 109
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 7-114 3.83e-13

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 65.57  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELS---IVMLTGH 83
Cdd:cd17546    3 VVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRrtpIIALTAN 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVL 114
Cdd:cd17546   83 ALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 4-116 4.34e-13

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 65.65  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17553   82 GELDMIQESKELGALTHFAKPFDIDEIRDAVKK 114
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 5-105 5.24e-13

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 64.83  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALD--QLSNAFEGVIiSDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEklQQGKDIDIVV-TDIVMPEMDGIELAREARKIDPDVKILFISG 80

                         90       100
                 ....*....|....*....|...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPF 105
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 5-105 6.70e-13

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 64.44  E-value: 6.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTG 82
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRrlKEDPETRHIPVIMITA 81

                         90       100
                 ....*....|....*....|...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPF 105
Cdd:cd17538   82 LDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 3-111 1.07e-12

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 64.58  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVML 80
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRrlKRDEMTRDIPIIML 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPRELV 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 7-115 1.21e-12

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 64.30  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDI 86
Cdd:cd17615    4 VVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKDSV 83

                         90       100
                 ....*....|....*....|....*....
gi 491647096  87 STAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd17615   84 EDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 5-116 1.32e-12

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 64.16  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17554    3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYS 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  85 DISTAVAAIRQGAYdfLEKPFSTDTLLDVLRR 116
Cdd:cd17554   83 EYKSDFSSWAADAY--VVKSSDLTELKETIKR 112
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 1-142 1.59e-12

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 66.52  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVML 80
Cdd:PRK11083   2 QQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFStdtlldvlrrgveKRQLVMENRELKRQLETQSAPGP 142
Cdd:PRK11083  82 TARSDEVDRLVGLEIGADDYVAKPFS-------------PREVAARVRTILRRVKKFAAPSP 130
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 5-104 2.57e-12

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 62.78  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELS---IVMLT 81
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGK-LRKNADFDtipVIFLT 79

                         90       100
                 ....*....|....*....|...
gi 491647096  82 GHGDISTAVAAIRQGAYDFLEKP 104
Cdd:cd19927   80 AKGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 5-116 2.89e-12

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 63.09  E-value: 2.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLqKALAVDSELSIVMLTGHG 84
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVL-KELRKTSQVPVLMLTARG 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFNPRELVarirAILRR 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 5-115 3.49e-12

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 62.89  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELLARLR 111
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 5-104 3.94e-12

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 62.14  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80

                         90       100
                 ....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKP 104
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
PRK10610 PRK10610
chemotaxis protein CheY;
7-120 1.38e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 61.53  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFAS-AIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTGH 83
Cdd:PRK10610  10 VVDDFSTMRRIVRNLLKELGFNNVEEAEdGVDALNKLQAGGFGFVISDWNMPNMDGLELLKtiRADGAMSALPVLMVTAE 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEK 120
Cdd:PRK10610  90 AKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 7-111 2.64e-11

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 60.36  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTGHG 84
Cdd:cd19937    2 VVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRilRSDPKTSSIPIIMLTAKG 81

                         90       100
                 ....*....|....*....|....*..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd19937   82 EEFDKVLGLELGADDYITKPFSPRELL 108
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 7-110 2.78e-11

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 60.48  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTL----DIE--GFqsrAfASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVdSELSIVML 80
Cdd:cd17541    5 IVDDSAVMRKLLSRILesdpDIEvvGT---A-RDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE-RPTPVVMV 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  81 TGHGDISTAVA--AIRQGAYDFLEKPFSTDTL 110
Cdd:cd17541   80 SSLTEEGAEITleALELGAVDFIAKPSGGISL 111
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 5-115 2.83e-11

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 60.37  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
ompR PRK09468
osmolarity response regulator; Provisional
 2-116 5.59e-11

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 62.30  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   2 TPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAiDALDQL--SNAFEgVIISDINMPQMDGMTFLQKALAVDSELSIVM 79
Cdd:PRK09468   5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLltRESFH-LMVLDLMLPGEDGLSICRRLRSQNNPTPIIM 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491647096  80 LTGHGDISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:PRK09468  83 LTAKGEEVDRIVGLEIGADDYLPKPFNPRELLarirAVLRR 123
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 146-276 6.68e-11

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 60.24  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 146 GNADAVKQLRRTLFHLKDLNddVLFQGERGTGKEMAARFLHDQGSRQDEPFVAIKCRRIPEALIAMELFGSEqhayasLP 225
Cdd:cd00009    2 GQEEAIEALREALELPPPKN--LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LV 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491647096 226 SYKNSKIAAAGKGTLFIDGIEALPPAVQEKLATLI--------GTENRPRIIASTRVDL 276
Cdd:cd00009   74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLetlndlriDRENVRVIGATNRPLL 132
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 5-104 5.00e-10

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 56.29  E-value: 5.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQ-LSNAFEgVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLaLTNEYD-LIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTAR 79

                         90       100
                 ....*....|....*....|.
gi 491647096  84 GDISTAVAAIRQGAYDFLEKP 104
Cdd:cd19935   80 DSVEDRVKGLDLGADDYLVKP 100
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 7-104 1.12e-09

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 55.24  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDI 86
Cdd:cd19926    3 VVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYGSL 82

                         90
                 ....*....|....*...
gi 491647096  87 STAVAAIRQGAYDFLEKP 104
Cdd:cd19926   83 DTAIEALKAGAFDFLTKP 100
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 5-115 2.23e-09

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 54.76  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLqKALAVDSELSIVMLTGH- 83
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLL-RTIRARSDVPIIIISGDr 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd17594   81 RDEIDRVVGLELGADDYLAKPFGLRELLARVR 112
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 3-111 2.23e-09

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 54.70  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTfLQKALAVDSELSIVMLTG 82
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLS-LTRELREQSEVGIILVTG 79

                         90       100
                 ....*....|....*....|....*....
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFNPRELL 108
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-116 2.25e-09

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 57.42  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIV 78
Cdd:PRK10161   1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKhlKRESMTRDIPVV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491647096  79 MLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:PRK10161  81 MLTARGEEEDRVRGLETGADDYITKPFSPKELVarikAVMRR 122
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 5-104 3.36e-09

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 53.71  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTGHG 84
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRR-LREWSAVPVIVLSARD 79

                         90       100
                 ....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKP 104
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 5-116 7.99e-09

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 53.31  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTG 82
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRllKEDPATRDIPVIALTA 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491647096  83 H---GDISTAVAAirqGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17548   82 YamkGDREKILEA---GCDGYISKPIDTREFLETVAK 115
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
 3-104 9.68e-09

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 53.49  E-value: 9.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   3 PEIWIIDDERTIRDALSQTL------DIEGFQSRAFASAIDALDQLSNAFEGV--IISDINMPQMDGMTFLQKALAVDSE 74
Cdd:cd17595    1 PIILTVDDDPQVLRAVARDLrrqygkDYRVLRADSGAEALDALKELKLRGEAValFLVDQRMPEMDGVEFLEKAMELFPE 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  75 LSIVMLTGHGDISTAVAAIRQGAYDF-LEKP 104
Cdd:cd17595   81 AKRVLLTAYADTDAAIRAINDVQLDYyLLKP 111
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 7-121 1.26e-08

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 52.93  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTL----DIEGFQSraFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd17532    3 IVDDEPLAREELRYLLeehpDIEIVGE--AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491647096  83 HGDIstAVAAIRQGAYDFLEKPFSTDTLLDVLRRgVEKR 121
Cdd:cd17532   81 YDEY--AVEAFELNAVDYLLKPFSEERLAEALAK-LRKR 116
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 5-111 1.33e-08

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 52.67  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVdSELSIVMLTGHG 84
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI-SNVPIIFISSRD 79

                         90       100
                 ....*....|....*....|....*..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLL 106
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 5-57 1.45e-08

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 50.64  E-value: 1.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 491647096     5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMP 57
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 5-105 1.49e-08

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 52.13  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQ--KALAVDSELSIVMLTG 82
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRrlKADPATRHIPVIFLTA 80

                         90       100
                 ....*....|....*....|...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPF 105
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
PRK10360 PRK10360
transcriptional regulator UhpA;
5-115 1.52e-08

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 54.60  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIE-GFQSRA-FASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKalaVDSELSIVMLTG 82
Cdd:PRK10360   4 VALIDDHLIVRSGFAQLLGLEpDLQVVAeFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQ---LPKGMATIMLSV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:PRK10360  81 HDSPALVEQALNAGARGFLSKRCSPDELIAAVH 113
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
 1-116 1.61e-08

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 55.03  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096    1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSE---LSI 77
Cdd:TIGR02154   1 MTRRILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRR-LRRRPEtraIPI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 491647096   78 VMLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:TIGR02154  80 IMLTARGEEEDRVRGLETGADDYITKPFSPRELLarikAVLRR 122
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 5-115 1.65e-08

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 52.47  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTGHG 84
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQ-IRAESGVPIVMLTAKS 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKPFKPKELVARIR 112
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 5-116 1.68e-08

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 52.38  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTGHG 84
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCRE-VREHSHVPILMLTART 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPFSPRELLarvrALLRR 116
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 5-110 2.24e-08

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 52.17  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIE-GFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSE---LSIVML 80
Cdd:cd17552    4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKK-LQANPEtqsIPVILL 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTL 110
Cdd:cd17552   83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 5-116 2.58e-08

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 52.04  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVdSELSIVMLTGHG 84
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT-SNVPIIMLTAKD 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKPFSNRELLarvkANLRR 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 5-116 3.26e-08

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 51.56  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDS--ELSIVMLTG 82
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDlkDIPVILLTT 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKY 114
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 5-116 4.04e-08

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 51.38  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFAS-AIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGh 83
Cdd:cd17593    3 VLICDDSSMARKQLARALPADWDVEITFAEnGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG- 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  84 gDI-STAVAAIRQ-GAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17593   82 -DVqPEAKERVLElGALAFLKKPFDPEKLAQLLEE 115
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 5-104 4.25e-08

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 50.66  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGmTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSG-TEVCRQLRARSNVPVIMVTAKD 79

                         90       100
                 ....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKP 104
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 7-116 6.80e-08

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 50.71  E-value: 6.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLD-IEGFQSRAFASAI-DALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd19925    5 IVEDDPMVAEIHRAYVEqVPGFTVIGTAGTGeEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTAAN 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd19925   85 DVETVREALRLGVVDYLIKPFTFERLRQRLER 116
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
4-116 7.96e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 52.88  E-value: 7.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEgVIISDINMPQMDGMTFLqKALAVDSELSIVMLTGH 83
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSID-LLLLDVMMPKKNGIDTL-KELRQTHQTPVIMLTAR 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRR 116
Cdd:PRK10955  81 GSELDRVLGLELGADDYLPKPFNDRELVarirAILRR 117
PRK10643 PRK10643
two-component system response regulator PmrA;
5-128 1.65e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 51.96  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENR 128
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQGENE 126
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
7-105 2.60e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 52.46  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTL----DIE-------GFQsrafasAIDALDQLSnafEGVIISDINMPQMDGMTFLQKALAVdSEL 75
Cdd:PRK00742   8 VVDDSAFMRRLISEILnsdpDIEvvgtapdGLE------AREKIKKLN---PDVITLDVEMPVMDGLDALEKIMRL-RPT 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 491647096  76 SIVM---LTGHG-DIStaVAAIRQGAYDFLEKPF 105
Cdd:PRK00742  78 PVVMvssLTERGaEIT--LRALELGAVDFVTKPF 109
PRK10766 PRK10766
two-component system response regulator TorR;
1-111 3.13e-07

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 50.81  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTfLQKALAVDSELSIVML 80
Cdd:PRK10766   1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLM-LTRELRSRSTVGIILV 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:PRK10766  80 TGRTDSIDRIVGLEMGADDYVTKPLELRELL 110
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 5-116 5.31e-07

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 48.21  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTL-DIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:cd17530    3 VLVLDDDPFQCMMAATILeDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491647096  84 GDI---STAVAAIRQGAY--DFLEKPFSTDTLLDVLRR 116
Cdd:cd17530   83 DGGileSAETLAGANGLNllGTLSKPFSPEELTELLTK 120
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 4-106 6.67e-07

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 47.76  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTfLQKALAVDSELSIVMLTGH 83
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLT-LCREIRRFSDVPIIMVTAR 79

                         90       100
                 ....*....|....*....|...
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFS 106
Cdd:cd19938   80 VEEIDRLLGLELGADDYICKPYS 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 5-111 1.05e-06

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 47.40  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80

                         90       100
                 ....*....|....*....|....*..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDELV 107
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 5-115 1.11e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 49.42  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFqsRAFASAI--DALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTG 82
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGM--RVFEAETlqRGLLEAATRKPDLIILDLGLPDGDGIEFIRD-LRQWSAIPVIVLSA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:PRK10529  81 RSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
5-114 1.22e-06

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 50.74  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTghg 84
Cdd:PRK10841 804 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVT--- 880

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  85 diSTAVAAIRQ-----GAYDFLEKPFSTDTLLDVL 114
Cdd:PRK10841 881 --ANALAEEKQrcleaGMDSCLSKPVTLDVLKQTL 913
PRK13856 PRK13856
two-component response regulator VirG; Provisional
 5-129 1.35e-06

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 49.43  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLqKALAVDSELSIVMLTGHG 84
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIV-RSLATKSDVPIIIISGDR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491647096  85 -DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENRE 129
Cdd:PRK13856  83 lEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRTKD 128
PRK15479 PRK15479
transcriptional regulator TctD;
7-115 1.42e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 48.95  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDI 86
Cdd:PRK15479   5 LAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARSAV 84

                         90       100
                 ....*....|....*....|....*....
gi 491647096  87 STAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:PRK15479  85 ADRVKGLNVGADDYLPKPFELEELDARLR 113
PRK11517 PRK11517
DNA-binding response regulator HprR;
4-115 1.60e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 48.74  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQkALAVDSELSIVMLTGH 83
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQ-TLRTAKQTPVICLTAR 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVKPFSFSELLARVR 112
dpiA PRK10046
two-component response regulator DpiA; Provisional
 7-127 1.62e-06

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 48.86  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTL-DIEGFQSRAFASAIDALDQLSNAFE-GVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:PRK10046   9 IVEDETPLAEMHAEYIrHIPGFSQILLAGNLAQARMMIERFKpGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAAS 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMEN 127
Cdd:PRK10046  89 DMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESI 131
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 8-104 1.87e-06

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 46.21  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   8 IDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGM---TFLQKALAVdSELSIVMLTGHG 84
Cdd:cd17602    4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYelcSLLRKSSAL-KDTPIIMLTGKD 82

                         90       100
                 ....*....|....*....|
gi 491647096  85 DISTAVAAIRQGAYDFLEKP 104
Cdd:cd17602   83 GLVDRIRAKMAGASGYLTKP 102
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 5-116 3.60e-06

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 45.80  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSrAFASAIDALDQLSNAFE---GVIISDINMPQMDGMTFLQKALAVDSELSIVMLT 81
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDFT-VVGEASSGEEGIELAERldpDLILLDLNMKGMSGLDTLKALREEGVSARIVILT 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  82 GHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd19931   80 VSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 5-111 4.19e-06

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 45.50  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80

                         90       100
                 ....*....|....*....|....*..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVLV 107
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 5-111 4.78e-06

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 45.48  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFAS-AIDALDQLSNAFEGVIISDINMPQMDGMTfLQKALAVDSELSIVMLTGH 83
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVGEASdGEEAVELAKKHKPDLVIMDVKMPRLDGIE-AAKIITSENIAPIVLLTAY 81

                         90       100
                 ....*....|....*....|....*...
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLL 111
Cdd:cd19932   82 SQQDLVERAKEAGAMAYLVKPFSESDLI 109
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 5-104 5.60e-06

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 45.06  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSN-AFEG--------VIISDINMPQMDGMTFLQKaLAVDSEL 75
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlAKEGndlskeldLIITDIEMPKMDGYELTFE-LRDDPRL 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  76 SIVMLTGHGDISTAVAAIR---QGAYDFLEKP 104
Cdd:cd19924   80 ANIPVILNSSLSGEFSRARgkkVGADAYLAKF 111
PRK10336 PRK10336
two-component system response regulator QseB;
5-116 6.48e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 46.81  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491647096  85 DISTAVAAIRQGAYDFLEKPFStdtLLDVLRR 116
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPFA---LIEVAAR 111
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
5-130 7.66e-06

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 48.58  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096    5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 491647096   85 DISTAVAAIRQGAYDFLEKPFSTDTLLDVLRRGVEKRQLVMENREL 130
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHL 1086
MtrAB_MtrA NF040689
MtrAB system response regulator MtrA;
5-105 1.06e-05

MtrAB system response regulator MtrA;


Pssm-ID: 468653 [Multi-domain]  Cd Length: 219  Bit Score: 46.40  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDqlsnAFEGV----IISDINMPQMDGMTfLQKALAVDSELSIVML 80
Cdd:NF040689   1 ILVVDDDPALAEMLGIVLRAEGFETVFCADGAEAVE----AFREVrpdlVLLDLMLPGMDGIE-VCRQIRAESGVPIIML 75

                         90       100
                 ....*....|....*....|....*
gi 491647096  81 TGHGDISTAVAAIRQGAYDFLEKPF 105
Cdd:NF040689  76 TAKSDTVDVVRGLEAGADDYVVKPF 100
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 49-116 2.31e-05

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 43.56  E-value: 2.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647096  49 VIISDINMPQMDGMTFLqKALAVDSELS---IVMLT---GHGDIstaVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd17557   55 LILLDLNMPRMDGFEVL-REIKADPDLRripVVVLTtsdAEEDI---ERAYELGANSYIVKPVDFEEFVEAIRS 124
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 7-84 2.45e-05

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 43.73  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   7 IIDDERTIRDALSQTLD-IEGFQSRAFA-SAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAvDSELSIVMLTGHG 84
Cdd:COG2197    6 IVDDHPLVREGLRALLEaEPDIEVVGEAaDGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLLT-PREREVLRLLAEG 84
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 5-116 2.94e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 45.02  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLdiegfqsrAFASAIDALDQLSNAFEGV----------IISDINMPQMDGMTFLQKALAVDSE 74
Cdd:PRK10651   9 ILLIDDHPMLRTGVKQLI--------SMAPDITVVGEASNGEQGIelaesldpdlILLDLNMPGMNGLETLDKLREKSLS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491647096  75 LSIVMLTGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:PRK10651  81 GRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQ 122
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 4-117 3.23e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.92  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   4 EIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGH 83
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491647096  84 GDISTAVAAIRQGAYDFLEKPFSTDTLL----DVLRRG 117
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAELLarvrTLLRRG 119
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
389-425 4.61e-05

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 40.45  E-value: 4.61e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 491647096  389 VERAILFDALNRHNGMLKEVQAELGLARKTLYEKLKK 425
Cdd:pfam02954   4 VEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 5-116 6.17e-05

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 42.26  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEG-FQSRAFASA-IDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDdLEVVAQASNgQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 491647096  83 HGDISTAVAAIRQGAYDFLEKPFSTDTLLDVLRR 116
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114
pleD PRK09581
response regulator PleD; Reviewed
 1-158 1.44e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 44.12  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   1 MTPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTfLQKALAVDSELS---I 77
Cdd:PRK09581   1 MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFE-VCRRLKSDPATThipV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096  78 VMLTGHGDISTAVAAIRQGAYDFLEKPFStDTLL--------------DVLR-RGVEKRQLVMENRELKRQLETQSapGP 142
Cdd:PRK09581  80 VMVTALDDPEDRVRGLEAGADDFLTKPIN-DVALfarvksltrlkmviDELRlRASTNAEIGVTALMIMAYANKDE--DG 156

                        170
                 ....*....|....*....
gi 491647096 143 RIL---GNADAVKQLRRTL 158
Cdd:PRK09581 157 RILlvdDDVSQAERIANIL 175
PRK10693 PRK10693
two-component system response regulator RssB;
37-104 1.84e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 43.06  E-value: 1.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491647096  37 DALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDISTAVAAIRQGAYDFLEKP 104
Cdd:PRK10693   8 DALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
 5-110 1.91e-04

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.71  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFA-SAIDALDQLSNAFEGVIISDINM-PQMDGMTFL-----QKALAVDSelSI 77
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVTRIDTAsSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLeelrhKKLISPST--VF 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491647096  78 VMLTGHGDISTAVAAIRQGAYDFLEKPFSTDTL 110
Cdd:cd17589   79 IMVTGESSRAMVLSALELEPDDYLLKPFTVSEL 111
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 5-104 2.29e-04

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 40.33  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLD------IEGFQSrafaSAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIV 78
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEdddlgeVVGEAD----NGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFI 76

                         90       100
                 ....*....|....*....|....*.
gi 491647096  79 MLTGHGDISTAVAAIRQGAYDFLEKP 104
Cdd:cd17565   77 MISQVSDKEMIGKAYQAGIEFFINKP 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 35-104 3.62e-04

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 39.69  E-value: 3.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647096  35 AIDALDQLSNAFEgVIISDINMPQMDGMTFLQKALAVDS--ELSIVMLTGHGDISTAVAAIRQGAYDFLEKP 104
Cdd:cd17582   34 AWDVLEDEQNEID-LILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 37-105 4.19e-04

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 39.51  E-value: 4.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647096  37 DALDQLSNAFEGVIISDINMPQMDGMTFLQK--ALAVDSELSIVMLTGHGDISTAVAAIRQGAYDFLEKPF 105
Cdd:cd17561   38 EALELIEEKEPDVLLLDIIMPHLDGIGVLEKlrRMRLEKRPKIIMLTAFGQEDITQRAVELGASYYILKPF 108
FleQ pfam06490
Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of ...
 5-116 4.83e-04

Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of sigma54-dependent transcriptional activators that are involved in regulation of flagellar motility e.g. FleQ in Pseudomonas aeruginosa. It is clearly related to pfam00072, but lacks the conserved aspartate residue that undergoes phosphorylation in the classic two-component system response regulator (pfam00072).


Pssm-ID: 428975 [Multi-domain]  Cd Length: 108  Bit Score: 39.48  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096    5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMpqmDGMTFLQKALAVDSELSIVMLTGHG 84
Cdd:pfam06490   2 ILVIDDDAERRHDLSTILEFLGEQCEAISSEDLSAALWSSRWEALAVILGSV---SAAELLKALAKWDPHLPVLLLGETD 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 491647096   85 DISTAVAAIRQgaydfLEKPFSTDTLLDVLRR 116
Cdd:pfam06490  79 DALELANVIGT-----LEEPLNYPQLTDLLHR 105
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 5-114 5.93e-04

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 39.30  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEG--VIISDINMPQMDGMTF---LQKALAVDSELSIVM 79
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEValrIRKLFGRRERPLIVA 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  80 LTGHGDISTAVAAIRQGAYDFLEKPFSTDTLLDVL 114
Cdd:cd19933   83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
5-104 6.02e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 41.79  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTL----DIE-------GFQSRAFASAiDALDqlsnafegVIISDINMPQMDGMTFLQKALAvDS 73
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALardpDHEvvwvatdGAQAVERCAA-QPPD--------VILMDLEMPRMDGVEATRRIMA-ER 72

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491647096  74 ELSIVMLTghGDISTAVA----AIRQGAYDFLEKP 104
Cdd:PRK12555  73 PCPILIVT--SLTERNASrvfeAMGAGALDAVDTP 105
PRK11173 PRK11173
two-component response regulator; Provisional
 2-105 8.95e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 40.77  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   2 TPEIWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMtFLQKALAVDSELSIVMLT 81
Cdd:PRK11173   3 TPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGL-LLARELREQANVALMFLT 81

                         90       100
                 ....*....|....*....|....
gi 491647096  82 GHGDISTAVAAIRQGAYDFLEKPF 105
Cdd:PRK11173  82 GRDNEVDKILGLEIGADDYITKPF 105
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 5-105 9.36e-04

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 38.48  E-value: 9.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   5 IWIIDDERTIRDALSQTLDIEGFQSRAFASAIDALDQL-SNAFEGVIISDINMP-QMDGMTFLQKALAVDSELSIVMLTG 82
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLeSGPDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80

                         90       100
                 ....*....|....*....|....
gi 491647096  83 HGDisTAVAAIRQGA-YDFLEKPF 105
Cdd:cd18161   81 YAE--NAIEGGDLAPgVDVLSKPF 102
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
38-103 1.31e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.86  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647096  38 ALDQLSNAFEGVIISDINMPQMDGMTFLQKALAVDSELSIVMLTGHGDISTAVAAIRQGAYDFLEK 103
Cdd:PRK09935  41 TIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSK 106
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 168-357 3.86e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 39.71  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 168 VLFQGERGTGKEMAARFLH----DQGSRQDE-PFVAIKCRRI---PEALIAmELFGSEQHAY--AslpsYKNSK--IAAA 235
Cdd:COG1221  133 TLILGPTGVGKSFFAELMYeyaiEIGVLPEDaPFVVFNCADYannPQLLMS-QLFGYVKGAFtgA----DKDKEglIEKA 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096 236 GKGTLFIDGIEALPPAVQEKLATLI--GTENRpriIASTRVDLAASVRLgrfDCAlyqalsgTT------LL--F----- 300
Cdd:COG1221  208 DGGILFLDEVHRLPPEGQEMLFTFMdkGIYRR---LGETEKTRKANVRI---IFA-------TTedpessLLktFlrrip 274

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647096 301 -----PPLRERD-DDVITLCQNFVRTTASRFG----VAPPVMNRdhkerLLQHPWKGNIREL---------RAYAE 357
Cdd:COG1221  275 mviklPSLEERSlEERLELIKHFFKEEAKRLNkpikVSKEVLKA-----LLLYDCPGNIGQLksdiqlacaKAFLN 345
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 9-115 5.50e-03

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 36.59  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647096   9 DDERTIRdALSQTLDIEGFQSRAFASAIDALDQLSNAFEGVIISDINMPQMDGMTFLQKaLAVDSELSIVMLTGHGDIST 88
Cdd:cd17622    8 DDPKLAR-LIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRD-LRPKYQGPILLLTALDSDID 85

                         90       100
                 ....*....|....*....|....*..
gi 491647096  89 AVAAIRQGAYDFLEKPFSTDTLLDVLR 115
Cdd:cd17622   86 HILGLELGADDYVVKPVEPAVLLARLR 112
 
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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