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Conserved domains on  [gi|657198221|ref|WP_029313876|]
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MULTISPECIES: sigma-54 dependent transcriptional regulator [Aeromonas]

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

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, ...
4-457 0e+00

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: 532.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   4 SKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSlvaqyrenfERSSFAGFIGASMAMQAVYRIIESAA 163
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR---------ENAEDSGLIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 164 PSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFL 243
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 244 DEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDI 323
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 324 LLLARELLLRYAGEENKRFRdFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPpplnggrtlapepavg 403
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP---------------- 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 657198221 404 iadpqsepvvvrrqvRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:COG2204  375 ---------------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRK 413
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
4-457 0e+00

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: 532.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   4 SKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSlvaqyrenfERSSFAGFIGASMAMQAVYRIIESAA 163
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR---------ENAEDSGLIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 164 PSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFL 243
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 244 DEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDI 323
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 324 LLLARELLLRYAGEENKRFRdFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPpplnggrtlapepavg 403
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP---------------- 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 657198221 404 iadpqsepvvvrrqvRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:COG2204  375 ---------------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRK 413
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
7-461 1.66e-127

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 377.65  E-value: 1.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQL-SSLVAQYRENFERSSFAGFIGASMAMQAVYRIIESAAPS 165
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMkKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 166 KATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDE 245
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 246 ICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILL 325
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 326 LARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNggrtlapEPAVGIA 405
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIR-------QPVCNAG 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 657198221 406 DPQSEPVVVRRQVRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRKKQSW 461
Cdd:PRK11361 399 EVKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEY 454
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
8-455 4.11e-127

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: 376.40  E-value: 4.11e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221    8 VLLVEDtrSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPD-----MSGMDILQQITERQLPCSVVV 82
Cdd:TIGR02915   1 LLIVED--DLGLQKQLKWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPPdadgaSEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLVAQYRENFERSSFAGFIGASMAMQAVYRIIESA 162
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRGLITSSPGMQKICRTIEKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  163 APSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLF 242
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  243 LDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGED 322
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  323 ILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILppplngGRTLAPepav 402
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDL------GLDARE---- 388
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657198221  403 giaDPQSEPVVVRRQVRPlwQVEKEAIEQAIASCDGNIPKAAALLEISPSTIY 455
Cdd:TIGR02915 389 ---RAETPLEVNLREVRE--RAEREAVRKAIARVDGNIARAAELLGITRPTLY 436
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-311 2.54e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 302.40  E-value: 2.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  145 FIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  225 AQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 657198221  305 RLHVIPL 311
Cdd:pfam00158 161 RLNVIPI 167
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
6-456 1.30e-99

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 308.34  E-value: 1.30e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDtRSLAVVYEQYLAQDGYE---VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQqiTERQLPCSV-- 80
Cdd:NF038308  28 PTVALCQQ-PDLPVDRLELLHDRRDRalaERVAADIEEVSPETEVRLVPVVLRDPWDFEEVYGALLD--FARAYPFDTen 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  81 ----VVIT-----AHGSVDVAVEAMRFGAfDFLTKPFDGKRLCATARN---AL-KHQQLSSlvAQYRENFERSSF--AGF 145
Cdd:NF038308 105 edylVHITtgthvAQICWFLLVEARYLPA-RLLQTSPPRDKEEGTYEIidlDLsRYDALAQ--RFAREQAEAVSFlkSGI 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 146 IGASMAMQAVYRIIESAAP-SKATVFITGESGTGKEVCAEAIHQCSPRRDQ---PFIALNCAAIPHDLMESEIFGHVKGS 221
Cdd:NF038308 182 ATRNAAFNRLIEQIERVALrSRAPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRGDLAMSELFGHVKGA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 222 FTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFRED 301
Cdd:NF038308 262 FTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFRED 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 302 LYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRFR-----DFDADAVQVLLDYPWPGNVRELQNVVRNIVVLN 376
Cdd:NF038308 342 LYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVRfnkeaRFRYLAFATSPEALWPGNFRELSASVTRMATLA 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 377 DGELVSPDILPPPLNGGRTLAPEPAVGIADPQSEPVVVRRQVR---PLWQVEKEAIEQAIASCDGNIPKAAALLEISPST 453
Cdd:NF038308 422 DGGRITEELVEEEIARLRAAWQSAPAAADDDALADLLGGEQLAeldLFDRVQLAAVLRVCRQSRSLSAAGRRLFGVSRQQ 501

                 ...
gi 657198221 454 IYR 456
Cdd:NF038308 502 KAS 504
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
140-457 1.49e-96

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 302.20  E-value: 1.49e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 140 SSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDqPFIALNCAAIPHDLMESEIFGHVK 219
Cdd:NF041552 264 DSFGKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKG-PFVPVNCSAIPEELFESEFFGYEE 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 220 GSFTGAqgDRKGAA---SLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDpLVE-VKA 295
Cdd:NF041552 343 GAFTGA--LKKGKIgkfELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKD-LKKmVKE 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 296 GRFREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVL 375
Cdd:NF041552 420 GKFREDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVL 499
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 376 NDGELVSPDILPPPL--NGGRTLAPEpavgiadpQSEPVVVRRQVRplwQVEKEAIEQAIASCDGNIPKAAALLEISPST 453
Cdd:NF041552 500 SKNGTITKDSIPEYIleSVKKKEDEE--------GDYPLDLNKAVE---KLEIDTIKKALEMSNGNKAKAAKLLNIPRST 568

                 ....
gi 657198221 454 IYRK 457
Cdd:NF041552 569 LYYK 572
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
8-128 1.39e-70

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: 219.38  E-value: 1.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSS 128
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
6-60 2.61e-12

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: 61.43  E-value: 2.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 657198221     6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
4-457 0e+00

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: 532.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   4 SKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSlvaqyrenfERSSFAGFIGASMAMQAVYRIIESAA 163
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR---------ENAEDSGLIGRSPAMQEVRRLIEKVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 164 PSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFL 243
Cdd:COG2204  152 PSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 244 DEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDI 323
Cdd:COG2204  232 DEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDI 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 324 LLLARELLLRYAGEENKRFRdFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPpplnggrtlapepavg 403
Cdd:COG2204  312 PLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP---------------- 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 657198221 404 iadpqsepvvvrrqvRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:COG2204  375 ---------------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRK 413
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
72-457 8.50e-151

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: 436.51  E-value: 8.50e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  72 TERQLPCSVVVITAHGSVDVAVEAMRfgafdfltkpfDGKRLCATARNALKHQQLSSLVAQYrenfersSFAGFIGASMA 151
Cdd:COG3829   85 KGKTVIVTAIPIFEDGEVIGAVETFR-----------DITELKRLERKLREEELERGLSAKY-------TFDDIIGKSPA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 152 MQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGA-QGDRK 230
Cdd:COG3829  147 MKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFTGAkKGGKP 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 231 GAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIP 310
Cdd:COG3829  227 GLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIP 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 311 LALPPLRERGEDILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPL 390
Cdd:COG3829  307 IHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYL 386
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198221 391 nggrtLAPEPAVGIADPQSEPVVVRrqvrplwQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:COG3829  387 -----LEEAEAASAAEEGSLKEALE-------EVEKELIEEALEKTGGNKSKAAKALGISRSTLYRK 441
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
7-461 1.66e-127

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 377.65  E-value: 1.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQL-SSLVAQYRENFERSSFAGFIGASMAMQAVYRIIESAAPS 165
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMkKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 166 KATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDE 245
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 246 ICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILL 325
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 326 LARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNggrtlapEPAVGIA 405
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIR-------QPVCNAG 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 657198221 406 DPQSEPVVVRRQVRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRKKQSW 461
Cdd:PRK11361 399 EVKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEY 454
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
8-455 4.11e-127

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: 376.40  E-value: 4.11e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221    8 VLLVEDtrSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPD-----MSGMDILQQITERQLPCSVVV 82
Cdd:TIGR02915   1 LLIVED--DLGLQKQLKWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPPdadgaSEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLVAQYRENFERSSFAGFIGASMAMQAVYRIIESA 162
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRGLITSSPGMQKICRTIEKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  163 APSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLF 242
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  243 LDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGED 322
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  323 ILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILppplngGRTLAPepav 402
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDL------GLDARE---- 388
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657198221  403 giaDPQSEPVVVRRQVRPlwQVEKEAIEQAIASCDGNIPKAAALLEISPSTIY 455
Cdd:TIGR02915 389 ---RAETPLEVNLREVRE--RAEREAVRKAIARVDGNIARAAELLGITRPTLY 436
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-457 6.04e-123

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 366.37  E-value: 6.04e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221    8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER--QLPcsVVVITA 85
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRhpQLP--VIVMTA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQlsSLVAQYRENFERSSFAGFIGASMAMQAVYRIIESAAPS 165
Cdd:TIGR01818  79 HSDLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ--EQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  166 KATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDE 245
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  246 ICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILL 325
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  326 LARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNGGRTLAPEPAVGIA 405
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQ 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198221  406 DPQSEPV--VVRRQV---------RPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:TIGR01818 397 DSWDEALeaWAKQALsrgeqglldRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRK 459
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-457 7.49e-119

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 355.11  E-value: 7.49e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSV 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  81 VVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLvaqyRENFERSSFAGFIGASMAMQAVYRIIE 160
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDA----ETPAVTASQFGMVGKSPAMQHLLSEIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 161 SAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGT 240
Cdd:PRK10365 157 LVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 241 LFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERG 320
Cdd:PRK10365 237 LFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 321 EDILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNGgrtlAPEP 400
Cdd:PRK10365 317 EDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIAS----TPIP 392
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 657198221 401 AVGIADpqsepvvvrrqVRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:PRK10365 393 LGQSQD-----------IQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAK 438
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
109-457 3.65e-115

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 351.51  E-value: 3.65e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 109 DGKRLCATARNALKHQQLSSLVAQYREnfeRSSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQ 188
Cdd:COG3284  290 DGRRLGALLRLRPARRAARAAPAGAPA---PAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 189 CSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQ-GDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQ 267
Cdd:COG3284  367 ASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARrKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVT 446
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 268 RVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERgEDILLLARELLLRYAGEEnkRFRDFDA 347
Cdd:COG3284  447 PLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAGR--GPLRLSP 523
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 348 DAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLnggrtlapepavgIADPQSEPVVVRRQVRPLWQVEKE 427
Cdd:COG3284  524 EALALLAAYPWPGNVRELRNVLRTALALADGGVITVEDLPDEL-------------RAELAAAAPAAAAPLTSLEEAERD 590
                        330       340       350
                 ....*....|....*....|....*....|
gi 657198221 428 AIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:COG3284  591 AILRALRACGGNVSAAARALGISRSTLYRK 620
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
8-457 9.34e-106

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 322.59  E-value: 9.34e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSlvaQYRENFERSSFAGFIGASMAMQAVYRIIESAAPSKA 167
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQ---QPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSSI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 168 TVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDEIC 247
Cdd:PRK10923 163 SVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 248 EMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILLLA 327
Cdd:PRK10923 243 DMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 328 RELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNGgrTLAPEPAVGIAdP 407
Cdd:PRK10923 323 RHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFE--STVPESTSQMQ-P 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198221 408 QSEPVVV----RRQVR---------PLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:PRK10923 400 DSWATLLaqwaDRALRsghqnllseAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRK 462
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
115-456 1.27e-102

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 315.57  E-value: 1.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 115 ATARNALKHQQL--SSLVAQYRENFERSSFAG---FIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQC 189
Cdd:PRK05022 154 ATLRNALLIEQLesQAELPQDVAEFLRQEALKegeMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAA 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 190 SPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRV 269
Cdd:PRK05022 234 SPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRV 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 270 GSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILLLarelllryAG---EENKR----- 341
Cdd:PRK05022 314 GSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLL--------AGyflEQNRArlglr 385
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 342 -FRdFDADAVQVLLDYPWPGNVRELQNVVRNIVVL-----NDGELV-SPDILPPPLNggrTLAPEPAVGIADPQSEPVVV 414
Cdd:PRK05022 386 sLR-LSPAAQAALLAYDWPGNVRELEHVISRAALLarargAGRIVTlEAQHLDLPAE---VALPPPEAAAAPAAVVSQNL 461
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 657198221 415 RRQVRplwQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYR 456
Cdd:PRK05022 462 REATE---AFQRQLIRQALAQHQGNWAAAARALELDRANLHR 500
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-311 2.54e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 302.40  E-value: 2.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  145 FIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  225 AQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 657198221  305 RLHVIPL 311
Cdd:pfam00158 161 RLNVIPI 167
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
6-456 1.30e-99

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 308.34  E-value: 1.30e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDtRSLAVVYEQYLAQDGYE---VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQqiTERQLPCSV-- 80
Cdd:NF038308  28 PTVALCQQ-PDLPVDRLELLHDRRDRalaERVAADIEEVSPETEVRLVPVVLRDPWDFEEVYGALLD--FARAYPFDTen 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  81 ----VVIT-----AHGSVDVAVEAMRFGAfDFLTKPFDGKRLCATARN---AL-KHQQLSSlvAQYRENFERSSF--AGF 145
Cdd:NF038308 105 edylVHITtgthvAQICWFLLVEARYLPA-RLLQTSPPRDKEEGTYEIidlDLsRYDALAQ--RFAREQAEAVSFlkSGI 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 146 IGASMAMQAVYRIIESAAP-SKATVFITGESGTGKEVCAEAIHQCSPRRDQ---PFIALNCAAIPHDLMESEIFGHVKGS 221
Cdd:NF038308 182 ATRNAAFNRLIEQIERVALrSRAPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRGDLAMSELFGHVKGA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 222 FTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFRED 301
Cdd:NF038308 262 FTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFRED 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 302 LYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRFR-----DFDADAVQVLLDYPWPGNVRELQNVVRNIVVLN 376
Cdd:NF038308 342 LYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVRfnkeaRFRYLAFATSPEALWPGNFRELSASVTRMATLA 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 377 DGELVSPDILPPPLNGGRTLAPEPAVGIADPQSEPVVVRRQVR---PLWQVEKEAIEQAIASCDGNIPKAAALLEISPST 453
Cdd:NF038308 422 DGGRITEELVEEEIARLRAAWQSAPAAADDDALADLLGGEQLAeldLFDRVQLAAVLRVCRQSRSLSAAGRRLFGVSRQQ 501

                 ...
gi 657198221 454 IYR 456
Cdd:NF038308 502 KAS 504
PRK15115 PRK15115
response regulator GlrR; Provisional
1-398 1.55e-97

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 300.60  E-value: 1.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSV 80
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  81 VVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSlVAQYRENFerssfagfIGASMAMQavyRIIE 160
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPAT-DERWREAI--------VTRSPLML---RLLE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 161 SA---APSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLAN 237
Cdd:PRK15115 149 QArmvAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 238 GGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLR 317
Cdd:PRK15115 229 GGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 318 ERGEDILLLARELLLRyAGEENKRF-RDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNGGRTL 396
Cdd:PRK15115 309 ERTEDIPLLANHLLRQ-AAERHKPFvRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTA 387

                 ..
gi 657198221 397 AP 398
Cdd:PRK15115 388 LP 389
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
140-457 1.49e-96

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 302.20  E-value: 1.49e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 140 SSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDqPFIALNCAAIPHDLMESEIFGHVK 219
Cdd:NF041552 264 DSFGKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKG-PFVPVNCSAIPEELFESEFFGYEE 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 220 GSFTGAqgDRKGAA---SLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDpLVE-VKA 295
Cdd:NF041552 343 GAFTGA--LKKGKIgkfELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKD-LKKmVKE 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 296 GRFREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVL 375
Cdd:NF041552 420 GKFREDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIPKIDKEVYDILQNYKWKGNIRELKNTIEHLVVL 499
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 376 NDGELVSPDILPPPL--NGGRTLAPEpavgiadpQSEPVVVRRQVRplwQVEKEAIEQAIASCDGNIPKAAALLEISPST 453
Cdd:NF041552 500 SKNGTITKDSIPEYIleSVKKKEDEE--------GDYPLDLNKAVE---KLEIDTIKKALEMSNGNKAKAAKLLNIPRST 568

                 ....
gi 657198221 454 IYRK 457
Cdd:NF041552 569 LYYK 572
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
144-456 5.89e-96

Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein for nitrogen fixation. The model produces scores between the trusted and noise cutoffs for a well-described NifA homolog in Aquifex aeolicus (which lacks nitrogenase), for transcriptional activators of alternative nitrogenases (VFe or FeFe instead of MoFe), and truncated forms. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, DNA interactions]


Pssm-ID: 273817 [Multi-domain]  Cd Length: 534  Bit Score: 299.32  E-value: 5.89e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  144 GFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFT 223
Cdd:TIGR01817 197 GIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFT 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  224 GAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLY 303
Cdd:TIGR01817 277 GAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLY 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  304 YRLHVIPLALPPLRERGEDILLLARELLLRYaGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSP 383
Cdd:TIGR01817 357 YRINVVPIFLPPLRERREDIPLLAEAFLEKF-NRENGRPLTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITR 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  384 DI--------LPPPLNGGRTLAPEPAVGIAD--PQSEPVVVRRQVRPLW----QVEKEAIEQAIASCDGNIPKAAALLEI 449
Cdd:TIGR01817 436 SDfscqsgqcLSPMLAKTCPHGHISIDPLAGttPPHSPASAALPGEPGLsgptLSERERLIAALEQAGWVQAKAARLLGM 515

                  ....*...
gi 657198221  450 SPSTI-YR 456
Cdd:TIGR01817 516 TPRQVgYA 523
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
109-384 2.97e-89

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 281.31  E-value: 2.97e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 109 DGKRLCATARNALK-----HQQLSSLvaqyrENFERSSFAGFIGASMAMQAVyriIESA---APSKATVFITGESGTGKE 180
Cdd:COG3283  170 EGKSILAGAVVTLKsaarlGEQLQAL-----QVNDDSGFDHIVASSPKMRQV---IRQAkkmAMLDAPLLIQGETGTGKE 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 181 VCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRF 260
Cdd:COG3283  242 LLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRF 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 261 IQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENK 340
Cdd:COG3283  322 LQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGR 401
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 657198221 341 RFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPD 384
Cdd:COG3283  402 PRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDELTPE 445
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
146-450 1.17e-77

psp operon transcriptional activator PspF; Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]


Pssm-ID: 274371 [Multi-domain]  Cd Length: 329  Bit Score: 245.28  E-value: 1.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  146 IGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGA 225
Cdd:TIGR02974   2 IGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  226 QGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYR 305
Cdd:TIGR02974  82 QKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  306 LHVIPLALPPLRERGEDILLLARELLLRYAGE-ENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGE----- 379
Cdd:TIGR02974 162 LAFDVITLPPLRERQEDIMLLAEHFAIRMARElGLPLFPGFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEeapid 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  380 ------LVSPDILPPPlnggRTLAPEPAVGIADPQSEPVVVRRQVRPL--WQ--VEKEAIEQAIASCDGNIPKAAALLEI 449
Cdd:TIGR02974 242 eiiidpFASPWRPKQA----APAVDEVNSTPTDLPSPSSIAAAFPLDLkqAQqdYEIELLQQALAEAQFNQRKAAELLGL 317

                  .
gi 657198221  450 S 450
Cdd:TIGR02974 318 T 318
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
81-460 5.74e-77

propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists for the catabolism of propionate by way of propionyl-CoA. Members of this family represent the transcriptional regulatory protein PrpR, whose gene is found in most cases divergently transcribed from an operon for the methylcitric acid cycle of propionate catabolism. 2-methylcitric acid, a catabolite by this pathway, is a coactivator of PrpR. [Regulatory functions, DNA interactions]


Pssm-ID: 274079 [Multi-domain]  Cd Length: 526  Bit Score: 249.78  E-value: 5.74e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   81 VVITAHGSVDVAVEAMRFGAF----DFLTKPFDGKRLCATARNAlkhQQLSSLVAQYRENFE-RSSFAGFIGASMAMQAV 155
Cdd:TIGR02329 148 AVVGAGLITDLAEQAGLHGVFlysaDSVRQAFDDALDVARATRL---RQAATLRSATRNQLRtRYRLDDLLGASAPMEQV 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  156 YRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGA-QGDRKGAAS 234
Cdd:TIGR02329 225 RALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTGArRGGRTGLIE 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  235 LANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALP 314
Cdd:TIGR02329 305 AAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALP 384
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  315 PLRERGEDILLLARELLLRYAGEENKRF----RDFDADAVQVLLDYPWPGNVRELQNVVRNIVV---LNDGELVSPDILp 387
Cdd:TIGR02329 385 PLRERPGDILPLAAEYLVQAAAALRLPDseaaAQVLAGVADPLQRYPWPGNVRELRNLVERLALelsAMPAGALTPDVL- 463
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198221  388 pplnggRTLAPEPAVGIADPQSEPVVVRRQVRplwqVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRKKQS 460
Cdd:TIGR02329 464 ------RALAPELAEASGKGKTSALSLRERSR----VEALAVRAALERFGGDRDAAAKALGISRTTLWRRLKA 526
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
111-421 1.10e-73

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 245.13  E-value: 1.10e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 111 KRLCATARNALKHQQLSSLVAQY-RENFE--------RSSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEV 181
Cdd:PRK15429 335 ERVAIAVDNALAYQEIHRLKERLvDENLAlteqlnnvDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKEL 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 182 CAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFI 261
Cdd:PRK15429 415 IARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVL 494
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 262 QTGTLQRVGSGKLETVDVRFVCATNRDpLVEVKAGR-FREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENK 340
Cdd:PRK15429 495 QEQEFERLGSNKIIQTDVRLIAATNRD-LKKMVADReFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGR 573
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 341 RFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDG---ELVSPDILPPPlnggrtlAPEPAVGIADPQSEPVVVRRQ 417
Cdd:PRK15429 574 NIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGnvlQLSLPDITLPE-------PETPPAATVVAQEGEDEYQLI 646

                 ....
gi 657198221 418 VRPL 421
Cdd:PRK15429 647 VRVL 650
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
167-457 1.24e-73

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: 235.13  E-value: 1.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 167 ATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESeifghvkgsftgaqgdrkgaaslanggtlfldei 246
Cdd:COG3604  116 AAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES---------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 247 cemdldlqskllrfIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILLL 326
Cdd:COG3604  162 --------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLL 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 327 ARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNVRELQNVVRNIVVLNDGELVSPDILPPPlnggrtlapepavgiad 406
Cdd:COG3604  228 AEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPG----------------- 290
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 657198221 407 pqsepvvvrrQVRPLWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:COG3604  291 ----------SREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSR 331
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
139-465 3.49e-71

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 235.00  E-value: 3.49e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 139 RSSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSP--------RRDQPFIALNCAAIPHDLM 210
Cdd:PRK15424 215 RYVLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHREYFarhdarqgKKSHPFVAVNCGAIAESLL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 211 ESEIFGHVKGSFTGAQ-GDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDP 289
Cdd:PRK15424 295 EAELFGYEEGAFTGSRrGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDL 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 290 LVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRfrdFDADAVQ-------VLLDYPWPGNV 362
Cdd:PRK15424 375 EEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAP---FSAALRQglqqcetLLLHYDWPGNV 451
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 363 RELQNVVRNIVVLNDGE---LVSPDILppplnggRTLAPEPAVGIADPQSEPvvvrrqvrplwqVEKEAIEQAIASCDGN 439
Cdd:PRK15424 452 RELRNLMERLALFLSVEptpDLTPQFL-------QLLLPELARESAKTPAPR------------LLAATLQQALERFNGD 512
                        330       340
                 ....*....|....*....|....*.
gi 657198221 440 IPKAAALLEISPSTIYRKKQSWEEAS 465
Cdd:PRK15424 513 KTAAANYLGISRTTLWRRLKAEAKAQ 538
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
8-128 1.39e-70

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: 219.38  E-value: 1.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSS 128
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
PRK10820 PRK10820
transcriptional regulator TyrR;
124-388 2.20e-70

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 232.27  E-value: 2.20e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 124 QQLSSLVAQyrenfERSSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCA 203
Cdd:PRK10820 190 RQLQNLAVN-----DDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCA 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 204 AIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVC 283
Cdd:PRK10820 265 SIPDDVVESELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVIC 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 284 ATNRDpLVE-VKAGRFREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRFRDFDADAVQVLLDYPWPGNV 362
Cdd:PRK10820 345 ATQKN-LVElVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNV 423
                        250       260
                 ....*....|....*....|....*..
gi 657198221 363 RELQNVV-RNIVVLNDGELVSPDILPP 388
Cdd:PRK10820 424 RQLKNAIyRALTQLEGYELRPQDILLP 450
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
163-447 2.61e-68

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 221.08  E-value: 2.61e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 163 APSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDRKGAASLANGGTLF 242
Cdd:PRK11608  26 APLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 243 LDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGED 322
Cdd:PRK11608 106 LDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQLPPLRERQSD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 323 ILLLARELLLRYAGEEN-KRFRDFDADAVQVLLDYPWPGNVRELQNVV-RNIVVLNDGELVSPDILpppLNGGRTLAPEP 400
Cdd:PRK11608 186 IMLMAEHFAIQMCRELGlPLFPGFTERARETLLNYRWPGNIRELKNVVeRSVYRHGTSEYPLDNII---IDPFKRRPAEE 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 657198221 401 AVGIADPQSEPVVvrrqvrPL----WQV--EKEAIEQAIASCDGNIPKAAALL 447
Cdd:PRK11608 263 AIAVSETTSLPTL------PLdlreWQHqqEKELLQRSLQQAKFNQKRAAELL 309
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
120-457 3.82e-66

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 223.79  E-value: 3.82e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 120 ALKHQQLSSLvaqyrenfeRSSFAGFIGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIA 199
Cdd:PRK11388 311 QLMTSQLGKV---------SHTFDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIA 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 200 LNCAAIPHDLMESEIFGhvkgsfTGAQGDRKGAAS---LANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLET 276
Cdd:PRK11388 382 VNCQLYPDEALAEEFLG------SDRTDSENGRLSkfeLAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIP 455
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 277 VDVRFVCATNRDPLVEVKAGRFREDLYYRLHVIPLALPPLRERGEDILLLARELLLRYAGEENKRFRdFDADAVQVLLDY 356
Cdd:PRK11388 456 VDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLK-IDDDALARLVSY 534
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 357 PWPGNVRELQNVVRNIVVLNDGELVSPDILPPPLNGGRtlapePAVGIADPQSEPVVVrrqvrpLWQVEKEAIEQAIASC 436
Cdd:PRK11388 535 RWPGNDFELRSVIENLALSSDNGRIRLSDLPEHLFTEQ-----ATDDVSATRLSTSLS------LAELEKEAIINAAQVC 603
                        330       340
                 ....*....|....*....|.
gi 657198221 437 DGNIPKAAALLEISPSTIYRK 457
Cdd:PRK11388 604 GGRIQEMAALLGIGRTTLWRK 624
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
157-385 4.42e-44

Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 162.31  E-value: 4.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 157 RIIES----AAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQ---PFIALNCAAIPHDLMESEIFGHVKGSFTGAQGDR 229
Cdd:COG4650  195 RLIEQiervAIRSRAPILLTGPTGAGKSQLARRIYELKKARHQvsgRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDR 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 230 KGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVGSGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYRLHVI 309
Cdd:COG4650  275 AGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLW 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 310 PLALPPLRERGEDILLLARELLLRYAGEENKRFRdFDADAVQVLLDY------PWPGNVRELQNVVRNIVVLNDGELVSP 383
Cdd:COG4650  355 TFRLPGLAERREDIEPNLDYELARFAREQGRRVR-FNKEARARYLAFatspeaLWSGNFRDLNASVTRMATLAEGGRITV 433

                 ..
gi 657198221 384 DI 385
Cdd:COG4650  434 AL 435
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
8-126 2.03e-34

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: 125.29  E-value: 2.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER--QLPcsVVVITA 85
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELdpDLP--VILITG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQL 126
Cdd:cd17549   79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRL 119
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
135-372 7.38e-34

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: 135.24  E-value: 7.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 135 ENFERSSFAGFIGA--SMAMQavyriIESAapsKATVF---------ITGESGTGKEVCAEAIHQ--CSPRR---DQPFI 198
Cdd:COG1221   96 NEEEEDPFDNLIGAngSLKNA-----IEQA---KAAILyppkglhtlILGPTGVGKSFFAELMYEyaIEIGVlpeDAPFV 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 199 ALNCAaiphD-------LMeSEIFGHVKGSFTGAQGDRKGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVG- 270
Cdd:COG1221  168 VFNCA----DyannpqlLM-SQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGe 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 271 SGKLETVDVRFVCATNRDP---LVEVkagrF--RedlyyrlhvIPL--ALPPLRERGED-----IlllarellLRYAGEE 338
Cdd:COG1221  243 TEKTRKANVRIIFATTEDPessLLKT----FlrR---------IPMviKLPSLEERSLEerlelI--------KHFFKEE 301
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 657198221 339 NKRF-RDF--DADAVQVLLDYPWPGNVRELQNVVRNI 372
Cdd:COG1221  302 AKRLnKPIkvSKEVLKALLLYDCPGNIGQLKSDIQLA 338
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
5-129 1.22e-31

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: 120.06  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   5 KPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 657198221  85 AHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSL 129
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVL 125
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
2-147 2.75e-30

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: 117.19  E-value: 2.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   2 AESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQLP---- 77
Cdd:COG3437    3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLL--RADPstrd 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  78 CSVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLVAQYRENFERSSFAGFIG 147
Cdd:COG3437   81 IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHDIG 150
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
8-118 3.77e-30

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: 113.02  E-value: 3.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221    8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 657198221   88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATAR 118
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
9-107 5.03e-30

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: 112.32  E-value: 5.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   9 LLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGS 88
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 657198221  89 VDVAVEAMRFGAFDFLTKP 107
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
8-122 1.56e-29

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: 111.43  E-value: 1.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
8-139 7.57e-29

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: 112.12  E-value: 7.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVED----TRSLAVVyeqyLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:COG4566    2 VYIVDDdeavRDSLAFL----LESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFL 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL-KHQQLSSLVAQYRENFER 139
Cdd:COG4566   78 TGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALaRDRARRAERARRAELRAR 134
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
5-115 1.62e-28

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: 110.77  E-value: 1.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   5 KPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQLPCS----V 80
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRL--RADPRTadipI 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 657198221  81 VVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:COG3706   79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLA 113
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
4-126 2.00e-28

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 109.29  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   4 SKPRVLLVEDTRSLAVVYEQYLAQ-DGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVV 81
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERlPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 657198221  82 VITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQL 126
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRL 126
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
146-316 8.83e-28

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 107.43  E-value: 8.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  146 IGASMAMQAVYRIIESAAPSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESeifghvkgsftga 225
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  226 qgdrkgaaslANGGTLFLDEICEMDLDLQSKLLRFIqtgtlqrvgsGKLETVDVRFVCATNRDPLVEVKAGRFREDLYYR 305
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLL----------AKAEGYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 657198221  306 LHVIPLALPPL 316
Cdd:pfam14532 128 LSALRLHVPPL 138
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-125 9.81e-28

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: 106.86  E-value: 9.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQL 76
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAlprlPDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 657198221  77 PcsVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQ 125
Cdd:COG0784   81 P--IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
3-109 6.60e-26

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: 103.46  E-value: 6.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   3 ESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVV 82
Cdd:COG4567    2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVV 81
                         90       100
                 ....*....|....*....|....*..
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFD 109
Cdd:COG4567   82 LTGYASIATAVEAIKLGADDYLAKPAD 108
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
6-109 3.04e-25

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: 99.65  E-value: 3.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITA 85
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                         90       100
                 ....*....|....*....|....
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFD 109
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFD 104
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
8-121 3.30e-25

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: 99.59  E-value: 3.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVED----TRSLAVVyeqyLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:cd17537    3 VYVVDDdeavRDSLAFL----LRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFI 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd17537   79 TGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
6-116 4.56e-24

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: 96.36  E-value: 4.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITA 85
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCAT 116
Cdd:cd17563   81 YASIATAVEAIKLGADDYLAKPADADEILAA 111
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
152-309 9.69e-24

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: 96.83  E-value: 9.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 152 MQAVYRIIESAA--PSKATVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMESEIFGHVkgsftgAQGDR 229
Cdd:cd00009    3 QEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221 230 KGAASLANGGTLFLDEICEMDLDLQSKLLRFIQTGTLQRVgsgklETVDVRFVCATNRDPLvevkaGRFREDLYYRLHVI 309
Cdd:cd00009   77 FELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPLL-----GDLDRALYDRLDIR 146
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
7-137 4.19e-23

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 97.58  E-value: 4.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQ-DGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 657198221  85 AHGsvDVAVEAMRFGAFDFLTKPFDGKRLCAT---ARNALKHQQLSSLVAQYRENF 137
Cdd:COG3279   83 AYD--EYALEAFEVNAVDYLLKPIDEERLAKAlekAKERLEAKAAAEASPEEKDRI 136
fixJ PRK09390
response regulator FixJ; Provisional
4-123 1.76e-22

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 94.68  E-value: 1.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   4 SKPRVLLVEDT----RSLAVVyeqyLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCS 79
Cdd:PRK09390   2 DKGVVHVVDDDeamrDSLAFL----LDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLP 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 657198221  80 VVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKH 123
Cdd:PRK09390  78 VIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQ 121
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
6-119 1.69e-21

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: 89.42  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGY-EVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQLPCS----V 80
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRL--RALPGLedvpI 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 657198221  81 VVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARN 119
Cdd:cd17551   79 VMITADTDREVRLRALEAGATDFLTKPFDPVELLARVRN 117
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
9-107 1.70e-21

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: 88.62  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   9 LLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGS 88
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 657198221  89 VDVAVEAMRFGAFDFLTKP 107
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
7-113 2.82e-20

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: 86.14  E-value: 2.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQ-DGYEV-QLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQvPGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                         90       100
                 ....*....|....*....|....*....
gi 657198221  85 AHGSVDVAVEAMRFGAFDFLTKPFDGKRL 113
Cdd:cd19925   82 AANDVETVREALRLGVVDYLIKPFTFERL 110
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
8-115 3.42e-20

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: 85.61  E-value: 3.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100
                 ....*....|....*....|....*...
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELLA 108
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
7-107 4.87e-20

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: 84.83  E-value: 4.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYL-AQDGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                         90       100
                 ....*....|....*....|...
gi 657198221  85 AHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
6-107 1.84e-19

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: 83.79  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDT----RSLAVvyeqYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVV 81
Cdd:cd17555    1 ATILVIDDDevvrESIAA----YLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVI 76
                         90       100
                 ....*....|....*....|....*.
gi 657198221  82 VITAHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd17555   77 VVSGAGVMSDAVEALRLGAWDYLTKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
8-122 3.28e-19

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: 83.12  E-value: 3.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSVVVITAHG 87
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS-QVPVLMLTARG 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFNPRELVARIRAILR 114
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
8-116 4.20e-19

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: 82.52  E-value: 4.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI-----TERQLPcsVVV 82
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrelegGGRRTP--IIA 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCAT 116
Cdd:cd17546   79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEV 112
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
8-107 9.43e-19

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: 81.06  E-value: 9.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE-RQLPcsVVVITAH 86
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREwSAVP--VIVLSAR 78
                         90       100
                 ....*....|....*....|.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd17620   79 DEESDKIAALDAGADDYLTKP 99
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
7-108 2.19e-18

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: 80.23  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVV 82
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEdpetRHIP--VIM 78
                         90       100
                 ....*....|....*....|....*.
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPF 108
Cdd:cd17538   79 ITALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
9-118 2.51e-18

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: 80.34  E-value: 2.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   9 LLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGS 88
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 657198221  89 VDVAVEAMRFGAFDFLTKPFDGKRLCATAR 118
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIR 110
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
8-107 2.49e-17

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: 77.19  E-value: 2.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 657198221  88 SVDVAVEAMRFGAFDFLTKP 107
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
6-85 3.34e-17

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: 77.26  E-value: 3.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER--QLPcsVVVI 83
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKkpDLP--VIIC 78

                 ..
gi 657198221  84 TA 85
Cdd:cd17554   79 TA 80
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
38-123 6.30e-17

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: 76.61  E-value: 6.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  38 GQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATA 117
Cdd:cd17536   34 GEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEAL 113

                 ....*.
gi 657198221 118 RNALKH 123
Cdd:cd17536  114 EKAKEE 119
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
8-118 1.12e-16

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: 75.78  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCATAR 118
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
7-109 1.62e-16

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: 75.28  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81
                         90       100
                 ....*....|....*....|...
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFD 109
Cdd:cd17553   82 GELDMIQESKELGALTHFAKPFD 104
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
8-121 1.86e-16

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: 75.24  E-value: 1.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDtrsLAVV---YEQYL-AQDGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVV 82
Cdd:cd17535    1 VLIVDD---HPLVregLRRLLeSEPDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIV 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd17535   78 LTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
7-110 2.13e-16

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: 75.12  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQD-GYEV-QLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSVVVIT 84
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDpDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAER-PTPVVMVS 80
                         90       100
                 ....*....|....*....|....*...
gi 657198221  85 AHGS--VDVAVEAMRFGAFDFLTKPFDG 110
Cdd:cd17541   81 SLTEegAEITLEALELGAVDFIAKPSGG 108
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
6-121 2.36e-16

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: 75.01  E-value: 2.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQL-ADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  85 AHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
3-131 5.65e-16

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 76.92  E-value: 5.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   3 ESKPRVLLVEDTRSLA--VVYEqyLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER--QLPc 78
Cdd:PRK11083   1 MQQPTILLVEDEQAIAdtLVYA--LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFhpALP- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 657198221  79 sVVVITA-HGSVDVAVeAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLVA 131
Cdd:PRK11083  78 -VIFLTArSDEVDRLV-GLEIGADDYVAKPFSPREVAARVRTILRRVKKFAAPS 129
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
8-107 7.72e-16

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: 72.86  E-value: 7.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 657198221  88 SVDVAVEAMRFGAFDFLTKP 107
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
7-138 1.37e-15

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: 74.99  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEV-QLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITeRQLPCSVVVITA 85
Cdd:COG3707    5 RVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQIS-EERPAPVILLTA 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKH----QQLSSLVAQYRENFE 138
Cdd:COG3707   84 YSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARfrelRALRRELAKLREALE 140
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
7-122 1.49e-15

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: 72.77  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd17615   81 DSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLR 116
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
7-127 1.51e-15

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 75.61  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALaQLLASPPPVVLLDLELPDMSGMDILQQITER-QLPcsVVVITA 85
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQAL-DLLDDSIDLLLLDVMMPKKNGIDTLKELRQThQTP--VIMLTA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLS 127
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWS 121
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
8-115 2.85e-15

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: 71.67  E-value: 2.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|....*...
gi 657198221  88 SVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDELVA 108
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
31-109 3.98e-15

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: 71.41  E-value: 3.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  31 EVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAhgsvDVAVEAMR----FGAFDFLTK 106
Cdd:cd17593   27 EITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG----DVQPEAKErvleLGALAFLKK 102

                 ...
gi 657198221 107 PFD 109
Cdd:cd17593  103 PFD 105
PRK15479 PRK15479
transcriptional regulator TctD;
7-130 4.94e-15

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 73.99  E-value: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKH--------QQLSSLV 130
Cdd:PRK15479  82 SAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRsagqvqevQQLGELI 133
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
8-108 3.15e-14

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: 68.31  E-value: 3.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDT-RSLAVVyEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVV 82
Cdd:cd19920    1 ILIVDDVpDNLRLL-SELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAdpatRHIP--VIF 77
                         90       100
                 ....*....|....*....|....*.
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPF 108
Cdd:cd19920   78 LTALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
8-107 6.46e-14

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: 67.47  E-value: 6.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER-QLPcsVVVITAH 86
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKsTLP--VIFLTSK 78
                         90       100
                 ....*....|....*....|.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd19936   79 DDEIDEVFGLRMGADDYITKP 99
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
8-122 7.31e-14

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: 67.79  E-value: 7.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI--TERQLPcsVVVITA 85
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLraAGNDLP--ILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALLR 115
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
8-116 9.84e-14

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: 67.10  E-value: 9.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI--TA 85
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIalTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 657198221  86 HGSVDVAVEAMRFGaFDF-LTKPFDGKRLCAT 116
Cdd:cd17580   81 YGQPEDRERALEAG-FDAhLVKPVDPDELIEL 111
PRK10336 PRK10336
two-component system response regulator QseB;
7-128 1.45e-13

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 69.92  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFD----GKRLCATARNAlkHQQLSS 128
Cdd:PRK10336  82 DALAERVEGLRLGADDYLCKPFAlievAARLEALMRRT--NGQASN 125
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
6-121 1.66e-13

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 66.66  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQ-LADCGQQALAQLLASPPPVVLLDLELP-DMSGMDILQQITERQlPCSVVVI 83
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKF-DIPVIFL 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd17534   80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
8-113 1.87e-13

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: 66.79  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRsLAVVYEQYL-AQDGY--EVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:cd17532    1 ALIVDDEP-LAREELRYLlEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVT 79
                         90       100
                 ....*....|....*....|....*....
gi 657198221  85 AHGsvDVAVEAMRFGAFDFLTKPFDGKRL 113
Cdd:cd17532   80 AYD--EYAVEAFELNAVDYLLKPFSEERL 106
orf27 CHL00148
Ycf27; Reviewed
1-157 2.43e-13

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 69.36  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI-TERQLPcs 79
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIrKESDVP-- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198221  80 VVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLVAQYRENferSSFA-GFIGASMAMQAVYR 157
Cdd:CHL00148  80 IIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIPNS---SIIRiGFLKIDLNKKQVYK 155
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
8-107 2.71e-13

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: 65.68  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER-QLPcsVVVITAH 86
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARsNVP--VIMVTAK 78
                         90       100
                 ....*....|....*....|.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd17621   79 DSEIDKVVGLELGADDYVTKP 99
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
7-122 2.79e-13

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: 66.24  E-value: 2.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER-QLPcsVVVITA 85
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHsHVP--ILMLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd19939   79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLR 115
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
7-121 3.34e-13

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: 65.86  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQLPcSVVVITAH 86
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREI--RRFS-DVPIIMVT 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  87 GSVDVA--VEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd19938   78 ARVEEIdrLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
6-115 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 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVV 81
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRdemtRDIP--II 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 657198221  82 VITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd17618   79 MLTARGEEEDKVRGLEAGADDYITKPFSPRELVA 112
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
8-109 1.25e-12

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: 64.19  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPP--VVLLDLELPDMSGMDILQQIT-ERQLPcsVVVIT 84
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEfdLVITDVHMPDMDGFEFLELIRlEMDLP--VIMMS 78
                         90       100
                 ....*....|....*....|....*
gi 657198221  85 AHGSVDVAVEAMRFGAFDFLTKPFD 109
Cdd:cd17584   79 ADGSTSTVMKGLAHGACDYLLKPVS 103
PRK10643 PRK10643
two-component system response regulator PmrA;
7-127 1.29e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 66.98  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARnAL--KHQQLS 127
Cdd:PRK10643  82 DTLEDRVAGLDVGADDYLVKPFALEELHARIR-ALirRHQGQG 123
dpiA PRK10046
two-component response regulator DpiA; Provisional
8-131 1.40e-12

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 66.96  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQ-DGY-EVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITA 85
Cdd:PRK10046   7 LLIVEDETPLAEMHAEYIRHiPGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTA 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARnalKHQQLSSLVA 131
Cdd:PRK10046  87 ASDMETVSEAVRCGVFDYLIKPIAYERLGQTLT---RFRQRKHMLE 129
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
6-122 2.03e-12

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: 63.58  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVED----TRSLAVVyeqyLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSV- 80
Cdd:cd17569    1 PTILLVDDepniLKALKRL----LRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY-PDTVr 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 657198221  81 VVITAHGSVDVAVEAMRFGA-FDFLTKPFDGKRLCATARNALK 122
Cdd:cd17569   76 ILLTGYADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
8-115 2.39e-12

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: 63.60  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER-QLPcsVVVITAH 86
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTsNVP--IIMLTAK 78
                         90       100
                 ....*....|....*....|....*....
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd17614   79 DSEVDKVLGLELGADDYVTKPFSNRELLA 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
6-60 2.61e-12

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: 61.43  E-value: 2.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 657198221     6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
7-121 2.70e-12

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: 63.26  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI-TERQLPcsVVVITA 85
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIrAESGVP--IVMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  86 HG-SVDVaVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd17626   80 KSdTVDV-VLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
6-119 1.05e-11

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: 61.63  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITA 85
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGIILVTGR 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 657198221  86 HGSVDVAVeAMRFGAFDFLTKPFDGKRLCATARN 119
Cdd:cd17619   81 DDEVDRIV-GLEIGADDYVTKPFNPRELLVRAKN 113
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
8-118 1.62e-11

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: 60.92  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER-QLPcsVVVITAH 86
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARsDVP--IIIISGD 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 657198221  87 GSVDVA-VEAMRFGAFDFLTKPFDGKRLCATAR 118
Cdd:cd17594   80 RRDEIDrVVGLELGADDYLAKPFGLRELLARVR 112
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
8-109 1.87e-11

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: 60.76  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQItERQLPCSVVVITAH- 86
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREI-RQISNVPIIFISSRd 79
                         90       100
                 ....*....|....*....|...
gi 657198221  87 GSVDVaVEAMRFGAFDFLTKPFD 109
Cdd:cd18159   80 DNMDQ-VMAINMGGDDYITKPFD 101
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
35-113 3.05e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 64.79  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  35 ADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSVVVI---TAHGSvDVAVEAMRFGAFDFLTKPFDGK 111
Cdd:PRK00742  35 APDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLR-PTPVVMVsslTERGA-EITLRALELGAVDFVTKPFLGI 112

                 ..
gi 657198221 112 RL 113
Cdd:PRK00742 113 SL 114
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
7-121 3.97e-11

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: 60.26  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQD-GYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVV 81
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQAnpetQSIP--VI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 657198221  82 VITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd17552   81 LLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
PRK11517 PRK11517
DNA-binding response regulator HprR;
7-124 4.23e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 62.61  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI-TERQLPcsVVVITA 85
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLrTAKQTP--VICLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQ 124
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQH 118
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
7-122 4.43e-11

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: 59.70  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI-TERQLPcsVVVITA 85
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLrPKYQGP--ILLLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
8-113 5.21e-11

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: 59.65  E-value: 5.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVVI 83
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSdpdlKDIP--VILL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRL 113
Cdd:cd17598   79 TTLSDPRDVIRGLECGADNFITKPYDEKYL 108
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
7-108 5.56e-11

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: 59.84  E-value: 5.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPP-PVVLLDLELPDMSGMDILQQITER----QLpcSVV 81
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDiKLVITDYNMPEMDGFELVREIRKKysrdQL--AII 79
                         90       100
                 ....*....|....*....|....*..
gi 657198221  82 VITAHGSVDVAVEAMRFGAFDFLTKPF 108
Cdd:cd17544   80 GISASGDNALSARFIKAGANDFLTKPF 106
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
168-289 7.03e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.08  E-value: 7.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   168 TVFITGESGTGKEVCAEAIHQCSPRRDQPFIALNCAAIPHDLMES---EIFGHVKGSFTGAQGDRKG--AASLANGGTLF 242
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 657198221   243 LDEICEMDLDLQSKLLRFIQtgtLQRVGSGKLETVDVRFVCATNRDP 289
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLE---ELRLLLLLKSEKNLTVILTTNDEK 127
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
7-122 1.31e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 61.09  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLR 117
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
8-122 1.46e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 60.97  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQL-PCSVVVITAH 86
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDL--RQWsAIPVIVLSAR 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:PRK10529  82 SEESDKIAALDAGADDYLSKPFGIGELQARLRVALR 117
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
7-118 1.47e-10

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: 58.58  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADC--GQQALAQLL-------ASPPPVVLLDLELPDMSGMDILQQITE---- 73
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVrdGEEALDFLRgegeyadAPRPDLILLDLNMPRMDGFEVLREIKAdpdl 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 657198221  74 RQLPcsVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATAR 118
Cdd:cd17557   81 RRIP--VVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
421-457 1.64e-10

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 55.86  E-value: 1.64e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 657198221  421 LWQVEKEAIEQAIASCDGNIPKAAALLEISPSTIYRK 457
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRK 37
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
8-115 1.68e-10

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: 58.21  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSVVVITAHG 87
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKH-PSIVVIVLSDN 79
                         90       100
                 ....*....|....*....|....*....
gi 657198221  88 -SVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd17573   80 pKTEQEIEAFKEGADDYIAKPFDFKVLVA 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
9-115 1.89e-10

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: 58.05  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   9 LLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI--TERQLPCSVVVITAH 86
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILrsDPKTSSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|....*....
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLA 109
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
7-118 2.51e-10

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: 57.70  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQLPCS----VVV 82
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKEL--RKLPAYkftpILM 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATAR 118
Cdd:cd17562   80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
7-85 3.17e-10

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 62.65  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITER----QLPcSVVV 82
Cdd:PRK11091 527 NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERypreDLP-PLVA 605

                 ...
gi 657198221  83 ITA 85
Cdd:PRK11091 606 LTA 608
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
5-108 4.26e-10

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: 56.85  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   5 KPRVLLVEDTRSLAVVYEQYLA-QDGYEV-QLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQL---PcS 79
Cdd:cd17561    1 KIKVLIADDNREFVQLLEEYLNsQPDMEVvGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLekrP-K 79
                         90       100
                 ....*....|....*....|....*....
gi 657198221  80 VVVITAHGSVDVAVEAMRFGAFDFLTKPF 108
Cdd:cd17561   80 IIMLTAFGQEDITQRAVELGASYYILKPF 108
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
7-116 5.61e-10

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: 56.78  E-value: 5.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVED---TRSLAV-VYEQYlaqdGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPc 78
Cdd:cd17548    1 KILIVEDnplNMKLARdLLESA----GYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEdpatRDIP- 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 657198221  79 sVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCAT 116
Cdd:cd17548   76 -VIALTAYAMKGDREKILEAGCDGYISKPIDTREFLET 112
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
7-121 6.61e-10

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: 56.65  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEV-QLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSVVVITA 85
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSEN-IAPIVLLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:cd19932   81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
7-107 1.04e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 59.89  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRsLAV-VYEQYLAQD-GYEV-QLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITeRQLPCSVVVI 83
Cdd:PRK12555   2 RIGIVNDSP-LAVeALRRALARDpDHEVvWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIM-AERPCPILIV 79
                         90       100
                 ....*....|....*....|....*.
gi 657198221  84 TA--HGSVDVAVEAMRFGAFDFLTKP 107
Cdd:PRK12555  80 TSltERNASRVFEAMGAGALDAVDTP 105
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
8-107 1.10e-09

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: 55.48  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVE-DTRSLAVVYEqYLAQDGYEVQLADCGQQALAQLLASPPPV--VLLDLELPDMSGMDILQQITE----RQLPcsV 80
Cdd:cd17582    1 VLLVEnDDSTRQIVTA-LLRKCSYEVTAASDGLQAWDVLEDEQNEIdlILTEVDLPVSSGFKLLSYIMRhkicKNIP--V 77
                         90       100
                 ....*....|....*....|....*..
gi 657198221  81 VVITAHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd17582   78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
6-128 1.35e-09

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: 56.22  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVED-TRSLAVVyeQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVIT 84
Cdd:cd17596    1 PTILVVDDeVRSLEAL--RRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIIS 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 657198221  85 AHGSVDVAVEAMR-FGAFDFLTKPFDGKRLCATARNALK-------HQQLSS 128
Cdd:cd17596   79 GYTDSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAARlfelqreNERLSL 130
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
8-107 1.43e-09

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: 55.20  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHG 87
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 657198221  88 SVDVAVEAMRFGAFDFLTKP 107
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
5-76 2.52e-09

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: 55.28  E-value: 2.52e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198221   5 KPRVLLVEDTRSLAVVYEQYL-AQDGYEVQL-ADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI-TERQL 76
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLeAEPDIEVVGeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLlTPRER 75
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
7-113 2.67e-09

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: 55.04  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI----TERQLPcsVV 81
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIradgALSHLP--VL 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 657198221  82 VITAHGSVDVAVEAMRFGAFDFLTKPFDGKRL 113
Cdd:cd19923   80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
7-122 2.67e-09

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 57.42  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVV 82
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKResmtRDIP--VVM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:PRK10161  82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
pleD PRK09581
response regulator PleD; Reviewed
7-109 3.25e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 58.76  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQI----TERQLPcsVVV 82
Cdd:PRK09581   4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLksdpATTHIP--VVM 81
                         90       100
                 ....*....|....*....|....*..
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFD 109
Cdd:PRK09581  82 VTALDDPEDRVRGLEAGADDFLTKPIN 108
ompR PRK09468
osmolarity response regulator; Provisional
1-124 7.43e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 56.14  E-value: 7.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSV 80
Cdd:PRK09468   1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 657198221  81 VVITAHGS-VD--VAVEAmrfGAFDFLTKPFDGKRLCATARNALKHQ 124
Cdd:PRK09468  81 IMLTAKGEeVDriVGLEI---GADDYLPKPFNPRELLARIRAVLRRQ 124
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
35-122 9.29e-09

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: 53.12  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  35 ADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLC 114
Cdd:cd19931   30 ASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLL 109

                 ....*...
gi 657198221 115 ATARNALK 122
Cdd:cd19931  110 EALKQAAS 117
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
7-108 3.07e-08

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: 51.35  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPP-PVVLLDLELPDMSGMDILQQITERQLPCSVVVITA 85
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                         90       100
                 ....*....|....*....|...
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPF 108
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
3-122 3.21e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 54.31  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   3 ESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQ---LPcs 79
Cdd:PRK10710   8 ENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREI--RRfsdIP-- 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 657198221  80 VVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:PRK10710  84 IVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILR 126
PRK10816 PRK10816
two-component system response regulator PhoP;
7-108 3.75e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 53.97  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAH 86
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                         90       100
                 ....*....|....*....|..
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPF 108
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTKPF 103
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
8-107 3.84e-08

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: 51.22  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVVI 83
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKssalKDTP--IIML 78
                         90       100
                 ....*....|....*....|....
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd17602   79 TGKDGLVDRIRAKMAGASGYLTKP 102
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
8-122 4.07e-08

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: 51.50  E-value: 4.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSL--AVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITA 85
Cdd:cd19930    1 VLIAEDQEMVrgALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  86 HGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
7-115 4.18e-08

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: 51.67  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVED---TRSLAVVYEQYLAQDgyEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:cd17530    2 RVLVLDDdpfQCMMAATILEDLGPG--NVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILM 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657198221  84 TAHG-----SVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:cd17530   80 SGLDggileSAETLAGANGLNLLGTLSKPFSPEELTE 116
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
8-108 4.30e-08

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: 50.81  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASP-PPVVLLDLELPD-MSGMDILQQITERQLPCSVVVITa 85
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTS- 79
                         90       100
                 ....*....|....*....|....
gi 657198221  86 hGSVDVAVEAMRFGA-FDFLTKPF 108
Cdd:cd18161   80 -GYAENAIEGGDLAPgVDVLSKPF 102
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
8-108 5.88e-08

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. 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. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 50.94  E-value: 5.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlPCSVVVITAHg 87
Cdd:cd19922    1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIK-PASVIIVLDH- 78
                         90       100
                 ....*....|....*....|....
gi 657198221  88 SVDVA---VEAMRFgAFDFLTKPF 108
Cdd:cd19922   79 WEDLQeelEEVQRF-AVSYVVKPV 101
PRK10610 PRK10610
chemotaxis protein CheY;
1-113 9.54e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 50.74  E-value: 9.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQ 75
Cdd:PRK10610   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAdgamSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 657198221  76 LPcsVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRL 113
Cdd:PRK10610  81 LP--VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATL 116
PRK10430 PRK10430
two-component system response regulator DcuR;
8-112 1.05e-07

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 52.80  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQ-DGYEVqladCG-----QQALAQLLASPPPV--VLLDLELPDMSGMDILQQITERQLPCS 79
Cdd:PRK10430   4 VLIVDDDAMVAELNRRYVAQiPGFQC----CGtastlEQAKEIIFNSDTPIdlILLDIYMQQENGLDLLPVLHEAGCKSD 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 657198221  80 VVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKR 112
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIKPFQASR 112
PRK10693 PRK10693
two-component system response regulator RssB;
34-107 1.31e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 53.07  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198221  34 LADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGSV-DVAvEAMRFGAFDFLTKP 107
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMaDIA-KALRLGVQDVLLKP 75
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1-136 1.48e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 51.95  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGyEVQL---ADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLP 77
Cdd:PRK10651   2 SNQEPATILLIDDHPMLRTGVKQLISMAP-DITVvgeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198221  78 CSVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRL------CATARNALKHQQLSSLVAQYREN 136
Cdd:PRK10651  81 GRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLlkalqqAAAGEMVLSEALTPVLAASLRAN 145
PRK14084 PRK14084
DNA-binding response regulator;
7-124 1.61e-07

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 52.45  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDtRSLAVVYEQYLAQ--DGYE-VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVI 83
Cdd:PRK14084   2 KALIVDD-EPLARNELTYLLNeiGGFEeINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657198221  84 TAHGSvdVAVEAMRFGAFDFLTKPFDGKRLcATARNALKHQ 124
Cdd:PRK14084  81 TAHDQ--FAVKAFELNATDYILKPFEQKRI-EQAVNKVRAT 118
PRK11697 PRK11697
two-component system response regulator BtsR;
50-132 2.19e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 51.77  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  50 PPVVLLDLELPDMSGMDILQQITERQLPcSVVVITAHGsvDVAVEAMRFGAFDFLTKPFDGKRLCATA---RNALKHQQL 126
Cdd:PRK11697  48 PDVVFLDIQMPRISGLELVGMLDPEHMP-YIVFVTAFD--EYAIKAFEEHAFDYLLKPIDPARLAKTLarlRQERSPQDV 124

                 ....*.
gi 657198221 127 SSLVAQ 132
Cdd:PRK11697 125 LLPEAQ 130
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
8-107 5.35e-07

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: 47.76  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVVI 83
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKnadfDTIP--VIFL 78
                         90       100
                 ....*....|....*....|....
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd19927   79 TAKGMTSDRIKGYNAGCDGYLSKP 102
PRK10766 PRK10766
two-component system response regulator TorR;
7-121 5.99e-07

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 50.04  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVED---TRSLAVvyeQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlpcSVVVI 83
Cdd:PRK10766   4 HILVVEDepvTRARLQ---GYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS---TVGII 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657198221  84 TAHG---SVDVAVeAMRFGAFDFLTKPFDGKRLCATARNAL 121
Cdd:PRK10766  78 LVTGrtdSIDRIV-GLEMGADDYVTKPLELRELLVRVKNLL 117
PRK15369 PRK15369
two component system response regulator;
7-106 7.14e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 49.69  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVED-------TRSLAVVYEQYL----AQDGYEVqladcgqqaLAQLLASPPPVVLLDLELPDMSGMDILQQITERQ 75
Cdd:PRK15369   5 KILLVDDheliingIKNMLAPYPRYKivgqVDNGLEV---------YNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRW 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 657198221  76 LPCSVVVITAHGSVDVAVEAMRFGAFDFLTK 106
Cdd:PRK15369  76 PAMNILVLTARQEEHMASRTLAAGALGYVLK 106
PRK11173 PRK11173
two-component response regulator; Provisional
6-144 8.75e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 50.01  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVED---TR-SLAVVYEQylaqDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQlpcSVV 81
Cdd:PRK11173   4 PHILIVEDelvTRnTLKSIFEA----EGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQA---NVA 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198221  82 VITAHG---SVDvAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLSSLVAQYRENFERSSFAG 144
Cdd:PRK11173  77 LMFLTGrdnEVD-KILGLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERRSVESYKFNG 141
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
7-107 3.84e-06

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: 45.85  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALaQLLASPPP---VVLLDLELPDMSGMDILQQITERQLPCS---V 80
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECL-NLLASAEHsfqLVLLDLCMPEMDGFEVALRIRKLFGRRErplI 80
                         90       100
                 ....*....|....*....|....*..
gi 657198221  81 VVITAHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd19933   81 VALTANTDDSTREKCLSLGMNGVITKP 107
PRK13856 PRK13856
two-component response regulator VirG; Provisional
8-122 4.69e-06

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 47.89  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQaLAQLLASPP-PVVLLDLELPDMSGMDILQQI-TERQLPcsvVVITA 85
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQ-FNRVLASETvDVVVVDLNLGREDGLEIVRSLaTKSDVP---IIIIS 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 657198221  86 HGSVDVA--VEAMRFGAFDFLTKPFDGKRLCATARNALK 122
Cdd:PRK13856  80 GDRLEEAdkVVALELGATDFIAKPFGTREFLARIRVALR 118
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
7-106 4.91e-06

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 45.25  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   7 RVLLVEDTRSLAVVYEQYLAQD-GYEVQLADCGQQALAqLLASPPP--VVLLDLELPDMSGMDILQQITERQLPCsvVVI 83
Cdd:cd19921    1 KVLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKA-LLEEGDDyfAALVDLNLPDAPNGEAVDLVLEKGIPV--IVL 77
                         90       100
                 ....*....|....*....|...
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTK 106
Cdd:cd19921   78 TGSFDEDKRETLLSKGVVDYVLK 100
PRK09483 PRK09483
response regulator; Provisional
10-106 7.69e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 47.02  E-value: 7.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  10 LVEDTRSLAVVYEqylaqdgyevqlADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGSV 89
Cdd:PRK09483  20 ILEDIKGIKVVGE------------ACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTVHTEN 87
                         90
                 ....*....|....*..
gi 657198221  90 DVAVEAMRFGAFDFLTK 106
Cdd:PRK09483  88 PLPAKVMQAGAAGYLSK 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
8-125 1.74e-05

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 47.37  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYE-VQLADCGqQALAQLLASPPPvvlLDLELPDMSGMDILQQIT--ERQLPCSVVVIT 84
Cdd:PRK13837 700 VLLVEPDDATLERYEEKLAALGYEpVGFSTLA-AAIAWISKGPER---FDLVLVDDRLLDEEQAAAalHAAAPTLPIILG 775
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657198221  85 AHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQ 125
Cdd:PRK13837 776 GNSKTMALSPDLLASVAEILAKPISSRTLAYALRTALATAR 816
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
6-67 4.85e-05

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 44.63  E-value: 4.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDI 67
Cdd:PRK10701   2 NKIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTI 63
PRK10360 PRK10360
transcriptional regulator UhpA;
38-120 6.35e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 43.81  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  38 GQQALAQLLASPPPVVLLDLELPDMSGMDILqqiteRQLP--CSVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCA 115
Cdd:PRK10360  36 GREALAGLPGRGVQVCICDISMPDISGLELL-----SQLPkgMATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELIA 110

                 ....*
gi 657198221 116 TARNA 120
Cdd:PRK10360 111 AVHTV 115
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
8-109 1.36e-04

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 41.30  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYL-AQDGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPcsvvVITAH 86
Cdd:cd17586    1 VLVLEDEPLIAMNLEDALeDLGGKEVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVADALKRRAIP----FIFAT 76
                         90       100
                 ....*....|....*....|...
gi 657198221  87 GSVDVAVEAMRFGAFDFLTKPFD 109
Cdd:cd17586   77 GYGDSHGIDSRLIDVPVLRKPFD 99
PRK13435 PRK13435
response regulator; Provisional
1-123 1.66e-04

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 41.58  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKPRVLLVEDTRSLAVVYEQYLAQDGYEVQ-LADCGQQALAQLLASPPPVVLLDLELPD-MSGMDILQQITERqlpC 78
Cdd:PRK13435   1 MFLRQLKVLIVEDEALIALELEKLVEEAGHEVVgIAMSSEQAIALGRRRQPDVALVDVHLADgPTGVEVARRLSAD---G 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 657198221  79 SVVVITAHGSVDVaVEAMRFGAFDFLTKPFDGKRLcataRNALKH 123
Cdd:PRK13435  78 GVEVVFMTGNPER-VPHDFAGALGVIAKPYSPRGV----ARALSY 117
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
32-107 2.66e-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: 2.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198221  32 VQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGSVDVAVEAMRFGAFDFLTKP 107
Cdd:cd17565   27 VGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVSDKEMIGKAYQAGIEFFINKP 102
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
31-109 4.43e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 42.91  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221  31 EVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQIteRQLPCS----VVVITAHGsvdVAVEAMRF---GAFDF 103
Cdd:PRK11107 693 HVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELI--RQLPHNqntpIIAVTAHA---MAGERERLlsaGMDDY 767

                 ....*.
gi 657198221 104 LTKPFD 109
Cdd:PRK11107 768 LAKPID 773
PRK13557 PRK13557
histidine kinase; Provisional
1-121 8.91e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 41.58  E-value: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKP---RVLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALaQLLASPPPVVLL--DLELPdmSGMD--ILQQITE 73
Cdd:PRK13557 408 RAIDRGgteTILIVDDRPDVAELARMILEDFGYRTLVASNGREAL-EILDSHPEVDLLftDLIMP--GGMNgvMLAREAR 484
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 657198221  74 RQLPCSVVVITAhGSVDVAVEamRFGA----FDFLTKPFDGKRLCATARNAL 121
Cdd:PRK13557 485 RRQPKIKVLLTT-GYAEASIE--RTDAggseFDILNKPYRRAELARRVRMVL 533
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
8-127 1.05e-03

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-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 the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.83  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQdGYEVQLADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITE----RQLPcsVVVI 83
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLSS-EHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSlertRQLP--ILAV 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 657198221  84 TAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARNALKHQQLS 127
Cdd:cd17539   78 ADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRRKRYT 121
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
6-121 1.16e-03

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 38.77  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSLAVVYEQYLAQDGYEV-QLADCGQQALAQLLASPPPVVLLDLELPD-MSGMDILQQITErQLPCSVVVI 83
Cdd:cd17540    1 TRVLIIEDEPLIAMDLEQIVEDLGHQVvGIARTRDEAVALARRERPDLILADIQLADgSSGIDAVNEILT-THDVPVIFV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 657198221  84 TAHGsvdvavEAMRFGAF---DFL-TKPFDGKRLCATARNAL 121
Cdd:cd17540   80 TAYP------ERLLTGERpepTFLiTKPFDPEMVKAAISQAL 115
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1-138 1.97e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 39.45  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   1 MAESKP-RVLLVEDTRSLAVVYEQYLAQD-GYEVQL-ADCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLP 77
Cdd:PRK10403   1 MPEATPfQVLIVDDHPLMRRGVRQLLELDpGFEVVAeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198221  78 CSVVVITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLCATARN-ALKHQQLSSLVAQY---RENFE 138
Cdd:PRK10403  81 AQIIILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAgAKGSKVFSERVNQYlreREMFG 145
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
8-113 2.15e-03

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. 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. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 38.12  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGYEVQLADCGQQALaQLLASPPP------------VVLLDLELPDMSGMDILQQITE-- 73
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRAL-EFLGLEDEedssnfnepkvnMIITDYCMPGMTGYDLLKKVKEss 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 657198221  74 --RQLPcsvVVITAHGSVDVAV-EAMRFGAFDFLTKPF---DGKRL 113
Cdd:cd17581   80 alKEIP---VVIMSSENIPTRIsRCLEEGAEDFLLKPVklaDVKRL 122
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
36-106 2.74e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 39.11  E-value: 2.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198221  36 DCGQQALAQLLASPPPVVLLDLELPDMSGMDILQQITERQLPCSVVVITAHGSVDVAVEAMRFGAFDFLTK 106
Cdd:PRK09958  32 TEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKNDHFYGKHCADAGANGFVSK 102
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
6-109 3.00e-03

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: 37.70  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   6 PRVLLVEDTRSL--AVVYE---QYlaQDGYEVQLADCGQQAL---AQLLASPPPVVLL--DLELPDMSGMDILQQITERQ 75
Cdd:cd17595    1 PIILTVDDDPQVlrAVARDlrrQY--GKDYRVLRADSGAEALdalKELKLRGEAVALFlvDQRMPEMDGVEFLEKAMELF 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 657198221  76 LPCSVVVITAHGSVDVAVEAMRFGAFDF-LTKPFD 109
Cdd:cd17595   79 PEAKRVLLTAYADTDAAIRAINDVQLDYyLLKPWD 113
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
8-114 6.73e-03

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: 36.47  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198221   8 VLLVEDTRSLAVVYEQYLAQDGY-EVQLADCGQQALAQLLASPPPVVLLDLELPD-MSGMDILQQITERQL--PCSVVV- 82
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLisPSTVFIm 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 657198221  83 ITAHGSVDVAVEAMRFGAFDFLTKPFDGKRLC 114
Cdd:cd17589   81 VTGESSRAMVLSALELEPDDYLLKPFTVSELR 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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