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Conserved domains on  [gi|1125487139|gb|OLE09710|]
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sigma-54-dependent Fis family transcriptional regulator [Delftia sp. 13_1_20CM_4_67_18]

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, ...
10-494 2.25e-174

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: 497.18  E-value: 2.25e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQgvggvpapgvmparspsvspaASPVLNGSGALDAMVGDSPAMQ 169
Cdd:COG2204    83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE---------------------RRRLRRENAEDSGLIGRSPAMQ 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 170 AVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRDGYF 249
Cdd:COG2204   142 EVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 250 QAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVLL 329
Cdd:COG2204   222 ELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIEL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 330 PPLRERREDLPALCRALLARLSQESGLPmPEIDELSVQQIARLPLPGNVRELENLLHRAITLGEDGPLRidpemqlpcgt 409
Cdd:COG2204   302 PPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVIT----------- 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 410 ppappappasaspspslspsrpvppggplsptdadlPRDLQAWLDERERGILVQALQENGFNRTATAARLGLSLRQIRYR 489
Cdd:COG2204   370 ------------------------------------AEDLPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRK 413

                  ....*
gi 1125487139 490 IDRLN 494
Cdd:COG2204   414 LKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
10-494 2.25e-174

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: 497.18  E-value: 2.25e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQgvggvpapgvmparspsvspaASPVLNGSGALDAMVGDSPAMQ 169
Cdd:COG2204    83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE---------------------RRRLRRENAEDSGLIGRSPAMQ 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 170 AVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRDGYF 249
Cdd:COG2204   142 EVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 250 QAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVLL 329
Cdd:COG2204   222 ELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIEL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 330 PPLRERREDLPALCRALLARLSQESGLPmPEIDELSVQQIARLPLPGNVRELENLLHRAITLGEDGPLRidpemqlpcgt 409
Cdd:COG2204   302 PPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVIT----------- 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 410 ppappappasaspspslspsrpvppggplsptdadlPRDLQAWLDERERGILVQALQENGFNRTATAARLGLSLRQIRYR 489
Cdd:COG2204   370 ------------------------------------AEDLPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRK 413

                  ....*
gi 1125487139 490 IDRLN 494
Cdd:COG2204   414 LKKYG 418
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
6-495 3.60e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 383.81  E-value: 3.60e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   6 LPAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCV 85
Cdd:PRK11361    1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  86 VMTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQGVGgvpapgvMPARSPSVSPAASPVLNGSGALDamvgDS 165
Cdd:PRK11361   81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQS-------MKKEIRHLHQALSTSWQWGHILT----NS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 166 PAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDR 245
Cdd:PRK11361  150 PAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 246 DGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVI 325
Cdd:PRK11361  230 QGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 326 EVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRA-------ITLGEDGPLR 398
Cdd:PRK11361  310 HLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAvvmnsgpIIFSEDLPPQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 399 IDPEMQLPCGtppappappasaspspslspsrpvppggplSPTDADLPRDLQAWLDERERGILVQALQENGFNRTATAAR 478
Cdd:PRK11361  390 IRQPVCNAGE------------------------------VKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALM 439
                         490
                  ....*....|....*..
gi 1125487139 479 LGLSLRQIRYRIDRLNI 495
Cdd:PRK11361  440 LGISRRALMYKLQEYGI 456
Sigma54_activat pfam00158
Sigma-54 interaction domain;
161-327 9.83e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 302.78  E-value: 9.83e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 161 MVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTG 240
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 241 ATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYY 320
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 1125487139 321 RLNVIEV 327
Cdd:pfam00158 161 RLNVIPI 167
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
143-498 4.37e-98

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: 306.26  E-value: 4.37e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 143 SVSPAASPVLNGSGALDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIP 222
Cdd:TIGR01817 180 LRDKAPEIARRRSGKEDGIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALS 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 223 ENLLEAEFFGARKGSYTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATH 302
Cdd:TIGR01817 260 ETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATN 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 303 RDLAADVQQGRFRQDLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMpEIDELSVQQIARLPLPGNVRELE 382
Cdd:TIGR01817 340 RDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPL-TITPSAIRVLMSCKWPGNVRELE 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 383 NLLHRAITLGEDGplRIDPEmQLPCGTPPAPPAPPASASPSPSLSPSRPVPPGGPLSPTDADLPRDLQAW---LDERERg 459
Cdd:TIGR01817 419 NCLERTATLSRSG--TITRS-DFSCQSGQCLSPMLAKTCPHGHISIDPLAGTTPPHSPASAALPGEPGLSgptLSERER- 494
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1125487139 460 iLVQALQENGFNRtATAAR-LGLSLRQIRYRIDRLNIALP 498
Cdd:TIGR01817 495 -LIAALEQAGWVQ-AKAARlLGMTPRQVGYALRKLNIEMK 532
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
12-111 7.99e-33

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: 120.72  E-value: 7.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
11-64 4.71e-13

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: 63.74  E-value: 4.71e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1125487139   11 SILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLP 64
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
10-494 2.25e-174

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: 497.18  E-value: 2.25e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQgvggvpapgvmparspsvspaASPVLNGSGALDAMVGDSPAMQ 169
Cdd:COG2204    83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE---------------------RRRLRRENAEDSGLIGRSPAMQ 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 170 AVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRDGYF 249
Cdd:COG2204   142 EVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 250 QAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVLL 329
Cdd:COG2204   222 ELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIEL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 330 PPLRERREDLPALCRALLARLSQESGLPmPEIDELSVQQIARLPLPGNVRELENLLHRAITLGEDGPLRidpemqlpcgt 409
Cdd:COG2204   302 PPLRERREDIPLLARHFLARFAAELGKP-VKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVIT----------- 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 410 ppappappasaspspslspsrpvppggplsptdadlPRDLQAWLDERERGILVQALQENGFNRTATAARLGLSLRQIRYR 489
Cdd:COG2204   370 ------------------------------------AEDLPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRK 413

                  ....*
gi 1125487139 490 IDRLN 494
Cdd:COG2204   414 LKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
158-495 7.57e-146

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: 425.72  E-value: 7.57e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 158 LDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGS 237
Cdd:COG3829   137 FDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGA 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 238 YTGATQ-DRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQ 316
Cdd:COG3829   217 FTGAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFRE 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 317 DLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITLGEDGp 396
Cdd:COG3829   297 DLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGD- 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 397 lRIDPEMqLPcgtppappappasaspspslspsrpVPPGGPLSPTDADLPRDLQAWLDERERGILVQALQENGFNRTATA 476
Cdd:COG3829   376 -VITPEH-LP-------------------------EYLLEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGNKSKAA 428
                         330
                  ....*....|....*....
gi 1125487139 477 ARLGLSLRQIRYRIDRLNI 495
Cdd:COG3829   429 KALGISRSTLYRKLKKYGI 447
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
6-495 3.60e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 383.81  E-value: 3.60e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   6 LPAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCV 85
Cdd:PRK11361    1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  86 VMTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQGVGgvpapgvMPARSPSVSPAASPVLNGSGALDamvgDS 165
Cdd:PRK11361   81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQS-------MKKEIRHLHQALSTSWQWGHILT----NS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 166 PAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDR 245
Cdd:PRK11361  150 PAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 246 DGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVI 325
Cdd:PRK11361  230 QGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 326 EVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRA-------ITLGEDGPLR 398
Cdd:PRK11361  310 HLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAvvmnsgpIIFSEDLPPQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 399 IDPEMQLPCGtppappappasaspspslspsrpvppggplSPTDADLPRDLQAWLDERERGILVQALQENGFNRTATAAR 478
Cdd:PRK11361  390 IRQPVCNAGE------------------------------VKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALM 439
                         490
                  ....*....|....*..
gi 1125487139 479 LGLSLRQIRYRIDRLNI 495
Cdd:PRK11361  440 LGISRRALMYKLQEYGI 456
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
12-492 1.94e-115

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 348.17  E-value: 1.94e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQFRLVVASA---AQGVGGVPapgvmparsPSVSPAASpvlngsgaldAMVGDSPAM 168
Cdd:PRK10365   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAlahTHSIDAET---------PAVTASQF----------GMVGKSPAM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 169 QAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRDGY 248
Cdd:PRK10365  149 QHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 249 FQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVL 328
Cdd:PRK10365  229 FVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 329 LPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITL--GEdgplrIDPEMQLP 406
Cdd:PRK10365  309 VPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLltGE-----YISERELP 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 407 CGTPPAPPappasaspspslspsrpvppggPLSPTDADLPrdlqawLDERERGILVQALQENGFNRTATAARLGLSLRQI 486
Cdd:PRK10365  384 LAIASTPI----------------------PLGQSQDIQP------LVEVEKEVILAALEKTGGNKTEAARQLGITRKTL 435

                  ....*.
gi 1125487139 487 RYRIDR 492
Cdd:PRK10365  436 LAKLSR 441
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
138-482 2.23e-105

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 328.01  E-value: 2.23e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 138 PARSPSVSPAASPVlngSGALDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVN 217
Cdd:COG3284   303 ARRAARAAPAGAPA---PAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVN 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 218 CGAIPENLLEAEFFGARKGSYTGA-TQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVR 296
Cdd:COG3284   380 CAAIPEELIESELFGYEPGAFTGArRKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVR 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 297 IVSATHRDLAADVQQGRFRQDLYYRLNVIEVLLPPLRErREDLPALCRALLARLSQESGLpmPEIDELSVQQIARLPLPG 376
Cdd:COG3284   460 LIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRE-REDLPALIEHLLRELAAGRGP--LRLSPEALALLAAYPWPG 536
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 377 NVRELENLLHRAITLGEDGPLRIDpemQLPcgtppappappasaSPSPSLSPSRPVPPGGPLSPtdadlprdlqawLDER 456
Cdd:COG3284   537 NVRELRNVLRTALALADGGVITVE---DLP--------------DELRAELAAAAPAAAAPLTS------------LEEA 587
                         330       340
                  ....*....|....*....|....*.
gi 1125487139 457 ERGILVQALQENGFNRTATAARLGLS 482
Cdd:COG3284   588 ERDAILRALRACGGNVSAAARALGIS 613
PRK15115 PRK15115
response regulator GlrR; Provisional
8-391 1.35e-104

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 320.25  E-value: 1.35e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   8 AAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVM 87
Cdd:PRK15115    4 KPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIIL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAaqgvggvpapgvMPARSPSVSPAASpvlngsgalDAMVGDSPA 167
Cdd:PRK15115   84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDA------------LEQSAPATDERWR---------EAIVTRSPL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 168 MQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRDG 247
Cdd:PRK15115  143 MLRLLEQARMVAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 248 YFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEV 327
Cdd:PRK15115  223 LFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSL 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125487139 328 LLPPLRERREDLPALCRALlarLSQESGLPMPEIDELSVQQIARL---PLPGNVRELENLLHRAITL 391
Cdd:PRK15115  303 KIPALAERTEDIPLLANHL---LRQAAERHKPFVRAFSTDAMKRLmtaSWPGNVRQLVNVIEQCVAL 366
Sigma54_activat pfam00158
Sigma-54 interaction domain;
161-327 9.83e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 302.78  E-value: 9.83e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 161 MVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTG 240
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 241 ATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYY 320
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 1125487139 321 RLNVIEV 327
Cdd:pfam00158 161 RLNVIPI 167
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
143-498 4.37e-98

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: 306.26  E-value: 4.37e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 143 SVSPAASPVLNGSGALDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIP 222
Cdd:TIGR01817 180 LRDKAPEIARRRSGKEDGIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALS 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 223 ENLLEAEFFGARKGSYTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATH 302
Cdd:TIGR01817 260 ETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATN 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 303 RDLAADVQQGRFRQDLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMpEIDELSVQQIARLPLPGNVRELE 382
Cdd:TIGR01817 340 RDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPL-TITPSAIRVLMSCKWPGNVRELE 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 383 NLLHRAITLGEDGplRIDPEmQLPCGTPPAPPAPPASASPSPSLSPSRPVPPGGPLSPTDADLPRDLQAW---LDERERg 459
Cdd:TIGR01817 419 NCLERTATLSRSG--TITRS-DFSCQSGQCLSPMLAKTCPHGHISIDPLAGTTPPHSPASAALPGEPGLSgptLSERER- 494
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1125487139 460 iLVQALQENGFNRtATAAR-LGLSLRQIRYRIDRLNIALP 498
Cdd:TIGR01817 495 -LIAALEQAGWVQ-AKAARlLGMTPRQVGYALRKLNIEMK 532
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
12-393 6.71e-96

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: 297.82  E-value: 6.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTlyELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLP---DGM--GMELLQDLRSQQRRERCVV 86
Cdd:TIGR02915   1 LLIVEDDLGLQK--QLKWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdaDGAseGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQGVGgvpapgvMPARSPSVSPAAspvlnGSGALDAMVGDSP 166
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYT-------LETENRRLQSAL-----GGTALRGLITSSP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 167 AMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRD 246
Cdd:TIGR02915 147 GMQKICRTIEKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 247 GYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIE 326
Cdd:TIGR02915 227 GKIEYAHGGTLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEIS 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125487139 327 VLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITLGE 393
Cdd:TIGR02915 307 ITIPPLRSRDGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAE 373
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
12-383 1.20e-94

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 295.24  E-value: 1.20e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQGVggvpapgvMPARSPSVSPAASPVLNgsgaldaMVGDSPAMQAV 171
Cdd:PRK10923   86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHY--------QEQQQPRNIQVNGPTTD-------IIGEAPAMQDV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 172 KQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQDRDGYFQA 251
Cdd:PRK10923  151 FRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 252 ARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVLLPP 331
Cdd:PRK10923  231 ADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPP 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1125487139 332 LRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELEN 383
Cdd:PRK10923  311 LRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLEN 362
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
161-481 5.85e-92

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 289.76  E-value: 5.85e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 161 MVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTG 240
Cdd:PRK05022  189 MIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTG 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 241 ATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYY 320
Cdd:PRK05022  269 AISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYH 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 321 RLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITL----GEDGP 396
Cdd:PRK05022  349 RLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLararGAGRI 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 397 LRIDPEM-QLPCGTPPAPPAPPASaspspslspsrpvppggPLSPTDADLpRDLqawLDERERGILVQALQENGFNRTAT 475
Cdd:PRK05022  429 VTLEAQHlDLPAEVALPPPEAAAA-----------------PAAVVSQNL-REA---TEAFQRQLIRQALAQHQGNWAAA 487

                  ....*.
gi 1125487139 476 AARLGL 481
Cdd:PRK05022  488 ARALEL 493
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
153-406 2.03e-87

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 277.84  E-value: 2.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 153 NGSGALDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFG 232
Cdd:COG3283   198 NDDSGFDHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFG 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 233 ARKGSYTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQG 312
Cdd:COG3283   278 YAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEG 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 313 RFRQDLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITLG 392
Cdd:COG3283   358 EFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLL 437
                         250
                  ....*....|....
gi 1125487139 393 EDGPLRIDpEMQLP 406
Cdd:COG3283   438 EGDELTPE-DLQLP 450
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
139-402 3.15e-76

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 249.64  E-value: 3.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 139 ARSPSVSPAASPVLNGSGA---LDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHA--------CSQ 207
Cdd:PRK15424  196 TRMTLRHNTHYATRNALRTryvLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHReyfarhdaRQG 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 208 RAHGPMVAVNCGAIPENLLEAEFFGARKGSYTGATQD-RDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLG 286
Cdd:PRK15424  276 KKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVG 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 287 SAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSV 366
Cdd:PRK15424  356 GHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAPFSAALRQGL 435
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1125487139 367 QQIARLPL----PGNVRELENLLHR-AITLGEDGPLRIDPE 402
Cdd:PRK15424  436 QQCETLLLhydwPGNVRELRNLMERlALFLSVEPTPDLTPQ 476
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
158-387 1.37e-72

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: 239.76  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 158 LDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGS 237
Cdd:TIGR02329 211 LDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGA 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 238 YTGATQD-RDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQ 316
Cdd:TIGR02329 291 FTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRR 370
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125487139 317 DLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIA----RLPLPGNVRELENLLHR 387
Cdd:TIGR02329 371 DLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAAQVLAGVAdplqRYPWPGNVRELRNLVER 445
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
161-495 5.82e-68

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 231.26  E-value: 5.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 161 MVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGSYTG 240
Cdd:PRK15429  378 IIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTG 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 241 ATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYY 320
Cdd:PRK15429  458 ASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYY 537
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 321 RLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITLGEDGPLRID 400
Cdd:PRK15429  538 RLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQLS 617
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 401 -PEMQLPCgtppappappasaspspslspsrpvppgGPLSPTDADLPRDlqawlDERERGILVQALQE-NGF--NRTATA 476
Cdd:PRK15429  618 lPDITLPE----------------------------PETPPAATVVAQE-----GEDEYQLIVRVLKEtNGVvaGPKGAA 664
                         330
                  ....*....|....*....
gi 1125487139 477 ARLGLSLRQIRYRIDRLNI 495
Cdd:PRK15429  665 QRLGLKRTTLLSRMKRLGI 683
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
187-495 1.72e-66

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: 218.18  E-value: 1.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 187 VHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAeffgarkgsytgatqdrdgyfqaarggtlfldeigdlp 266
Cdd:COG3604   120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 267 lamqakllraIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQDLYYRLNVIEVLLPPLRERREDLPALCRAL 346
Cdd:COG3604   162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 347 LARLSQESGLPMPEIDELSVQQIARLPLPGNVRELENLLHRAITLGEDGPLRIDpemqlpcgtppappappasaspspsl 426
Cdd:COG3604   232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDAD-------------------------- 285
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125487139 427 spsrpvppggplsptdaDLPRDLQAWLDERERGILVQALQENGFNRTATAARLGLSLRQIRYRIDRLNI 495
Cdd:COG3604   286 -----------------DLAPGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGI 337
PRK10820 PRK10820
transcriptional regulator TyrR;
153-406 1.75e-64

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 218.02  E-value: 1.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 153 NGSGALDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFG 232
Cdd:PRK10820  198 NDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFG 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 233 ARKGSYTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQG 312
Cdd:PRK10820  278 HAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKG 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 313 RFRQDLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMPEID-ELSvQQIARLPLPGNVRELENLLHRAITL 391
Cdd:PRK10820  358 EFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAaDLN-TVLTRYGWPGNVRQLKNAIYRALTQ 436
                         250
                  ....*....|....*
gi 1125487139 392 GEDGPLRIDpEMQLP 406
Cdd:PRK10820  437 LEGYELRPQ-DILLP 450
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
158-487 1.73e-63

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 209.91  E-value: 1.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 158 LDAMVGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGARKGS 237
Cdd:PRK11608    5 KDNLLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 238 YTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQD 317
Cdd:PRK11608   85 FTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRAD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 318 LYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPM-PEIDELSVQQIARLPLPGNVRELENLLHRAITL--GED 394
Cdd:PRK11608  165 LLDRLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPLfPGFTERARETLLNYRWPGNIRELKNVVERSVYRhgTSE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 395 GPLR---IDPEMQLPcgtppappappasaspspslspsrPVPPGGPLSPTDA-DLPRDLQAWLDERERGILVQALQENGF 470
Cdd:PRK11608  245 YPLDniiIDPFKRRP------------------------AEEAIAVSETTSLpTLPLDLREWQHQQEKELLQRSLQQAKF 300
                         330
                  ....*....|....*..
gi 1125487139 471 NRTATAARLGLSLRQIR 487
Cdd:PRK11608  301 NQKRAAELLGLTYHQLR 317
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
158-388 1.26e-49

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 180.26  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 158 LDAMVGDSPAMQAVkQRIAK-VARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGarkG 236
Cdd:PRK11388  324 FDHMPQDSPQMRRL-IHFGRqAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---S 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 237 SYTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSAQEEAADVRIVSATHRDLAADVQQGRFRQ 316
Cdd:PRK11388  400 DRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSR 479
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125487139 317 DLYYRLNVIEVLLPPLRERREDLPALCRALLARLSQESGLPMpEIDELSVQQIARLPLPGNVRELENLLHRA 388
Cdd:PRK11388  480 QLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRL-KIDDDALARLVSYRWPGNDFELRSVIENL 550
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
12-111 7.99e-33

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: 120.72  E-value: 7.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
10-126 2.37e-30

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: 117.36  E-value: 2.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:COG0745    82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
12-126 3.13e-30

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: 114.22  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQdlRSQQRRERC--VVMTA 89
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILK--WIQERSLPTsvIVITA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:cd17572    79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALK 115
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
13-111 7.80e-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: 7.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  13 LVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYGS 92
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90
                  ....*....|....*....
gi 1125487139  93 AENAVEALRSGAFDYLTKP 111
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
12-122 1.12e-29

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 112.24  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQFRLVVA 122
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
12-124 1.17e-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: 109.94  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERC--VVMTA 89
Cdd:COG0784     8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIpiIALTA 87
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASA 124
Cdd:COG0784    88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
11-116 4.28e-28

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: 107.91  E-value: 4.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:cd17563    82 ASIATAVEAIKLGADDYLAKPADADE 107
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
9-125 1.67e-27

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: 108.46  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   9 AASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRER--CVV 86
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADipIIF 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAA 125
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVA 119
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
7-126 2.50e-27

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 109.48  E-value: 2.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   7 PAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERC-- 84
Cdd:COG3437     4 GQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIpv 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1125487139  85 VVMTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:COG3437    84 IFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
12-126 5.35e-27

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 105.82  E-value: 5.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLR-EGYR-VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:COG4565     6 VLIVEDDPMVAELLRRYLERlPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITA 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:COG4565    86 ARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
7-144 3.07e-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: 105.00  E-value: 3.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   7 PAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV 86
Cdd:COG4567     2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVV 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDLKQfrlVVASAAQGVGGVPAPgvmPARSPSV 144
Cdd:COG4567    82 LTGYASIATAVEAIKLGADDYLAKPADADD---LLAALERAEGDAPAP---PENPMSL 133
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
12-126 1.46e-25

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: 101.41  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPdGM-GMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMP-GMdGLELLAQIRELDPDLPVILITGH 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:cd17549    80 GDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALE 115
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
12-121 1.79e-25

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 101.02  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPdGM-GMELLQDLRSQQRRERCVVMTAY 90
Cdd:COG5803     5 ILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMP-GMdGIEILKEIKEIDPDIPVIMMTAY 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVDLKQFRLVV 121
Cdd:COG5803    84 GELDMVEEAKELGAKGYFTKPFDIDELREAV 114
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
162-332 1.88e-24

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 98.57  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 162 VGDSPAMQAVKQRIAKVARGMAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEaeffgarkgsytga 241
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLE-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 242 tqdrdgyfqAARGGTLFLDEIGDLPLAMQAKLLRAIQErrvrplgsaqEEAADVRIVSATHRDLAADVQQGRFRQDLYYR 321
Cdd:pfam14532  67 ---------QAKGGTLYLKDIADLSKALQKGLLLLLAK----------AEGYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 1125487139 322 LNVIEVLLPPL 332
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
12-124 2.57e-24

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: 97.57  E-value: 2.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQFRLVVASA 124
Cdd:cd17550    81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERA 113
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
13-111 4.56e-24

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: 96.32  E-value: 4.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  13 LVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYGS 92
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                          90
                  ....*....|....*....
gi 1125487139  93 AENAVEALRSGAFDYLTKP 111
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
11-126 7.20e-24

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: 96.32  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPD-LRTLYeLTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd17569     2 TILLVDDEPNiLKALK-RLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1125487139  90 YGSAENAVEALRSGA-FDYLTKPVDLKQFRLVVASAAQ 126
Cdd:cd17569    81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
11-111 2.18e-23

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 94.46  E-value: 2.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLRE-GYR-VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMT 88
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEaGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                          90       100
                  ....*....|....*....|...
gi 1125487139  89 AYGSAENAVEALRSGAFDYLTKP 111
Cdd:COG4753    81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
10-114 4.57e-23

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: 93.82  E-value: 4.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
                          90       100
                  ....*....|....*....|....*
gi 1125487139  90 YGSAENAVEALRSGAfdYLTKPVDL 114
Cdd:cd17554    81 YSEYKSDFSSWAADA--YVVKSSDL 103
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
157-383 6.36e-23

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: 102.88  E-value: 6.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 157 ALDAMVGDSPAM-QAVKQriAKVA-----RGMaPVLVHGESGTGKELVARALH--ACSQR---AHGPMVAVNCGAIPEN- 224
Cdd:COG1221   102 PFDNLIGANGSLkNAIEQ--AKAAilyppKGL-HTLILGPTGVGKSFFAELMYeyAIEIGvlpEDAPFVVFNCADYANNp 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 225 -LLEAEFFGARKGSYTGATQDRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLG-SAQEEAADVRIVSATH 302
Cdd:COG1221   179 qLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATT 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 303 RDLAAdvqqgrfrqdlyYRLN--------VIEvlLPPLRER----REDLpalcraLLARLSQES---GLPMpEIDELSVQ 367
Cdd:COG1221   259 EDPES------------SLLKtflrripmVIK--LPSLEERsleeRLEL------IKHFFKEEAkrlNKPI-KVSKEVLK 317
                         250
                  ....*....|....*.
gi 1125487139 368 QIARLPLPGNVRELEN 383
Cdd:COG1221   318 ALLLYDCPGNIGQLKS 333
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
12-126 1.52e-22

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: 92.79  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVE---TAASVGEAREQLQTQRFDVVITDMRLPdGM-GMELLQDLRSQQRRERCVVM 87
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHKPDIVITDIRMP-GMdGLELIEKIRELYPDIKIIIL 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:cd17536    80 SGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
166-331 2.28e-22

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: 93.36  E-value: 2.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 166 PAMQAVKQRIAKVARG--MAPVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEAEFFGarkgsyTGATQ 243
Cdd:cd00009     1 VGQEEAIEALREALELppPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFG------HFLVR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 244 DRDGYFQAARGGTLFLDEIGDLPLAMQAKLLRAIQERRVRPLGSaqeeaADVRIVSATHRDLAadvqqGRFRQDLYYRLN 323
Cdd:cd00009    75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDR-----ENVRVIGATNRPLL-----GDLDRALYDRLD 144

                  ....*...
gi 1125487139 324 vIEVLLPP 331
Cdd:cd00009   145 -IRIVIPL 151
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
12-124 7.71e-21

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: 90.16  E-value: 7.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQFRLVVASA 124
Cdd:COG4566    82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRA 114
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
11-116 7.79e-21

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: 87.71  E-value: 7.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:cd19919    82 SDLDSAVSAYQGGAFEYLPKPFDIDE 107
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
12-115 1.01e-20

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: 87.13  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV--MTA 89
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAiaLTG 80
                          90       100
                  ....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGaFD-YLTKPVDLK 115
Cdd:cd17580    81 YGQPEDRERALEAG-FDaHLVKPVDPD 106
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
12-111 1.18e-20

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: 86.83  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTAYG 91
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR-EWSAVPVIVLSARD 79
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd17620    80 EESDKIAALDAGADDYLTKP 99
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
12-121 5.46e-20

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: 85.21  E-value: 5.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERC---VVMT 88
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRtpiIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125487139  89 AYGSAENAVEALRSGAFDYLTKPVDLKQFRLVV 121
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
12-118 7.86e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 88.33  E-value: 7.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLR-EGYR-VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:COG3279     4 ILIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83
                          90       100
                  ....*....|....*....|....*....
gi 1125487139  90 YgsAENAVEALRSGAFDYLTKPVDLKQFR 118
Cdd:COG3279    84 Y--DEYALEAFEVNAVDYLLKPIDEERLA 110
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
12-111 9.11e-20

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: 84.99  E-value: 9.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQR-RERCVVM-TA 89
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMtRDIPIIMlTA 82
                          90       100
                  ....*....|....*....|..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKP 111
Cdd:cd17618    83 RGEEEDKVRGLEAGADDYITKP 104
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
12-118 8.55e-19

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: 81.91  E-value: 8.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLR-EGYRV-ETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd19925     3 VLIVEDDPMVAEIHRAYVEQvPGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82
                          90       100
                  ....*....|....*....|....*....
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFR 118
Cdd:cd19925    83 ANDVETVREALRLGVVDYLIKPFTFERLR 111
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
12-115 1.29e-18

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: 81.38  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                          90       100
                  ....*....|....*....|....
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLK 115
Cdd:cd17624    81 GVDDRVAGLDAGADDYLVKPFALE 104
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
12-112 1.49e-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: 81.00  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQR-RERCVVM-TA 89
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPEtRHIPVIMiTA 81
                          90       100
                  ....*....|....*....|...
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPV 112
Cdd:cd17538    82 LDDREDRIRGLEAGADDFLSKPI 104
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
10-119 6.65e-18

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: 79.41  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGY-RVETAASVGEAREQLQTQRFDVVITDMRLPdGM-GMELLQDLRSQQRRERC--V 85
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMP-GMdGLEFIRRLRALPGLEDVpiV 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1125487139  86 VMTAYGSAENAVEALRSGAFDYLTKPVDLKQFRL 119
Cdd:cd17551    80 MITADTDREVRLRALEAGATDFLTKPFDPVELLA 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
10-112 1.08e-17

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: 78.78  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80
                          90       100
                  ....*....|....*....|...
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPV 112
Cdd:cd17555    81 AGVMSDAVEALRLGAWDYLTKPI 103
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
12-122 2.38e-17

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: 77.78  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQfrlVVA 122
Cdd:cd17615    82 SVEDRIAGLTAGGDDYVTKPFSLEE---VVA 109
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
13-111 2.95e-17

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: 77.70  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  13 LVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVM--TAY 90
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIImlTAK 80
                          90       100
                  ....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKP 111
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKP 101
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
12-118 1.35e-16

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: 75.74  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQL--QTQRFDVVITDMRLPDGMGMELLQDLRSQqRRERCVVMTA 89
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                          90       100
                  ....*....|....*....|....*....
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFR 118
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
13-119 1.46e-16

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: 75.72  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  13 LVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYGS 92
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                          90       100
                  ....*....|....*....|....*..
gi 1125487139  93 AENAVEALRSGAFDYLTKPVDLKQFRL 119
Cdd:cd17625    81 VEDRVKGLDLGADDYLPKPFSLAELLA 107
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
12-111 1.90e-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: 74.78  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd19935    81 SVEDRVKGLDLGADDYLVKP 100
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
12-110 2.64e-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: 74.86  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPdlrtlyeltLLREGYR-----------VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQR 80
Cdd:cd17535     1 VLIVDDHP---------LVREGLRrllesepdievVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYP 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 1125487139  81 RERCVVMTAYGSAENAVEALRSGAFDYLTK 110
Cdd:cd17535    72 DLKVIVLTAHDDPEYVLRALKAGAAGYLLK 101
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
12-111 3.75e-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: 74.63  E-value: 3.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKP 100
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
11-111 1.40e-15

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 72.76  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGYR-VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQR-RERCVVM- 87
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGAlSHLPVLMv 81
                          90       100
                  ....*....|....*....|....
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKP 111
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKP 105
fixJ PRK09390
response regulator FixJ; Provisional
7-154 1.42e-15

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 75.42  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   7 PAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV 86
Cdd:PRK09390    1 SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVD----LKQFRLVVASAAQGVGGVPAPGVMPARSPSVSPAASPVLNG 154
Cdd:PRK09390   81 MTGHGDVPLAVEAMKLGAVDFIEKPFEderlIGAIERALAQAPEAAKSEAVAADIRARIASLSERERQVMDG 152
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
10-113 1.54e-15

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: 72.63  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTlyELTLLRE--GYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVM 87
Cdd:cd17537     1 ATVYVVDDDEAVRD--SLAFLLRsvGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFI 78
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17537    79 TGHGDVPMAVEAMKAGAVDFLEKPFR 104
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
12-111 1.30e-14

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: 69.71  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRER--CVVMTA 89
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTipVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKP 111
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
12-112 1.42e-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: 69.46  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPD-LRTLYELtLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV--MT 88
Cdd:cd19920     1 ILIVDDVPDnLRLLSEL-LRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVifLT 79
                          90       100
                  ....*....|....*....|....
gi 1125487139  89 AYGSAENAVEALRSGAFDYLTKPV 112
Cdd:cd19920    80 ALTDTEDKVKGFELGAVDYITKPF 103
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
10-122 1.70e-14

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: 69.64  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLR--SQQRRERCVVM 87
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRklPAYKFTPILML 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVA 122
Cdd:cd17562    81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
12-123 2.79e-14

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: 69.12  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQFRLVVAS 123
Cdd:cd17553    83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKK 114
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
12-111 3.07e-14

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: 68.68  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd19928    81 TLMTAVKAAERGAFEYLPKP 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
10-116 5.64e-14

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: 68.18  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTA 89
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR-EQSEVGIILVTG 79
                          90       100
                  ....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:cd17619    80 RDDEVDRIVGLEIGADDYVTKPFNPRE 106
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
9-124 5.87e-14

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 70.37  E-value: 5.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   9 AASILVVDDEPDLRTLYELTLLREGYRV-ETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLrSQQRRERCVVM 87
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI-SEERPAPVILL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASA 124
Cdd:COG3707    82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELA 118
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
11-126 6.69e-14

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: 68.55  E-value: 6.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPdlRTLYELT-LLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd17596     2 TILVVDDEV--RSLEALRrTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1125487139  90 YGSAENAVEALR-SGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:cd17596    80 YTDSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAAR 117
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
12-126 1.30e-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: 67.18  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTlyELT-LLREGYRVETAASVG---EAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVM 87
Cdd:cd17532     1 ALIVDDEPLARE--ELRyLLEEHPDIEIVGEAEngeEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFV 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1125487139  88 TAYgsAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:cd17532    79 TAY--DEYAVEAFELNAVDYLLKPFSEERLAEALAKLRK 115
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
12-123 1.90e-13

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: 66.79  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV--MTA 89
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPViaLTA 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQFRLVVAS 123
Cdd:cd17548    82 YAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
PRK10643 PRK10643
two-component system response regulator PmrA;
12-117 2.12e-13

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 69.29  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQF 117
Cdd:PRK10643   83 TLEDRVAGLDVGADDYLVKPFALEEL 108
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
12-116 3.44e-13

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: 65.87  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100
                  ....*....|....*....|....*
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:cd17627    81 SVSDRVAGLDAGADDYLVKPFALEE 105
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
12-111 4.32e-13

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: 65.16  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTAYG 91
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR-QKSTLPVIFLTSKD 79
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:cd19936    80 DEIDEVFGLRMGADDYITKP 99
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
11-64 4.71e-13

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: 63.74  E-value: 4.71e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1125487139   11 SILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLP 64
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
9-159 4.73e-13

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 68.59  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   9 AASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQ--QRRERCVV 86
Cdd:PRK10161    2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKREsmTRDIPVVM 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQGVGGVPAPGVMPARSPSVSPAASPVLNGSGALD 159
Cdd:PRK10161   82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLDPTSHRVMAGEEPLE 154
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
10-156 8.04e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 67.91  E-value: 8.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTA 89
Cdd:PRK10529    2 TNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR-QWSAIPVIVLSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVdlkqfrlvvasaaqGVGGVPAPGVMPARSPSVSPAASPVLNGSG 156
Cdd:PRK10529   81 RSEESDKIAALDAGADDYLSKPF--------------GIGELQARLRVALRRHSATPAPDPLVKFSD 133
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
12-111 8.62e-13

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: 64.75  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsqQRRERCVVM-TAY 90
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR--KTSNVPIIMlTAK 78
                          90       100
                  ....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKP 111
Cdd:cd17614    79 DSEVDKVLGLELGADDYVTKP 99
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
12-111 1.51e-12

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: 64.46  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQR-FDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGIS 82
                          90       100
                  ....*....|....*....|...
gi 1125487139  91 GSAENAVEA--LRSGAFDYLTKP 111
Cdd:cd17544    83 ASGDNALSArfIKAGANDFLTKP 105
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
12-113 2.45e-12

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: 63.45  E-value: 2.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYR-VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82
                          90       100
                  ....*....|....*....|...
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17542    83 GQEEMVKEAIKAGAKDFIVKPFQ 105
PRK10816 PRK10816
two-component system response regulator PhoP;
12-116 5.08e-12

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 65.53  E-value: 5.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                          90       100
                  ....*....|....*....|....*
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:PRK10816   83 SWQDKVEVLSAGADDYVTKPFHIEE 107
PRK10766 PRK10766
two-component system response regulator TorR;
11-121 5.63e-12

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 65.44  E-value: 5.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRErCVVMTAY 90
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVG-IILVTGR 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVDLKQfrLVV 121
Cdd:PRK10766   83 TDSIDRIVGLEMGADDYVTKPLELRE--LLV 111
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
12-111 5.73e-12

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: 62.13  E-value: 5.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQR-FDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                          90       100
                  ....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKP 111
Cdd:cd18160    82 AAAAPELLSDAVGDNATLKKP 102
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
10-124 6.55e-12

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: 62.42  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRV-ETAASVGEAREQLQTQRFDVVITDMRLPDGM-GMELLQDLRsQQRRERCVVM 87
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKGDMdGIEAAREIR-EKFDIPVIFL 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASA 124
Cdd:cd17534    80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELA 116
ompR PRK09468
osmolarity response regulator; Provisional
12-111 7.02e-12

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 65.38  E-value: 7.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAKG 87
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:PRK09468   88 EEVDRIVGLEIGADDYLPKP 107
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
12-113 7.33e-12

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: 62.04  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAaSVGEAREQL-QTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAY 90
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTT-DLGEEGLDLgKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGL 79
                          90       100
                  ....*....|....*....|...
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17616    80 ADIEDKVKGLGFGADDYMTKPFH 102
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
12-112 1.14e-11

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: 61.21  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQ-TQRFDVVITDMRLPDGM-GMELLQDLRSQQRRERCVVMTa 89
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLEsGPDIDLLVTDVIMPGGMnGSQLAEEARRRRPDLKVLLTS- 79
                          90       100
                  ....*....|....*....|....
gi 1125487139  90 yGSAENAVEALRSGA-FDYLTKPV 112
Cdd:cd18161    80 -GYAENAIEGGDLAPgVDVLSKPF 102
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
12-118 2.12e-11

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: 60.74  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGY-RVETAASVGEAREQLQTQRFDVVITDMRLPDGM-GMELLQDLRSQQ--RRERCVVM 87
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKGKnGQQLLEELRHKKliSPSTVFIM 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1125487139  88 -TAYGSAENAVEALRSGAFDYLTKPVDLKQFR 118
Cdd:cd17589    81 vTGESSRAMVLSALELEPDDYLLKPFTVSELR 112
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
12-115 2.16e-11

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: 60.91  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                          90       100
                  ....*....|....*....|....
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLK 115
Cdd:cd17573    81 KTEQEIEAFKEGADDYIAKPFDFK 104
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
12-113 2.52e-11

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: 60.78  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsqQRRERCVVM-TAY 90
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR--KTSQVPVLMlTAR 78
                          90       100
                  ....*....|....*....|...
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17623    79 GDDIDRILGLELGADDYLPKPFN 101
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
184-322 2.65e-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: 61.62  E-value: 2.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  184 PVLVHGESGTGKELVARALHACSQRAHGPMVAVNCGAIPENLLEA---EFFGARKGSYTGATQDRDGyFQAARG---GTL 257
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLA-LALARKlkpDVL 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125487139  258 FLDEIGDLPLAMQAKLLRAIQERRvrpLGSAQEEAADVRIVSATHR--DLAADVQQGRFRQDLYYRL 322
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELR---LLLLLKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLL 146
PRK15347 PRK15347
two component system sensor kinase;
1-126 4.44e-11

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 65.43  E-value: 4.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   1 MPLnsLPAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLR-SQQ 79
Cdd:PRK15347  684 LPL--QPWQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRdDPN 761
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1125487139  80 RRER-C--VVMTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:PRK15347  762 NLDPdCmiVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAE 811
pleD PRK09581
response regulator PleD; Reviewed
10-113 5.26e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 64.54  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQR-RERCVVM- 87
Cdd:PRK09581    3 ARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPAtTHIPVVMv 82
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVD 113
Cdd:PRK09581   83 TALDDPEDRVRGLEAGADDFLTKPIN 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
12-113 9.43e-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: 59.10  E-value: 9.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLRE-GYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRER--CVVMT 88
Cdd:cd17552     4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSipVILLT 83
                          90       100
                  ....*....|....*....|....*
gi 1125487139  89 AYGSAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17552    84 AKAQPSDRQRFASLGVAGVIAKPFD 108
orf27 CHL00148
Ycf27; Reviewed
12-111 3.69e-10

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 60.12  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQrrERCVVM-TAY 90
Cdd:CHL00148    9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES--DVPIIMlTAL 86
                          90       100
                  ....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKP 111
Cdd:CHL00148   87 GDVSDRITGLELGADDYVVKP 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
12-117 4.72e-10

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: 57.07  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISGDRR 81
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQF 117
Cdd:cd17594    82 DEIDRVVGLELGADDYLAKPFGLREL 107
PRK15479 PRK15479
transcriptional regulator TctD;
12-116 4.82e-10

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 59.73  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82
                          90       100
                  ....*....|....*....|....*
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:PRK15479   83 AVADRVKGLNVGADDYLPKPFELEE 107
dpiA PRK10046
two-component response regulator DpiA; Provisional
11-112 5.76e-10

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 59.65  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLY-ELTLLREGY-RVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMT 88
Cdd:PRK10046    6 TLLIVEDETPLAEMHaEYIRHIPGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTT 85
                          90       100
                  ....*....|....*....|....
gi 1125487139  89 AYGSAENAVEALRSGAFDYLTKPV 112
Cdd:PRK10046   86 AASDMETVSEAVRCGVFDYLIKPI 109
PRK10610 PRK10610
chemotaxis protein CheY;
13-111 8.80e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 56.91  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  13 LVVDDEPDLRTLYElTLLRE-GYR-VETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVM--T 88
Cdd:PRK10610    9 LVVDDFSTMRRIVR-NLLKElGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLmvT 87
                          90       100
                  ....*....|....*....|...
gi 1125487139  89 AYGSAENAVEALRSGAFDYLTKP 111
Cdd:PRK10610   88 AEAKKENIIAAAQAGASGYVVKP 110
PRK10336 PRK10336
two-component system response regulator QseB;
12-114 1.14e-09

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 58.37  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK10336    3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                          90       100
                  ....*....|....*....|...
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDL 114
Cdd:PRK10336   83 ALAERVEGLRLGADDYLCKPFAL 105
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
5-217 3.19e-09

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 59.75  E-value: 3.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139    5 SLPAAASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERC 84
Cdd:PRK09959   954 TLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   85 VVMTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVASAAQGVGGVPApgvmparspsvspaaspvlngSGALDamvgd 164
Cdd:PRK09959  1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQ---------------------YRHLD----- 1087
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125487139  165 spaMQAVKQRIAKVARGMAPVLVHGESGTGKELVA----------RALHACSQRAHGPMVAVN 217
Cdd:PRK09959  1088 ---IEALKNNTANDLQLMQEILMTFQHETHKDLPAafhaleagdnRTFHQCIHRIHGAANILN 1147
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
12-113 4.29e-09

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: 54.31  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRErCVVMTAYG 91
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGP-ILLLTALD 81
                          90       100
                  ....*....|....*....|..
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17622    82 SDIDHILGLELGADDYVVKPVE 103
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
9-114 5.19e-09

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 56.58  E-value: 5.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   9 AASILVVDDEPDLRT-LYELTLLREGYRVETAASVGEAREQLQTQ-RFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV 86
Cdd:PRK10651    6 PATILLIDDHPMLRTgVKQLISMAPDITVVGEASNGEQGIELAESlDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVV 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTK---PVDL 114
Cdd:PRK10651   86 FSVSNHEEDVVTALKRGADGYLLKdmePEDL 116
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
12-116 1.16e-08

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: 53.19  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEP----DLRTLYEltllREGYRVETAASVG-EAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVV 86
Cdd:cd19932     3 VLIAEDEAlirmDLREMLE----EAGYEVVGEASDGeEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT-SENIAPIVL 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:cd19932    78 LTAYSQQDLVERAKEAGAMAYLVKPFSESD 107
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
12-115 1.17e-08

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 53.10  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV--MTA 89
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVilLTT 80
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLK 115
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYDEK 106
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
12-111 1.35e-08

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: 53.16  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGyRVE---TAASVGEAREQLQTQRFDVVITDMRLPdGM-GMELLQDLRSQQRReRCVVM 87
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDP-DIEvvgTARDGEEALEKIKELKPDVITLDIEMP-VMdGLEALRRIMAERPT-PVVMV 79
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  88 TAYGS--AENAVEALRSGAFDYLTKP 111
Cdd:cd17541    80 SSLTEegAEITLEALELGAVDFIAKP 105
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
12-111 1.43e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 55.58  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASvGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTAYG 91
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHD-GEQALDLLDDSIDLLLLDVMMPKKNGIDTLKELR-QTHQTPVIMLTARG 81
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:PRK10955   82 SELDRVLGLELGADDYLPKP 101
PRK13557 PRK13557
histidine kinase; Provisional
12-111 1.62e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 56.99  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQ-RFDVVITDMRLPDGM-GMELLQDLRSQQRRERCVVMTA 89
Cdd:PRK13557  418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPGGMnGVMLAREARRRQPKIKVLLTTG 497
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  90 YgsAENAVEalRSGA----FDYLTKP 111
Cdd:PRK13557  498 Y--AEASIE--RTDAggseFDILNKP 519
PRK11697 PRK11697
two-component system response regulator BtsR;
11-113 2.84e-08

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 54.47  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTlyELTLLREGYR-VETAASVGEAREQLQT---QRFDVVITDMRLPDGMGMELLQDLRSQqRRERCVV 86
Cdd:PRK11697    3 KVLIVDDEPLARE--ELRELLQEEGdIEIVGECSNAIEAIGAihrLKPDVVFLDIQMPRISGLELVGMLDPE-HMPYIVF 79
                          90       100
                  ....*....|....*....|....*..
gi 1125487139  87 MTAYGsaENAVEALRSGAFDYLTKPVD 113
Cdd:PRK11697   80 VTAFD--EYAIKAFEEHAFDYLLKPID 104
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
12-111 3.21e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 54.20  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK11083    6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTARS 85
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:PRK11083   86 DEVDRLVGLEIGADDYVAKP 105
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
3-116 3.75e-08

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 56.14  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139   3 LNSLPAAAS---------ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQ 73
Cdd:PRK10841  786 ANALPSTDKavsdnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQ 865
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1125487139  74 DLRSQQRRERCVVMTAYGSAENAVEALRSGAFDYLTKPV---DLKQ 116
Cdd:PRK10841  866 RLRQLGLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVtldVLKQ 911
PRK14084 PRK14084
DNA-binding response regulator;
12-126 4.61e-08

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 53.99  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRT--LYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:PRK14084    3 ALIVDDEPLARNelTYLLNEIGGFEEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFATA 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1125487139  90 YGSAenAVEALRSGAFDYLTKPVDLKQFRLVVASAAQ 126
Cdd:PRK14084   83 HDQF--AVKAFELNATDYILKPFEQKRIEQAVNKVRA 117
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
12-82 4.73e-08

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: 51.82  E-value: 4.73e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125487139  12 ILVVDDEPDLRTLYELTLLRE-GYRV-ETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRE 82
Cdd:COG2197     4 VLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLLTPRERE 76
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
12-115 6.36e-08

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: 51.21  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQL-----------QTQRFDVVITDMRLPDGMGMELLQDLR-SQQ 79
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnfNEPKVNMIITDYCMPGMTGYDLLKKVKeSSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1125487139  80 RRERCVVMTaygSAENAVE----ALRSGAFDYLTKPVDLK 115
Cdd:cd17581    81 LKEIPVVIM---SSENIPTrisrCLEEGAEDFLLKPVKLA 117
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
12-111 7.38e-08

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 50.27  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsqQRRERCVVM-TAY 90
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR--ARSNVPVIMvTAK 78
                          90       100
                  ....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKP 111
Cdd:cd17621    79 DSEIDKVVGLELGADDYVTKP 99
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
10-116 9.04e-08

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 50.55  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRErCVVMTA 89
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVP-IVMLTA 79
                          90       100
                  ....*....|....*....|....*..
gi 1125487139  90 YGSAENAVEALRSGAFDYLTKPVDLKQ 116
Cdd:cd17626    80 KSDTVDVVLGLESGADDYVAKPFKPKE 106
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
453-492 1.51e-07

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 47.77  E-value: 1.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1125487139 453 LDERERGILVQALQENGFNRTATAARLGLSLRQIRYRIDR 492
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
12-111 1.84e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 51.85  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:PRK09836   83 TIEHRVKGLELGADDYLVKP 102
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
12-111 2.19e-07

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 49.30  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQ---------TQRFDVVITDMRLPDGMGMELLQDLRSQQRRE 82
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125487139  83 RCVVM--TAYGSAENAVEALRSGAFDYLTKP 111
Cdd:cd19924    81 NIPVIlnSSLSGEFSRARGKKVGADAYLAKF 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
11-123 2.36e-07

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: 49.72  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGYRVE-TAASVGEA------REQLQTQ--RFDVVITDMRLPDGMGMELLQDLRSQQR- 80
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNElHVVRDGEEaldflrGEGEYADapRPDLILLDLNMPRMDGFEVLREIKADPDl 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1125487139  81 RERCVVM-TAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVVAS 123
Cdd:cd17557    81 RRIPVVVlTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
12-119 1.05e-06

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: 48.10  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEP--------DLRTLYeltllREGYRVETAASVGEAREQLQ--TQRFDVV---ITDMRLPDGMGMELLQ---DL 75
Cdd:cd17595     3 ILTVDDDPqvlravarDLRRQY-----GKDYRVLRADSGAEALDALKelKLRGEAValfLVDQRMPEMDGVEFLEkamEL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1125487139  76 RSQQRRercVVMTAYGSAENAVEALRSGAFD-YLTKPVDLKQFRL 119
Cdd:cd17595    78 FPEAKR---VLLTAYADTDAAIRAINDVQLDyYLLKPWDPPEEKL 119
PRK11173 PRK11173
two-component response regulator; Provisional
12-111 3.64e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 48.09  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEP----DLRTLYEltllREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVM 87
Cdd:PRK11173    6 ILIVEDELvtrnTLKSIFE----AEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR-EQANVALMFL 80
                          90       100
                  ....*....|....*....|....
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKP 111
Cdd:PRK11173   81 TGRDNEVDKILGLEIGADDYITKP 104
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
12-111 6.21e-06

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: 45.08  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDlrTLYELT-LLRE-GYRVETAASVGEAREQLQTQRF--DVVITDMRLPDGMGMELLQDLRSQQRRER--CV 85
Cdd:cd17582     1 VLLVENDDS--TRQIVTaLLRKcSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNipVI 78
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  86 VMTAYGSAENAVEALRSGAFDYLTKP 111
Cdd:cd17582    79 MMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
12-110 6.59e-06

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 45.42  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRT-LYELTLLREGYRVETAASVGEAREQL-QTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd19931     1 VLLIDDHPLLRKgIKQLIELDPDFTVVGEASSGEEGIELaERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                          90       100
                  ....*....|....*....|.
gi 1125487139  90 YGSAENAVEALRSGAFDYLTK 110
Cdd:cd19931    81 SDAEDDVVTALRAGADGYLLK 101
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
12-111 1.31e-05

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: 44.29  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsqQRRERCVVM-TAY 90
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR--RFSDVPIIMvTAR 79
                          90       100
                  ....*....|....*....|.
gi 1125487139  91 GSAENAVEALRSGAFDYLTKP 111
Cdd:cd19938    80 VEEIDRLLGLELGADDYICKP 100
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
12-114 1.39e-05

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: 44.19  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTAYG 91
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR-QISNVPIIFISSRD 79
                          90       100
                  ....*....|....*....|...
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDL 114
Cdd:cd18159    80 DNMDQVMAINMGGDDYITKPFDL 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
184-335 1.91e-05

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 44.21  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 184 PVLVHGESGTGK-ELVARALHACSQRahgPMVAVNCgaiPENLLEAEFFGARKgSYTGATQDRDG--YFQAARGGTLFLD 260
Cdd:pfam07728   1 GVLLVGPPGTGKtELAERLAAALSNR---PVFYVQL---TRDTTEEDLFGRRN-IDPGGASWVDGplVRAAREGEIAVLD 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125487139 261 EIGDLPLAMQAKLLRAIQERRVRPL---GSAQEEAADVRIVSATHrdlaadvqqgrfrqDLYYRLNvieVLLPPLRER 335
Cdd:pfam07728  74 EINRANPDVLNSLLSLLDERRLLLPdggELVKAAPDGFRLIATMN--------------PLDRGLN---ELSPALRSR 134
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
12-152 1.97e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 46.68  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLyeLT-LLREGYRVETAASVG---EAREQLQTQRFDVVITDMRLP--DGmgmelLQDLRSQQRRERC- 84
Cdd:PRK00742    6 VLVVDDSAFMRRL--ISeILNSDPDIEVVGTAPdglEAREKIKKLNPDVITLDVEMPvmDG-----LDALEKIMRLRPTp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  85 VVM----TAYGsAENAVEALRSGAFDYLTKPV-----DLKQFR--LV--VASAAQ----GVGGVPAPGVMPARSPSVSPA 147
Cdd:PRK00742   79 VVMvsslTERG-AEITLRALELGAVDFVTKPFlgislGMDEYKeeLAekVRAAARarvrALPPRAAAAARAAAAAPAALA 157

                  ....*
gi 1125487139 148 ASPVL 152
Cdd:PRK00742  158 AAPLL 162
PRK13856 PRK13856
two-component response regulator VirG; Provisional
12-117 4.65e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 44.80  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:PRK13856    4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKSDVPIIIISGDRL 83
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  92 SAENAVEALRSGAFDYLTKPVDLKQF 117
Cdd:PRK13856   84 EEADKVVALELGATDFIAKPFGTREF 109
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
12-141 5.03e-05

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 44.63  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRErCVVMTAYG 91
Cdd:PRK10701    4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQGP-IVLLTSLD 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125487139  92 SAENAVEALRSGAFDYLTK----PVDLKQFRLVV--ASAAQGVGGVPAPGVMPARS 141
Cdd:PRK10701   83 SDMNHILALEMGACDYILKttppAVLLARLRLHLrqNEQATQTKGLQETSLTPYKA 138
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
12-110 5.41e-05

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 42.64  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLR-TLYELTLLREGYRVETAASVG-EAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd19930     1 VLIAEDQEMVRgALAALLELEDDLEVVAQASNGqEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                          90       100
                  ....*....|....*....|.
gi 1125487139  90 YGSAENAVEALRSGAFDYLTK 110
Cdd:cd19930    81 FGRPGYFRRALAAGVDGYVLK 101
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
11-122 7.28e-05

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: 42.36  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRsQQRRERCVVMTAY 90
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR-EHSHVPILMLTAR 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1125487139  91 GSAENAVEALRSGAFDYLTKPVdlkQFRLVVA 122
Cdd:cd19939    80 TEEMDRVLGLEMGADDYLCKPF---SPRELLA 108
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
10-114 8.85e-05

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 43.71  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  10 ASILVVDDEPDLRTLYELtLLREGYRVETAASVGEAREQ---LQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVV 86
Cdd:PRK09935    4 ASVIIMDTHPIIRMSIEV-LLQKNSELQIVLKTDDYRITidyLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLF 82
                          90       100
                  ....*....|....*....|....*...
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDL 114
Cdd:PRK09935   83 LSSKSECFYAGRAIQAGANGFVSKCNDQ 110
PRK11517 PRK11517
DNA-binding response regulator HprR;
12-111 9.16e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 43.73  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRErCVVMTAYG 91
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQTP-VICLTARD 81
                          90       100
                  ....*....|....*....|
gi 1125487139  92 SAENAVEALRSGAFDYLTKP 111
Cdd:PRK11517   82 SVDDRVRGLDSGANDYLVKP 101
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
11-116 9.30e-05

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 45.23  E-value: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEP-DLRTLYelTLLREgyRVET--AASVG-EAREQLQTQRFDVVITDMRLPDGMGMELLQDLR--SQQRRERC 84
Cdd:PRK11107  669 TVMAVDDNPaNLKLIG--ALLEE--QVEHvvLCDSGhQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRqlPHNQNTPI 744
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125487139  85 VVMTAYGSAENAVEALRSGAFDYLTKPVD---LKQ 116
Cdd:PRK11107  745 IAVTAHAMAGERERLLSAGMDDYLAKPIDeamLKQ 779
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
12-111 2.23e-04

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 40.67  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDL-RTLYELTLLREGYRVETAASVG-EAREQLQTQRFDVVITDMRLP--DGMG-MELLQDLRsQQRRERCVV 86
Cdd:cd17561     4 VLIADDNREFvQLLEEYLNSQPDMEVVGVAHNGqEALELIEEKEPDVLLLDIIMPhlDGIGvLEKLRRMR-LEKRPKIIM 82
                          90       100
                  ....*....|....*....|....*
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKP 111
Cdd:cd17561    83 LTAFGQEDITQRAVELGASYYILKP 107
PRK10430 PRK10430
two-component system response regulator DcuR;
12-117 2.87e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 42.40  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLR-EGYR-VETAASVGEAREQLQ--TQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVM 87
Cdd:PRK10430    4 VLIVDDDAMVAELNRRYVAQiPGFQcCGTASTLEQAKEIIFnsDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSDVIVI 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTKPVDLKQF 117
Cdd:PRK10430   84 SSAADAATIKDSLHYGVVDYLIKPFQASRF 113
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
12-111 3.95e-04

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: 39.66  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLR-SQQRRERCVVMTay 90
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRkSSALKDTPIIML-- 78
                          90       100
                  ....*....|....*....|....
gi 1125487139  91 GSAENAVEALRS---GAFDYLTKP 111
Cdd:cd17602    79 TGKDGLVDRIRAkmaGASGYLTKP 102
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
12-113 6.06e-04

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: 39.60  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPdlrTLYE--LTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQR-RERCVVMT 88
Cdd:cd17539     1 VLLVDDRP---SSAEriAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERtRQLPILAV 77
                          90       100
                  ....*....|....*....|....*.
gi 1125487139  89 A-YGSAENAVEALRSGAFDYLTKPVD 113
Cdd:cd17539    78 AdPGDRGRLIRALEIGVNDYLVRPID 103
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
44-113 1.29e-03

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: 38.67  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125487139  44 EAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYGSAEnAVEALRS-GAFDYLTKPVD 113
Cdd:cd17593    36 EALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSGDVQPE-AKERVLElGALAFLKKPFD 105
PRK10693 PRK10693
two-component system response regulator RssB;
38-118 1.99e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 40.36  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  38 TAASVG-EAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYGSAENAVEALRSGAFDYLTKPV-DLK 115
Cdd:PRK10693    1 VLAANGvDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVkDLN 80

                  ...
gi 1125487139 116 QFR 118
Cdd:PRK10693   81 RLR 83
PRK15369 PRK15369
two component system response regulator;
11-110 2.28e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 39.68  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDD-EPDLRTLYELTLLREGYRVETAASVG-EAREQLQTQRFDVVITDMRLPdGM-GMELLQDLRSQQRRERCVVM 87
Cdd:PRK15369    5 KILLVDDhELIINGIKNMLAPYPRYKIVGQVDNGlEVYNACRQLEPDIVILDLGLP-GMnGLDVIPQLHQRWPAMNILVL 83
                          90       100
                  ....*....|....*....|...
gi 1125487139  88 TAYGSAENAVEALRSGAFDYLTK 110
Cdd:PRK15369   84 TARQEEHMASRTLAAGALGYVLK 106
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
12-121 4.27e-03

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: 37.38  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQT--QRFDVVITDMRLPDGMGMEL---LQDLRSQQRRERCVV 86
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEValrIRKLFGRRERPLIVA 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125487139  87 MTAYGSAENAVEALRSGAFDYLTKPVDLKQFRLVV 121
Cdd:cd19933    83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
12-112 6.92e-03

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: 36.30  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  12 ILVVDDEPDLRTLYELTLLREGYRVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTAYG 91
Cdd:cd19922     1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHWE 80
                          90       100
                  ....*....|....*....|.
gi 1125487139  92 SAENAVEALRSGAFDYLTKPV 112
Cdd:cd19922    81 DLQEELEEVQRFAVSYVVKPV 101
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
11-125 7.19e-03

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: 36.65  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLRTLYELTLLREGY-RVETAASVGEAREQLQTQRFDVVITDMRLPDGMGMELLQDLRSQQRRERCVVMTA 89
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1125487139  90 YG-----SAENAVEALRSGAFDYLTKPVDLKQFRLVVASAA 125
Cdd:cd17530    82 LDggileSAETLAGANGLNLLGTLSKPFSPEELTELLTKYT 122
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
185-262 7.47e-03

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 36.80  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139 185 VLVHGESGTGKELVARALhacSQRAHGPMVAVNCGAIpenlleaeffgarKGSYTGATQDR-DGYFQAARGGT---LFLD 260
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV---AKELGAPFIEISGSEL-------------VSKYVGESEKRlRELFEAAKKLApcvIFID 64

                  ..
gi 1125487139 261 EI 262
Cdd:pfam00004  65 EI 66
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
11-183 8.62e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 38.32  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  11 SILVVDDEPDLR-TLYELTLLREGYRVETAASVG-EAREQLQTQRFDVVITDMRLPDGMGMELLQdlRSQQRRERCVVMT 88
Cdd:PRK12555    2 RIGIVNDSPLAVeALRRALARDPDHEVVWVATDGaQAVERCAAQPPDVILMDLEMPRMDGVEATR--RIMAERPCPILIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125487139  89 AYGSAENAV---EALRSGAFDYLTKPV-------DLKQFRLV--VASAAQGVGGVPAPGVMPARSPSVSPAASPVL---- 152
Cdd:PRK12555   80 TSLTERNASrvfEAMGAGALDAVDTPTlgigaglEEYAAELLakIDQIGRLLGRRLAPAAAPAAASAAPFRTTPRLvaig 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1125487139 153 ---NGSGALDAMVG----DSPAMQAVKQRI-AKVARGMA 183
Cdd:PRK12555  160 asaGGPAALAVLLGglpaDFPAAIVIVQHVdAAFAAGMA 198
 
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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