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Conserved domains on  [gi|1509073841|ref|WP_122554744|]
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MULTISPECIES: sigma-54 dependent transcriptional regulator [Pseudomonas]

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, ...
1-443 0e+00

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


:

Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 528.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVKPFEPKALIELVAR---HALGVISASEGEGPIAFEPASAQLLELAARVARSDSTVLIS 157
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERaleRRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 158 GESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLG 237
Cdd:COG2204   161 GESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 238 LQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLN 317
Cdd:COG2204   241 LQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 318 NHVKKMKHaQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDfclamgsgaaplptlapapmvaeieta 397
Cdd:COG2204   321 RFAAELGK-PVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAED--------------------------- 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1509073841 398 gaLGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:COG2204   373 --LPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-443 0e+00

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 528.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVKPFEPKALIELVAR---HALGVISASEGEGPIAFEPASAQLLELAARVARSDSTVLIS 157
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERaleRRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 158 GESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLG 237
Cdd:COG2204   161 GESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 238 LQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLN 317
Cdd:COG2204   241 LQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 318 NHVKKMKHaQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDfclamgsgaaplptlapapmvaeieta 397
Cdd:COG2204   321 RFAAELGK-PVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAED--------------------------- 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1509073841 398 gaLGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:COG2204   373 --LPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-441 3.26e-133

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 391.90  E-value: 3.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKALiELVARHALGV-------------ISASEGEGPI-AFEPASAQLLELAARVAR 149
Cdd:PRK11361   86 AEVETAVEALRCGAFDYVIKPFDLDEL-NLIVQRALQLqsmkkeirhlhqaLSTSWQWGHIlTNSPAMMDICKDTAKIAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 150 SDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLD 229
Cdd:PRK11361  165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 230 EISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADII 309
Cdd:PRK11361  245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 310 PLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFclamgsgaaPLPTLAPAP 389
Cdd:PRK11361  325 LLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDL---------PPQIRQPVC 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1509073841 390 MVAEIETAGA----LGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKL 441
Cdd:PRK11361  396 NAGEVKTAPVgernLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKL 451
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
5-441 1.44e-125

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 372.53  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVAR---HALGVISASEGEGP-------IAFEPASAQLLELAARVARSDSTV 154
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERalaHAQEQVALPADAGEaedsaelIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 155 LISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEM 234
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 235 PLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAER 314
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 315 LLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCLAMgsGAAPLPTLAPAPMVAE- 393
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAEL--ALTGRPASAPDSDGQDs 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1509073841 394 ----IET----------AGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKL 441
Cdd:TIGR01818 399 wdeaLEAwakqalsrgeQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKL 460
Sigma54_activat pfam00158
Sigma-54 interaction domain;
131-296 9.73e-104

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 305.87  E-value: 9.73e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 131 IAFEPASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGA 210
Cdd:pfam00158   2 IGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 211 IAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYR 290
Cdd:pfam00158  82 DSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYYR 161

                  ....*.
gi 1509073841 291 LSVFPL 296
Cdd:pfam00158 162 LNVIPI 167
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
6-447 8.88e-100

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 308.34  E-value: 8.88e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA--- 82
Cdd:NF038308   30 VALCQQPDLPVDRLELLHDRRDRALAERVAADIEEVSPETEVRLVPVVLRDPWDFEEVYGALLDFARAYPFDTENEDylv 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  83 ------HGA---VERAVDAMRQGAaDYLVKPFEPK------ALIEL-VARH-ALGVISASEGEGPIAFE--------PAS 137
Cdd:NF038308  110 hittgtHVAqicWFLLVEARYLPA-RLLQTSPPRDkeegtyEIIDLdLSRYdALAQRFAREQAEAVSFLksgiatrnAAF 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 138 AQLLELAARVA-RSDSTVLISGESGTGKEVLARYIHQQSTRA---KQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAA 213
Cdd:NF038308  189 NRLIEQIERVAlRSRAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVKGAFTGAQAD 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 214 QAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSV 293
Cdd:NF038308  269 RAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINL 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 294 FPLAWRPLRERPADIIPLAERLLNNHVKKMKH-----AQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQP 368
Cdd:NF038308  349 WTFRLPGLRERREDIEPNLDYELDRFARELGRqvrfnKEARFRYLAFATSPEALWPGNFRELSASVTRMATLADGGRITE 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 369 QD-----FCLAMGSGAAPLPTLAPAPMVAEIETAGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISprtlRYKLAQ 443
Cdd:NF038308  429 ELveeeiARLRAAWQSAPAAADDDALADLLGGEQLAELDLFDRVQLAAVLRVCRQSRSLSAAGRRLFGVS----RQQKAS 504

                  ....
gi 1509073841 444 MRDA 447
Cdd:NF038308  505 PNDA 508
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
5-117 9.32e-41

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: 141.86  E-value: 9.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:cd17549    81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRA 113
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
153-291 3.77e-12

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: 63.93  E-value: 3.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  153 TVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEA--TLFGHEKGSFTGAIAAQAGKFEQA---DGGTIL 227
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQllLIIVGGKKASGSGELRLRLALALArklKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509073841  228 LDEISEMPLGLQAKLLRVLQErevERVGARKPIQLDIRVVATTNR--DLAGEVAAGRFREDLFYRL 291
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLL 146
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-443 0e+00

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 528.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVKPFEPKALIELVAR---HALGVISASEGEGPIAFEPASAQLLELAARVARSDSTVLIS 157
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERaleRRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 158 GESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLG 237
Cdd:COG2204   161 GESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 238 LQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLN 317
Cdd:COG2204   241 LQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFLA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 318 NHVKKMKHaQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDfclamgsgaaplptlapapmvaeieta 397
Cdd:COG2204   321 RFAAELGK-PVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAED--------------------------- 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1509073841 398 gaLGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:COG2204   373 --LPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
135-443 8.53e-153

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: 441.52  E-value: 8.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAA- 213
Cdd:COG3829   145 PAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKKGg 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 214 QAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSV 293
Cdd:COG3829   225 KPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNV 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 294 FPLAWRPLRERPADIIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCL 373
Cdd:COG3829   305 IPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPE 384
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 374 AMGSGAAPLPTLAPAPmvaeietagaLGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:COG3829   385 YLLEEAEAASAAEEGS----------LKEALEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKK 444
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-441 3.26e-133

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 391.90  E-value: 3.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKALiELVARHALGV-------------ISASEGEGPI-AFEPASAQLLELAARVAR 149
Cdd:PRK11361   86 AEVETAVEALRCGAFDYVIKPFDLDEL-NLIVQRALQLqsmkkeirhlhqaLSTSWQWGHIlTNSPAMMDICKDTAKIAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 150 SDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLD 229
Cdd:PRK11361  165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 230 EISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADII 309
Cdd:PRK11361  245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 310 PLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFclamgsgaaPLPTLAPAP 389
Cdd:PRK11361  325 LLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDL---------PPQIRQPVC 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1509073841 390 MVAEIETAGA----LGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKL 441
Cdd:PRK11361  396 NAGEVKTAPVgernLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKL 451
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
5-441 1.44e-125

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


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 372.53  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVAR---HALGVISASEGEGP-------IAFEPASAQLLELAARVARSDSTV 154
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERalaHAQEQVALPADAGEaedsaelIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 155 LISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEM 234
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 235 PLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAER 314
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 315 LLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCLAMgsGAAPLPTLAPAPMVAE- 393
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAEL--ALTGRPASAPDSDGQDs 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1509073841 394 ----IET----------AGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKL 441
Cdd:TIGR01818 399 wdeaLEAwakqalsrgeQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKL 460
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
3-443 4.55e-115

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 345.09  E-value: 4.55e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:PRK10365    6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPFEPKALIELVAR---HA------LGVISASEGeGPIAFEPASAQLLELAARVARSDST 153
Cdd:PRK10365   86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKalaHThsidaeTPAVTASQF-GMVGKSPAMQHLLSEIALVAPSEAT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 154 VLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISE 233
Cdd:PRK10365  165 VLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 234 MPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAE 313
Cdd:PRK10365  245 ISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAG 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 314 RLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCLAMGSGAAPL-PTLAPAPMVa 392
Cdd:PRK10365  325 HFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLgQSQDIQPLV- 403
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1509073841 393 EIETagalgddlrrrefQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:PRK10365  404 EVEK-------------EVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
5-433 1.91e-110

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 339.18  E-value: 1.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVvsdvnmpgmdGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:COG3284   212 RLRLHFLPEFLGSLSEGLLAFDEDGRIVAANRAARRLLGLADAALL----------GRPLEELFGLDLEALPDGARRAPA 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  85 AVERAVDamRQGAADYlvkpfepkALIELVARHALGVISASEGEGPIAFE------PASAQLLELAARVARSDSTVLISG 158
Cdd:COG3284   282 SPRPLRL--RDGRRLG--------ALLRLRPARRAARAAPAGAPAPAALAalaggdPAMRRALRRARRLADRDIPVLILG 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 159 ESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIA-AQAGKFEQADGGTILLDEISEMPLG 237
Cdd:COG3284   352 ETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRkGRPGKIEQADGGTLFLDEIGDMPLA 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 238 LQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERpADIIPLAERLLN 317
Cdd:COG3284   432 LQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLR 510
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 318 NHVKkmKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDfclamgsgaapLPTLAPAPMVAEIETA 397
Cdd:COG3284   511 ELAA--GRGPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITVED-----------LPDELRAELAAAAPAA 577
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1509073841 398 GALGDDLRRREFQMIIDTLRSERGRRKEAAERLGIS 433
Cdd:COG3284   578 AAPLTSLEEAERDAILRALRACGGNVSAAARALGIS 613
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
118-443 3.47e-108

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 329.44  E-value: 3.47e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 118 ALGVISASEGEgPIAFEPASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEA 197
Cdd:PRK05022  178 FLRQEALKEGE-MIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAES 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 198 TLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGE 277
Cdd:PRK05022  257 ELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREE 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 278 VAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRA 357
Cdd:PRK05022  337 VRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRA 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 358 LIL----QQGG--LIQPQDFCLAMGSgAAPLPTLAPAPMVAEIETAGALGDDLRRrefQMIIDTLRSERGRRKEAAERLG 431
Cdd:PRK05022  417 ALLararGAGRivTLEAQHLDLPAEV-ALPPPEAAAAPAAVVSQNLREATEAFQR---QLIRQALAQHQGNWAAAARALE 492
                         330
                  ....*....|..
gi 1509073841 432 ISPRTLrYKLAQ 443
Cdd:PRK05022  493 LDRANL-HRLAK 503
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-444 3.57e-106

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 323.36  E-value: 3.57e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:PRK10923    5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPF---EPKALIELVARH-----------ALGVISASEGEGPiafepASAQLLELAARVAR 149
Cdd:PRK10923   85 SDLDAAVSAYQQGAFDYLPKPFdidEAVALVERAISHyqeqqqprniqVNGPTTDIIGEAP-----AMQDVFRIIGRLSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 150 SDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLD 229
Cdd:PRK10923  160 SSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 230 EISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADII 309
Cdd:PRK10923  240 EIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 310 PLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCLAMGSGAAPLPTLAPAP 389
Cdd:PRK10923  320 RLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQP 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509073841 390 -----MVAEIET-------AGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQM 444
Cdd:PRK10923  400 dswatLLAQWADralrsghQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKEL 466
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
5-437 2.22e-104

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: 317.85  E-value: 2.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLllAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMP-----GMDGHQLLSLLRARQPQLPVLL 79
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSF--ADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEPKAL------------IELVARHALGVISASEGEGPIAFEPASAQLLELAARV 147
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLklivdrafhlytLETENRRLQSALGGTALRGLITSSPGMQKICRTIEKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 148 ARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTIL 227
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 228 LDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPAD 307
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 308 IIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCLamgsgaaplptlaP 387
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLGL-------------D 385
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1509073841 388 APMVAEIETAGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTL 437
Cdd:TIGR02915 386 ARERAETPLEVNLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTL 435
Sigma54_activat pfam00158
Sigma-54 interaction domain;
131-296 9.73e-104

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 305.87  E-value: 9.73e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 131 IAFEPASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGA 210
Cdd:pfam00158   2 IGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 211 IAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYR 290
Cdd:pfam00158  82 DSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYYR 161

                  ....*.
gi 1509073841 291 LSVFPL 296
Cdd:pfam00158 162 LNVIPI 167
PRK15115 PRK15115
response regulator GlrR; Provisional
2-388 5.39e-103

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 314.08  E-value: 5.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   2 AIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:PRK15115    5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKAL---IELVARHALGVISASEGEGPIAFEPASAQLLELAARVARSDSTVLISG 158
Cdd:PRK15115   85 AHGSIPDAVAATQQGVFSFLTKPVDRDALykaIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARMVAQSDVSVLING 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 159 ESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLGL 238
Cdd:PRK15115  165 QSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 239 QAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLNN 318
Cdd:PRK15115  245 QVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLLRQ 324
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 319 HVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDFCLAMGSGAAPLPTLAPA 388
Cdd:PRK15115  325 AAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEA 394
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
135-444 3.69e-102

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: 315.12  E-value: 3.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQ 214
Cdd:TIGR01817 203 PAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQR 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 215 AGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVF 294
Cdd:TIGR01817 283 KGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVV 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 295 PLAWRPLRERPADIIPLAERLLnnhvKKMKHAQAR---LSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQPQDF 371
Cdd:TIGR01817 363 PIFLPPLRERREDIPLLAEAFL----EKFNRENGRpltITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRSDF 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 372 CLAMG---------SGAAPLPTLAPAPMVAEIETAGALGDDL-------RRREFQMIIDTLRSERGRRKEAAERLGISPR 435
Cdd:TIGR01817 439 SCQSGqclspmlakTCPHGHISIDPLAGTTPPHSPASAALPGepglsgpTLSERERLIAALEQAGWVQAKAARLLGMTPR 518

                  ....*....
gi 1509073841 436 TLRYKLAQM 444
Cdd:TIGR01817 519 QVGYALRKL 527
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
6-447 8.88e-100

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 308.34  E-value: 8.88e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA--- 82
Cdd:NF038308   30 VALCQQPDLPVDRLELLHDRRDRALAERVAADIEEVSPETEVRLVPVVLRDPWDFEEVYGALLDFARAYPFDTENEDylv 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  83 ------HGA---VERAVDAMRQGAaDYLVKPFEPK------ALIEL-VARH-ALGVISASEGEGPIAFE--------PAS 137
Cdd:NF038308  110 hittgtHVAqicWFLLVEARYLPA-RLLQTSPPRDkeegtyEIIDLdLSRYdALAQRFAREQAEAVSFLksgiatrnAAF 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 138 AQLLELAARVA-RSDSTVLISGESGTGKEVLARYIHQQSTRA---KQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAA 213
Cdd:NF038308  189 NRLIEQIERVAlRSRAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVKGAFTGAQAD 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 214 QAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSV 293
Cdd:NF038308  269 RAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINL 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 294 FPLAWRPLRERPADIIPLAERLLNNHVKKMKH-----AQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQP 368
Cdd:NF038308  349 WTFRLPGLRERREDIEPNLDYELDRFARELGRqvrfnKEARFRYLAFATSPEALWPGNFRELSASVTRMATLADGGRITE 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 369 QD-----FCLAMGSGAAPLPTLAPAPMVAEIETAGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISprtlRYKLAQ 443
Cdd:NF038308  429 ELveeeiARLRAAWQSAPAAADDDALADLLGGEQLAELDLFDRVQLAAVLRVCRQSRSLSAAGRRLFGVS----RQQKAS 504

                  ....
gi 1509073841 444 MRDA 447
Cdd:NF038308  505 PNDA 508
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
117-433 3.58e-97

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 301.34  E-value: 3.58e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 117 HALGVISASEGEGPIAFEPASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLE 196
Cdd:COG3283   193 QALQVNDDSGFDHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAE 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 197 ATLFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAG 276
Cdd:COG3283   273 SELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAE 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 277 EVAAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQR 356
Cdd:COG3283   353 LVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYR 432
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509073841 357 ALILQQGGLIQPQDFclamgsgaaPLPTLAPAPMVAEIETAGALGDDLRRREFQMIIDTLRSERGRRKeAAERLGIS 433
Cdd:COG3283   433 AVSLLEGDELTPEDL---------QLPEYAASAGLLDDLLEGSLDEIVKRFERSLLRRLYPSYPSTRK-LAKRLGVS 499
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
147-452 7.78e-86

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 276.71  E-value: 7.78e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 147 VARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQADGGTI 226
Cdd:PRK15429  395 VAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSL 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 227 LLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRPLRERPA 306
Cdd:PRK15429  475 FLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPE 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 307 DIIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQpqdfcLAMGSGAAPLPTLA 386
Cdd:PRK15429  555 DIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQ-----LSLPDITLPEPETP 629
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1509073841 387 PAPMVAEIEtagalGDDlrrrEFQMIIDTLRSERG---RRKEAAERLGISPRTLrykLAQMRDAGMDVE 452
Cdd:PRK15429  630 PAATVVAQE-----GED----EYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTL---LSRMKRLGIDKS 686
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
135-443 2.60e-82

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 263.50  E-value: 2.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVARSDSTVLISGESGTGKEVLARYIH--------QQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGS 206
Cdd:PRK15424  226 PQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfarhdARQGKKSHPFVAVNCGAIAESLLEAELFGYEEGA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 207 FTGAI-AAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFRE 285
Cdd:PRK15424  306 FTGSRrGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRR 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 286 DLFYRLSVFPLAWRPLRERPADIIPLAERLLNNHVKKM-----KHAQARLSAeAQACLIAYPWPGNVRELDNAIQRalil 360
Cdd:PRK15424  386 DLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALsapfsAALRQGLQQ-CETLLLHYDWPGNVRELRNLMER---- 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 361 qqggliqpqdfcLAMGSGAAPLPTLAPAPMVAeieTAGALGDDLR-----RREFQMIIDTLRSERGRRKEAAERLGISPR 435
Cdd:PRK15424  461 ------------LALFLSVEPTPDLTPQFLQL---LLPELARESAktpapRLLAATLQQALERFNGDKTAAANYLGISRT 525

                  ....*...
gi 1509073841 436 TLRYKLAQ 443
Cdd:PRK15424  526 TLWRRLKA 533
PRK10820 PRK10820
transcriptional regulator TyrR;
119-441 4.04e-80

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 257.31  E-value: 4.04e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 119 LGVISASEGEGPIAFEPASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEAT 198
Cdd:PRK10820  195 LAVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESE 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 199 LFGHEKGSFTGAIAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEV 278
Cdd:PRK10820  275 LFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELV 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 279 AAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRAL 358
Cdd:PRK10820  355 QKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRAL 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 359 ILQQGGLIQPQDFClamgsgaapLPTLAPAPMVAEIETAGALGDDLRRREFQMIIDTLRSERGRRKeAAERLGISPRTLR 438
Cdd:PRK10820  435 TQLEGYELRPQDIL---------LPDYDAAVAVGEDAMEGSLDEITSRFERSVLTRLYRNYPSTRK-LAKRLGVSHTAIA 504

                  ...
gi 1509073841 439 YKL 441
Cdd:PRK10820  505 NKL 507
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
135-437 2.78e-77

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


Pssm-ID: 274079 [Multi-domain]  Cd Length: 526  Bit Score: 250.16  E-value: 2.78e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGA-IAA 213
Cdd:TIGR02329 219 APMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTGArRGG 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 214 QAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSV 293
Cdd:TIGR02329 299 RTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLFYRLSI 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 294 FPLAWRPLRERPADIIPLAERLLNNHVKKMK----HAQARLSAEAQACLIAYPWPGNVRELDNAIQRALIlqqggliqpq 369
Cdd:TIGR02329 379 LRIALPPLRERPGDILPLAAEYLVQAAAALRlpdsEAAAQVLAGVADPLQRYPWPGNVRELRNLVERLAL---------- 448
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1509073841 370 dFCLAMGSGA-APLPTLAPAPMVAEIET-AGALGDDLRRR---EFQMIIDTLRSERGRRKEAAERLGISPRTL 437
Cdd:TIGR02329 449 -ELSAMPAGAlTPDVLRALAPELAEASGkGKTSALSLRERsrvEALAVRAALERFGGDRDAAAKALGISRTTL 520
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
141-438 1.02e-76

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


Pssm-ID: 274371 [Multi-domain]  Cd Length: 329  Bit Score: 242.59  E-value: 1.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 141 LELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKFEQ 220
Cdd:TIGR02974  12 LEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGAQKRHQGRFER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 221 ADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAWRP 300
Cdd:TIGR02974  92 ADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDRLAFDVITLPP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 301 LRERPADIIPLAERLLNNHVKKMK-HAQARLSAEAQACLIAYPWPGNVRELDNAIQRALiLQQGGLIQPQD--------- 370
Cdd:TIGR02974 172 LRERQEDIMLLAEHFAIRMARELGlPLFPGFTPQAREQLLEYHWPGNVRELKNVVERSV-YRHGLEEAPIDeiiidpfas 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1509073841 371 -FCLAMGSGAAPLPTLAPAPMVAEIETAGALGDDLRRR----EFQMIIDTLRSERGRRKEAAERLGISPRTLR 438
Cdd:TIGR02974 251 pWRPKQAAPAVDEVNSTPTDLPSPSSIAAAFPLDLKQAqqdyEIELLQQALAEAQFNQRKAAELLGLTYHQLR 323
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
119-441 8.30e-75

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: 237.82  E-value: 8.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 119 LGVISAsEGEGPIAFEPASAQLLELAARVArsdsTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEAt 198
Cdd:COG3604    88 LGVLTL-DSRRPGAFSEEDLRLLETLASLA----AVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES- 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 199 lfghekgsftgaiaaqagkfeqadggtilldeisemplglqakllrvLQEREVERVGARKPIQLDIRVVATTNRDLAGEV 278
Cdd:COG3604   162 -----------------------------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 279 AAGRFREDLFYRLSVFPLAWRPLRERPADIIPLAERLLNNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRAL 358
Cdd:COG3604   195 AEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAV 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 359 ILQQGGLIQPQDFclamgsgaaplptlapapmvaeietAGALGDDLRRREFQMIIDTLRSERGRRKEAAERLGISPRTLR 438
Cdd:COG3604   275 ILAEGGVLDADDL-------------------------APGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLR 329

                  ...
gi 1509073841 439 YKL 441
Cdd:COG3604   330 SRM 332
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
139-438 5.08e-70

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 225.32  E-value: 5.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 139 QLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQAGKF 218
Cdd:PRK11608   17 EVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 219 EQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVFPLAW 298
Cdd:PRK11608   97 ERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 299 RPLRERPADIIPLAERLLNNHVKKMKHAQ-ARLSAEAQACLIAYPWPGNVRELDNAIQRALILQqggliqpqdfclamGS 377
Cdd:PRK11608  177 PPLRERQSDIMLMAEHFAIQMCRELGLPLfPGFTERARETLLNYRWPGNIRELKNVVERSVYRH--------------GT 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1509073841 378 GAAPLPTL-------APAPMVAEIETAGALGD---DLR----RREFQMIIDTLRSERGRRKEAAERLGISPRTLR 438
Cdd:PRK11608  243 SEYPLDNIiidpfkrRPAEEAIAVSETTSLPTlplDLRewqhQQEKELLQRSLQQAKFNQKRAAELLGLTYHQLR 317
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
135-443 1.54e-61

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 211.08  E-value: 1.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGhekGSFTGAIAAQ 214
Cdd:PRK11388  332 PQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTDSENGR 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 215 AGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYRLSVF 294
Cdd:PRK11388  409 LSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAF 488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 295 PLAWRPLRERPADIIPLAERLLnNHVKKMKHAQARLSAEAQACLIAYPWPGNVRELDNAIQRALILQQGGLIQ----PQD 370
Cdd:PRK11388  489 EITIPPLRMRREDIPALVNNKL-RSLEKRFSTRLKIDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIRlsdlPEH 567
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1509073841 371 FCLAMGSGAAPLPTLAPAPMVAEIETagalgddlrrrefQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:PRK11388  568 LFTEQATDDVSATRLSTSLSLAELEK-------------EAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQ 627
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
135-430 3.20e-47

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


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 170.40  E-value: 3.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVA-RSDSTVLISGESGTGKEVLARYIH---QQSTRAKQPFIAINCAAIPDNMLEATLFGHEKGSFTGA 210
Cdd:COG4650   191 AAFNRLIEQIERVAiRSRAPILLTGPTGAGKSQLARRIYelkKARHQVSGRFVEVNCATLRGDGAMSALFGHVKGAFTGA 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 211 IAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPIQLDIRVVATTNRDLAGEVAAGRFREDLFYR 290
Cdd:COG4650   271 VSDRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLAR 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 291 LSVFPLAWRPLRERPADIIPLAERLLNNHVKKMKHaQARLSAEAQACLIAY------PWPGNVRELDNAIQRALILQQGG 364
Cdd:COG4650   351 INLWTFRLPGLAERREDIEPNLDYELARFAREQGR-RVRFNKEARARYLAFatspeaLWSGNFRDLNASVTRMATLAEGG 429
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 365 LI----------------QPQDfclaMGSGAAPLPTLAPAPMVAEIetagalgDDLRRREFQMIIDTLR-----SERGRR 423
Cdd:COG4650   430 RItvalvdeeiarlrrlwQRAE----AATGDDLLAELLGAEQAAEL-------DLFDRVQLAAVIRVCRrsrslSEAGRT 498

                  ....*..
gi 1509073841 424 KEAAERL 430
Cdd:COG4650   499 LFAVSRQ 505
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
5-117 9.32e-41

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: 141.86  E-value: 9.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:cd17549    81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRA 113
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
4-116 1.96e-34

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: 127.76  E-value: 1.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTAR 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:COG0745    83 DDEEDRVRGLEAGADDYLTKPFDPE---ELLAR 112
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-117 3.33e-32

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: 119.18  E-value: 3.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQ--PQLPVL 78
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDIPII 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:COG0784    84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
5-116 4.34e-32

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: 120.98  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:COG4566    82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRR 113
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
5-115 1.45e-31

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: 116.87  E-value: 1.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVA 115
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
6-104 6.46e-31

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: 114.63  E-value: 6.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHGA 85
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90
                  ....*....|....*....
gi 1509073841  86 VERAVDAMRQGAADYLVKP 104
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
2-116 2.16e-30

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: 115.78  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   2 AIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRA--RQPQLPVLL 79
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAdpRTADIPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEPKAL---IELVAR 116
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELlarVDLVAR 120
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
4-116 4.46e-30

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: 112.75  E-value: 4.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:cd19919    82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVER 114
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-117 4.24e-29

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: 113.72  E-value: 4.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQP--QLPVL 78
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIPVI 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:COG3437    85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
5-119 1.19e-28

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: 109.22  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVaRHAL 119
Cdd:cd17537    83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAI-EQAL 116
fixJ PRK09390
response regulator FixJ; Provisional
5-116 7.20e-28

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 109.71  E-value: 7.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:PRK09390    6 VHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHG 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:PRK09390   86 DVPLAVEAMKLGAVDFIEKPFEDERLIGAIER 117
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
4-104 9.07e-28

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: 106.01  E-value: 9.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADtLLLAGHDYRAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:COG4753     1 KVLIVDDEPLIREGLKR-ILEWEAGFEVVGEAENGEEALElleEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIIL 79
                          90       100
                  ....*....|....*....|....
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVKP 104
Cdd:COG4753    80 SGYSDFEYAQEAIKLGADDYLLKP 103
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
5-119 1.14e-27

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: 106.43  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIeLVARHAL 119
Cdd:cd17550    81 TIETAVKATKLGAYDFIEKPLSLDRLL-LTIERAL 114
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
6-104 2.36e-26

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: 102.10  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHGA 85
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                          90
                  ....*....|....*....
gi 1509073841  86 VERAVDAMRQGAADYLVKP 104
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
6-116 4.37e-26

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: 101.91  E-value: 4.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHGA 85
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1509073841  86 VERAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:cd17625    81 VEDRVKGLDLGADDYLPKPF---SLAELLAR 108
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-118 6.09e-26

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 102.36  E-value: 6.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLL-LAGHDY-RAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVL 78
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLErLPGFEVvGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARHA 118
Cdd:COG4565    82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
5-119 6.99e-26

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: 101.51  E-value: 6.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIeLVARHAL 119
Cdd:cd17572    81 SVDIAVEAMRLGAYDFLEKPFDADRLR-VTVRNAL 114
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
4-118 1.55e-25

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: 102.69  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGY 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKALIELVARHA 118
Cdd:COG4567    86 ASIATAVEAIKLGADDYLAKPADADDLLAALERAE 120
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
5-116 2.80e-25

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: 99.87  E-value: 2.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:cd17624    81 GVDDRVAGLDAGADDYLVKPF---ALEELLAR 109
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
5-116 5.44e-25

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: 98.95  E-value: 5.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAED---ALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEVVGEAENgeeALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:cd17536    81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEK 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
5-110 1.13e-23

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: 95.39  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQ--ESFSLVVSDVNMPGMDGHQLLSLLRArQPQLPVLLMTA 82
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLREnkDEFDLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMSA 79
                          90       100
                  ....*....|....*....|....*...
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPFEPKAL 110
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
5-114 1.24e-23

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: 95.22  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQP--QLPVLLMTA 82
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPFEPKALIELV 114
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
5-104 2.63e-23

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: 93.66  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                          90       100
                  ....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKP 104
Cdd:cd19935    81 SVEDRVKGLDLGADDYLVKP 100
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
154-355 2.80e-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: 103.26  E-value: 2.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 154 VLISGESGTGKEVLARYIHQ-----QSTRAKQPFIAINCAAIPDN--MLEATLFGHEKGSFTGAIAAQAGKFEQADGGTI 226
Cdd:COG1221   133 TLILGPTGVGKSFFAELMYEyaieiGVLPEDAPFVVFNCADYANNpqLLMSQLFGYVKGAFTGADKDKEGLIEKADGGIL 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 227 LLDEISEMPLGLQAKLLRVLQEREVERVG-ARKPIQLDIRVV-ATTnrdlagevaagrfrEDL-------FYR-----LS 292
Cdd:COG1221   213 FLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIfATT--------------EDPessllktFLRripmvIK 278
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1509073841 293 VFPLAWRPLRERpADIIplaERLLNNHVKKMKHaQARLSAEAQACLIAYPWPGNVRELDNAIQ 355
Cdd:COG1221   279 LPSLEERSLEER-LELI---KHFFKEEAKRLNK-PIKVSKEVLKALLLYDCPGNIGQLKSDIQ 336
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
5-114 4.77e-23

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: 93.69  E-value: 4.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRA---RQPQLPVLLMT 81
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALIELV 114
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
131-292 5.09e-23

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: 94.91  E-value: 5.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 131 IAFEPASAQLLELAARvaRSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGHEkgsftgA 210
Cdd:cd00009     1 VGQEEAIEALREALEL--PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------L 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 211 IAAQAGKFEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARkpiqlDIRVVATTNRDLagevaAGRFREDLFYR 290
Cdd:cd00009    73 VRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPL-----LGDLDRALYDR 142

                  ..
gi 1509073841 291 LS 292
Cdd:cd00009   143 LD 144
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
4-118 2.88e-22

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: 91.49  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKALIELVARHA 118
Cdd:cd17555    82 GVMSDAVEALRLGAWDYLTKPIEDLAVLEHAVRRA 116
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
3-114 8.08e-22

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: 90.48  E-value: 8.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhdYRAVGSAEDALEAVEQ---ESFSLVVSDVNMPGMDGHQLLSLLRA--RQPQLPV 77
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELG--FNNVEEAEDGVDALEKlkaGGFDFVITDWNMPNMDGLELLKTIRAdgALSHLPV 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  78 LLMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELV 114
Cdd:cd19923    79 LMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
3-116 1.24e-21

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 93.34  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADtlLLAGH-DYRAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVL 78
Cdd:COG3279     2 MKILIVDDEPLARERLER--LLEKYpDLEVVGEASNGEEALElleEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPII 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1509073841  79 LMTAHGavERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:COG3279    80 FTTAYD--EYALEAFEVNAVDYLLKPIDEERLAKALEK 115
PRK10643 PRK10643
two-component system response regulator PmrA;
3-116 1.91e-21

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 92.41  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:PRK10643    1 MKILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:PRK10643   81 RDTLEDRVAGLDVGADDYLVKPF---ALEELHAR 111
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
4-104 2.04e-21

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: 89.04  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                          90       100
                  ....*....|....*....|.
gi 1509073841  84 GAVERAVDAMRQGAADYLVKP 104
Cdd:cd17563    82 ASIATAVEAIKLGADDYLAKP 102
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
5-116 6.84e-21

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: 87.72  E-value: 6.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKPFHIE---ELLAR 109
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-117 7.80e-21

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: 87.54  E-value: 7.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:COG5803     1 MMKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMM 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:COG5803    81 TAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKL 117
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
135-301 7.96e-21

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 88.17  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 135 PASAQLLELAARVARSDSTVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLeatlfghekgsftgaiaaq 214
Cdd:pfam14532   5 AAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELL------------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 215 agkfEQADGGTILLDEISEMPLGLQAKLLRVLQEREVERVgarkpiqldiRVVATTNRDLAGEVAAGRFREDLFYRLSVF 294
Cdd:pfam14532  66 ----EQAKGGTLYLKDIADLSKALQKGLLLLLAKAEGYRV----------RLVCTSSKDLPQLAAAGLFDEQLYFELSAL 131

                  ....*..
gi 1509073841 295 PLAWRPL 301
Cdd:pfam14532 132 RLHVPPL 138
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
4-116 8.43e-21

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: 87.30  E-value: 8.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQ--PQLPVLLMT 81
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEmtRDIPIIMLT 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd17618    82 ARGEEEDKVRGLEAGADDYITKPFSPR---ELVAR 113
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
3-119 9.15e-21

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 87.46  E-value: 9.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALAdtLLLAGHDYRAV--GSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:cd17569     1 PTILLVDDEPNILKALK--RLLRREGYEVLtaTSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509073841  81 TAHGAVERAVDAMRQGAAD-YLVKPFEPKALIELVaRHAL 119
Cdd:cd17569    79 TGYADLDAAIEAINEGEIYrFLTKPWDDEELKETI-RQAL 117
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
5-118 1.08e-20

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: 87.18  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALAdTLLLAGHDYRAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:cd17535     1 VLIVDDHPLVREGLR-RLLESEPDIEVVGEAADGEEALAllrELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALIELVARHA 118
Cdd:cd17535    80 AHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
4-116 1.13e-20

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: 86.97  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRArQPQ---LPVLLM 80
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRK-LPAykfTPILML 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1509073841  81 TAHGAveravDAMRQ-----GAADYLVKPFEPKALIELVAR 116
Cdd:cd17562    81 TTESS-----DEKKQegkaaGATGWLVKPFDPEQLLEVVKK 116
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
5-116 6.08e-20

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: 85.05  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARqPQLPVLLMTAHG 84
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTARG 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  85 A-VERAVdAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd17623    80 DdIDRIL-GLELGADDYLPKPFNPR---ELVAR 108
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
4-103 1.08e-19

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: 84.19  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                          90       100
                  ....*....|....*....|
gi 1509073841  84 GavERAVDAMRQGAADYLVK 103
Cdd:cd17554    82 S--EYKSDFSSWAADAYVVK 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
4-116 1.82e-19

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: 83.56  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:cd17615    81 DSVEDRIAGLTAGGDDYVTKPF---SLEEVVAR 110
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
5-116 3.63e-19

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: 82.82  E-value: 3.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:cd17627    81 SVSDRVAGLDAGADDYLVKPF---ALEELLAR 109
PRK15479 PRK15479
transcriptional regulator TctD;
3-116 4.57e-19

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 85.54  E-value: 4.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHdyrAVGSAEDALEA---VEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLL 79
Cdd:PRK15479    1 MRLLLAEDNRELAHWLEKALVQNGF---AVDCVFDGLAAdhlLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLL 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEpkaLIELVAR 116
Cdd:PRK15479   78 LTARSAVADRVKGLNVGADDYLPKPFE---LEELDAR 111
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
4-116 1.36e-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: 81.33  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALadTLLLAGHDYRAVGSAEDALEAV---EQESFSLVVSDVNMPGMDGHQLLSLLRARQP--QLPVL 78
Cdd:cd17551     2 RILIVDDNPTNLLLL--EALLRSAGYLEVVSFTDPREALawcRENPPDLILLDYMMPGMDGLEFIRRLRALPGleDVPIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPkalIELVAR 116
Cdd:cd17551    80 MITADTDREVRLRALEAGATDFLTKPFDP---VELLAR 114
cztR_silR_copR TIGR01387
heavy metal response regulator; Members of this family contain a response regulator receiver ...
5-116 2.03e-18

heavy metal response regulator; Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system. [Regulatory functions, DNA interactions]


Pssm-ID: 130454 [Multi-domain]  Cd Length: 218  Bit Score: 83.70  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:TIGR01387   1 ILVVEDEQKTAEYLQQGLSESGYVVDAASNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLRRSGKQTPVLFLTARD 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEpkaLIELVAR 116
Cdd:TIGR01387  81 SVADKVKGLDLGADDYLVKPFS---FSELLAR 109
PRK11517 PRK11517
DNA-binding response regulator HprR;
3-116 3.81e-18

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 83.02  E-value: 3.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLMTA 82
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK-QTPVICLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:PRK11517   80 RDSVDDRVRGLDSGANDYLVKPF---SFSELLAR 110
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
5-104 6.92e-18

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: 78.57  E-value: 6.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLR--ARQPQLPVLLMTA 82
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRknADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKP 104
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
ompR PRK09468
osmolarity response regulator; Provisional
4-179 8.69e-18

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 82.33  E-value: 8.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:PRK09468    7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  84 GA-VERAVdAMRQGAADYLVKPFEPKaliELVAR-HALGVISASEGEGPIAFEPASAQL----LELAARVARSDSTV--L 155
Cdd:PRK09468   87 GEeVDRIV-GLEIGADDYLPKPFNPR---ELLARiRAVLRRQAPELPGAPSQEEEVIAFgkfkLNLGTRELFRGDEPmpL 162
                         170       180
                  ....*....|....*....|....
gi 1509073841 156 ISGESGTGKeVLARYIHQQSTRAK 179
Cdd:PRK09468  163 TTGEFAVLK-ALVSHPREPLSRDK 185
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
5-105 1.04e-17

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: 78.32  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRA--RQPQLPVLLMTA 82
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAdpATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPF 105
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-116 2.99e-17

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 80.39  E-value: 2.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:PRK11083    2 QQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  81 TA-HGAVERAVdAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:PRK11083   82 TArSDEVDRLV-GLEIGADDYVAKPFSPR---EVAAR 114
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
3-116 3.46e-17

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: 77.32  E-value: 3.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhdYRAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLL 79
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAG--YEVVGEAANGEEAVEkykELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:cd17542    79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEK 115
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-107 5.80e-17

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: 76.79  E-value: 5.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADtlLLAGHDYR--AVGSAEDALEAVEQES-FSLVVSDVNMPGMDGHQLLSLLRARQP--QLPV 77
Cdd:cd17544     1 IKVLVVDDSATSRNHLRA--LLRRHNFQvlEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSrdQLAI 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  78 LLMTAHGavERAVDA--MRQGAADYLVKPFEP 107
Cdd:cd17544    79 IGISASG--DNALSArfIKAGANDFLTKPFLP 108
orf27 CHL00148
Ycf27; Reviewed
4-116 9.23e-17

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 79.38  E-value: 9.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAH 83
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR-KESDVPIIMLTAL 86
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:CHL00148   87 GDVSDRITGLELGADDYVVKPFSPK---ELEAR 116
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
5-104 1.48e-16

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: 74.85  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                          90       100
                  ....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKP 104
Cdd:cd19928    81 TLMTAVKAAERGAFEYLPKP 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-115 2.62e-16

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: 76.92  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHD-YRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLrARQPQLPVLL 79
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI-SEERPAPVIL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVA 115
Cdd:COG3707    81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
6-116 6.55e-16

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: 73.46  E-value: 6.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLR--ARQPQLPVLLMTAH 83
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRsdPKTSSIPIIMLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPR---ELLAR 110
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
4-105 7.58e-16

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: 72.92  E-value: 7.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQ--PQLPVLLMT 81
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPetRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPF 105
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
5-116 1.04e-15

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: 72.96  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADtlLLAGH-DYRAVGSAED---ALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:cd17532     1 ALIVDDEPLAREELRY--LLEEHpDIEIVGEAENgeeALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFV 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1509073841  81 TAHGavERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:cd17532    79 TAYD--EYAVEAFELNAVDYLLKPFSEERLAEALAK 112
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
4-105 1.06e-15

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: 72.53  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQES-FSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                          90       100
                  ....*....|....*....|...
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPF 105
Cdd:cd18160    81 GAAAAPELLSDAVGDNATLKKPF 103
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
4-116 1.17e-15

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: 72.96  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRArQPQL---PVLLM 80
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPATrdiPVIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1509073841  81 TAH---GAVERAVDAmrqGAADYLVKPFEPKALIELVAR 116
Cdd:cd17548    80 TAYamkGDREKILEA---GCDGYISKPIDTREFLETVAK 115
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
4-111 6.09e-15

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: 70.87  E-value: 6.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAH 83
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR-PKYQGPILLLTAL 80
                          90       100
                  ....*....|....*....|....*...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKALI 111
Cdd:cd17622    81 DSDIDHILGLELGADDYVVKPVEPAVLL 108
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
5-104 8.12e-15

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: 69.89  E-value: 8.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAHG 84
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR-EWSAVPVIVLSARD 79
                          90       100
                  ....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKP 104
Cdd:cd17620    80 EESDKIAALDAGADDYLTKP 99
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
5-104 1.38e-14

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: 69.49  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKP 104
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
4-116 1.64e-14

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: 69.42  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRArQPQLPVLLMTAH 83
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd17626    81 SDTVDVVLGLESGADDYVAKPFKPK---ELVAR 110
PRK10336 PRK10336
two-component system response regulator QseB;
3-137 2.55e-14

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 71.85  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPF---EPKALIELVARHALGVISASEGEGPIAFEPAS 137
Cdd:PRK10336   81 RDALAERVEGLRLGADDYLCKPFaliEVAARLEALMRRTNGQASNELRHGNVMLDPGK 138
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
3-113 2.58e-14

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: 68.97  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHD-YRAVGSAEDALEAVEQESFSLVVSDVNMPG-MDGHQLLSLLRARQPqLPVLLM 80
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKFD-IPVIFL 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1509073841  81 TAH---GAVERAVDAMRQGaadYLVKPFEPKAL---IEL 113
Cdd:cd17534    80 TAYsdeETLERAKETNPYG---YLVKPFNERELkaaIEL 115
PRK10610 PRK10610
chemotaxis protein CheY;
3-112 4.03e-14

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 68.85  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhdYRAVGSAED---ALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRA--RQPQLPV 77
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKELG--FNNVEEAEDgvdALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAdgAMSALPV 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  78 LLMTAHGAVERAVDAMRQGAADYLVKPFEPKALIE 112
Cdd:PRK10610   84 LMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEE 118
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
4-116 5.01e-14

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: 68.17  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAH 83
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR-EHSHVPILMLTAR 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd19939    80 TEEMDRVLGLEMGADDYLCKPFSPR---ELLAR 109
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
5-104 8.43e-14

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: 67.40  E-value: 8.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQ---------ESFSLVVSDVNMPGMDGHQLLSLLRA--RQP 73
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1509073841  74 QLPVLLMTAHGAVERAVDAMRQGAADYLVKP 104
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
4-120 8.62e-14

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: 67.58  E-value: 8.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTL-LLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRArQP---QLPVLL 79
Cdd:cd17552     3 RILVIDDEEDIREVVQACLeKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPetqSIPVIL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1509073841  80 MTAHG-AVERA-VDAMrqGAADYLVKPFEPKALIELVArHALG 120
Cdd:cd17552    82 LTAKAqPSDRQrFASL--GVAGVIAKPFDPLTLAEQIA-KLLG 121
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
5-116 1.00e-13

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: 67.41  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAHG 84
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR-EQSEVGIILVTGRD 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  85 -AVERAVdAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd17619    82 dEVDRIV-GLEIGADDYVTKPFNPR---ELLVR 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
3-104 1.14e-13

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: 67.42  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhDYRAVGSAEDALEAVEQ-ESFS--LVVSDVNMPGMDGHQLLSLLRARQPqLPVLL 79
Cdd:cd17541     1 IRVLIVDDSAVMRKLLSRILESDP-DIEVVGTARDGEEALEKiKELKpdVITLDIEMPVMDGLEALRRIMAERP-TPVVM 78
                          90       100
                  ....*....|....*....|....*..
gi 1509073841  80 MTAHGA--VERAVDAMRQGAADYLVKP 104
Cdd:cd17541    79 VSSLTEegAEITLEALELGAVDFIAKP 105
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
5-105 1.58e-13

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: 66.22  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQES-FSLVVSDVNMPG-MDGHQLLSLLRARQPQLPVLLMTa 82
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTS- 79
                          90       100
                  ....*....|....*....|....
gi 1509073841  83 hGAVERAVDAMRQGA-ADYLVKPF 105
Cdd:cd18161    80 -GYAENAIEGGDLAPgVDVLSKPF 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
5-104 1.70e-13

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: 66.27  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVE-DDRALREALAdtlLLAGHDYRaVGSAEDALEAV-----EQESFSLVVSDVNMPGMDGHQLLSLL---RARQpQL 75
Cdd:cd17582     1 VLLVEnDDSTRQIVTA---LLRKCSYE-VTAASDGLQAWdvledEQNEIDLILTEVDLPVSSGFKLLSYImrhKICK-NI 75
                          90       100
                  ....*....|....*....|....*....
gi 1509073841  76 PVLLMTAHGAVERAVDAMRQGAADYLVKP 104
Cdd:cd17582    76 PVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
5-119 1.83e-13

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: 66.66  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKaliELVAR-HAL 119
Cdd:cd17616    81 DIEDKVKGLGFGADDYMTKPFHKD---ELVARiHAI 113
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
4-114 2.05e-13

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: 66.32  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLMTAH 83
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISGD 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  84 GAVERAVD-AMRQGAADYLVKPFEPKALIELV 114
Cdd:cd17594    80 RRDEIDRVvGLELGADDYLAKPFGLRELLARV 111
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
5-104 2.42e-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: 65.93  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLMTAHG 84
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                          90       100
                  ....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKP 104
Cdd:cd19936    80 DEIDEVFGLRMGADDYITKP 99
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
3-173 3.33e-13

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 68.80  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHdyrAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLL 79
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGF---VVDLADNGLNGYHlamTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFepkALIELVA------RHALGVISASEgegpiaFEPASAQLLELAARVARSDST 153
Cdd:PRK09836   78 LTALGTIEHRVKGLELGADDYLVKPF---AFAELLArvrtllRRGAAVIIESQ------FQVADLMVDLVSRKVTRSGTR 148
                         170       180
                  ....*....|....*....|
gi 1509073841 154 VLISGESGTGKEVLARyiHQ 173
Cdd:PRK09836  149 ITLTSKEFTLLEFFLR--HQ 166
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
4-116 3.96e-13

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: 65.90  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRA----LREALADTLLlaGHDYRAVGSAEDALEAVEQE-SFS------LVVSDVNMPGMDGHQLLSLLRArQ 72
Cdd:cd17557     1 TILLVEDNPGdaelIQEAFKEAGV--PNELHVVRDGEEALDFLRGEgEYAdaprpdLILLDLNMPRMDGFEVLREIKA-D 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1509073841  73 PQL---PVLLMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:cd17557    78 PDLrriPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-106 4.71e-13

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: 65.34  E-value: 4.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADtlLLAGHDYRAV----GSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVL 78
Cdd:cd19925     1 INVLIVEDDPMVAEIHRA--YVEQVPGFTVigtaGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVI 78
                          90       100
                  ....*....|....*....|....*...
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFE 106
Cdd:cd19925    79 VVTAANDVETVREALRLGVVDYLIKPFT 106
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
4-116 7.51e-13

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 67.91  E-value: 7.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEqESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAH 83
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELR-QTHQTPVIMLTAR 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:PRK10955   81 GSELDRVLGLELGADDYLPKPFNDR---ELVAR 110
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
5-116 1.24e-12

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: 64.22  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGhDYRAVGSA---EDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELED-DLEVVAQAsngQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVT 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1509073841  82 AH---GAVERAVDAmrqGAADYLVKPFEPKALIELVAR 116
Cdd:cd19930    80 TFgrpGYFRRALAA---GVDGYVLKDRPIEELADAIRT 114
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
3-111 3.69e-12

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: 62.82  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDyrAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQlPVLL 79
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYE--VVGEASDGEEAVElakKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVL 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  80 MTAHGA---VERAVDAmrqGAADYLVKPFEPKALI 111
Cdd:cd19932    78 LTAYSQqdlVERAKEA---GAMAYLVKPFSESDLI 109
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
153-291 3.77e-12

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: 63.93  E-value: 3.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  153 TVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEA--TLFGHEKGSFTGAIAAQAGKFEQA---DGGTIL 227
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQllLIIVGGKKASGSGELRLRLALALArklKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1509073841  228 LDEISEMPLGLQAKLLRVLQErevERVGARKPIQLDIRVVATTNR--DLAGEVAAGRFREDLFYRL 291
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLL 146
PRK15369 PRK15369
two component system response regulator;
1-103 5.21e-12

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 65.10  E-value: 5.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADtLLLAGHDYRAVGSAEDAL---EAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPV 77
Cdd:PRK15369    2 KNYKILLVDDHELIINGIKN-MLAPYPRYKIVGQVDNGLevyNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI 80
                          90       100
                  ....*....|....*....|....*.
gi 1509073841  78 LLMTAHGAVERAVDAMRQGAADYLVK 103
Cdd:PRK15369   81 LVLTARQEEHMASRTLAAGALGYVLK 106
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-169 5.83e-12

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 66.71  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVeDDRAL-REALADtLLLAGHDYRAVGSAEDALEAVEQ-ESFS--LVVSDVNMPGMDGHQLLSLLRARQPqLP 76
Cdd:PRK00742    2 MKIRVLVV-DDSAFmRRLISE-ILNSDPDIEVVGTAPDGLEAREKiKKLNpdVITLDVEMPVMDGLDALEKIMRLRP-TP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  77 VLL---MTAHGAvERAVDAMRQGAADYLVKPFE------PKALIELVA--RHALGV-ISASEGEGPIAFEPASAQLLELA 144
Cdd:PRK00742   79 VVMvssLTERGA-EITLRALELGAVDFVTKPFLgislgmDEYKEELAEkvRAAARArVRALPPRAAAAARAAAAAPAALA 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 1509073841 145 ARVARSDSTVLIsGESgTG-----KEVLAR 169
Cdd:PRK00742  158 AAPLLSSKLVAI-GTS-TGgpealQKVLTP 185
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
5-131 6.02e-12

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 65.05  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADtLLLAGHDYRAVGSA---EDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:PRK10651    9 ILLIDDHPMLRTGVKQ-LISMAPDITVVGEAsngEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFS 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALIELVARHALGVISASEGEGPI 131
Cdd:PRK10651   88 VSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPV 137
PRK10816 PRK10816
two-component system response regulator PhoP;
3-116 1.13e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 64.37  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDyraVGSAEDALEA---VEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLL 79
Cdd:PRK10816    1 MRVLVVEDNALLRHHLKVQLQDAGHQ---VDAAEDAKEAdyyLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILV 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEpkaLIELVAR 116
Cdd:PRK10816   78 LTARESWQDKVEVLSAGADDYVTKPFH---IEEVMAR 111
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
4-116 1.18e-11

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: 61.24  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRaRQPQLPVLLMTAH 83
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-RFSDVPIIMVTAR 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd19938    80 VEEIDRLLGLELGADDYICKPYSPR---EVVAR 109
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
5-111 1.20e-11

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 61.57  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRArQPQL---PVLLMT 81
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKS-DPDLkdiPVILLT 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALI 111
Cdd:cd17598    80 TLSDPRDVIRGLECGADNFITKPYDEKYLL 109
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
3-57 1.86e-11

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: 59.12  E-value: 1.86e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1509073841    3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMP 57
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
5-112 2.53e-11

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: 60.44  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADtLLLAGHDYRAVG---SAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:cd19931     1 VLLIDDHPLLRKGIKQ-LIELDPDFTVVGeasSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILT 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALIE 112
Cdd:cd19931    80 VSDAEDDVVTALRAGADGYLLKDMEPEDLLE 110
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
5-116 3.65e-11

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: 60.41  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLlAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRA--RQPQLPVLLMTA 82
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLS-SEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSleRTRQLPILAVAD 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd17539    80 PGDRGRLIRALEIGVNDYLVRPIDPN---ELLAR 110
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
4-106 3.67e-11

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: 60.26  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81
                          90       100
                  ....*....|....*....|...
gi 1509073841  84 GAVERAVDAMRQGAADYLVKPFE 106
Cdd:cd17553    82 GELDMIQESKELGALTHFAKPFD 104
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
5-111 7.12e-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: 58.98  E-value: 7.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHG 84
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                          90       100
                  ....*....|....*....|....*..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALI 111
Cdd:cd17573    81 KTEQEIEAFKEGADDYIAKPFDFKVLV 107
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-116 1.42e-10

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 61.27  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALAdtLLLAGHDYRAVgSAEDALEAVEQ--ESF-SLVVSDVNMPGMDGHQLLSLLR--ARQPQL 75
Cdd:PRK10161    1 MARRILVVEDEAPIREMVC--FVLEQNGFQPV-EAEDYDSAVNQlnEPWpDLILLDWMLPGGSGIQFIKHLKreSMTRDI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1509073841  76 PVLLMTAHGAVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:PRK10161   78 PVVMLTARGEEEDRVRGLETGADDYITKPFSPK---ELVAR 115
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
5-117 1.96e-10

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: 58.06  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRArQPQLPVLLMTAHG 84
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ-ISNVPIIFISSRD 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:cd18159    80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAI 112
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
3-84 4.85e-10

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: 57.21  E-value: 4.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALAdTLLLAGHDYRAVGSA---EDALEAVEQESFSLVVSDVNMPGMDGHQLLS-LLRARQPQlpVL 78
Cdd:COG2197     2 IRVLIVDDHPLVREGLR-ALLEAEPDIEVVGEAadgEEALELLEELRPDVVLLDIRMPGMDGLEALRrLLTPRERE--VL 78

                  ....*.
gi 1509073841  79 LMTAHG 84
Cdd:COG2197    79 RLLAEG 84
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
404-443 7.31e-10

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 53.94  E-value: 7.31e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1509073841 404 LRRREFQMIIDTLRSERGRRKEAAERLGISPRTLRYKLAQ 443
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
PRK11697 PRK11697
two-component system response regulator BtsR;
3-116 1.09e-09

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 58.70  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADtLLLAGHDYRAVGSAEDALEA---VEQESFSLVVSDVNMPGMDGHQLLSLLR-ARQPQlpVL 78
Cdd:PRK11697    2 IKVLIVDDEPLAREELRE-LLQEEGDIEIVGECSNAIEAigaIHRLKPDVVFLDIQMPRISGLELVGMLDpEHMPY--IV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1509073841  79 LMTAHGavERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:PRK11697   79 FVTAFD--EYAIKAFEEHAFDYLLKPIDPARLAKTLAR 114
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
5-114 1.23e-09

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 56.22  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLllaGHDYR--AVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:cd17596     3 ILVVDDEVRSLEALRRTL---EEDFDvlTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  83 HGAVERAVDAMRQ-GAADYLVKPFEPKALIELV 114
Cdd:cd17596    80 YTDSEDIIAGINEaGIYQYLTKPWHPDQLLLTV 112
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
5-108 1.74e-09

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: 55.45  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVED---DRALREaladtLLLAGHDYR--AVGSAEDALE-----------AVEQESFSLVVSDVNMPGMDGHQLLSLL 68
Cdd:cd17581     1 VLAVDDslvDRKVIE-----RLLRISSCRvtAVDSGKRALEflgledeedssNFNEPKVNMIITDYCMPGMTGYDLLKKV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1509073841  69 RARQP--QLPVLLMTAHGAVERAVDAMRQGAADYLVKPFEPK 108
Cdd:cd17581    76 KESSAlkEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLA 117
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
5-116 3.01e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 57.39  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGhqlLSLLRA--RQPQLPVLLMTA 82
Cdd:PRK10710   13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDG---LTLCREirRFSDIPIVMVTA 89
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  83 H-GAVERAVdAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:PRK10710   90 KiEEIDRLL-GLEIGADDYICKPYSPR---EVVAR 120
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
3-105 3.21e-09

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: 54.15  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADtLLLAGHDYRAVGSA---EDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQ--PQLPV 77
Cdd:cd17561     2 IKVLIADDNREFVQLLEE-YLNSQPDMEVVGVAhngQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRleKRPKI 80
                          90       100
                  ....*....|....*....|....*...
gi 1509073841  78 LLMTAHGAVERAVDAMRQGAADYLVKPF 105
Cdd:cd17561    81 IMLTAFGQEDITQRAVELGASYYILKPF 108
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
5-116 3.50e-09

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: 54.35  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLMTAHG 84
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  85 AVERAVDAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:cd17614    80 SEVDKVLGLELGADDYVTKPFSNR---ELLAR 108
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
5-104 3.75e-09

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: 53.74  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLMTAHG 84
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTAKD 79
                          90       100
                  ....*....|....*....|
gi 1509073841  85 AVERAVDAMRQGAADYLVKP 104
Cdd:cd17621    80 SEIDKVVGLELGADDYVTKP 99
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
12-117 4.93e-09

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: 54.08  E-value: 4.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841  12 RALREALADTLLLAGHdyravgsAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA---HGAVER 88
Cdd:cd17593    18 RALPADWDVEITFAEN-------GEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSGdvqPEAKER 90
                          90       100
                  ....*....|....*....|....*....
gi 1509073841  89 AVDAmrqGAADYLVKPFEPKALIELVARH 117
Cdd:cd17593    91 VLEL---GALAFLKKPFDPEKLAQLLEEL 116
PRK15347 PRK15347
two component system sensor kinase;
3-115 6.13e-09

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 58.50  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLR----ARQPQLPVL 78
Cdd:PRK15347  691 LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRddpnNLDPDCMIV 770
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPKAL---IELVA 115
Cdd:PRK15347  771 ALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLaraLELAA 810
PRK10766 PRK10766
two-component system response regulator TorR;
1-116 9.58e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 55.43  E-value: 9.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLM 80
Cdd:PRK10766    1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILV 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1509073841  81 TAHG-AVERAVdAMRQGAADYLVKPFEPKaliELVAR 116
Cdd:PRK10766   80 TGRTdSIDRIV-GLEMGADDYVTKPLELR---ELLVR 112
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
5-107 2.48e-08

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: 52.34  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALA-DTLLLAGHDYRAV--GSAEDALEAVEQ-----ESFSLVVSDVNMPGMDGHQLLSLLRARQPQLP 76
Cdd:cd17595     3 ILTVDDDPQVLRAVArDLRRQYGKDYRVLraDSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1509073841  77 VLLMTAHGAVERAVDAMRQGAAD-YLVKPFEP 107
Cdd:cd17595    83 RVLLTAYADTDAAIRAINDVQLDyYLLKPWDP 114
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
3-104 2.53e-08

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 56.52  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhdYRaVGSAED---ALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLL 79
Cdd:PRK10841  802 MMILVVDDHPINRRLLADQLGSLG--YQ-CKTANDgvdALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIG 878
                          90       100
                  ....*....|....*....|....*...
gi 1509073841  80 MTAHGAVE---RAVDAmrqGAADYLVKP 104
Cdd:PRK10841  879 VTANALAEekqRCLEA---GMDSCLSKP 903
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
5-112 1.41e-07

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: 49.95  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAG-HDYRAVGSAEDALEAVEQESFSLVVSDVNM-PGMDGHQLLSLLRARQ---PQLPVLL 79
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGvTRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELRHKKlisPSTVFIM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509073841  80 MTA-------HGAVERAVDamrqgaaDYLVKPFEPKALIE 112
Cdd:cd17589    81 VTGessramvLSALELEPD-------DYLLKPFTVSELRE 113
PRK10693 PRK10693
two-component system response regulator RssB;
36-104 1.68e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 52.69  E-value: 1.68e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1509073841  36 EDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTAHGAVERAVDAMRQGAADYLVKP 104
Cdd:PRK10693    7 VDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
pleD PRK09581
response regulator PleD; Reviewed
4-116 1.92e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 52.98  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVeDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLR--ARQPQLPVLLMT 81
Cdd:PRK09581  157 RILLV-DDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRskERTRYVPILLLV 235
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPkalIELVAR 116
Cdd:PRK09581  236 DEDDDPRLVKALELGVNDYLMRPIDK---NELLAR 267
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
3-120 1.93e-07

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: 49.32  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQE--SFSLVVSDVNMPGMDGHQLLSLLRARQPQL-PVLL 79
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAehSFQLVLLDLCMPEMDGFEVALRIRKLFGRReRPLI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1509073841  80 MTAHGAVERAVDA--MRQGAADYLVKPfepkalielVARHALG 120
Cdd:cd19933    81 VALTANTDDSTREkcLSLGMNGVITKP---------VSLHALG 114
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
3-105 3.24e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 52.81  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841    3 IKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:PRK09959   959 LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
                           90       100
                   ....*....|....*....|...
gi 1509073841   83 HGAVERAVDAMRQGAADYLVKPF 105
Cdd:PRK09959  1039 NAQANEREKGLSCGMNLCLFKPL 1061
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-118 5.81e-07

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 52.16  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRA-LReaLADTLL--LAGHdyraVGSAEDALEAVEQ---ESFSLVVSDVNMPGMDGHQLLSLLR--ARQ 72
Cdd:PRK11107  666 LPLTVMAVDDNPAnLK--LIGALLeeQVEH----VVLCDSGHQAVEQakqRPFDLILMDIQMPGMDGIRACELIRqlPHN 739
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1509073841  73 PQLPVLLMTAH---GAVERavdAMRQGAADYLVKPFEPKALIELVARHA 118
Cdd:PRK11107  740 QNTPIIAVTAHamaGERER---LLSAGMDDYLAKPIDEAMLKQVLLRYK 785
PRK13557 PRK13557
histidine kinase; Provisional
6-114 1.11e-06

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 50.82  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   6 LLVEDDRALREALADTLLL-AGHDYRAVGSAEDALEAVEQES-FSLVVSDVNMPG-MDGHQLLSLLRARQPQLPVLLMT- 81
Cdd:PRK13557  418 ILIVDDRPDVAELARMILEdFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTTg 497
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1509073841  82 -AHGAVERAvDAMRqGAADYLVKPFEPKALIELV 114
Cdd:PRK13557  498 yAEASIERT-DAGG-SEFDILNKPYRRAELARRV 529
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
3-116 1.20e-06

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 47.40  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDD----RALREALADTlllAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQP--QLP 76
Cdd:cd17575     1 IMVLLVDDQaiigEAVRRALADE---EDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPAtrDIP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1509073841  77 VLLMTAHGAVERAVDAMRQGAADYLVKPFEPkalIELVAR 116
Cdd:cd17575    78 IIVLSTKEEPEVKSEAFALGANDYLVKLPDK---IELVAR 114
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
3-104 2.79e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 49.11  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhDYRAVGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPqLPVLL 79
Cdd:PRK12555    1 MRIGIVNDSPLAVEALRRALARDP-DHEVVWVATDGAQAVErcaAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILI 78
                          90       100
                  ....*....|....*....|....*..
gi 1509073841  80 MTA--HGAVERAVDAMRQGAADYLVKP 104
Cdd:PRK12555   79 VTSltERNASRVFEAMGAGALDAVDTP 105
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
4-118 4.34e-06

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: 45.90  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYraVGSAEDALEAV---EQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPGN--VDEADDGREALvilLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILM 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1509073841  81 TAHG-----AVERAVDAMRQGAADYLVKPFEPKALIELVARHA 118
Cdd:cd17530    80 SGLDggileSAETLAGANGLNLLGTLSKPFSPEELTELLTKYT 122
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
154-272 4.39e-06

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: 46.13  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 154 VLISGESGTGK----EVLARYIHQQSTRAKQpfiaincaaIPDNMLEATLFGH-----EKGSFTGAIAAQAGKfeqaDGG 224
Cdd:pfam07728   2 VLLVGPPGTGKtelaERLAAALSNRPVFYVQ---------LTRDTTEEDLFGRrnidpGGASWVDGPLVRAAR----EGE 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1509073841 225 TILLDEISEMPLGLQAKLLRVLQERE---VERVGARKPIQLDIRVVATTNR 272
Cdd:pfam07728  69 IAVLDEINRANPDVLNSLLSLLDERRlllPDGGELVKAAPDGFRLIATMNP 119
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
5-154 6.11e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 47.11  E-value: 6.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALadTLLLAGHDYRaVGSAEDA----LEAVEQESfSLVVSDVNMPGMDGHQLLSLLRARQPqLPVLLM 80
Cdd:PRK10529    4 VLIVEDEQAIRRFL--RTALEGDGMR-VFEAETLqrglLEAATRKP-DLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVKPFepkALIELVARH--ALGVISASEGEGPIA-FEPASAQLleLAARVARSDSTV 154
Cdd:PRK10529   79 SARSEESDKIAALDAGADDYLSKPF---GIGELQARLrvALRRHSATPAPDPLVkFSDVTVDL--AARVIHRGEEEV 150
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
49-104 9.49e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 44.28  E-value: 9.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1509073841  49 LVVSDVNMPGMDGHQLLSLLRARQ--PQLPVLLMTAHGAVERAVDAMRQGAADYLVKP 104
Cdd:cd17602    45 LILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
COG1777 COG1777
Predicted transcriptional regulator, ArsR family [Transcription];
398-455 1.01e-05

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441383  Cd Length: 113  Bit Score: 44.64  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1509073841 398 GALGDDLRRRefqmIIDTLRSERGRRKEAAERLGISPRTLRYKLAQMRDAGMdVEAYL 455
Cdd:COG1777    12 DALGNPTRRR----ILALLSEEPAYVSELARELGVSRQAVYKHLRKLEEAGL-VESYR 64
PRK11173 PRK11173
two-component response regulator; Provisional
4-110 3.40e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 45.01  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDyraVGSAEDALE---AVEQESFSLVVSDVNMPGMDGhqlLSLLRARQPQLPVLLM 80
Cdd:PRK11173    5 HILIVEDELVTRNTLKSIFEAEGYD---VFEATDGAEmhqILSENDINLVIMDINLPGKNG---LLLARELREQANVALM 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  81 TAHGAvERAVD---AMRQGAADYLVKPFEPKAL 110
Cdd:PRK11173   79 FLTGR-DNEVDkilGLEIGADDYITKPFNPREL 110
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1-126 3.41e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 44.84  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADtLLLAGHDYRAVGSAEDALEAVEQE---SFSLVVSDVNMPGMDGHQLLSLLRARQPQLPV 77
Cdd:PRK10403    5 TPFQVLIVDDHPLMRRGVRQ-LLELDPGFEVVAEAGDGASAIDLAnrlDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1509073841  78 LLMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARHALGVISASE 126
Cdd:PRK10403   84 IILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSE 132
pleD PRK09581
response regulator PleD; Reviewed
1-111 5.09e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 45.66  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRA--RQPQLPVL 78
Cdd:PRK09581    1 MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSdpATTHIPVV 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPKALI 111
Cdd:PRK09581   81 MVTALDDPEDRVRGLEAGADDFLTKPINDVALF 113
PRK10360 PRK10360
transcriptional regulator UhpA;
3-120 5.69e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 43.81  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGhDYRAV---GSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLrarqPQ-LPVL 78
Cdd:PRK10360    2 ITVALIDDHLIVRSGFAQLLGLEP-DLQVVaefGSGREALAGLPGRGVQVCICDISMPDISGLELLSQL----PKgMATI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1509073841  79 LMTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARHALG 120
Cdd:PRK10360   77 MLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATG 118
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
4-111 6.55e-05

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 44.24  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADtlLLAGHDYRAV--GSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQpQLPVLLMT 81
Cdd:PRK10701    3 KIVFVEDDAEVGSLIAA--YLAKHDIDVTvePRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKW-QGPIVLLT 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1509073841  82 AHGAVERAVDAMRQGAADYLVKPFEPKALI 111
Cdd:PRK10701   80 SLDSDMNHILALEMGACDYILKTTPPAVLL 109
PRK09483 PRK09483
response regulator; Provisional
3-111 7.73e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 43.94  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLllagHDYRA---VGSAEDALEAVE---QESFSLVVSDVNMPGMDGHQLLSLLRARQPQLP 76
Cdd:PRK09483    2 INVLLVDDHELVRAGIRRIL----EDIKGikvVGEACCGEDAVKwcrTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVK 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1509073841  77 VLLMTAHGAVERAVDAMRQGAADYLVKPFEPKALI 111
Cdd:PRK09483   78 IIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVV 112
PLN03029 PLN03029
type-a response regulator protein; Provisional
5-104 8.71e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 43.87  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVED---DRALREALadtLLLAGHDYRAVGSAEDALEAV-------------------EQE-SFSLVVSDVNMPGMDG 61
Cdd:PLN03029   11 VLAVDDsliDRKLIEKL---LKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspnsHQEvEVNLIITDYCMPGMTG 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1509073841  62 HQLLSLLRARQP--QLPVLLMTAHGAVERAVDAMRQGAADYLVKP 104
Cdd:PLN03029   88 YDLLKKIKESSSlrNIPVVIMSSENVPSRITRCLEEGAEEFFLKP 132
FleQ pfam06490
Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of ...
4-91 3.06e-04

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


Pssm-ID: 428975 [Multi-domain]  Cd Length: 108  Bit Score: 40.25  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNmpgMDGHQLLSLLRARQPQLPVLLMTAH 83
Cdd:pfam06490   1 KILVIDDDAERRHDLSTILEFLGEQCEAISSEDLSAALWSSRWEALAVILGS---VSAAELLKALAKWDPHLPVLLLGET 77

                  ....*...
gi 1509073841  84 GAVERAVD 91
Cdd:pfam06490  78 DDALELAN 85
PRK13558 PRK13558
bacterio-opsin activator; Provisional
2-140 3.42e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 42.90  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   2 AIKVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMT 81
Cdd:PRK13558    7 TRGVLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGLALLEAVRQTTAVPPVVVVP 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1509073841  82 AHG---AVERAVDAmrqGAADYlVKPFEPKALIELVAR---HALGVISASEGEGPIAFEPASAQL 140
Cdd:PRK13558   87 TAGdeaVARRAVDA---DAAAY-VPAVSDDATAAIAERiesAVPEHSRDTEARMPISDLTVESDR 147
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
149-252 4.93e-04

MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350658 [Multi-domain]  Cd Length: 311  Bit Score: 41.94  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 149 RSDSTVLISGESGTGKEVLARYIHQQSTRAKqpFIAINCAAIPDnmLEATLfghEKGSFTGAIAAQAGKFEQADGGTILL 228
Cdd:cd17706    39 RGDIHILLVGDPGTAKSQILKYVLKIAPRGV--YTSGKGSSGAG--LTAAV---VRDSETGEWYLEAGALVLADGGVCCI 111
                          90       100
                  ....*....|....*....|....
gi 1509073841 229 DEISEMPLGLQAKLLRVLQEREVE 252
Cdd:cd17706   112 DEFDKMKELDRTALHEAMEQQTIS 135
HTH_20 pfam12840
Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in ...
395-449 1.02e-03

Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in transcriptional regulatory proteins.


Pssm-ID: 432824 [Multi-domain]  Cd Length: 61  Bit Score: 37.13  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1509073841 395 ETAGALGDDLRRRefqmIIDTLRSERGR-RKEAAERLGISPRTLRYKLAQMRDAGM 449
Cdd:pfam12840   2 DVAEALADPTRLR----ILRALVGDEPLtASELARRLDISRNTLSYHLRKLEEAGL 53
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
399-448 1.45e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 37.28  E-value: 1.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1509073841 399 ALGDDLRRRefqmIIDTLRSERGRRKEAAERLGISPRTLRYKLAQMRDAG 448
Cdd:cd00090     3 ALSDPTRLR----ILRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAG 48
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
2-143 1.53e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 41.08  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   2 AIKVLLVED-------DRALREALadtlllaGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQP- 73
Cdd:PRK11091  525 ALNILLVEDielnvivARSVLEKL-------GNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPr 597
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1509073841  74 -QLPVLL-MTAHgaVERAVDAMRQ-GAADYLVKPFEPKALIELVARhaLGVISASEGEGPIAFEP--ASAQLLEL 143
Cdd:PRK11091  598 eDLPPLVaLTAN--VLKDKKEYLDaGMDDVLSKPLSVPALTAMIKK--FWDTQDDEESTVTTEESskANEALLDI 668
dpiA PRK10046
two-component response regulator DpiA; Provisional
3-117 1.79e-03

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 39.62  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTL--LLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLL-SLLRARQPQlPVLL 79
Cdd:PRK10046    5 LTLLIVEDETPLAEMHAEYIrhIPGFSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLhELVQAHYPG-DVVF 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1509073841  80 MTAHGAVERAVDAMRQGAADYLVKPFEPKALIELVARH 117
Cdd:PRK10046   84 TTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRF 121
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
38-82 1.80e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 39.49  E-value: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1509073841  38 ALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:PRK09958   37 AVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSA 81
PRK13856 PRK13856
two-component response regulator VirG; Provisional
5-116 2.80e-03

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 39.41  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLrARQPQLPVLLMTAHG 84
Cdd:PRK13856    4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSL-ATKSDVPIIIISGDR 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1509073841  85 AVE-RAVDAMRQGAADYLVKPFepkALIELVAR 116
Cdd:PRK13856   83 LEEaDKVVALELGATDFIAKPF---GTREFLAR 112
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
7-104 3.13e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 37.25  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   7 LVEDDRALREALADtlLLAGHDY-RAVGSAEDALEAVEQESF---SLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:cd17565     3 IVDDDKNIIKILSD--IIEDDDLgEVVGEADNGAQAYDEILFlqpDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80
                          90       100
                  ....*....|....*....|..
gi 1509073841  83 HGAVERAVDAMRQGAADYLVKP 104
Cdd:cd17565    81 VSDKEMIGKAYQAGIEFFINKP 102
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
1-103 3.69e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 38.70  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   1 MAIKVLLVEDDRAlrealadTLLLAGHDYRavgsaeDALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:PRK09935   17 MSIEVLLQKNSEL-------QIVLKTDDYR------ITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFL 83
                          90       100
                  ....*....|....*....|...
gi 1509073841  81 TAHGAVERAVDAMRQGAADYLVK 103
Cdd:PRK09935   84 SSKSECFYAGRAIQAGANGFVSK 106
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
4-83 4.92e-03

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 39.50  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   4 KVLLVEDDRALREALADTLLLAGHDYRAVGSAEDALEAV-EQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLLMTA 82
Cdd:PRK11466  683 RLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLqNSEPFAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSA 762

                  .
gi 1509073841  83 H 83
Cdd:PRK11466  763 H 763
PRK14084 PRK14084
DNA-binding response regulator;
3-108 7.25e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 38.19  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREALADTLLLAGHdYRAVGSAE---DALEAVEQESFSLVVSDVNMPGMDGHQLLSLLRARQPQLPVLL 79
Cdd:PRK14084    1 MKALIVDDEPLARNELTYLLNEIGG-FEEINEAEnvkETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIF 79
                          90       100
                  ....*....|....*....|....*....
gi 1509073841  80 MTAHGAVerAVDAMRQGAADYLVKPFEPK 108
Cdd:PRK14084   80 ATAHDQF--AVKAFELNATDYILKPFEQK 106
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
138-235 7.68e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.10  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841 138 AQLLELAARVARSD-STVLISGESGTGKEVLARYIHQQSTRAKQPFIAINCAAIPDNMLEATLFGheKGSFTGAIAAQAG 216
Cdd:pfam13191  10 EQLLDALDRVRSGRpPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALT--REGLLRQLLDELE 87
                          90
                  ....*....|....*....
gi 1509073841 217 KFEQADGGTILLDEISEMP 235
Cdd:pfam13191  88 SSLLEAWRAALLEALAPVP 106
PRK10430 PRK10430
two-component system response regulator DcuR;
3-106 8.64e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 37.78  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   3 IKVLLVEDDRALREaLADTLL--LAGHDYRAVGS----AEDALEAVEQEsFSLVVSDVNMPGMDGHQLLSLLRARQPQLP 76
Cdd:PRK10430    2 INVLIVDDDAMVAE-LNRRYVaqIPGFQCCGTAStleqAKEIIFNSDTP-IDLILLDIYMQQENGLDLLPVLHEAGCKSD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1509073841  77 VLLMTAHGAVERAVDAMRQGAADYLVKPFE 106
Cdd:PRK10430   80 VIVISSAADAATIKDSLHYGVVDYLIKPFQ 109
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
5-116 9.82e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 38.51  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1509073841   5 VLLVEDDRALREALADTLLLAGhdYRAVGSAE--DALEAVEQ--ESFSLVVsdVNMPGMDGHQLLSLLRARQPQLPVLLM 80
Cdd:PRK13837  700 VLLVEPDDATLERYEEKLAALG--YEPVGFSTlaAAIAWISKgpERFDLVL--VDDRLLDEEQAAAALHAAAPTLPIILG 775
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1509073841  81 TAhGAVERAVDAMRQGAADYLVKPFEPKALIELVAR 116
Cdd:PRK13837  776 GN-SKTMALSPDLLASVAEILAKPISSRTLAYALRT 810
 
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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