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Conserved domains on  [gi|782651413|ref|WP_045591719|]
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sigma-54 dependent transcriptional regulator [Burkholderia pseudomallei]

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, ...
13-439 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: 519.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVILLTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSlraqlsgERPLLGSAPAMQRVHALIDAIGPTSA 172
Cdd:COG2204   83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-------DSGLIGRSPAMQEVRRLIEKVAPSDA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 173 DVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELE 251
Cdd:COG2204  156 TVLITGESGTGKELVARAIHRLSpRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 252 SMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELF 331
Cdd:COG2204  236 EMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 332 SHFLRAAAVRFEKPEPVwTQEDMMRWQLYDWPGNVRELKNTAERFCLGLEDGLprspAGFDSLASRMVSAERAYIEEALR 411
Cdd:COG2204  316 RHFLARFAAELGKPVKL-SPEALEALLAYDWPGNVRELENVIERAVILADGEV----ITAEDLPEALEEVERELIERALE 390
                        410       420
                 ....*....|....*....|....*...
gi 782651413 412 NAGGQVAKAAELLGLPRKTLYDKITRHG 439
Cdd:COG2204  391 ETGGNVSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
13-439 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: 519.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVILLTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSlraqlsgERPLLGSAPAMQRVHALIDAIGPTSA 172
Cdd:COG2204   83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-------DSGLIGRSPAMQEVRRLIEKVAPSDA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 173 DVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELE 251
Cdd:COG2204  156 TVLITGESGTGKELVARAIHRLSpRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 252 SMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELF 331
Cdd:COG2204  236 EMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 332 SHFLRAAAVRFEKPEPVwTQEDMMRWQLYDWPGNVRELKNTAERFCLGLEDGLprspAGFDSLASRMVSAERAYIEEALR 411
Cdd:COG2204  316 RHFLARFAAELGKPVKL-SPEALEALLAYDWPGNVRELENVIERAVILADGEV----ITAEDLPEALEEVERELIERALE 390
                        410       420
                 ....*....|....*....|....*...
gi 782651413 412 NAGGQVAKAAELLGLPRKTLYDKITRHG 439
Cdd:COG2204  391 ETGGNVSRAAELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
13-435 6.88e-132

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: 388.33  E-value: 6.88e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKA-HPrdaDIPVILMT 91
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKrHP---QLPVIVMT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   92 GHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQLSGERPLLGSAPAMQRVHALIDAIGPTS 171
Cdd:TIGR01818  78 AHSDLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  172 ADVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDEL 250
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSpRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  251 ESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPEL 330
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  331 FSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCL----------GLEDGLPRSP------------ 388
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVmasgdevlvsDLPAELALTGrpasapdsdgqd 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 782651413  389 ---------------AGFDSLASRMVSA-ERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKI 435
Cdd:TIGR01818 398 swdealeawakqalsRGEQGLLDRALPEfERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKL 460
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
10-441 1.60e-119

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 356.47  E-value: 1.60e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  10 REAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDAdiPVIL 89
Cdd:PRK11361   4 INRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRT--PVIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQLS---GERPLLGSAPAMQRVHALIDA 166
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALStswQWGHILTNSPAMMDICKDTAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 167 IGPTSADVLIIGETGTGKEVLARALHAASRR-TGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTL 245
Cdd:PRK11361 162 IALSQASVLISGESGTGKELIARAIHYNSRRaKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 246 FLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTD 325
Cdd:PRK11361 242 LLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRRE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 326 DIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCLG------LEDGLPR------------- 386
Cdd:PRK11361 322 DISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMnsgpiiFSEDLPPqirqpvcnagevk 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 782651413 387 -SPAGFDSLASRMVSAERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGID 441
Cdd:PRK11361 402 tAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Sigma54_activat pfam00158
Sigma-54 interaction domain;
150-316 2.56e-97

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 288.92  E-value: 2.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  150 LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTG 228
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSpRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  229 AQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYF 308
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 782651413  309 RLNVASIE 316
Cdd:pfam00158 161 RLNVIPIE 168
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
58-432 1.04e-85

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 271.75  E-value: 1.04e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  58 IVSDVRLPGMGGLALLDSMKAHPRDADIPVIL--MTGHGDVA-----MAVGAMRCGAyDFIEKPFHSDR---LVDTVRRA 127
Cdd:NF038308  77 VLRDPWDFEEVYGALLDFARAYPFDTENEDYLvhITTGTHVAqicwfLLVEARYLPA-RLLQTSPPRDKeegTYEIIDLD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 128 LEhRKLVIENRSLRAQLSGERPLLGSA----PAMQRVHALIDAIGPTS-ADVLIIGETGTGKEVLARALHAASRR----T 198
Cdd:NF038308 156 LS-RYDALAQRFAREQAEAVSFLKSGIatrnAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRrhqvS 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 199 GPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVS 278
Cdd:NF038308 235 GPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKE 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 279 VAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAA------VRFEKPepvwtqe 352
Cdd:NF038308 315 VSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYELDRFArelgrqVRFNKE------- 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 353 dmmRWQLYD---------WPGNVRELKNTAERFC-------------------LGLEDGLPRSPAGFDSLASRMVS---- 400
Cdd:NF038308 388 ---ARFRYLafatspealWPGNFRELSASVTRMAtladggriteelveeeiarLRAAWQSAPAAADDDALADLLGGeqla 464
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 782651413 401 -------AERAYIEEALRNAGGQVAKAAELLGLPRKTLY 432
Cdd:NF038308 465 eldlfdrVQLAAVLRVCRQSRSLSAAGRRLFGVSRQQKA 503
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
13-144 3.12e-63

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: 200.41  E-value: 3.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILITG 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQL 144
Cdd:cd17549   79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
174-310 2.43e-10

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: 58.54  E-value: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   174 VLIIGETGTGKEVLARALHA-ASRRTGPFVALNCAALPEAVFES---EIFGHEPGAFTGAQQRRIG--KFEYASGGTLFL 247
Cdd:smart00382   5 ILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLIL 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 782651413   248 DELESMPLSLQAKLLRALQErsiERLGSNVSVAVDVRVIAAV--KQDLKQLVADGLFRSDLYFRL 310
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTndEKDLGPALLRRRFDRRIVLLL 146
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
13-439 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: 519.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVILLTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSlraqlsgERPLLGSAPAMQRVHALIDAIGPTSA 172
Cdd:COG2204   83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-------DSGLIGRSPAMQEVRRLIEKVAPSDA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 173 DVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELE 251
Cdd:COG2204  156 TVLITGESGTGKELVARAIHRLSpRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 252 SMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELF 331
Cdd:COG2204  236 EMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 332 SHFLRAAAVRFEKPEPVwTQEDMMRWQLYDWPGNVRELKNTAERFCLGLEDGLprspAGFDSLASRMVSAERAYIEEALR 411
Cdd:COG2204  316 RHFLARFAAELGKPVKL-SPEALEALLAYDWPGNVRELENVIERAVILADGEV----ITAEDLPEALEEVERELIERALE 390
                        410       420
                 ....*....|....*....|....*...
gi 782651413 412 NAGGQVAKAAELLGLPRKTLYDKITRHG 439
Cdd:COG2204  391 ETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
123-441 6.54e-142

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: 413.40  E-value: 6.54e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 123 TVRRALEHRKLVIENRSLRAQLSGERPLLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAAS-RRTGPF 201
Cdd:COG3829  113 TELKRLERKLREEELERGLSAKYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASpRRDGPF 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 202 VALNCAALPEAVFESEIFGHEPGAFTGA-QQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVA 280
Cdd:COG3829  193 VAVNCAAIPENLLESELFGYEKGAFTGAkKGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIP 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 281 VDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLY 360
Cdd:COG3829  273 VDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAY 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 361 DWPGNVRELKNTAER---FCLG------------LEDGLPRSPAGFDSLASRMVSAERAYIEEALRNAGGQVAKAAELLG 425
Cdd:COG3829  353 DWPGNVRELENVIERavvLSEGdvitpehlpeylLEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGNKSKAAKALG 432
                        330
                 ....*....|....*.
gi 782651413 426 LPRKTLYDKITRHGID 441
Cdd:COG3829  433 ISRSTLYRKLKKYGIK 448
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
13-435 6.88e-132

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: 388.33  E-value: 6.88e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKA-HPrdaDIPVILMT 91
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKrHP---QLPVIVMT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   92 GHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQLSGERPLLGSAPAMQRVHALIDAIGPTS 171
Cdd:TIGR01818  78 AHSDLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  172 ADVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDEL 250
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSpRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  251 ESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPEL 330
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  331 FSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCL----------GLEDGLPRSP------------ 388
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVmasgdevlvsDLPAELALTGrpasapdsdgqd 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 782651413  389 ---------------AGFDSLASRMVSA-ERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKI 435
Cdd:TIGR01818 398 swdealeawakqalsRGEQGLLDRALPEfERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKL 460
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
10-441 1.60e-119

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 356.47  E-value: 1.60e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  10 REAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDAdiPVIL 89
Cdd:PRK11361   4 INRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRT--PVIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQLS---GERPLLGSAPAMQRVHALIDA 166
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALStswQWGHILTNSPAMMDICKDTAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 167 IGPTSADVLIIGETGTGKEVLARALHAASRR-TGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTL 245
Cdd:PRK11361 162 IALSQASVLISGESGTGKELIARAIHYNSRRaKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 246 FLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTD 325
Cdd:PRK11361 242 LLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRRE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 326 DIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCLG------LEDGLPR------------- 386
Cdd:PRK11361 322 DISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMnsgpiiFSEDLPPqirqpvcnagevk 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 782651413 387 -SPAGFDSLASRMVSAERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGID 441
Cdd:PRK11361 402 tAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
43-440 2.70e-119

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: 355.60  E-value: 2.70e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   43 AESALAALKRDPPAAIVSDVRLP-----GMGGLALLDSM-KAHPrdaDIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFH 116
Cdd:TIGR02915  29 RESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQIlAIAP---DTKVIVITGNDDRENAVKAIGLGAYDFYQKPID 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  117 SDRLVDTVRRALEHRKLVIENRSLRAQLSGE--RPLLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAA 194
Cdd:TIGR02915 106 PDVLKLIVDRAFHLYTLETENRRLQSALGGTalRGLITSSPGMQKICRTIEKIAPSDITVLLLGESGTGKEVLARALHQL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  195 S-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERL 273
Cdd:TIGR02915 186 SdRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLFLDEIGDLPLNLQAKLLRFLQERVIERL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  274 GSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEPVWTQED 353
Cdd:TIGR02915 266 GGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGDAVLLANAFLERFARELKRKTKGFTDDA 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  354 MMRWQLYDWPGNVRELKNTAER------------FCLGLEDGlpRSPAGFDSLASRMV--SAERAYIEEALRNAGGQVAK 419
Cdd:TIGR02915 346 LRALEAHAWPGNVRELENKVKRavimaegnqitaEDLGLDAR--ERAETPLEVNLREVreRAEREAVRKAIARVDGNIAR 423
                         410       420
                  ....*....|....*....|.
gi 782651413  420 AAELLGLPRKTLYDKITRHGI 440
Cdd:TIGR02915 424 AAELLGITRPTLYDLMKKHGI 444
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
10-441 2.64e-113

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 341.08  E-value: 2.64e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  10 REAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMK-AHPRdadIPVI 88
Cdd:PRK10923   3 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKqRHPM---LPVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  89 LMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLviENRSLRAQLSGE-RPLLGSAPAMQRVHALIDAI 167
Cdd:PRK10923  80 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQE--QQQPRNIQVNGPtTDIIGEAPAMQDVFRIIGRL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 168 GPTSADVLIIGETGTGKEVLARALHAASRRT-GPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLF 246
Cdd:PRK10923 158 SRSSISVLINGESGTGKELVAHALHRHSPRAkAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 247 LDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDD 326
Cdd:PRK10923 238 LDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERRED 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 327 IPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNT-------------------AERFCLGLEDGLPR- 386
Cdd:PRK10923 318 IPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTcrwltvmaagqevliqdlpGELFESTVPESTSQm 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 782651413 387 SPAGF-----------------DSLASRMVSAERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGID 441
Cdd:PRK10923 398 QPDSWatllaqwadralrsghqNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
13-437 3.60e-112

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 337.39  E-value: 3.60e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAvrlGCS--QALaLEGIG--VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVI 88
Cdd:PRK10365   8 ILVVDDDIS---HCTilQAL-LRGWGynVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAIPVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  89 LMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEH-RKLVIENRSLRAQLSGerpLLGSAPAMQRVHALIDAI 167
Cdd:PRK10365  82 IMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHtHSIDAETPAVTASQFG---MVGKSPAMQHLLSEIALV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 168 GPTSADVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLF 246
Cdd:PRK10365 159 APSEATVLIHGDSGTGKELVARAIHASSaRSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 247 LDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDD 326
Cdd:PRK10365 239 LDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRRED 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 327 IPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCLGL------EDGLPRS------PAGFDSL 394
Cdd:PRK10365 319 IPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLtgeyisERELPLAiastpiPLGQSQD 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 782651413 395 ASRMVSAERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITR 437
Cdd:PRK10365 399 IQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
116-439 6.00e-103

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 319.15  E-value: 6.00e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 116 HSDRLVDTVRRALEHRKLVIENRSLRAQLSGERPLLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAAS 195
Cdd:COG3284  289 RDGRRLGALLRLRPARRAARAAPAGAPAPAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAAS 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 196 -RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQR-RIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERL 273
Cdd:COG3284  369 pRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPL 448
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 274 GSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTdDIPELFSHFLRAAAVRFEkpEPVWTQED 353
Cdd:COG3284  449 GGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRERE-DLPALIEHLLRELAAGRG--PLRLSPEA 525
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 354 MMRWQLYDWPGNVRELKNTAERFCLGLEDG------LP---------RSPAGFDSLaSRMVSAERAYIEEALRNAGGQVA 418
Cdd:COG3284  526 LALLAAYPWPGNVRELRNVLRTALALADGGvitvedLPdelraelaaAAPAAAAPL-TSLEEAERDAILRALRACGGNVS 604
                        330       340
                 ....*....|....*....|.
gi 782651413 419 KAAELLGLPRKTLYDKITRHG 439
Cdd:COG3284  605 AAARALGISRSTLYRKLKRYG 625
PRK15115 PRK15115
response regulator GlrR; Provisional
30-446 2.58e-99

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 304.45  E-value: 2.58e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  30 LALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSM-KAHPrdaDIPVILMTGHGDVAMAVGAMRCGAY 108
Cdd:PRK15115  25 LTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIqKVQP---GMPVIILTAHGSIPDAVAATQQGVF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 109 DFIEKPFHSDRLVDTVRRALEHRKLVIENRsLRAQLsgerplLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLA 188
Cdd:PRK15115 102 SFLTKPVDRDALYKAIDDALEQSAPATDER-WREAI------VTRSPLMLRLLEQARMVAQSDVSVLINGQSGTGKEILA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 189 RALHAASRRTG-PFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQE 267
Cdd:PRK15115 175 QAIHNASPRASkPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQE 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 268 RSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEP 347
Cdd:PRK15115 255 RKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLLRQAAERHKPFVR 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 348 VWTQEDMMRWQLYDWPGNVRELKNTAERfCLGLEDglprSPAGFDSLASRMVSA---------------ERAYIEEALRN 412
Cdd:PRK15115 335 AFSTDAMKRLMTASWPGNVRQLVNVIEQ-CVALTS----SPVISDALVEQALEGentalptfvearnqfELNYLRKLLQI 409
                        410       420       430
                 ....*....|....*....|....*....|....
gi 782651413 413 AGGQVAKAAELLGLPRKTLYDKITRHGIDMTAFR 446
Cdd:PRK15115 410 TKGNVTHAARMAGRNRTEFYKLLSRHELDANDFK 443
Sigma54_activat pfam00158
Sigma-54 interaction domain;
150-316 2.56e-97

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 288.92  E-value: 2.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  150 LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTG 228
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSpRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  229 AQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYF 308
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 782651413  309 RLNVASIE 316
Cdd:pfam00158 161 RLNVIPIE 168
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
126-432 6.20e-91

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 284.76  E-value: 6.20e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 126 RALEHRKLVIENRS--LRAQLSGERPLLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAASRR-TGPFV 202
Cdd:PRK05022 163 EQLESQAELPQDVAefLRQEALKEGEMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRaDKPLV 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 203 ALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVD 282
Cdd:PRK05022 243 YLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVD 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 283 VRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDW 362
Cdd:PRK05022 323 VRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDW 402
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 363 PGNVRELKNT--------------------AERFCLGLEDGLPRSPAG-------FDSLASRMVSAERAYIEEALRNAGG 415
Cdd:PRK05022 403 PGNVRELEHVisraallarargagrivtleAQHLDLPAEVALPPPEAAaapaavvSQNLREATEAFQRQLIRQALAQHQG 482
                        330
                 ....*....|....*..
gi 782651413 416 QVAKAAELLGLPRKTLY 432
Cdd:PRK05022 483 NWAAAARALELDRANLH 499
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
109-445 1.32e-87

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: 276.98  E-value: 1.32e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  109 DFIEKPFHSDRLVDTVRRALEHRKLVIENrslraqlsgerpLLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLA 188
Cdd:TIGR01817 169 LIAEAVQLSKQLRDKAPEIARRRSGKEDG------------IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  189 RALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQE 267
Cdd:TIGR01817 237 KAIHYLSpRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQE 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  268 RSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEP 347
Cdd:TIGR01817 317 GEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPLT 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  348 VwTQEDMMRWQLYDWPGNVRELKNTAERFCLGLEDGL----------------------------------------PRS 387
Cdd:TIGR01817 397 I-TPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTitrsdfscqsgqclspmlaktcphghisidplagttpphsPAS 475
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 782651413  388 ---PAGFDSLASRMvsAERAYIEEALRNAGGQVAKAAELLGL-PRKTLYdKITRHGIDMTAF 445
Cdd:TIGR01817 476 aalPGEPGLSGPTL--SERERLIAALEQAGWVQAKAARLLGMtPRQVGY-ALRKLNIEMKKL 534
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
150-372 5.50e-86

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 272.06  E-value: 5.50e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 150 LLGSAPAMQRV------HALIDAigPtsadVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHE 222
Cdd:COG3283  206 IVASSPKMRQVirqakkMAMLDA--P----LLIQGETGTGKELLARACHLASpRGDKPFLALNCAALPDDVAESELFGYA 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 223 PGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLF 302
Cdd:COG3283  280 PGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEF 359
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 303 RSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNT 372
Cdd:COG3283  360 REDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENA 429
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
58-432 1.04e-85

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 271.75  E-value: 1.04e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  58 IVSDVRLPGMGGLALLDSMKAHPRDADIPVIL--MTGHGDVA-----MAVGAMRCGAyDFIEKPFHSDR---LVDTVRRA 127
Cdd:NF038308  77 VLRDPWDFEEVYGALLDFARAYPFDTENEDYLvhITTGTHVAqicwfLLVEARYLPA-RLLQTSPPRDKeegTYEIIDLD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 128 LEhRKLVIENRSLRAQLSGERPLLGSA----PAMQRVHALIDAIGPTS-ADVLIIGETGTGKEVLARALHAASRR----T 198
Cdd:NF038308 156 LS-RYDALAQRFAREQAEAVSFLKSGIatrnAAFNRLIEQIERVALRSrAPILLTGPTGAGKSFLARRIYELKKRrhqvS 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 199 GPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVS 278
Cdd:NF038308 235 GPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKE 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 279 VAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAA------VRFEKPepvwtqe 352
Cdd:NF038308 315 VSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYELDRFArelgrqVRFNKE------- 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 353 dmmRWQLYD---------WPGNVRELKNTAERFC-------------------LGLEDGLPRSPAGFDSLASRMVS---- 400
Cdd:NF038308 388 ---ARFRYLafatspealWPGNFRELSASVTRMAtladggriteelveeeiarLRAAWQSAPAAADDDALADLLGGeqla 464
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 782651413 401 -------AERAYIEEALRNAGGQVAKAAELLGLPRKTLY 432
Cdd:NF038308 465 eldlfdrVQLAAVLRVCRQSRSLSAAGRRLFGVSRQQKA 503
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
122-432 3.53e-85

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 270.82  E-value: 3.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 122 DTVRRALEHR----KLVIENRSLRAQLSGERP------LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARAL 191
Cdd:PRK15424 183 ATVRQAFEDAldmtRMTLRHNTHYATRNALRTryvlgdLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAI 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 192 HAA---------SRRTGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQR-RIGKFEYASGGTLFLDELESMPLSLQAKL 261
Cdd:PRK15424 263 HREyfarhdarqGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRL 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 262 LRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAA--- 338
Cdd:PRK15424 343 LRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSlaa 422
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 339 -AVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCLGL----EDGLPR------SPAGFDSLAS-RMVSAERAYI 406
Cdd:PRK15424 423 lSAPFSAALRQGLQQCETLLLHYDWPGNVRELRNLMERLALFLsvepTPDLTPqflqllLPELARESAKtPAPRLLAATL 502
                        330       340
                 ....*....|....*....|....*.
gi 782651413 407 EEALRNAGGQVAKAAELLGLPRKTLY 432
Cdd:PRK15424 503 QQALERFNGDKTAAANYLGISRTTLW 528
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
150-426 4.36e-85

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: 263.77  E-value: 4.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  150 LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAASRR-TGPFVALNCAALPEAVFESEIFGHEPGAFTG 228
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRwQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  229 AQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYF 308
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  309 RLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPE-PVWTQEDMMRWQLYDWPGNVRELKNTAER--FCLGLEDGL- 384
Cdd:TIGR02974 161 RLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLfPGFTPQAREQLLEYHWPGNVRELKNVVERsvYRHGLEEAPi 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 782651413  385 ------------------------PRSPAGFDS-----------LASRMVSAERAYIEEALRNAGGQVAKAAELLGL 426
Cdd:TIGR02974 241 deiiidpfaspwrpkqaapavdevNSTPTDLPSpssiaaafpldLKQAQQDYEIELLQQALAEAQFNQRKAAELLGL 317
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
130-441 9.48e-83

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 268.24  E-value: 9.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 130 HR---KLVIENRSLRAQLSGERP----LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAASRRTGP-F 201
Cdd:PRK15429 351 HRlkeRLVDENLALTEQLNNVDSefgeIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRrM 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 202 VALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAV 281
Cdd:PRK15429 431 VKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQT 510
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 282 DVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYD 361
Cdd:PRK15429 511 DVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNME 590
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 362 WPGNVRELKNTAERFCL-----GLEDGLP-RSPAGFDSLASRMVSA-----ERAYIEEALRNAGGQVA---KAAELLGLP 427
Cdd:PRK15429 591 WPGNVRELENVIERAVLltrgnVLQLSLPdITLPEPETPPAATVVAqegedEYQLIVRVLKETNGVVAgpkGAAQRLGLK 670
                        330
                 ....*....|....
gi 782651413 428 RKTLYDKITRHGID 441
Cdd:PRK15429 671 RTTLLSRMKRLGID 684
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
150-432 1.46e-80

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: 258.64  E-value: 1.46e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  150 LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHA-ASRRTGPFVALNCAALPEAVFESEIFGHEPGAFTG 228
Cdd:TIGR02329 214 LLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQlSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTG 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  229 AQQ-RRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLY 307
Cdd:TIGR02329 294 ARRgGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLF 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  308 FRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKP-EPVWTQE---DMMRWQLYDWPGNVRELKNTAERFCLGL--- 380
Cdd:TIGR02329 374 YRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPdSEAAAQVlagVADPLQRYPWPGNVRELRNLVERLALELsam 453
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 782651413  381 ---------------EDGLPRSPAGFDSLASRMVSAERAY-IEEALRNAGGQVAKAAELLGLPRKTLY 432
Cdd:TIGR02329 454 pagaltpdvlralapELAEASGKGKTSALSLRERSRVEALaVRAALERFGGDRDAAAKALGISRTTLW 521
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
150-440 2.11e-72

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 231.10  E-value: 2.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 150 LLGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHAASRR-TGPFVALNCAALPEAVFESEIFGHEPGAFTG 228
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRwQGPFISLNCAALNENLLDSELFGHEAGAFTG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 229 AQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYF 308
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 309 RLNVASIELPPLRRRTDDIPELFSHFlrAAAVRFEKPEPVWTQ-EDMMRWQL--YDWPGNVRELKNTAER--FCLGLEDG 383
Cdd:PRK11608 168 RLAFDVVQLPPLRERQSDIMLMAEHF--AIQMCRELGLPLFPGfTERARETLlnYRWPGNIRELKNVVERsvYRHGTSEY 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 384 ---------LPRSPAGFDSLASRMVSA--------------ERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGI 440
Cdd:PRK11608 246 pldniiidpFKRRPAEEAIAVSETTSLptlpldlrewqhqqEKELLQRSLQQAKFNQKRAAELLGLTYHQLRALLKKHQI 325
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
176-441 1.61e-71

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: 229.35  E-value: 1.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 176 IIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESeifghepgaftgaqqrrigkfeyasggtlfldelesmp 254
Cdd:COG3604  120 ILGETGTGKELVANAIHELSpRADKPFVKVNCAALPESLLES-------------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 255 lslqakllraLQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRRRTDDIPELFSHF 334
Cdd:COG3604  162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 335 LRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAERFCLGLEDGLPRSPAGFDSLASRMVSAERAYIEEALRNAG 414
Cdd:COG3604  232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSREALEEVEREHILEALERTG 311
                        250       260
                 ....*....|....*....|....*..
gi 782651413 415 GQVAKAAELLGLPRKTLYDKITRHGID 441
Cdd:COG3604  312 GNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK10820 PRK10820
transcriptional regulator TyrR;
84-375 1.52e-65

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 218.79  E-value: 1.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  84 DIPVILMTGHGDVAMAVGAMRCgaydfiekpfhsdrLVDTVRRALEHRKLVIENRSLRAQLsgerplLGSAPAMQRVHAL 163
Cdd:PRK10820 160 EITPVYLQDENDQHVLVGAVVM--------------LRSTARMGRQLQNLAVNDDSAFSQI------VAVSPKMRQVVEQ 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 164 IDAIGPTSADVLIIGETGTGKEVLARALHAASRRTG-PFVALNCAALPEAVFESEIFGHEPGAFTGAQQRRIGKFEYASG 242
Cdd:PRK10820 220 ARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKkPFLALNCASIPDDVVESELFGHAPGAYPNALEGKKGFFEQANG 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 243 GTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVASIELPPLRR 322
Cdd:PRK10820 300 GSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYYRLNVLTLNLPPLRD 379
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 782651413 323 RTDDIPELFSHFLRAAAVRFEKPEPVWTQEDMMRWQLYDWPGNVRELKNTAER 375
Cdd:PRK10820 380 RPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYR 432
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
13-144 3.12e-63

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: 200.41  E-value: 3.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILITG 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQL 144
Cdd:cd17549   79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
150-445 6.28e-60

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 206.45  E-value: 6.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 150 LLGSAPAMQRV-----HAlIDAIGPtsadVLIIGETGTGKEVLARALHAAS-RRTGPFVALNCAALPEAVFESEIFGHEP 223
Cdd:PRK11388 327 MPQDSPQMRRLihfgrQA-AKSSFP----VLLCGEEGVGKALLAQAIHNESeRAAGPYIAVNCQLYPDEALAEEFLGSDR 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 224 gafTGAQQRRIGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFR 303
Cdd:PRK11388 402 ---TDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFS 478
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 304 SDLYFRLNVASIELPPLRRRTDDIPELFSHFLRAAAVRFEKPEPVwTQEDMMRWQLYDWPGNVRELKNTAER---FC--- 377
Cdd:PRK11388 479 RQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLKI-DDDALARLVSYRWPGNDFELRSVIENlalSSdng 557
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 378 -LGLEDgLP-----RSPAGfDSLASRMVS------AERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGIDMTAF 445
Cdd:PRK11388 558 rIRLSD-LPehlftEQATD-DVSATRLSTslslaeLEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQF 635
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
13-144 1.99e-42

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: 148.32  E-value: 1.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA--RGSPLPVIFLTG 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQL 144
Cdd:COG4566   80 HGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAEL 131
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
13-128 6.58e-37

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: 131.18  E-value: 6.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPIIFITG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17537   81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
fixJ PRK09390
response regulator FixJ; Provisional
9-132 6.28e-36

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 131.28  E-value: 6.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   9 GREAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVI 88
Cdd:PRK09390   2 DKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKA--RGSPLPVI 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 782651413  89 LMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRK 132
Cdd:PRK09390  80 VMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAP 123
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
162-369 4.65e-34

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: 133.80  E-value: 4.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 162 ALIDAI----GPTSADVLIIGETGTGKEVLARALHA--ASRR--TGPFVALNCAALPEAVFESEIFGHEPGAFTGAQQRR 233
Cdd:COG4650  195 RLIEQIervaIRSRAPILLTGPTGAGKSQLARRIYElkKARHqvSGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDR 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 234 IGKFEYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSNVSVAVDVRVIAAVKQDLKQLVADGLFRSDLYFRLNVA 313
Cdd:COG4650  275 AGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLW 354
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 782651413 314 SIELPPLRRRTDDIPELFSHFLRAAA------VRFEK------------PEPVwtqedmmrwqlydWPGNVREL 369
Cdd:COG4650  355 TFRLPGLAERREDIEPNLDYELARFAreqgrrVRFNKeararylafatsPEAL-------------WSGNFRDL 415
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
13-129 7.05e-34

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: 122.99  E-value: 7.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE--KYPDLPVIMISG 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALE 129
Cdd:cd17550   79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
13-133 1.38e-32

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: 119.61  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMkaHPRDADIPVILMTG 92
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWI--QERSLPTSVIVITA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKL 133
Cdd:cd17572   79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKL 119
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
11-128 3.23e-32

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: 118.53  E-value: 3.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  11 EAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKA-HPrdaDIPVIL 89
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQrHP---DLPVII 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd19919   78 MTAHSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
13-150 1.94e-31

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: 119.88  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:COG3437    9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLTA 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQLSGERPL 150
Cdd:COG3437   89 LADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPL 146
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
13-132 6.60e-29

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 109.94  E-value: 6.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALTA 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRK 132
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
13-125 4.59e-28

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: 107.24  E-value: 4.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPrdADIPVILMTG 92
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 782651413   93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
15-126 9.16e-27

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 105.76  E-value: 9.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHG 94
Cdd:COG3706    6 VVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLTALD 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 782651413  95 DVAMAVGAMRCGAYDFIEKPFHSDRL---VDTVRR 126
Cdd:COG3706   86 DEEDRARALEAGADDYLTKPFDPEELlarVDLVAR 120
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
13-132 1.12e-25

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: 103.50  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRdaDIPVILMTG 92
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIMLTA 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRK 132
Cdd:COG0745   82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
15-114 4.23e-24

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: 95.76  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRdaDIPVILMTGHG 94
Cdd:cd00156    2 IVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVIVLTAKA 79
                         90       100
                 ....*....|....*....|
gi 782651413  95 DVAMAVGAMRCGAYDFIEKP 114
Cdd:cd00156   80 DEEDAVRALELGADDYLVKP 99
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
174-371 8.36e-24

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: 104.80  E-value: 8.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 174 VLIIGETGTGKEVLARALHAASRRTG------PFVALNCAAL---PEAVFeSEIFGHEPGAFTGAQQRRIGKFEYASGGT 244
Cdd:COG1221  133 TLILGPTGVGKSFFAELMYEYAIEIGvlpedaPFVVFNCADYannPQLLM-SQLFGYVKGAFTGADKDKEGLIEKADGGI 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 245 LFLDELESMPLSLQAKLLRALQERSIERLG-SNVSVAVDVRVIAAVKQDLKQLVADGLFRsdlyfRLNVaSIELPPLRRR 323
Cdd:COG1221  212 LFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPESSLLKTFLR-----RIPM-VIKLPSLEER 285
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 782651413 324 TddIPE---LFSHFLRAAAVRFEKPEPVwTQEDMMRWQLYDWPGNVRELKN 371
Cdd:COG1221  286 S--LEErleLIKHFFKEEAKRLNKPIKV-SKEVLKALLLYDCPGNIGQLKS 333
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
13-139 1.32e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 95.81  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALA-LEGIG-VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDadIPVILM 90
Cdd:COG4565    6 VLIVEDDPMVAELLRRYLErLPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPD--VDVIVI 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRS 139
Cdd:COG4565   84 TAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
13-148 1.81e-21

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: 91.13  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVILMTG 92
Cdd:COG4567    7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRER--DPDARIVVLTG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQLSGER 148
Cdd:COG4567   85 YASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLDRLEWEH 140
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
13-114 1.65e-20

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 85.98  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQAL-ALEGIG-VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILM 90
Cdd:COG4753    2 VLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE--LDPDTKIIIL 79
                         90       100
                 ....*....|....*....|....
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKP 114
Cdd:COG4753   80 SGYSDFEYAQEAIKLGADDYLLKP 103
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
160-319 2.02e-20

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: 87.59  E-value: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 160 VHALIDAI-GPTSADVLIIGETGTGKEVLARALHAASRRTG-PFVALNCAALPEAVFESEIFGHEpgaftgAQQRRIGKF 237
Cdd:cd00009    7 IEALREALeLPPPKNLLLYGPPGTGKTTLARAIANELFRPGaPFLYLNASDLLEGLVVAELFGHF------LVRLLFELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 238 EYASGGTLFLDELESMPLSLQAKLLRALQERSIERLGSnvsvaVDVRVIAAVKQDLkqlvaDGLFRSDLYFRLNVaSIEL 317
Cdd:cd00009   81 EKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDR-----ENVRVIGATNRPL-----LGDLDRALYDRLDI-RIVI 149

                 ..
gi 782651413 318 PP 319
Cdd:cd00009  150 PL 151
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
151-320 3.87e-19

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 83.55  E-value: 3.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  151 LGSAPAMQRVHALIDAIGPTSADVLIIGETGTGKEVLARALHA-ASRRTGPFVALNCAALPEAVFESeifghepgaftga 229
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNpSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  230 qqrrigkfeyASGGTLFLDELESMPLSLQAKLLRALQErsIERlgsnvsvaVDVRVIAAVKQDLKQLVADGLFRSDLYFR 309
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAK--AEG--------YRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 782651413  310 LNVASIELPPL 320
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
13-130 7.94e-18

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: 78.92  E-value: 7.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIG---VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVIL 89
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE--LYPDIKIII 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEH 130
Cdd:cd17536   79 LSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
11-114 6.31e-17

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: 76.33  E-value: 6.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  11 EAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVILM 90
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAL--QPDARIVVL 78
                         90       100
                 ....*....|....*....|....
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17563   79 TGYASIATAVEAIKLGADDYLAKP 102
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
13-114 4.21e-16

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 74.16  E-value: 4.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLgcSQALALE--GIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILM 90
Cdd:cd17555    3 ILVIDDDEVVRE--SIAAYLEdsGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVIVV 78
                         90       100
                 ....*....|....*....|....
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17555   79 SGAGVMSDAVEALRLGAWDYLTKP 102
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
16-115 1.98e-15

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: 71.77  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  16 IEDDAAVRLGC-SQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHG 94
Cdd:cd19920    3 IVDDVPDNLRLlSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTALT 82
                         90       100
                 ....*....|....*....|.
gi 782651413  95 DVAMAVGAMRCGAYDFIEKPF 115
Cdd:cd19920   83 DTEDKVKGFELGAVDYITKPF 103
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
13-121 2.35e-15

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: 71.90  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLTA 82
                         90       100
                 ....*....|....*....|....*....
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLV 121
Cdd:cd17618   83 RGEEEDKVRGLEAGADDYITKPFSPRELV 111
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
15-114 5.44e-15

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: 70.51  E-value: 5.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRdaDIPVILMTGHG 94
Cdd:cd17574    2 VVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGS--DIPIIMLTAKD 79
                         90       100
                 ....*....|....*....|
gi 782651413  95 DVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17574   80 EEEDKVLGLELGADDYITKP 99
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
13-114 1.38e-14

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 69.40  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTG 92
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLTS 77
                         90       100
                 ....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd19936   78 KDDEIDEVFGLRMGADDYITKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
13-115 1.61e-14

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: 69.78  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALA-LEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMT 91
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRsAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMIT 82
                         90       100
                 ....*....|....*....|....
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEKPF 115
Cdd:cd17551   83 ADTDREVRLRALEAGATDFLTKPF 106
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
14-128 2.77e-14

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: 68.84  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  14 YVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGH 93
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 782651413  94 GDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
46-128 3.04e-14

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: 68.89  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  46 ALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17598   34 ALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113

                 ...
gi 782651413 126 RAL 128
Cdd:cd17598  114 YIL 116
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
37-129 3.12e-14

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: 68.97  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  37 VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDsmKAHPRDADIPVILMTGHGDVAMAVGAM-RCGAYDFIEKPF 115
Cdd:cd17569   27 VLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLK--RVRERYPDTVRILLTGYADLDAAIEAInEGEIYRFLTKPW 104
                         90
                 ....*....|....
gi 782651413 116 HSDRLVDTVRRALE 129
Cdd:cd17569  105 DDEELKETIRQALE 118
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
12-128 7.95e-14

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 67.71  E-value: 7.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  12 AVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMT 91
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-133 9.51e-14

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 70.62  E-value: 9.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   1 MMNadnaygreaVYVIEDDAAVRLGCSQALA-LEGIG-VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKA 78
Cdd:COG3279    1 MMK---------ILIVDDEPLARERLERLLEkYPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 782651413  79 hpRDADIPVILMTGHGDvaMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKL 133
Cdd:COG3279   72 --LDPPPPIIFTTAYDE--YALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEA 122
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
13-129 1.76e-13

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: 66.77  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALE--GIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILM 90
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpdIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALE 129
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
11-128 2.47e-13

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 66.42  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  11 EAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILM 90
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKV--IDENIRVIIM 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17553   79 TAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
15-128 5.31e-13

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: 65.27  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSqaLALEGIGVREFEGAES---ALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMT 91
Cdd:cd17552    6 VIDDEEDIREVVQ--ACLEKLAGWEVLTASSgqeGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLT 83
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17552   84 AKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
13-151 9.71e-13

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: 66.52  E-value: 9.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGV-REFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKahpRDADIPVILMT 91
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQIS---EERPAPVILLT 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL----EHRKLVIENRSLRAQLSgERPLL 151
Cdd:COG3707   83 AYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALarfrELRALRRELAKLREALE-ERKLI 145
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
13-126 1.20e-12

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: 64.10  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTA 81
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  93 H---GD--VAMAVGamrCGAYdfIEKPFHSDRLVDTVRR 126
Cdd:cd17548   82 YamkGDreKILEAG---CDGY--ISKPIDTREFLETVAK 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
15-125 1.37e-12

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 64.04  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGHG 94
Cdd:cd17624    3 LVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 782651413  95 DVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELLARLR 111
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
13-128 2.13e-12

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 63.48  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPrdaDIPVILMTG 92
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17623   78 RGDDIDRILGLELGADDYLPKPFNPRELVARIRAIL 113
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
13-115 2.17e-12

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 63.29  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAI-VSDVRLPGMGGLALLdsMKAHPRDADIPVILMT 91
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIvVTDIVMPEMDGIELA--REARKIDPDVKILFIS 79
                         90       100
                 ....*....|....*....|....
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEKPF 115
Cdd:cd18160   80 GGAAAAPELLSDAVGDNATLKKPF 103
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
15-124 2.58e-12

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: 63.26  E-value: 2.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRD-ADIPVILMTGH 93
Cdd:cd17546    3 VVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgRRTPIIALTAN 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 782651413  94 GDVAMAVGAMRCGAYDFIEKPFHSDRLVDTV 124
Cdd:cd17546   83 ALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
12-144 4.79e-12

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: 63.15  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  12 AVYVIEDDAAVRLGCSQALAlEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMT 91
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRE--RWPEVVRIIIS 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 782651413  92 GHGDVA-MAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRAQL 144
Cdd:cd17596   79 GYTDSEdIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLEL 132
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
15-115 1.24e-11

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: 60.97  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHG 94
Cdd:cd17538    4 VVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMITALD 83
                         90       100
                 ....*....|....*....|.
gi 782651413  95 DVAMAVGAMRCGAYDFIEKPF 115
Cdd:cd17538   84 DREDRIRGLEAGADDFLSKPI 104
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
13-125 1.52e-11

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: 61.21  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVILMTG 92
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLTA 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17615   80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
13-128 1.77e-11

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: 60.86  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
13-128 1.92e-11

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: 60.72  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAAL--KRDPPAAIVSDVRLPGMGGLALLDSMKAHPrdaDIPVILM 90
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
13-155 2.20e-11

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 63.58  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALehRKL-------VIENRSLRAQLSGERPLLGSAP 155
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM--RRIspmaveeVIEMQGLSLDPTSHRVMAGEEP 152
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
13-124 3.60e-11

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: 59.78  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTV 124
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
orf27 CHL00148
Ycf27; Reviewed
10-128 4.99e-11

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 62.43  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  10 REAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKahpRDADIPVIL 89
Cdd:CHL00148   6 KEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR---KESDVPIIM 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:CHL00148  83 LTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
13-114 5.68e-11

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: 58.93  E-value: 5.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK10336 PRK10336
two-component system response regulator QseB;
13-147 6.62e-11

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 61.83  E-value: 6.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDAdiPVILMTG 92
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQRE--PVLILTA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFH----SDRLVDTVRRA-------LEHRKLVIENRSLRAQLSGE 147
Cdd:PRK10336  81 RDALAERVEGLRLGADDYLCKPFAlievAARLEALMRRTngqasneLRHGNVMLDPGKRIATLAGE 146
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
15-127 1.20e-10

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: 58.39  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGHG 94
Cdd:cd17554    5 VVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICTAYS 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 782651413  95 DVAMAVGAMRCGAYdfIEKPFHSDRLVDTVRRA 127
Cdd:cd17554   83 EYKSDFSSWAADAY--VVKSSDLTELKETIKRL 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
13-115 1.54e-10

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: 58.30  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIV-SDVRLPGMGGLALLDSM-KAHPRDaDIPVILM 90
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLViTDYNMPEMDGFELVREIrKKYSRD-QLAIIGI 81
                         90       100
                 ....*....|....*....|....*
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPF 115
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKPF 106
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
15-125 1.55e-10

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: 58.39  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGHG 94
Cdd:cd17625    2 VVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTALD 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 782651413  95 DVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17625   80 AVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
43-129 2.17e-10

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: 58.02  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  43 AESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADipVILMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLvd 122
Cdd:cd19925   35 GEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVD--VIVVTAANDVETVREALRLGVVDYLIKPFTFERL-- 110

                 ....*..
gi 782651413 123 tvRRALE 129
Cdd:cd19925  111 --RQRLE 115
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
37-128 2.23e-10

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: 57.73  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  37 VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFH 116
Cdd:cd19923   28 VEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFT 107
                         90
                 ....*....|..
gi 782651413 117 SDRLVDTVRRAL 128
Cdd:cd19923  108 AATLKEKLEKIF 119
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
174-310 2.43e-10

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: 58.54  E-value: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   174 VLIIGETGTGKEVLARALHA-ASRRTGPFVALNCAALPEAVFES---EIFGHEPGAFTGAQQRRIG--KFEYASGGTLFL 247
Cdd:smart00382   5 ILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLIL 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 782651413   248 DELESMPLSLQAKLLRALQErsiERLGSNVSVAVDVRVIAAV--KQDLKQLVADGLFRSDLYFRL 310
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTndEKDLGPALLRRRFDRRIVLLL 146
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
13-131 4.66e-10

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: 56.91  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS--EGRATPVLILTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVrRALEHR 131
Cdd:cd19934   79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARL-RALIRR 116
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
13-114 1.23e-09

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 55.24  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPrdADIPVILMTG 92
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRL--PQTPVAVITA 78
                         90       100
                 ....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
13-125 1.57e-09

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 55.47  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTG 92
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILVTG 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
15-128 1.80e-09

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: 55.36  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAA-VRLGCSQALALEG-IGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVILMTG 92
Cdd:cd17542    4 LIVDDAAfMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI--DPNAKVIMCSA 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17542   82 MGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
13-128 3.86e-09

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: 54.40  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhprDADIPVILMTG 92
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA---ESGVPIVMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
13-125 5.92e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 56.12  E-value: 5.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:PRK11083   6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA--FHPALPVIFLTA 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 782651413  93 -HGDVAMAVGaMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:PRK11083  84 rSDEVDRLVG-LEIGADDYVAKPFSPREVAARVR 116
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
13-125 2.05e-08

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: 52.06  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhprDADIPVILMTG 92
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA---RSDVPIIIISG 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 782651413  93 HGDVAMA-VGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17594   79 DRRDEIDrVVGLELGADDYLAKPFGLRELLARVR 112
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
42-125 2.38e-08

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 52.39  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  42 GAEsALAALKRDPPAAIVSDVRLPGMGGLALLDS-MKAHPrdadIPVILMTGH--GDVAMAVGAMRCGAYDFIEKPF--- 115
Cdd:cd17541   35 GEE-ALEKIKELKPDVITLDIEMPVMDGLEALRRiMAERP----TPVVMVSSLteEGAEITLEALELGAVDFIAKPSggi 109
                         90
                 ....*....|....*.
gi 782651413 116 ------HSDRLVDTVR 125
Cdd:cd17541  110 sldleeIAEELIEKIK 125
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
13-115 3.10e-08

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 51.19  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDP-PAAIVSDVRLPG-MGGLALLDSMKAHPRdaDIPVILM 90
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRRRP--DLKVLLT 78
                         90       100
                 ....*....|....*....|....*
gi 782651413  91 TGHGDVAMAVGAMRCGaYDFIEKPF 115
Cdd:cd18161   79 SGYAENAIEGGDLAPG-VDVLSKPF 102
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
13-114 3.22e-08

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: 51.35  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                         90       100
                 ....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd19928   79 QNTLMTAVKAAERGAFEYLPKP 100
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
13-114 1.19e-07

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: 49.47  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLdsmkahpRD----ADIPVI 88
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVI-------RRlrewSAVPVI 73
                         90       100
                 ....*....|....*....|....*.
gi 782651413  89 LMTGHGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17620   74 VLSARDEESDKIAALDAGADDYLTKP 99
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
402-437 1.60e-07

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 47.39  E-value: 1.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 782651413  402 ERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITR 437
Cdd:pfam02954   5 EKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
58-114 2.59e-07

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: 48.55  E-value: 2.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 782651413  58 IVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17582   48 ILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
13-125 2.90e-07

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: 48.94  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTG 92
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRL--AKVKTPILILSG 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK15479 PRK15479
transcriptional regulator TctD;
28-131 4.56e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 50.49  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  28 QALALEGIGVrefEGAESALAA---LKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGHGDVAMAVGAMR 104
Cdd:PRK15479  18 KALVQNGFAV---DCVFDGLAAdhlLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLLLTARSAVADRVKGLN 92
                         90       100
                 ....*....|....*....|....*..
gi 782651413 105 CGAYDFIEKPFHSDRLvDTVRRALEHR 131
Cdd:PRK15479  93 VGADDYLPKPFELEEL-DARLRALLRR 118
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
15-126 4.81e-07

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 48.57  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAA-VRLgcsQALALEGIGV----REFEGAESALAALKRDP-------PAAIVSDVRLPGMGGLALLDSMKAHPRD 82
Cdd:cd17557    4 LVEDNPGdAEL---IQEAFKEAGVpnelHVVRDGEEALDFLRGEGeyadaprPDLILLDLNMPRMDGFEVLREIKADPDL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 782651413  83 ADIPVILMT---GHGDVAMavgAMRCGAYDFIEKPFHSDRLVDTVRR 126
Cdd:cd17557   81 RRIPVVVLTtsdAEEDIER---AYELGANSYIVKPVDFEEFVEAIRS 124
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
13-114 6.77e-07

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 47.76  E-value: 6.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALK---------RDPPAAIVSDVRLPGMGGLALLDSMKAHPRDA 83
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 782651413  84 DIPVILMTGHGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
37-132 9.79e-07

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: 47.53  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  37 VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLAL---LDSMKAHPRdadipVILMTGHGDvaMAVGAMRCGAYDFIEK 113
Cdd:cd17532   27 VGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELakkLSKLAKPPL-----IVFVTAYDE--YAVEAFELNAVDYLLK 99
                         90
                 ....*....|....*....
gi 782651413 114 PFHSDRLVDTVRRALEHRK 132
Cdd:cd17532  100 PFSEERLAEALAKLRKRLS 118
PRK10610 PRK10610
chemotaxis protein CheY;
37-129 1.20e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 47.66  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  37 VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFH 116
Cdd:PRK10610  33 VEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFT 112
                         90
                 ....*....|...
gi 782651413 117 SDRLVDTVRRALE 129
Cdd:PRK10610 113 AATLEEKLNKIFE 125
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
13-128 1.29e-06

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: 46.89  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTG 92
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI---SNVPIIFISS 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd18159   78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
173-323 1.39e-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: 47.29  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  173 DVLIIGETGTGKEVLARALHAASRRTGPFVALNCAALPeavfESEIFG----------HEPGAFTGAQQrrigkfeyaSG 242
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTT----EEDLFGrrnidpggasWVDGPLVRAAR---------EG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  243 GTLFLDELESMPLSLQAKLLRALQER--SIERLGSNVSVAVD-VRVIAAVkqdlkqlvadglfrSDLYFRLNVASielPP 319
Cdd:pfam07728  68 EIAVLDEINRANPDVLNSLLSLLDERrlLLPDGGELVKAAPDgFRLIATM--------------NPLDRGLNELS---PA 130

                  ....
gi 782651413  320 LRRR 323
Cdd:pfam07728 131 LRSR 134
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
13-128 1.50e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 49.03  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTG 92
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQW---SAIPVIVLSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:PRK10529  81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVAL 116
pleD PRK09581
response regulator PleD; Reviewed
42-143 1.53e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 50.28  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  42 GAEsALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFhsDRLV 121
Cdd:PRK09581  35 GAE-AIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPI--NDVA 111
                         90       100
                 ....*....|....*....|...
gi 782651413 122 DTVR-RALEHRKLVIENRSLRAQ 143
Cdd:PRK09581 112 LFARvKSLTRLKMVIDELRLRAS 134
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
13-128 1.67e-06

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: 46.60  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPrdaDIPVILMTG 92
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd19938   79 RVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
13-73 2.17e-06

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: 46.81  E-value: 2.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 782651413  13 VYVIEDDAAVRLGCSQALALE-GIGV-REFEGAESALAALKRDPPAAIVSDVRLPGMGGLALL 73
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEAL 66
ompR PRK09468
osmolarity response regulator; Provisional
10-131 2.40e-06

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 48.43  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  10 REAVYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVIL 89
Cdd:PRK09468   5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIM 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHR 131
Cdd:PRK09468  83 LTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQ 124
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
13-128 5.83e-06

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: 45.09  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGV-REFEGAESALAALKRDPPAAIVSDVRLPG-MGGLALLDSMKahpRDADIPVILM 90
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIR---EKFDIPVIFL 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17534   80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
PRK10643 PRK10643
two-component system response regulator PmrA;
15-131 7.23e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 46.95  E-value: 7.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGHG 94
Cdd:PRK10643   5 IVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ--KKYTLPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  95 DVAMAVGAMRCGAYDFIEKPFHSDRLVDTVrRALEHR 131
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFALEELHARI-RALIRR 118
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
13-129 8.03e-06

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: 44.96  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIG--VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVILM 90
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDDLevVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREE--LPDTKVLIV 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALE 129
Cdd:cd19930   79 TTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
402-441 8.41e-06

DNA-binding protein Fis (factor for inversion stimulation) [Transcription];


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 43.65  E-value: 8.41e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 782651413 402 ERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGID 441
Cdd:COG2901   44 EKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGLL 83
PRK10360 PRK10360
transcriptional regulator UhpA;
13-127 8.73e-06

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 46.51  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEG--IGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMkahPRdaDIPVILM 90
Cdd:PRK10360   4 VALIDDHLIVRSGFAQLLGLEPdlQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQL---PK--GMATIML 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  91 TGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRA 127
Cdd:PRK10360  79 SVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTV 115
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
13-114 1.03e-05

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: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTG 92
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
13-128 1.24e-05

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: 44.29  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMkahPRDADIPVILMTG 92
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDL---RPKYQGPILLLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
dpiA PRK10046
two-component response regulator DpiA; Provisional
50-139 1.28e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 46.16  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  50 LKRDPPAAIVSDVRLPGMGGLALL-DSMKAH-PRDadipVILMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRA 127
Cdd:PRK10046  46 IERFKPGLILLDNYLPDGRGINLLhELVQAHyPGD----VVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRF 121
                         90
                 ....*....|..
gi 782651413 128 LEHRKLVIENRS 139
Cdd:PRK10046 122 RQRKHMLESIDS 133
PRK13856 PRK13856
two-component response regulator VirG; Provisional
13-142 3.19e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 45.19  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLallDSMKAHPRDADIPVILMTG 92
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGL---EIVRSLATKSDVPIIIISG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 782651413  93 HG-DVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALEHRKLVIENRSLRA 142
Cdd:PRK13856  81 DRlEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRTKDRRS 131
PRK10816 PRK10816
two-component system response regulator PhoP;
13-121 3.99e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 44.73  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprDADIPVILMTG 92
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSN--DVSLPILVLTA 80
                         90       100
                 ....*....|....*....|....*....
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLV 121
Cdd:PRK10816  81 RESWQDKVEVLSAGADDYVTKPFHIEEVM 109
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
31-125 4.35e-05

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: 42.74  E-value: 4.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  31 ALEGIGVREfEGAESALAALKRDppaAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMTGHGDVAMAVGAMRCGAYDF 110
Cdd:cd17581   34 ALEFLGLED-EEDSSNFNEPKVN---MIITDYCMPGMTGYDLLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDF 109
                         90
                 ....*....|....*
gi 782651413 111 IEKPFhsdRLVDTVR 125
Cdd:cd17581  110 LLKPV---KLADVKR 121
PRK11517 PRK11517
DNA-binding response regulator HprR;
13-128 5.01e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 44.50  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDadiPVILMTG 92
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT---PVICLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL 115
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
13-128 8.91e-05

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: 41.95  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEG--IGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILM 90
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPdfTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  91 TGH-GDVamaVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd19931   81 SDAeDDV---VTALRAGADGYLLKDMEPEDLLEALKQAA 116
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
13-128 1.44e-04

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: 41.25  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGV-REFEGAESALAALKRDPPAAIVSDVRLPGMGGLallDSMKAHPRDADIPVILMT 91
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGI---EAAKIITSENIAPIVLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd19932   80 AYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
13-128 1.53e-04

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: 41.20  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTG 92
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd19939   79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
46-189 2.13e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.21  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  46 ALAALKRDPPAAIVSDVRLPGMGGLALLDS-MKAHPrdadIPVIL---MTGHG-DVAMAvgAMRCGAYDFIEKPFHSDR- 119
Cdd:PRK00742  41 AREKIKKLNPDVITLDVEMPVMDGLDALEKiMRLRP----TPVVMvssLTERGaEITLR--ALELGAVDFVTKPFLGISl 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413 120 --------LVDTVRRALEHRKlvienRSLRAQLSGERPLLGSAPAMQRVHALidaigpTSADVLIIGeTGTG-----KEV 186
Cdd:PRK00742 115 gmdeykeeLAEKVRAAARARV-----RALPPRAAAAARAAAAAPAALAAAPL------LSSKLVAIG-TSTGgpealQKV 182

                 ...
gi 782651413 187 LAR 189
Cdd:PRK00742 183 LTP 185
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
13-114 2.15e-04

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: 40.26  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTG 92
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR---SNVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKP 114
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
13-113 3.35e-04

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: 40.47  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALE-GIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHPRDADIPVILMT 91
Cdd:cd17575    3 VLLVDDQAIIGEAVRRALADEeDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLS 82
                         90       100
                 ....*....|....*....|..
gi 782651413  92 GHGDVAMAVGAMRCGAYDFIEK 113
Cdd:cd17575   83 TKEEPEVKSEAFALGANDYLVK 104
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
42-128 4.54e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 41.59  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  42 GAEsALAALKRDPPAAIVSDVRLPGMGGLALLDSMKahpRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLV 121
Cdd:PRK10710  43 GDE-VLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---RFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVV 118

                 ....*..
gi 782651413 122 DTVRRAL 128
Cdd:PRK10710 119 ARVKTIL 125
PRK10693 PRK10693
two-component system response regulator RssB;
46-124 4.64e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.90  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  46 ALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFHS-DRLVDTV 124
Cdd:PRK10693   9 ALELLGGFTPDLIICDLAMPRMNGIEFVEHLRN--RGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKDlNRLREMV 86
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
13-128 6.51e-04

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 40.94  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKrDPPAAIVSDVRLPGMGGLALLDSMKAHPRdadIPVILMTG 92
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQ---TPVIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  93 HGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
PRK11173 PRK11173
two-component response regulator; Provisional
15-131 1.19e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 40.38  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdADIPVILMTGH- 93
Cdd:PRK11173   8 IVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ---ANVALMFLTGRd 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 782651413  94 GDVAMAVGaMRCGAYDFIEKPFHSDRLvdTVR-RALEHR 131
Cdd:PRK11173  85 NEVDKILG-LEIGADDYITKPFNPREL--TIRaRNLLSR 120
PRK13557 PRK13557
histidine kinase; Provisional
9-129 1.53e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 40.81  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413   9 GREAVYVIEDDAAVrlgcsQALA---LEGIGVREfEGAESALAALKR----DPPAAIVSDVRLPG-MGGLALldSMKAHP 80
Cdd:PRK13557 414 GTETILIVDDRPDV-----AELArmiLEDFGYRT-LVASNGREALEIldshPEVDLLFTDLIMPGgMNGVML--AREARR 485
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 782651413  81 RDADIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVRRALE 129
Cdd:PRK13557 486 RQPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLD 534
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
13-128 1.59e-03

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


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 38.22  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIG-VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAHprdaDIPVILMT 91
Cdd:cd17586    1 VLVLEDEPLIAMNLEDALEDLGGKeVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVADALKRR----AIPFIFAT 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 782651413  92 GHGDVAMAvgAMRCGAYDFIEKPFHSDRLVDTVRRAL 128
Cdd:cd17586   77 GYGDSHGI--DSRLIDVPVLRKPFDADSALAALAMLL 111
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
58-121 1.61e-03

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: 38.18  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 782651413  58 IVSDVRLPGMGGLALLDSMKA-HPRdadIPVILMTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLV 121
Cdd:cd17573   46 VLVSDKLPDGNGLSIVSRIKEkHPS---IVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLV 107
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
13-120 1.78e-03

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 38.19  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALALEGIG-VREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLdsMKAHPRDADIPVILMT 91
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFL--RHLAESHSNAAVILMS 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 782651413  92 GHGDV---AMAVGAMRCGAY--DFIEKPFHSDRL 120
Cdd:cd17530   81 GLDGGileSAETLAGANGLNllGTLSKPFSPEEL 114
PRK01905 PRK01905
Fis family transcriptional regulator;
402-440 2.13e-03

Fis family transcriptional regulator;


Pssm-ID: 179348 [Multi-domain]  Cd Length: 77  Bit Score: 36.71  E-value: 2.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 782651413 402 ERAYIEEALRNAGGQVAKAAELLGLPRKTLYDKITRHGI 440
Cdd:PRK01905  38 EKPLLEVVMEQAGGNQSLAAEYLGINRNTLRKKLQQHGL 76
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
15-113 2.34e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 39.11  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  15 VIEDDAAVRLGCSQALALEGIGV-REFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLDSMKAhpRDADIPVILMTGH 93
Cdd:PRK09958   5 IIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRK--RQYSGIIIIVSAK 82
                         90       100
                 ....*....|....*....|
gi 782651413  94 GDVAMAVGAMRCGAYDFIEK 113
Cdd:PRK09958  83 NDHFYGKHCADAGANGFVSK 102
PRK09483 PRK09483
response regulator; Provisional
13-125 2.86e-03

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 38.93  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  13 VYVIEDDAAVRLGCSQALA-LEGIGVR-EFEGAESALAALKRDPPAAIVSDVRLPGMGGL-ALLDSMKAHPrdaDIPVIL 89
Cdd:PRK09483   4 VLLVDDHELVRAGIRRILEdIKGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLeATRKILRYTP---DVKIIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 782651413  90 MTGHGDVAMAVGAMRCGAYDFIEKPFHSDRLVDTVR 125
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
11-128 7.60e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 38.89  E-value: 7.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782651413  11 EAVYVIEDDAAVRLGCSQ---ALALEGIGVREFEGAESALAALKRDPPAAIVSDVRLPGMGGLALLdsmkaHPRDADIPV 87
Cdd:PRK13837 698 ETVLLVEPDDATLERYEEklaALGYEPVGFSTLAAAIAWISKGPERFDLVLVDDRLLDEEQAAAAL-----HAAAPTLPI 772
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 782651413  88 ILMTGHGDVAMAVGAMRCGAyDFIEKPFHSDRLVDTVRRAL 128
Cdd:PRK13837 773 ILGGNSKTMALSPDLLASVA-EILAKPISSRTLAYALRTAL 812
 
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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