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Conserved domains on  [gi|2221781758|ref|WP_244405801|]
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MULTISPECIES: sigma-54 dependent transcriptional regulator [Agrobacterium]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-503 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: 527.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE--EPPDLVLLDLRMPGMDGLELLRELRALDPDLPVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRrgrsnavnftDIVSASPAMLRVIELAQ 160
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS----------GLIGRSPAMQEVRRLIE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 161 RAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGT 240
Cdd:COG2204   149 KVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 241 LFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRK 320
Cdd:COG2204   229 LFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERR 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 321 EDIPHLARVFAERFSAEQKLPNPvgLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQIalqlpefstg 400
Cdd:COG2204   309 EDIPLLARHFLARFAAELGKPVK--LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA---------- 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 401 dyaedairspsgsslklaaysppapavenhvvtdepadvsttiyrggslisstdetgnirkLAEIEEELIRFALRFYRGQ 480
Cdd:COG2204   377 -------------------------------------------------------------LEEVERELIERALEETGGN 395
                         490       500
                  ....*....|....*....|...
gi 2221781758 481 MSQVARKLGIGRSTLYRKLKDYG 503
Cdd:COG2204   396 VSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-503 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: 527.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE--EPPDLVLLDLRMPGMDGLELLRELRALDPDLPVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRrgrsnavnftDIVSASPAMLRVIELAQ 160
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS----------GLIGRSPAMQEVRRLIE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 161 RAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGT 240
Cdd:COG2204   149 KVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 241 LFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRK 320
Cdd:COG2204   229 LFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERR 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 321 EDIPHLARVFAERFSAEQKLPNPvgLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQIalqlpefstg 400
Cdd:COG2204   309 EDIPLLARHFLARFAAELGKPVK--LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA---------- 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 401 dyaedairspsgsslklaaysppapavenhvvtdepadvsttiyrggslisstdetgnirkLAEIEEELIRFALRFYRGQ 480
Cdd:COG2204   377 -------------------------------------------------------------LEEVERELIERALEETGGN 395
                         490       500
                  ....*....|....*....|...
gi 2221781758 481 MSQVARKLGIGRSTLYRKLKDYG 503
Cdd:COG2204   396 VSRAAELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
5-501 4.71e-127

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: 378.70  E-value: 4.71e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALAR--GQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL--KLDRREAKARTGRRGRSnavnfTDIVSASPAMLRVIELAQRA 162
Cdd:TIGR01818  79 HSDLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALahAQEQVALPADAGEAEDS-----AELIGEAPAMQEVFRAIGRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 163 AQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLF 242
Cdd:TIGR01818 154 SRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 243 LDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKED 322
Cdd:TIGR01818 234 LDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERRED 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 323 IPHLARVFAERFSAEQKLPnPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPqialqlPEfstgdy 402
Cdd:TIGR01818 314 IPRLARHFLALAARELDVE-PKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLP------AE------ 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 403 aedairspsgsslkLAAYSPPApaveNHVVTDEPADVSTTIYRGGSLISSTDETGNI-RKLAEIEEELIRFALRFYRGQM 481
Cdd:TIGR01818 381 --------------LALTGRPA----SAPDSDGQDSWDEALEAWAKQALSRGEQGLLdRALPEFERPLLEAALQHTRGHK 442
                         490       500
                  ....*....|....*....|
gi 2221781758 482 SQVARKLGIGRSTLYRKLKD 501
Cdd:TIGR01818 443 QEAAALLGWGRNTLTRKLKE 462
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-505 1.19e-124

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 372.26  E-value: 1.19e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI--HPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRRGRSNAVNFTDIVSASPAMLRVIELAQRAAQ 164
Cdd:PRK11361   85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 165 SSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLD 244
Cdd:PRK11361  165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 245 EIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIP 324
Cdd:PRK11361  245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 325 HLARVFAERFSAEQKLpNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQialqlpefstgdyae 404
Cdd:PRK11361  325 LLANHFLQKFSSENQR-DIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPP--------------- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 405 dAIRSPSGSslklAAYSPPAPAVENhvvtdepadvsttiyrggslisstdetgNIRKLA-EIEEELIRFALRFYRGQMSQ 483
Cdd:PRK11361  389 -QIRQPVCN----AGEVKTAPVGER----------------------------NLKEEIkRVEKRIIMEVLEQQEGNRTR 435
                         490       500
                  ....*....|....*....|..
gi 2221781758 484 VARKLGIGRSTLYRKLKDYGID 505
Cdd:PRK11361  436 TALMLGISRRALMYKLQEYGID 457
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-312 1.91e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 304.32  E-value: 1.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 145 IVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 225 ATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 2221781758 305 RLNVFPIT 312
Cdd:pfam00158 161 RLNVIPIE 168
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
136-503 1.05e-100

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 314.52  E-value: 1.05e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 136 RSNAVNFTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANkPFITVNCGAIPHNLVESILF 215
Cdd:NF041552  260 KISEDSFGKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKG-PFVPVNCSAIPEELFESEFF 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 216 GHEKGAFTGATEK-HVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVK 294
Cdd:NF041552  339 GYEEGAFTGALKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVK 418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 295 EGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPvGLDASALALLTAYDWPGNIRQLENAVFRAV 374
Cdd:NF041552  419 EGKFREDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIP-KIDKEVYDILQNYKWKGNIRELKNTIEHLV 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 375 VLSQGGELSDADFPqialqlpefstgdyaedairspsgsslklaaysppapaveNHVVtdepADVSTTIYRGGSliSSTD 454
Cdd:NF041552  498 VLSKNGTITKDSIP----------------------------------------EYIL----ESVKKKEDEEGD--YPLD 531
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2221781758 455 ETGNIRKLaeiEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYG 503
Cdd:NF041552  532 LNKAVEKL---EIDTIKKALEMSNGNKAKAAKLLNIPRSTLYYKLKQYG 577
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
85-380 2.46e-96

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 301.41  E-value: 2.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAfDFVVKPVSPERIGAAISN-ALKLDRREAKARTGRRGRSNAVNF--TDIVSASPAMLRVIELAQR 161
Cdd:NF038308  119 QICWFLLVEARYLPA-RLLQTSPPRDKEEGTYEIiDLDLSRYDALAQRFAREQAEAVSFlkSGIATRNAAFNRLIEQIER 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 162 AAQSSI-PVVLEGESGVGKEMVARAIQSAGDRANK---PFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEAD 237
Cdd:NF038308  198 VALRSRaPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAAD 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 238 GGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALR 317
Cdd:NF038308  278 GGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGLR 357
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758 318 RRKEDIPHLARVFAERFSAEQKLPNPVGLDAS----ALALLTAYDWPGNIRQLENAVFRAVVLSQGG 380
Cdd:NF038308  358 ERREDIEPNLDYELDRFARELGRQVRFNKEARfrylAFATSPEALWPGNFRELSASVTRMATLADGG 424
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
5-121 2.05e-28

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: 108.74  E-value: 2.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKE--RRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:cd17550    79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
4-59 7.00e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 60.27  E-value: 7.00e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221781758    4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMP 59
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE--EKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-503 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: 527.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE--EPPDLVLLDLRMPGMDGLELLRELRALDPDLPVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRrgrsnavnftDIVSASPAMLRVIELAQ 160
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDS----------GLIGRSPAMQEVRRLIE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 161 RAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGT 240
Cdd:COG2204   149 KVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 241 LFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRK 320
Cdd:COG2204   229 LFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERR 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 321 EDIPHLARVFAERFSAEQKLPNPvgLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQIalqlpefstg 400
Cdd:COG2204   309 EDIPLLARHFLARFAAELGKPVK--LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEA---------- 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 401 dyaedairspsgsslklaaysppapavenhvvtdepadvsttiyrggslisstdetgnirkLAEIEEELIRFALRFYRGQ 480
Cdd:COG2204   377 -------------------------------------------------------------LEEVERELIERALEETGGN 395
                         490       500
                  ....*....|....*....|...
gi 2221781758 481 MSQVARKLGIGRSTLYRKLKDYG 503
Cdd:COG2204   396 VSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
116-505 1.08e-159

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: 461.16  E-value: 1.08e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 116 ISNALKLDRREAKARTgRRGRSNAVNFTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANK 195
Cdd:COG3829   112 ITELKRLERKLREEEL-ERGLSAKYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 196 PFITVNCGAIPHNLVESILFGHEKGAFTGATEK-HVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARV 274
Cdd:COG3829   191 PFVAVNCAAIPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKP 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 275 QKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPvGLDASALALL 354
Cdd:COG3829   271 IPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIK-GISPEALELL 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 355 TAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQIALQlpefstgdyAEDAIRSPSGSSLKLAaysppapavenhvvtd 434
Cdd:COG3829   350 LAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLE---------EAEAASAAEEGSLKEA---------------- 404
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2221781758 435 epadvsttiyrggslisstdetgnirkLAEIEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYGID 505
Cdd:COG3829   405 ---------------------------LEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
5-501 4.71e-127

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: 378.70  E-value: 4.71e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALAR--GQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL--KLDRREAKARTGRRGRSnavnfTDIVSASPAMLRVIELAQRA 162
Cdd:TIGR01818  79 HSDLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALahAQEQVALPADAGEAEDS-----AELIGEAPAMQEVFRAIGRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 163 AQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLF 242
Cdd:TIGR01818 154 SRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 243 LDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKED 322
Cdd:TIGR01818 234 LDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERRED 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 323 IPHLARVFAERFSAEQKLPnPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPqialqlPEfstgdy 402
Cdd:TIGR01818 314 IPRLARHFLALAARELDVE-PKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLP------AE------ 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 403 aedairspsgsslkLAAYSPPApaveNHVVTDEPADVSTTIYRGGSLISSTDETGNI-RKLAEIEEELIRFALRFYRGQM 481
Cdd:TIGR01818 381 --------------LALTGRPA----SAPDSDGQDSWDEALEAWAKQALSRGEQGLLdRALPEFERPLLEAALQHTRGHK 442
                         490       500
                  ....*....|....*....|
gi 2221781758 482 SQVARKLGIGRSTLYRKLKD 501
Cdd:TIGR01818 443 QEAAALLGWGRNTLTRKLKE 462
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
85-503 7.11e-126

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 380.79  E-value: 7.11e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDfvVKPVsPERIGAAISNALKLDRREAKARTGRRGRSNAVNFTDIVSASPAMLRVIELAQRAAQ 164
Cdd:COG3284   266 GLDLEALPDGARRAPAS--PRPL-RLRDGRRLGALLRLRPARRAARAAPAGAPAPAALAALAGGDPAMRRALRRARRLAD 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 165 SSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEK-HVGKFMEADGGTLFL 243
Cdd:COG3284   343 RDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKgRPGKIEQADGGTLFL 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 244 DEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRkEDI 323
Cdd:COG3284   423 DEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDL 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 324 PHLARVFAERFSAEQklpNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPqialqlpefstgdya 403
Cdd:COG3284   502 PALIEHLLRELAAGR---GPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITVEDLP--------------- 563
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 404 eDAIRSPSgsslklaaySPPAPAVENHVVTdepadvsttiyrggslisstdetgnirkLAEIEEELIRFALRFYRGQMSQ 483
Cdd:COG3284   564 -DELRAEL---------AAAAPAAAAPLTS----------------------------LEEAERDAILRALRACGGNVSA 605
                         410       420
                  ....*....|....*....|
gi 2221781758 484 VARKLGIGRSTLYRKLKDYG 503
Cdd:COG3284   606 AARALGISRSTLYRKLKRYG 625
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-505 1.19e-124

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 372.26  E-value: 1.19e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI--HPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRRGRSNAVNFTDIVSASPAMLRVIELAQRAAQ 164
Cdd:PRK11361   85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 165 SSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLD 244
Cdd:PRK11361  165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 245 EIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIP 324
Cdd:PRK11361  245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 325 HLARVFAERFSAEQKLpNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQialqlpefstgdyae 404
Cdd:PRK11361  325 LLANHFLQKFSSENQR-DIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPP--------------- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 405 dAIRSPSGSslklAAYSPPAPAVENhvvtdepadvsttiyrggslisstdetgNIRKLA-EIEEELIRFALRFYRGQMSQ 483
Cdd:PRK11361  389 -QIRQPVCN----AGEVKTAPVGER----------------------------NLKEEIkRVEKRIIMEVLEQQEGNRTR 435
                         490       500
                  ....*....|....*....|..
gi 2221781758 484 VARKLGIGRSTLYRKLKDYGID 505
Cdd:PRK11361  436 TALMLGISRRALMYKLQEYGID 457
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
5-499 3.25e-118

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 355.11  E-value: 3.25e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLEllkQYSGEI-NVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALE---QVREQVfDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKlDRREAKARTGRRGRSNavnfTDIVSASPAMLRVIELAQRAA 163
Cdd:PRK10365   85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA-HTHSIDAETPAVTASQ----FGMVGKSPAMQHLLSEIALVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 164 QSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFL 243
Cdd:PRK10365  160 PSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 244 DEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDI 323
Cdd:PRK10365  240 DEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 324 PHLARVFAERFsAEQKLPNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPqialqlpefstgdya 403
Cdd:PRK10365  320 PLLAGHFLQRF-AERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELP--------------- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 404 edairspsgsslkLAAYSPPAPAvenhvvtdepadvsttiyrGGSLisstdetgNIRKLAEIEEELIRFALRFYRGQMSQ 483
Cdd:PRK10365  384 -------------LAIASTPIPL-------------------GQSQ--------DIQPLVEVEKEVILAALEKTGGNKTE 423
                         490
                  ....*....|....*.
gi 2221781758 484 VARKLGIGRSTLYRKL 499
Cdd:PRK10365  424 AARQLGITRKTLLAKL 439
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
94-506 4.30e-113

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 344.08  E-value: 4.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  94 AMRAGAFDfvvkPVSPERI-------GAAISNALKLDRREAKARTGRRG----RSNAVNFTDIVSASPAMLRV---IELA 159
Cdd:PRK05022  131 ALDPGQFD----AFSDEELralaalaAATLRNALLIEQLESQAELPQDVaeflRQEALKEGEMIGQSPAMQQLkkeIEVV 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 160 qraAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGG 239
Cdd:PRK05022  207 ---AASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGG 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 240 TLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRR 319
Cdd:PRK05022  284 TLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRER 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 320 KEDIPHLARVFAERFSAEQKLPNpVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGelSDADFPQIALQLPEFSt 399
Cdd:PRK05022  364 GDDVLLLAGYFLEQNRARLGLRS-LRLSPAAQAALLAYDWPGNVRELEHVISRAALLARAR--GAGRIVTLEAQHLDLP- 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 400 gdyAEDAIRSPSgsslklAAYSPPAPAvenhvvtdepadvsttiyrGGSLISSTDETgnirklaeiEEELIRFALRFYRG 479
Cdd:PRK05022  440 ---AEVALPPPE------AAAAPAAVV-------------------SQNLREATEAF---------QRQLIRQALAQHQG 482
                         410       420
                  ....*....|....*....|....*..
gi 2221781758 480 QMSQVARKLGIGRSTLYRKLKDYGIDP 506
Cdd:PRK05022  483 NWAAAARALELDRANLHRLAKRLGLKD 509
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
5-505 1.20e-108

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 331.45  E-value: 1.20e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEinVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPD--VLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTgrrgRSNAVNFTDIVSASPAMLRVIELAQRAAQ 164
Cdd:PRK10923   84 HSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRN----IQVNGPTTDIIGEAPAMQDVFRIIGRLSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 165 SSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLD 244
Cdd:PRK10923  160 SSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 245 EIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIP 324
Cdd:PRK10923  240 EIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 325 HLARVF----AERFSAEQKLPNPvgldaSALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQialQLPEFSTG 400
Cdd:PRK10923  320 RLARHFlqvaARELGVEAKLLHP-----ETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPG---ELFESTVP 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 401 DYAEDAirSPSGSSLKLAAYsppapavenhvvtdepadvSTTIYRGG--SLISSTdetgnirkLAEIEEELIRFALRFYR 478
Cdd:PRK10923  392 ESTSQM--QPDSWATLLAQW-------------------ADRALRSGhqNLLSEA--------QPELERTLLTTALRHTQ 442
                         490       500
                  ....*....|....*....|....*..
gi 2221781758 479 GQMSQVARKLGIGRSTLYRKLKDYGID 505
Cdd:PRK10923  443 GHKQEAARLLGWGRNTLTRKLKELGME 469
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
5-504 8.22e-108

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: 328.63  E-value: 8.22e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGhlALLAENGKAGLELLKQYsgEINVVVLDLMMP-----EMDGLGFLKAVGELGVDVPV 79
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFADYE--LAVAADRESAIALVRRH--EPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  80 IVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRRGRSNAvNFTDIVSASPAMLRVIELA 159
Cdd:TIGR02915  77 IVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGT-ALRGLITSSPGMQKICRTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 160 QRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGG 239
Cdd:TIGR02915 156 EKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 240 TLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRR 319
Cdd:TIGR02915 236 TLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSR 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 320 KEDIPHLARVFAERFSAEQKlPNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADfpqiaLQLPEfst 399
Cdd:TIGR02915 316 DGDAVLLANAFLERFARELK-RKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAED-----LGLDA--- 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 400 gdyAEDAIRsPSGSSLKLAAysppapavenhvvtdepadvsttiyrggslisstdetgnirklAEIEEELIRFALRFYRG 479
Cdd:TIGR02915 387 ---RERAET-PLEVNLREVR-------------------------------------------ERAEREAVRKAIARVDG 419
                         490       500
                  ....*....|....*....|....*
gi 2221781758 480 QMSQVARKLGIGRSTLYRKLKDYGI 504
Cdd:TIGR02915 420 NIARAAELLGITRPTLYDLMKKHGI 444
PRK15115 PRK15115
response regulator GlrR; Provisional
2-397 2.89e-107

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 327.18  E-value: 2.89e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:PRK15115    5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNR--EKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVII 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLdRREAKARTGRRgrsnavnftDIVSASPAMLRVIELAQR 161
Cdd:PRK15115   83 LTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQ-SAPATDERWRE---------AIVTRSPLMLRLLEQARM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 162 AAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTL 241
Cdd:PRK15115  153 VAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 242 FLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKE 321
Cdd:PRK15115  233 FLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 322 DIPHLARVFAeRFSAEQKLPNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADFPQiALQ-----LPE 396
Cdd:PRK15115  313 DIPLLANHLL-RQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQ-ALEgentaLPT 390

                  .
gi 2221781758 397 F 397
Cdd:PRK15115  391 F 391
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
129-504 3.88e-103

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 318.67  E-value: 3.88e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 129 ARTGRR----GRSNAVNFTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGA 204
Cdd:COG3283   186 ARLGEQlqalQVNDDSGFDHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAA 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 205 IPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISA 284
Cdd:COG3283   266 LPDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICA 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 285 TNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPvGLDASALALLTAYDWPGNIR 364
Cdd:COG3283   346 TQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRP-RLSPDLVDFLQSYPWPGNVR 424
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 365 QLENAVFRAVVLSQGGELSDADfpqiaLQLPEFSTGD-YAEDAIrspsgsslklaaysppapavenhvvtdepadvstti 443
Cdd:COG3283   425 QLENALYRAVSLLEGDELTPED-----LQLPEYAASAgLLDDLL------------------------------------ 463
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2221781758 444 yrGGSLisstDEtgnIRKlaEIEEELIRfalRFYRGQMS--QVARKLGIGRSTLYRKLKDYGI 504
Cdd:COG3283   464 --EGSL----DE---IVK--RFERSLLR---RLYPSYPStrKLAKRLGVSHTAIANKLREYGI 512
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-312 1.91e-102

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 304.32  E-value: 1.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 145 IVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 225 ATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 2221781758 305 RLNVFPIT 312
Cdd:pfam00158 161 RLNVIPIE 168
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
122-387 7.77e-101

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: 313.58  E-value: 7.77e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 122 LDRREAKARTGRRGRSNAvnftdIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVN 201
Cdd:TIGR01817 180 LRDKAPEIARRRSGKEDG-----IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVN 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 202 CGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRL 281
Cdd:TIGR01817 255 CAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRL 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 282 ISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLpnPVGLDASALALLTAYDWPG 361
Cdd:TIGR01817 335 VAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGR--PLTITPSAIRVLMSCKWPG 412
                         250       260
                  ....*....|....*....|....*.
gi 2221781758 362 NIRQLENAVFRAVVLSQGGELSDADF 387
Cdd:TIGR01817 413 NVRELENCLERTATLSRSGTITRSDF 438
TF_PrdR NF041552
sigma-54 dependent transcriptional regulator PrdR;
136-503 1.05e-100

sigma-54 dependent transcriptional regulator PrdR;


Pssm-ID: 469437 [Multi-domain]  Cd Length: 577  Bit Score: 314.52  E-value: 1.05e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 136 RSNAVNFTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANkPFITVNCGAIPHNLVESILF 215
Cdd:NF041552  260 KISEDSFGKIIGKSKKIIKKIEIAKQVAKTNSSVLITGESGTGKEVFARAIHQASGRKG-PFVPVNCSAIPEELFESEFF 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 216 GHEKGAFTGATEK-HVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVK 294
Cdd:NF041552  339 GYEEGAFTGALKKgKIGKFELANNGTLFLDEIGDMPLSMQAKLLRVLQEKQVRRVGGEKYIKINVRIISATNKDLKKMVK 418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 295 EGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPvGLDASALALLTAYDWPGNIRQLENAVFRAV 374
Cdd:NF041552  419 EGKFREDLYYRLNVVEIELPPLRERKEDIPLLINYFLKEICKENNKEIP-KIDKEVYDILQNYKWKGNIRELKNTIEHLV 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 375 VLSQGGELSDADFPqialqlpefstgdyaedairspsgsslklaaysppapaveNHVVtdepADVSTTIYRGGSliSSTD 454
Cdd:NF041552  498 VLSKNGTITKDSIP----------------------------------------EYIL----ESVKKKEDEEGD--YPLD 531
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2221781758 455 ETGNIRKLaeiEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYG 503
Cdd:NF041552  532 LNKAVEKL---EIDTIKKALEMSNGNKAKAAKLLNIPRSTLYYKLKQYG 577
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
85-380 2.46e-96

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 301.41  E-value: 2.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAfDFVVKPVSPERIGAAISN-ALKLDRREAKARTGRRGRSNAVNF--TDIVSASPAMLRVIELAQR 161
Cdd:NF038308  119 QICWFLLVEARYLPA-RLLQTSPPRDKEEGTYEIiDLDLSRYDALAQRFAREQAEAVSFlkSGIATRNAAFNRLIEQIER 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 162 AAQSSI-PVVLEGESGVGKEMVARAIQSAGDRANK---PFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEAD 237
Cdd:NF038308  198 VALRSRaPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAAD 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 238 GGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALR 317
Cdd:NF038308  278 GGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGLR 357
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758 318 RRKEDIPHLARVFAERFSAEQKLPNPVGLDAS----ALALLTAYDWPGNIRQLENAVFRAVVLSQGG 380
Cdd:NF038308  358 ERREDIEPNLDYELDRFARELGRQVRFNKEARfrylAFATSPEALWPGNFRELSASVTRMATLADGG 424
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
149-502 8.49e-87

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: 270.32  E-value: 8.49e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 149 SPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEK 228
Cdd:TIGR02974   5 SNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGAQKR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 229 HVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNV 308
Cdd:TIGR02974  85 HQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDRLAF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 309 FPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPVGLDASALALLTAYDWPGNIRQLENAVFRAVVlsqggELSDADFP 388
Cdd:TIGR02974 165 DVITLPPLRERQEDIMLLAEHFAIRMARELGLPLFPGFTPQAREQLLEYHWPGNVRELKNVVERSVY-----RHGLEEAP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 389 QIALQLPEFSTGDYAEDAIrspsgsslklaayspPAPAVENHVVTDEPADVSTTIYRGGSLisstdetgnIRKLAEIEEE 468
Cdd:TIGR02974 240 IDEIIIDPFASPWRPKQAA---------------PAVDEVNSTPTDLPSPSSIAAAFPLDL---------KQAQQDYEIE 295
                         330       340       350
                  ....*....|....*....|....*....|....
gi 2221781758 469 LIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDY 502
Cdd:TIGR02974 296 LLQQALAEAQFNQRKAAELLGLTYHQLRGLLRKH 329
PRK10820 PRK10820
transcriptional regulator TyrR;
129-400 4.85e-83

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 266.94  E-value: 4.85e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 129 ARTGRRGRSNAVN----FTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGA 204
Cdd:PRK10820  186 ARMGRQLQNLAVNddsaFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCAS 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 205 IPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISA 284
Cdd:PRK10820  266 IPDDVVESELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICA 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 285 TNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPVgLDASALALLTAYDWPGNIR 364
Cdd:PRK10820  346 TQKNLVELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPK-LAADLNTVLTRYGWPGNVR 424
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2221781758 365 QLENAVFRAVVLSQGGELSDADfpqiaLQLPEFSTG 400
Cdd:PRK10820  425 QLKNAIYRALTQLEGYELRPQD-----ILLPDYDAA 455
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
110-507 3.67e-80

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 263.62  E-value: 3.67e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 110 ERIGAAISNAL------KLDRREAKARTGRRGRSNAVN--FTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEM 181
Cdd:PRK15429  335 ERVAIAVDNALayqeihRLKERLVDENLALTEQLNNVDseFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKEL 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 182 VARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAV 261
Cdd:PRK15429  415 IARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVL 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 262 QQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFsAEQKLP 341
Cdd:PRK15429  495 QEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKI-ARRMGR 573
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 342 NPVGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSdadfpqiaLQLPEfstgdyaedairspsgsslkLAAYS 421
Cdd:PRK15429  574 NIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQ--------LSLPD--------------------ITLPE 625
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 422 PPAPAVENHVVTDepadvsttiyrggslisstdetgnirklAEIEEELIRFALRFYRGQMS---QVARKLGIGRSTLYRK 498
Cdd:PRK15429  626 PETPPAATVVAQE----------------------------GEDEYQLIVRVLKETNGVVAgpkGAAQRLGLKRTTLLSR 677

                  ....*....
gi 2221781758 499 LKDYGIDPD 507
Cdd:PRK15429  678 MKRLGIDKS 686
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
149-505 1.31e-76

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: 244.37  E-value: 1.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 149 SPAMLRVIE-LAQRAAQSsipvvLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESIlfghekgaftgate 227
Cdd:COG3604   102 SEEDLRLLEtLASLAAVA-----ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLESL-------------- 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 228 khvgkfmeadggtlfldeigdlpldvqvkllravQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLN 307
Cdd:COG3604   163 ----------------------------------QEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 308 VFPITIPALRRRKEDIPHLARVFAERFSAEQKLPNPvGLDASALALLTAYDWPGNIRQLENAVFRAVVLSQGGELSDADF 387
Cdd:COG3604   209 VFPIRLPPLRERREDIPLLAEHFLEKFSRRLGKPIL-RLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDL 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 388 PQIALQlpefstgdyaedairspsgsslklaaysppapavenhvvtdepadvsttiyrggslisstdetgnirKLAEIEE 467
Cdd:COG3604   288 APGSRE-------------------------------------------------------------------ALEEVER 300
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2221781758 468 ELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYGID 505
Cdd:COG3604   301 EHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
67-500 5.26e-75

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: 245.93  E-value: 5.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  67 LKAVGelgvdVPVIVQTGQGgIDTVVQAMRAGAFDFvvkpvSPERIGAAISNALKLDR--REAKARTGRRGRSNAVN--- 141
Cdd:TIGR02329 141 LRARG-----IGAVVGAGLI-TDLAEQAGLHGVFLY-----SADSVRQAFDDALDVARatRLRQAATLRSATRNQLRtry 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 142 -FTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKG 220
Cdd:TIGR02329 210 rLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEG 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 221 AFTGATEK-HVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFR 299
Cdd:TIGR02329 290 AFTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFR 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 300 EDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLP-NPV---GLDASALALLtAYDWPGNIRQLENAVFRAVV 375
Cdd:TIGR02329 370 RDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPdSEAaaqVLAGVADPLQ-RYPWPGNVRELRNLVERLAL 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 376 lsqggELSDADFPQIALQLpefstgdyaedairspsgsslkLAAYSPpapavenhvvtdEPADVSTtiyRGGSLISStde 455
Cdd:TIGR02329 449 -----ELSAMPAGALTPDV----------------------LRALAP------------ELAEASG---KGKTSALS--- 483
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2221781758 456 tgnIRKLAEIEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLK 500
Cdd:TIGR02329 484 ---LRERSRVEALAVRAALERFGGDRDAAAKALGISRTTLWRRLK 525
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
67-500 3.54e-74

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 244.24  E-value: 3.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  67 LKAVGelgvdVPVIVQTGQGgIDTVVQAMRAGAFDFvvkpvSPERIGAAISNALKLDR---REAKARTGRRGRSNAVNFT 143
Cdd:PRK15424  151 LKANG-----IEAVVGAGLI-TDLAEEAGMTGIFIY-----SAATVRQAFEDALDMTRmtlRHNTHYATRNALRTRYVLG 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 144 DIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSA-----GDRANK---PFITVNCGAIPHNLVESILF 215
Cdd:PRK15424  220 DLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHREyfarhDARQGKkshPFVAVNCGAIAESLLEAELF 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 216 GHEKGAFTGATEK-HVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVK 294
Cdd:PRK15424  300 GYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVR 379
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 295 EGRFREDLYYRLNVFPITIPALRRRKEDIPHLARVFAERFSAEQKLPnpvgLDASALA-------LLTAYDWPGNIRQLE 367
Cdd:PRK15424  380 QGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAP----FSAALRQglqqcetLLLHYDWPGNVRELR 455
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 368 NAVFRAVVLsqggeLSDADFPQIALQLpefstgdyaedairspsgsslkLAAYSPPAPavenhvvtdepadvsttiyrgg 447
Cdd:PRK15424  456 NLMERLALF-----LSVEPTPDLTPQF----------------------LQLLLPELA---------------------- 486
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2221781758 448 slISSTDETGNIRKLAEIEEELIRFalrfyRGQMSQVARKLGIGRSTLYRKLK 500
Cdd:PRK15424  487 --RESAKTPAPRLLAATLQQALERF-----NGDKTAAANYLGISRTTLWRRLK 532
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
142-512 1.02e-73

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 245.36  E-value: 1.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 142 FTDIVSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGhekGA 221
Cdd:PRK11388  324 FDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SD 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 222 FTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFRED 301
Cdd:PRK11388  401 RTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQ 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 302 LYYRLNVFPITIPALRRRKEDIP----HLARVFAERFSAEQKlpnpvgLDASALALLTAYDWPGNIRQLENAVFRAVVLS 377
Cdd:PRK11388  481 LYYALHAFEITIPPLRMRREDIPalvnNKLRSLEKRFSTRLK------IDDDALARLVSYRWPGNDFELRSVIENLALSS 554
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 378 QGGELSDADFPQIALQlpEFSTGDyaedairspsgsslklaaysppapavenhvVTDEPADVSTTiyrggslisstdetg 457
Cdd:PRK11388  555 DNGRIRLSDLPEHLFT--EQATDD------------------------------VSATRLSTSLS--------------- 587
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2221781758 458 nirkLAEIEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYGIDPDDPLRD 512
Cdd:PRK11388  588 ----LAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQFKRR 638
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
151-374 3.51e-69

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 224.55  E-value: 3.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 151 AMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEKGAFTGATEKHV 230
Cdd:PRK11608   14 SFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 231 GKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFP 310
Cdd:PRK11608   94 GRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2221781758 311 ITIPALRRRKEDIPHLARVFAERFSAEQKLPNPVGLDASALALLTAYDWPGNIRQLENAVFRAV 374
Cdd:PRK11608  174 VQLPPLRERQSDIMLMAEHFAIQMCRELGLPLFPGFTERARETLLNYRWPGNIRELKNVVERSV 237
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
120-385 5.89e-48

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: 173.87  E-value: 5.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 120 LKLDRREAKARTGRRGRSNAVNF--TDIVSASPAMLRVIELAQR-AAQSSIPVVLEGESGVGKEMVARAI--------QS 188
Cdd:COG4650   159 LDLSRYDAIASRFAQEQQEAVSFlkSGIATRNAAFNRLIEQIERvAIRSRAPILLTGPTGAGKSQLARRIyelkkarhQV 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 189 AGdrankPFITVNC------GAIphnlveSILFGHEKGAFTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQ 262
Cdd:COG4650   239 SG-----RFVEVNCatlrgdGAM------SALFGHVKGAFTGAVSDRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIE 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 263 QGEIETVGSARVQKVNVRLISATNKNLIEEVKEGRFREDLYYRLNVFPITIPALRRRKEDI-PHLARVFaERFSAEQKlp 341
Cdd:COG4650   308 EKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPGLAERREDIePNLDYEL-ARFAREQG-- 384
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2221781758 342 NPVGLDASALALLTAYD------WPGNIRQLENAVFRAVVLSQGGELSDA 385
Cdd:COG4650   385 RRVRFNKEARARYLAFAtspealWSGNFRDLNASVTRMATLAEGGRITVA 434
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
2-146 1.92e-30

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 117.36  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER--PDLILLDLMLPGMDGLEVCRRLRARPSDIPIIM 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALkldrreakartgRRGRSNAVNFTDIV 146
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL------------RRRAAEVLRVGDLL 131
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
5-116 2.33e-30

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 114.17  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER--PDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-125 2.78e-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: 111.87  E-value: 2.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAV--GELGVDVP 78
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA--GPPDLILLDINMPGMDGLELLRRIraLPRLPDIP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRR 125
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
142-370 2.91e-29

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: 122.14  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 142 FTDIVSASPAMLRVIELAqRAAQS----SIPVVLEGESGVGKEMVAR-----AIQSAGDRANKPFITVNCGAIPHN--LV 210
Cdd:COG1221   103 FDNLIGANGSLKNAIEQA-KAAILyppkGLHTLILGPTGVGKSFFAElmyeyAIEIGVLPEDAPFVVFNCADYANNpqLL 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 211 ESILFGHEKGAFTGATEKHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAVQQGEIETVG-SARVQKVNVRLISATNKNl 289
Cdd:COG1221   182 MSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTED- 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 290 IEEVkegrfredLyyrLNVF----PITI--PALRRR--KEDIpHLARVFaerFSAE-QKLPNPVGLDASALALLTAYDWP 360
Cdd:COG1221   261 PESS--------L---LKTFlrriPMVIklPSLEERslEERL-ELIKHF---FKEEaKRLNKPIKVSKEVLKALLLYDCP 325
                         250
                  ....*....|
gi 2221781758 361 GNIRQLENAV 370
Cdd:COG1221   326 GNIGQLKSDI 335
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-145 7.20e-29

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 113.72  E-value: 7.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGEL--GVDVP 78
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP--PDLILLDVRMPGMDGFELLRLLRADpsTRDIP 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRRGRSNAVNFTDI 145
Cdd:COG3437    83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHDI 149
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
5-121 2.05e-28

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: 108.74  E-value: 2.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKE--RRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:cd17550    79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
6-106 5.73e-28

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: 107.31  E-value: 5.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   6 LVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTGQ 85
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLRE--ERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 2221781758  86 GGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
4-134 5.82e-28

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: 110.19  E-value: 5.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGkagLELLKQYSGEIN-VVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASA---EAFLAALDPDRPgCLLLDVRMPGMSGLELQEELAARGSPLPVIFL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRR 134
Cdd:COG4566    78 TGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRA 129
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
2-116 7.35e-28

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 109.61  E-value: 7.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGEL--GVDVPV 79
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR--PDLILLDLEMPDMDGLELCRRLRADprTADIPI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  80 IVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:COG3706    79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-121 1.63e-27

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 107.36  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALL--AENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVP 78
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVgvASSGEEALALLAEH--RPDLILLDIYLPDGDGLELLRELRARGPDVD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
5-125 5.90e-27

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: 105.26  E-value: 5.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLK-QYSGeinVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSpDFPG---VVISDIRMPGMDGLELLAQIRELDPDLPVILIT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLdRR 125
Cdd:cd17549    78 GHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEK-RR 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
3-108 1.58e-26

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: 103.82  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSE--QPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVV 78
                          90       100
                  ....*....|....*....|....*.
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKPIE 104
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
5-106 1.72e-26

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: 103.31  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYG--HLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHK--PDLVITDINMPGMDGLELLEAIRELDPDTKIIIL 79
                          90       100
                  ....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:COG4753    80 SGYSDFEYAQEAIKLGADDYLLKP 103
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
5-126 5.98e-26

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 102.28  E-value: 5.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQP--PDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRRE 126
Cdd:cd17572    79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLT 120
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
6-106 3.06e-24

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 96.71  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   6 LVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTGQ 85
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELARE--EQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAK 78
                          90       100
                  ....*....|....*....|.
gi 2221781758  86 GGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd17574    79 DEEEDKVLGLELGADDYITKP 99
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-121 5.17e-24

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 96.79  E-value: 5.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:COG5803     1 MMKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELK--PDLVLLDMKMPGMDGIEILKEIKEIDPDIPVI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:COG5803    79 MMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
4-119 1.09e-23

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 97.68  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP--PDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLT 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNA 119
Cdd:COG4567    84 GYASIATAVEAIKLGADDYLAKPADADDLLAALERA 119
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
5-121 2.35e-23

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 95.10  E-value: 2.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAV--ERYG-HLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGfEVVGEAENGEEALELIEEH--KPDIVITDIRMPGMDGLELIEKIRELYPDIKIII 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:cd17536    79 LSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
3-120 1.22e-22

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: 93.04  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGhlaLLAENGKAGLELLKQYSGEIN-VVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:cd17537     1 ATVYVVDDDEAVRDSLAFLLRSVG---LAVKTFTSASAFLAAAPPDQPgCLVLDVRMPGMSGLELQDELLARGSNIPIIF 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd17537    78 ITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
5-112 1.24e-22

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: 92.69  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEINVVVLDLMMPEMDGLGFLKAVGELgVDVPVIVQTG 84
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                          90       100
                  ....*....|....*....|....*...
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERI 112
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDL 107
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
4-137 1.05e-21

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 93.73  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVVGEasNGEEALELLEEH--KPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221781758  82 QTGQggIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRRGRS 137
Cdd:COG3279    81 TTAY--DEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
fixJ PRK09390
response regulator FixJ; Provisional
3-129 3.50e-20

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 88.52  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:PRK09390    4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGL--RFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVM 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKA 129
Cdd:PRK09390   82 TGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAAKS 128
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
5-109 4.93e-20

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: 85.91  E-value: 4.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHL--ALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQ 82
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKELK--PDVITLDIEMPVMDGLEALRRIMAER-PTPVVMV 79
                          90       100
                  ....*....|....*....|....*....
gi 2221781758  83 TG--QGGIDTVVQAMRAGAFDFVVKPVSP 109
Cdd:cd17541    80 SSltEEGAEITLEALELGAVDFIAKPSGG 108
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
150-307 9.99e-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: 85.66  E-value: 9.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 150 PAMLRVIELAQRAAQSSIP--VVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESILFGHEkgaftgATE 227
Cdd:cd00009     1 VGQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 228 KHVGKFMEADGGTLFLDEIGDLPLDVQVKLLRAvqqgeIETVGSARVQKVNVRLISATNKNLieevkEGRFREDLYYRLN 307
Cdd:cd00009    75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRV-----LETLNDLRIDRENVRVIGATNRPL-----LGDLDRALYDRLD 144
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
5-110 1.11e-19

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: 84.70  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALL-AENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAV---GELGvDVPVI 80
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKA--GGFDFVITDWNMPNMDGLELLKTIradGALS-HLPVL 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPE 110
Cdd:cd19923    80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAA 109
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
5-116 1.19e-19

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 84.44  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGF---LKAVGELGVDVPVIV 81
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKE--EPFDLVLMDLQMPVMDGLEAtrrIRELEGGGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17546    79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
3-131 1.23e-19

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


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 84.42  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLA-ENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGEL--GVDVPV 79
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCREN--PPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2221781758  80 IVQTGQGGIDTVVQAMRAGAFDFVVKPVsperigaaisnalklDRREAKART 131
Cdd:cd17551    79 VMITADTDREVRLRALEAGATDFLTKPF---------------DPVELLARV 115
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
5-120 1.26e-19

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: 84.25  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYG-HLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELK--PDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd17542    81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
4-115 1.74e-19

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: 83.65  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEK--PDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLT 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAA 115
Cdd:cd17563    80 GYASIATAVEAIKLGADDYLAKPADADEILAA 111
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
146-316 2.99e-19

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 83.93  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 146 VSASPAMLRVIELAQRAAQSSIPVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESilfghekgaftga 225
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 226 tekhvgkfmeADGGTLFLDEIGDLPLDVQVKLLRAVQQGEietvgsarvqKVNVRLISATNKNLIEEVKEGRFREDLYYR 305
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 2221781758 306 LNVFPITIPAL 316
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
4-107 8.17e-19

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 81.78  E-value: 8.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDglGF-----LKAVGELGvDVP 78
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEE--LPDLILLDVMMPGMD--GFevcrrLKEDPETR-HIP 75
                          90       100
                  ....*....|....*....|....*....
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPV 107
Cdd:cd17538    76 VIMITALDDREDRIRGLEAGADDFLSKPI 104
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
5-121 9.10e-19

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: 82.07  E-value: 9.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE--PVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2221781758  85 QGGIDTVVQAMRAGA-FDFVVKPVSPERIGAAISNALK 121
Cdd:cd17569    81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
5-107 3.48e-18

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: 79.86  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGF---LKAvGELGVDVPVIV 81
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE--PPDLILLDVMMPGMDGFEVcrrLKA-DPATRHIPVIF 77
                          90       100
                  ....*....|....*....|....*.
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPV 107
Cdd:cd19920    78 LTALTDTEDKVKGFELGAVDYITKPF 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
5-116 4.11e-18

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: 80.25  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVVGEaaDGEEALALLREL--RPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
5-106 1.18e-17

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 78.25  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALT--NEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTA 78
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd19935    79 RDSVEDRVKGLDLGADDYLVKP 100
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
4-118 2.86e-17

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 77.58  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAV-ERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:cd17593     2 KVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILRE--GRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVV 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2221781758  83 TGqggiDTVVQAMR----AGAFDFVVKPVSPERIGAAISN 118
Cdd:cd17593    80 SG----DVQPEAKErvleLGALAFLKKPFDPEKLAQLLEE 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
6-108 3.56e-17

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: 77.26  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   6 LVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLkqYSGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTGQ 85
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYA--LSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTAL 78
                          90       100
                  ....*....|....*....|...
gi 2221781758  86 GGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:cd17625    79 DAVEDRVKGLDLGADDYLPKPFS 101
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
4-117 4.35e-17

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: 77.28  E-value: 4.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYG--HLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQ--PDLILLDIYLPDGNGLDLLRELRAAGHDVDVIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAIS 117
Cdd:cd19925    80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLE 115
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
3-105 6.42e-17

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 76.49  E-value: 6.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLE--SEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIIC 78
                          90       100
                  ....*....|....*....|...
gi 2221781758  83 TGQGGIDTVVQAMRAGAfdFVVK 105
Cdd:cd17554    79 TAYSEYKSDFSSWAADA--YVVK 99
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
5-116 7.15e-17

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: 76.37  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALA--SGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17624    79 RDGVDDRVAGLDAGADDYLVKPFALEELLARL 110
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
3-116 1.51e-16

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 75.80  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELGV--DVPVI 80
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQ--SKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17562    79 MLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
orf27 CHL00148
Ycf27; Reviewed
4-121 3.91e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 77.83  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQT 83
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQ--PDLVILDVMMPKLDGYGVCQEIRKES-DVPIIMLT 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:CHL00148   85 ALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLR 122
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
5-116 9.04e-16

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: 73.26  E-value: 9.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEinVVVLDLMMPEMDGLGFLKAVGEL--GVDVPVIVQ 82
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPD--VILSDIGMPGMDGYELARRLRELpwLANTPAIAL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2221781758  83 TGQGGIDTVVQAMRAGaFDF-VVKPVSPERIGAAI 116
Cdd:cd17580    79 TGYGQPEDRERALEAG-FDAhLVKPVDPDELIELI 112
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
5-106 3.88e-15

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 71.04  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEinVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQTG 84
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPD--LIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSA 77
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTKP 99
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-130 5.55e-15

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 73.45  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALL-AENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGvDVPV 79
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVREL--KPDLVIVDIDMPDRDGLEAARQISEER-PAPV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2221781758  80 IVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKAR 130
Cdd:COG3707    79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALR 129
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
5-114 6.15e-15

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 71.23  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEinVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPD--AVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTA 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGA 114
Cdd:cd17615    80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVA 109
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
5-120 9.56e-15

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: 70.39  E-value: 9.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEE--PYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAIsNAL 120
Cdd:cd19934    79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARL-RAL 113
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
5-116 1.13e-14

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 70.10  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGN--RPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFALEELLARV 110
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
6-109 1.51e-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: 69.99  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   6 LVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAV--GELGVDVPVIVQT 83
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAK--DEKPDLIILDLMLPGIDGLEVCRILrsDPKTSSIPIIMLT 78
                          90       100
                  ....*....|....*....|....*..
gi 2221781758  84 GQGG-IDTVVqAMRAGAFDFVVKPVSP 109
Cdd:cd19937    79 AKGEeFDKVL-GLELGADDYITKPFSP 104
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
5-117 1.59e-14

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: 70.16  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALL-AENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEDLGPGNVDeADDGREALVILLCNA--PDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  84 GQGG--IDTVVQAMRAGAFDFV---VKPVSPERIGAAIS 117
Cdd:cd17530    81 GLDGgiLESAETLAGANGLNLLgtlSKPFSPEELTELLT 119
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-151 1.70e-14

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 74.80  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALL--AENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELgVDVP 78
Cdd:PRK00742    2 MKIRVLVVDDSAFMRRLISEILNSDPDIEVVgtAPDGLEAREKIKKLN--PDVITLDVEMPVMDGLDALEKIMRL-RPTP 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221781758  79 VIV---QTGQGGiDTVVQAMRAGAFDFVVKPVSPERIGAAISNALKLDRREAKARTGRRGRSNAVNFTDIVSASPA 151
Cdd:PRK00742   79 VVMvssLTERGA-EITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVRALPPRAAAAARAAAAAP 153
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
5-106 1.97e-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: 69.66  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGF---LKAVGELGvDVPVIV 81
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTL--VISDIVMPEMDGYELcrkIKSDPDLK-DIPVIL 77
                          90       100
                  ....*....|....*....|....*
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd17598    78 LTTLSDPRDVIRGLECGADNFITKP 102
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
3-116 2.65e-14

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: 69.20  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAV--GELGVDVPVI 80
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVE--PRPDLILLDWMLPGGSGIQFIRRLkrDEMTRDIPII 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17618    79 MLTARGEEEDKVRGLEAGADDYITKPFSPRELVARI 114
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
5-106 4.03e-14

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: 68.84  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd19919     3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALA--SSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd19919    81 HSDLDSAVSAYQGGAFEYLPKP 102
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
5-121 4.28e-14

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: 68.53  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEasSGEEGIELAERL--DPDLILLDLNMKGMSGLDTLKALREEGVSARIVIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
3-119 5.06e-14

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 71.21  E-value: 5.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:PRK10651    7 ATILLIDDHPMLRTGVKQLISMAPDITVVGEasNGEQGIELAESL--DPDLILLDLNMPGMNGLETLDKLREKSLSGRIV 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNA 119
Cdd:PRK10651   85 VFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQA 123
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
4-110 1.81e-13

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 67.16  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgEINVVVLDLMMPEMDGLGFLKAVGEL--GVDVPVIV 81
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHP-DIKLVITDYNMPEMDGFELVREIRKKysRDQLAIIG 80
                          90       100
                  ....*....|....*....|....*....
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPE 110
Cdd:cd17544    81 ISASGDNALSARFIKAGANDFLTKPFLPE 109
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
5-106 6.49e-13

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 64.83  E-value: 6.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQySGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQ-GKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd18160    81 GAAAAPELLSDAVGDNATLKKP 102
pleD PRK09581
response regulator PleD; Reviewed
1-108 1.17e-12

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 69.93  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLL--KNAVERYGhlALLAENGKAGLELLKQysGEINVVVLDLMMPEMDglGF-----LKAvGEL 73
Cdd:PRK09581    1 MTARILVVDDIPANVKLLeaKLLAEYYT--VLTASSGAEAIAICER--EQPDIILLDVMMPGMD--GFevcrrLKS-DPA 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2221781758  74 GVDVPVIVQTGQGGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:PRK09581   74 TTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPIN 108
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
5-106 1.23e-12

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: 64.32  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQY-------SGEINVVVLDLMMPEMDGLGFLKAVGE--LGV 75
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlSKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2221781758  76 DVPVIVQTGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
5-116 1.61e-12

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 63.97  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDI--ILLDLNLPDMSGYEVLRTLRLAKVKTPILILSG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17616    79 LADIEDKVKGLGFGADDYMTKPFHKDELVARI 110
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
5-116 2.34e-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: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGElGVDVPVIVQTG 84
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALL--EGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2221781758  85 QGG-IDTVVqAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17623    78 RGDdIDRIL-GLELGADDYLPKPFNPRELVARI 109
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
5-112 6.43e-12

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 65.98  E-value: 6.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYG--HLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVD--VPVI 80
Cdd:COG5801     7 VLIADDNREFCELLEEYLSSQPdmEVVGVAYNGLEALELIEEK--KPDVVILDIIMPHLDGLGVLEKLREMNLEkrPKVI 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  81 VQT--GQggiDTVVQ-AMRAGAFDFVVKP----VSPERI 112
Cdd:COG5801    85 MLTafGQ---EDITQrAVELGADYYILKPfdldVLAERI 120
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
4-59 7.00e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 60.27  E-value: 7.00e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221781758    4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMP 59
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE--EKPDLILLDIMMP 55
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
5-122 7.47e-12

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: 62.17  E-value: 7.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALL--AENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQ 82
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEEL--KPDVVFLDIQMPGLDGLELAKKLSKLA-KPPLIVF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2221781758  83 TgqggidTV-----VQAMRAGAFDFVVKPVSPERIGAAISNALKL 122
Cdd:cd17532    78 V------TAydeyaVEAFELNAVDYLLKPFSEERLAEALAKLRKR 116
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
2-120 1.28e-11

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 61.80  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERY-GHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGE--LGVDVP 78
Cdd:cd17552     1 SKRILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATE--QPDAILLDVMMPDMDGLATLKKLQAnpETQSIP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd17552    79 VILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
5-109 1.82e-11

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: 61.23  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELL-----KQYSG----EINVVVLDLMMPEMDGLGFLKAVGELG- 74
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeEDSSNfnepKVNMIITDYCMPGMTGYDLLKKVKESSa 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  75 -VDVPVIVQTGQGGIDTVVQAMRAGAFDFVVKPVSP 109
Cdd:cd17581    81 lKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
5-106 2.99e-11

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: 59.86  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLA--SEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITA 78
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd19926    79 YGSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
3-112 4.06e-11

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 60.09  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQ 82
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQD--IDLVLLDINLPGKDGLSLTRELREQS-EVGIILV 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2221781758  83 TGQGG-IDTVVqAMRAGAFDFVVKPVSPERI 112
Cdd:cd17619    78 TGRDDeVDRIV-GLEIGADDYVTKPFNPREL 107
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
4-111 4.24e-11

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: 60.51  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALL--AENGKAGLELLKQ---YSGEI--NVVVLDLMMPEMDGLGFLKAV--GELG 74
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELhvVRDGEEALDFLRGegeYADAPrpDLILLDLNMPRMDGFEVLREIkaDPDL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  75 VDVPVIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPER 111
Cdd:cd17557    81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEE 117
ompR PRK09468
osmolarity response regulator; Provisional
2-127 5.89e-11

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 62.68  E-value: 5.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:PRK09468    5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRES--FHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIM 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221781758  82 QTGQGG-IDTVVqAMRAGAFDFVVKPVSPERIGAAISNALkldRREA 127
Cdd:PRK09468   83 LTAKGEeVDRIV-GLEIGADDYLPKPFNPRELLARIRAVL---RRQA 125
PRK10610 PRK10610
chemotaxis protein CheY;
6-108 6.46e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 59.99  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   6 LVIDDDPVQRRLLKNAVERYG-HLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELG--VDVPVIVQ 82
Cdd:PRK10610    9 LVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQ--AGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLMV 86
                          90       100
                  ....*....|....*....|....*.
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:PRK10610   87 TAEAKKENIIAAAQAGASGYVVKPFT 112
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
5-116 7.96e-11

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 59.49  E-value: 7.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDL--VLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17553    81 YGELDMIQESKELGALTHFAKPFDIDEIRDAV 112
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
5-117 8.81e-11

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: 59.09  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGF---LKAVGELgVDVPVIV 81
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDL--ILMDIQLPGMDGLEAtrlLKEDPAT-RDIPVIA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2221781758  82 QTGqggidtvvQAMR--------AGAFDFVVKPVSPERIGAAIS 117
Cdd:cd17548    79 LTA--------YAMKgdrekileAGCDGYISKPIDTREFLETVA 114
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
5-106 1.21e-10

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: 58.28  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEE--GEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSA 78
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd19928    79 QNTLMTAVKAAERGAFEYLPKP 100
PRK10643 PRK10643
two-component system response regulator PmrA;
5-106 2.17e-10

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 60.43  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKqySGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLE--SGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTA 80
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:PRK10643   81 RDTLEDRVAGLDVGADDYLVKP 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
5-106 2.63e-10

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: 57.41  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEINVVVLDLMMPEMDGLGFLKAVGELGV--DVPVIVQ 82
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMM 80
                          90       100
                  ....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd17582    81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
5-116 3.25e-10

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 57.41  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEINVVVLDLMMPEMDGLGFLKAVGEL--GVDVPVIVQ 82
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLfgRRERPLIVA 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2221781758  83 -TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd19933    83 lTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
5-120 5.96e-10

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 57.04  E-value: 5.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLAL-LAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLgflKAVGELGVD--VPVIV 81
Cdd:cd19932     3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKH--KPDLVIMDVKMPRLDGI---EAAKIITSEniAPIVL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd19932    78 LTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
PRK10766 PRK10766
two-component system response regulator TorR;
1-109 1.53e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 58.13  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGvDVPVI 80
Cdd:PRK10766    1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQN--QHVDLILLDINLPGEDGLMLTRELRSRS-TVGII 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2221781758  81 VQTGQG-GIDTVVqAMRAGAFDFVVKPVSP 109
Cdd:PRK10766   78 LVTGRTdSIDRIV-GLEMGADDYVTKPLEL 106
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
5-85 1.87e-09

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: 55.05  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgEINVVVLDLMMP-EMDGLGFLKAVGELGVDVPVIVQT 83
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGP-DIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTS 79

                  ..
gi 2221781758  84 GQ 85
Cdd:cd18161    80 GY 81
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
462-505 2.18e-09

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


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 54.05  E-value: 2.18e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2221781758 462 LAEIEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYGID 505
Cdd:COG2901    40 LAEVEKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGLL 83
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
462-500 3.01e-09

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 52.40  E-value: 3.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2221781758 462 LAEIEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLK 500
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLK 39
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
5-106 4.89e-09

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: 53.92  E-value: 4.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGE--LGVDVPVIVQ 82
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQY--IPDLIISDIIMPGVDGYSLLGKLRKnaDFDTIPVIFL 78
                          90       100
                  ....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd19927    79 TAKGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
4-107 7.54e-09

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 53.60  E-value: 7.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVgELGVDVPVIVQT 83
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRR--VDLVLLDLRLGQESGLDLLRTI-RARSDVPIIIIS 77
                          90       100
                  ....*....|....*....|....*.
gi 2221781758  84 GQGG--IDTVVqAMRAGAFDFVVKPV 107
Cdd:cd17594    78 GDRRdeIDRVV-GLELGADDYLAKPF 102
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
32-106 9.13e-09

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 53.00  E-value: 9.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758  32 AENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAV--GELGVDVPVIVQTGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd17561    33 AHNGQEALELIEEK--EPDVLLLDIIMPHLDGIGVLEKLrrMRLEKRPKIIMLTAFGQEDITQRAVELGASYYILKP 107
PRK10336 PRK10336
two-component system response regulator QseB;
5-106 9.44e-09

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 55.67  E-value: 9.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLkqYSGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK10336    3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEAL--YSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTA 80
                          90       100
                  ....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKP 106
Cdd:PRK10336   81 RDALAERVEGLRLGADDYLCKP 102
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
4-120 1.02e-08

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: 53.15  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQT 83
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDL--ILLDLMLPGTDGLTLCREIRRFS-DVPIIMVT 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2221781758  84 GQ-GGIDTVVqAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd19938    78 ARvEEIDRLL-GLELGADDYICKPYSPREVVARVKAIL 114
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-121 1.26e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 55.49  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGV--DVP 78
Cdd:PRK10161    1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDL--ILLDWMLPGGSGIQFIKHLKRESMtrDIP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:PRK10161   79 VVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
5-137 1.44e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 56.43  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALL--AENGKAGLELLKQYSGEinVVVLDLMMPEMDGLGFLKAVGELgVDVPVIVQ 82
Cdd:PRK12555    3 IGIVNDSPLAVEALRRALARDPDHEVVwvATDGAQAVERCAAQPPD--VILMDLEMPRMDGVEATRRIMAE-RPCPILIV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221781758  83 TG--QGGIDTVVQAMRAGAFDFVVKPV---------SPERIGAAISNALKLDRREAKARTGRRGRS 137
Cdd:PRK12555   80 TSltERNASRVFEAMGAGALDAVDTPTlgigagleeYAAELLAKIDQIGRLLGRRLAPAAAPAAAS 145
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
3-116 1.56e-08

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 52.86  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQ 82
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDL--VLLDLMLPGIDGIEVCRQIRAES-GVPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARI 111
PRK10693 PRK10693
two-component system response regulator RssB;
31-108 1.63e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 56.15  E-value: 1.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2221781758  31 LAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTGQGGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:PRK10693    2 LAANGVDALELLGGFTPDL--IICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
5-116 1.67e-08

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 52.66  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQ 82
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDDLEVVAQasNGQEALRLVLKHS--PDVAILDIEMPGRTGLEVAAELREELPDTKVLIV 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:cd19930    79 TTFGRPGYFRRALAAGVDGYVLKDRPIEELADAI 112
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
5-120 3.14e-08

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: 52.02  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGH-LALLAENGKAGLELLKQYSgeINVVVLDLMMP-EMDGLGFLKAVGELGvDVPVIVQ 82
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYeVVGIADSGEEAIELAEENK--PDLILMDINLKgDMDGIEAAREIREKF-DIPVIFL 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd17534    80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
2-70 3.61e-08

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 52.20  E-value: 3.61e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAV 70
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEaaDGEEALELLEEL--RPDVVLLDIRMPGMDGLEALRRL 69
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
5-121 3.92e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.04  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysgEINVVVLDLMMPEMDGLGFLKAVgELGVDVPVIVQTG 84
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD---SIDLLLLDVMMPKKNGIDTLKEL-RQTHQTPVIMLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:PRK10955   80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAILR 116
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
4-80 6.05e-08

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 55.37  E-value: 6.05e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:PRK10841  803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK--NHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVI 877
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-131 7.09e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 53.43  E-value: 7.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQysGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:PRK11083    2 QQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQ--QPPDLVILDVGLPDISGFELCRQLLAFHPALPVI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2221781758  81 VQTGQGG-IDTVVqAMRAGAFDFVVKPVSPERIGAAISNALkldRREAKART 131
Cdd:PRK11083   80 FLTARSDeVDRLV-GLEIGADDYVAKPFSPREVAARVRTIL---RRVKKFAA 127
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
5-121 8.45e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 53.00  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELlkQYSGEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHL--AMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:PRK09836   81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLR 117
PRK10816 PRK10816
two-component system response regulator PhoP;
5-116 9.17e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 52.82  E-value: 9.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEINVVvlDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIV--DLGLPDEDGLSLIRRWRSNDVSLPILVLTA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:PRK10816   81 RESWQDKVEVLSAGADDYVTKPFHIEEVMARM 112
PRK11517 PRK11517
DNA-binding response regulator HprR;
5-108 9.71e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.98  E-value: 9.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVgELGVDVPVIVQTG 84
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDD--YALIILDIMLPGMDGWQILQTL-RTAKQTPVICLTA 79
                          90       100
                  ....*....|....*....|....
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:PRK11517   80 RDSVDDRVRGLDSGANDYLVKPFS 103
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
5-122 1.06e-07

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: 50.83  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLaLLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17596     3 ILVVDDEVRSLEALRRTLEEDFDV-LTAASAEEALAILEEE--WVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  85 QGGIDTVVQAMR-AGAFDFVVKPVSPERIGAAISNALKL 122
Cdd:cd17596    80 YTDSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAARL 118
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
5-120 1.82e-07

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: 49.59  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEinVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQTG 84
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPD--LVLLDINLPYFDGFYWCREIRQIS-NVPIIFISS 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNAL 120
Cdd:cd18159    78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
3-146 1.99e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 51.73  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLelLKQYSGEINVVVLDLMMPEMDGLGFLKAVGELGVdVPVIVQ 82
Cdd:PRK10529    2 TNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGL--LEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2221781758  83 TGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALkldRREAKARTgrrgRSNAVNFTDIV 146
Cdd:PRK10529   79 SARSEESDKIAALDAGADDYLSKPFGIGELQARLRVAL---RRHSATPA----PDPLVKFSDVT 135
PLN03029 PLN03029
type-a response regulator protein; Provisional
4-107 3.46e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 51.19  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSG------------------EINVVVLDLMMPEMDGLG 65
Cdd:PLN03029   10 HVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDdrsnpdtpsvspnshqevEVNLIITDYCMPGMTGYD 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2221781758  66 FLKAVGELGV--DVPVIVQTGQGGIDTVVQAMRAGAFDFVVKPV 107
Cdd:PLN03029   90 LLKKIKESSSlrNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
5-121 3.95e-07

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: 48.91  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELgVDVPVIVQTG 84
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDA--VLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:cd17622    80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
PRK15479 PRK15479
transcriptional regulator TctD;
5-121 4.66e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 50.88  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEM--YALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:PRK15479   81 RSAVADRVKGLNVGADDYLPKPFELEELDARLRALLR 117
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
168-319 6.59e-07

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: 48.44  E-value: 6.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758 168 PVVLEGESGVGKEMVARAIQSAGDraNKPFITVNCGAiphNLVESILFGHEKGAfTGATEKHVGKFMEA--DGGTLFLDE 245
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALS--NRPVFYVQLTR---DTTEEDLFGRRNID-PGGASWVDGPLVRAarEGEIAVLDE 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758 246 IGDLPLDVQVKLLRAVQQGEI---ETVGSARVQKVNVRLISATNknlieevkegrfreDLYYRLNVFPitiPALRRR 319
Cdd:pfam07728  75 INRANPDVLNSLLSLLDERRLllpDGGELVKAAPDGFRLIATMN--------------PLDRGLNELS---PALRSR 134
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
4-121 9.78e-07

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: 47.75  E-value: 9.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELgVDVPVIVQT 83
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSL--VVLDIMLPGMDGLTVCREVREH-SHVPILMLT 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2221781758  84 GQGG-IDTVVqAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:cd19939    78 ARTEeMDRVL-GLEMGADDYLCKPFSPRELLARVRALLR 115
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
5-108 1.10e-06

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 47.42  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQTG 84
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDL--ILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTA 77
                          90       100
                  ....*....|....*....|....*
gi 2221781758  85 QGG-IDTVVqAMRAGAFDFVVKPVS 108
Cdd:cd17614    78 KDSeVDKVL-GLELGADDYVTKPFS 101
PRK15347 PRK15347
two component system sensor kinase;
4-124 1.34e-06

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 51.18  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLK----AVGELGVDVPV 79
Cdd:PRK15347  692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQH--RFDLVLMDIRMPGLDGLETTQlwrdDPNNLDPDCMI 769
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221781758  80 IVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNA--LKLDR 124
Cdd:PRK15347  770 VALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAaeYQLLR 816
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
4-116 1.34e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 49.47  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAE--NGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:PRK10403    8 QVLIVDDHPLMRRGVRQLLELDPGFEVVAEagDGASAIDLANRLD--PDVILLDLNMKGMSGLDTLNALRRDGVTAQIII 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAI 116
Cdd:PRK10403   86 LTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAI 120
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
168-306 1.44e-06

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: 48.14  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758  168 PVVLEGESGVGKEMVARAIQSAGDRANKPFITVNCGAIPHNLVESIL-FGHEKGAFTGATEKHVGKFME----ADGGTLF 242
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLlIIVGGKKASGSGELRLRLALAlarkLKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221781758  243 LDEIGDLPLDVQVKLLravQQGEIETVGSARVQKVNVRLISATN--KNLIEEVKEGRFREDLYYRL 306
Cdd:smart00382  84 LDEITSLLDAEQEALL---LLLEELRLLLLLKSEKNLTVILTTNdeKDLGPALLRRRFDRRIVLLL 146
PRK10430 PRK10430
two-component system response regulator DcuR;
5-118 1.99e-06

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 48.95  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVER------YGHLALLAEngkaGLELLKQYSGEINVVVLDLMMPEMDGLGFLKAVGELGVDVP 78
Cdd:PRK10430    4 VLIVDDDAMVAELNRRYVAQipgfqcCGTASTLEQ----AKEIIFNSDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISN 118
Cdd:PRK10430   80 VIVISSAADAATIKDSLHYGVVDYLIKPFQASRFEEALTG 119
dpiA PRK10046
two-component response regulator DpiA; Provisional
51-117 2.11e-06

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 48.86  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221781758  51 VVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAIS 117
Cdd:PRK10046   53 LILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLT 119
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
5-106 3.10e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 45.82  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLAL-LAENGKAGLELLkqySGEINVVVLDLMMPEMDGL---GFLKAVGELGvDVPVI 80
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVvIDDPLRALTTLL---NSKPDLILIDIDMPDLDGYelcSLLRKSSALK-DTPII 76
                          90       100
                  ....*....|....*....|....*.
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVKP 106
Cdd:cd17602    77 MLTGKDGLVDRIRAKMAGASGYLTKP 102
PRK11173 PRK11173
two-component response regulator; Provisional
2-109 7.07e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 47.32  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGvDVPVIV 81
Cdd:PRK11173    3 TPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEN--DINLVIMDINLPGKNGLLLARELREQA-NVALMF 79
                          90       100
                  ....*....|....*....|....*....
gi 2221781758  82 QTGQGG-IDTVVqAMRAGAFDFVVKPVSP 109
Cdd:PRK11173   80 LTGRDNeVDKIL-GLEIGADDYITKPFNP 107
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
5-108 1.17e-05

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: 44.34  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGlellkQYSGEI---NVVVLDLMMPEMDGLGFLKAVGELGVDVPVIV 81
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDG-----EYYIDIrnyDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIV 75
                          90       100
                  ....*....|....*....|....*..
gi 2221781758  82 QTGQGGIDTVVQAMRAGAFDFVVKPVS 108
Cdd:cd17573    76 LSDNPKTEQEIEAFKEGADDYIAKPFD 102
PRK13856 PRK13856
two-component response regulator VirG; Provisional
4-134 1.21e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 46.73  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   4 HVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGElGVDVPVIVQT 83
Cdd:PRK13856    3 HVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASET--VDVVVVDLNLGREDGLEIVRSLAT-KSDVPIIIIS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2221781758  84 GQ--GGIDTVVqAMRAGAFDFVVKPVSPERIGAAISNALKLdrREAKARTGRR 134
Cdd:PRK13856   80 GDrlEEADKVV-ALELGATDFIAKPFGTREFLARIRVALRV--RPNVVRTKDR 129
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1-126 1.57e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 46.22  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGvDVPVI 80
Cdd:PRK10710    9 NTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDL--ILLDLMLPGTDGLTLCREIRRFS-DIPIV 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221781758  81 VQTGQ-GGIDTVVqAMRAGAFDFVVKPVSPERIGAAISNALKLDRRE 126
Cdd:PRK10710   86 MVTAKiEEIDRLL-GLEIGADDYICKPYSPREVVARVKTILRRCKPQ 131
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
7-107 3.31e-05

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 43.03  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   7 VIDDDPVQRRLLKNAVERY--GHLALLAENGKAGLELLKQYsgEINVVVLDLMMPEMDGLGFLKAVGELGVDVPVIVQTG 84
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFL--QPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80
                          90       100
                  ....*....|....*....|...
gi 2221781758  85 QGGIDTVVQAMRAGAFDFVVKPV 107
Cdd:cd17565    81 VSDKEMIGKAYQAGIEFFINKPI 103
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
5-106 9.81e-05

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: 41.28  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQTG 84
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARP--PDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTS 77
                          90       100
                  ....*....|....*....|...
gi 2221781758  85 QGG-IDTVVqAMRAGAFDFVVKP 106
Cdd:cd19936    78 KDDeIDEVF-GLRMGADDYITKP 99
fis PRK00430
DNA-binding transcriptional regulator Fis;
462-504 1.00e-04

DNA-binding transcriptional regulator Fis;


Pssm-ID: 179020 [Multi-domain]  Cd Length: 95  Bit Score: 41.20  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2221781758 462 LAEIEEELIRFALRFYRGQMSQVARKLGIGRSTLYRKLKDYGI 504
Cdd:PRK00430   52 LAEVEAPLLDMVMQYTRGNQTRAALMLGINRGTLRKKLKKYGM 94
PRK15369 PRK15369
two component system response regulator;
1-121 1.63e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 43.14  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   1 MTAHVLVIDDDPVQRRLLKNAVERYGHLALLA--ENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGVDVP 78
Cdd:PRK15369    2 KNYKILLVDDHELIINGIKNMLAPYPRYKIVGqvDNGLEVYNACRQLEPDI--VILDLGLPGMNGLDVIPQLHQRWPAMN 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNALK 121
Cdd:PRK15369   80 ILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAV 122
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
5-109 2.19e-04

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 41.17  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDP-VQRRLLKNAVERYG--HLALLAENGKAGLELLKQYS--GE-INVVVLDLMMPEMDGLGFLKAVGELGVDVP 78
Cdd:cd17595     3 ILTVDDDPqVLRAVARDLRRQYGkdYRVLRADSGAEALDALKELKlrGEaVALFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2221781758  79 VIVQTGQGGIDTVVQAMRAGAFDF-VVKPVSP 109
Cdd:cd17595    83 RVLLTAYADTDAAIRAINDVQLDYyLLKPWDP 114
PRK11697 PRK11697
two-component system response regulator BtsR;
5-111 2.36e-04

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 42.91  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAgLELLKQysgeIN-----VVVLDLMMPEMDGLgflKAVGELGVDV-P 78
Cdd:PRK11697    4 VLIVDDEPLAREELRELLQEEGDIEIVGECSNA-IEAIGA----IHrlkpdVVFLDIQMPRISGL---ELVGMLDPEHmP 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2221781758  79 VIVqtgqggIDTV-----VQAMRAGAFDFVVKPVSPER 111
Cdd:PRK11697   76 YIV------FVTAfdeyaIKAFEEHAFDYLLKPIDPAR 107
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
3-105 2.54e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.56  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   3 AHVLVIDDDPVQRRLLKNAVERYGHLALLAENG--KAGLELLKQYSgeINVVVLDLMMPEMDGLGFLKAVGELGVDVPVI 80
Cdd:PRK09935    4 ASVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDdyRITIDYLRTRP--VDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVL 81
                          90       100
                  ....*....|....*....|....*
gi 2221781758  81 VQTGQGGIDTVVQAMRAGAFDFVVK 105
Cdd:PRK09935   82 FLSSKSECFYAGRAIQAGANGFVSK 106
PRK13557 PRK13557
histidine kinase; Provisional
2-106 5.35e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 42.74  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   2 TAHVLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQySGEINVVVLDLMMP-EMDGLGFLKAVGELGVDVPVI 80
Cdd:PRK13557  415 TETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDS-HPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVL 493
                          90       100       110
                  ....*....|....*....|....*....|
gi 2221781758  81 VQTGQGgiDTVVQamRAGA----FDFVVKP 106
Cdd:PRK13557  494 LTTGYA--EASIE--RTDAggseFDILNKP 519
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
5-106 5.73e-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: 39.10  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGKAGLELLKQYSGEInvVVLDLMMPEMDGLGFLKAVGELGvDVPVIVQTG 84
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADI--VLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTA 77
                          90       100
                  ....*....|....*....|...
gi 2221781758  85 QGG-IDTVVqAMRAGAFDFVVKP 106
Cdd:cd17621    78 KDSeIDKVV-GLELGADDYVTKP 99
HTH_50 pfam18024
Helix-turn-helix domain; The TyrR protein of Haemophilus influenzae is a 36-kD transcription ...
461-504 6.05e-04

Helix-turn-helix domain; The TyrR protein of Haemophilus influenzae is a 36-kD transcription factor whose major function is to control the expression of genes important in the biosynthesis and transport of aromatic amino acids. This entry represents the C-terminal helix-turn-helix DNA-binding domain of TyrR and related proteins.


Pssm-ID: 407862 [Multi-domain]  Cd Length: 50  Bit Score: 37.78  E-value: 6.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2221781758 461 KLAEIEEELIRFALRFYrGQMSQVARKLGIGRSTLYRKLKDYGI 504
Cdd:pfam18024   7 YVSYIERELIGAAYENY-KSARKVAKALGLSHTTIANKMKRYGI 49
PRK10360 PRK10360
transcriptional regulator UhpA;
5-119 4.41e-03

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 38.42  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221781758   5 VLVIDDDPVQRRLLKNAVERYGHLALLAENGkAGLELLKQYSGE-INVVVLDLMMPEMDGLGFLkavGELGVDVPVIVQT 83
Cdd:PRK10360    4 VALIDDHLIVRSGFAQLLGLEPDLQVVAEFG-SGREALAGLPGRgVQVCICDISMPDISGLELL---SQLPKGMATIMLS 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2221781758  84 GQGGIDTVVQAMRAGAFDFVVKPVSPERIGAAISNA 119
Cdd:PRK10360   80 VHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTV 115
HTH_7 pfam02796
Helix-turn-helix domain of resolvase;
460-501 9.67e-03

Helix-turn-helix domain of resolvase;


Pssm-ID: 397088 [Multi-domain]  Cd Length: 45  Bit Score: 34.25  E-value: 9.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2221781758 460 RKLAeIEEELIRFALRFYRGQMS--QVARKLGIGRSTLYRKLKD 501
Cdd:pfam02796   2 RPPK-LNEEDINEVITLLEEGISikQIAKIFGISRSTVYRYLAA 44
 
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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