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Conserved domains on  [gi|446047443|ref|WP_000125298|]
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MULTISPECIES: acetoacetate metabolism transcriptional regulator AtoC [Enterobacteriaceae]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 11485325)

sigma-54-dependent Fis family transcriptional regulator containing a REC domain, similar to Escherichia coli transcriptional regulators AtoC and NR(I), which function in the regulation of genes involved in acetoacetate metabolism and nitrogen assimilation, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-457 0e+00

acetoacetate metabolism transcriptional regulator AtoC;


:

Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 925.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVI 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEA 400
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEV 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446047443 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
 
Name Accession Description Interval E-value
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-457 0e+00

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 925.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVI 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEA 400
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEV 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446047443 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 6-455 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: 595.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQalstswqwghILTNSPAMMDICKDTAKIALS 165
Cdd:COG2204   84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKVAPS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
Cdd:COG2204  154 DATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
Cdd:COG2204  234 IGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPL 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 326 LANHFLQKFSSENQRDIIdIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPpqirqpvcnageaktapv 405
Cdd:COG2204  314 LARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP------------------ 374

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 446047443 406 gernlkEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYG 455
Cdd:COG2204  375 ------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
 7-453 2.34e-154

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: 446.11  E-value: 2.34e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQwghILTNSPAMMDICKDTAKIALSQ 166
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEAEDSAE---LIGEAPAMQEVFRAIGRLSRSD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEI 246
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  247 GEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI-------RQPVCNAGE 399
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELaltgrpaSAPDSDGQD 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446047443  400 AKTAPV----------GERNLKEEI-KRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQE 453
Cdd:TIGR01818 398 SWDEALeawakqalsrGEQGLLDRAlPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
42-457 1.11e-115

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 349.56  E-value: 1.11e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  42 HLFADI-----HPDVVL--MDIRMPEMDGIKALKEMRSNETRTPVILMTAYAE------------VETAVEALRCGAfDY 102
Cdd:NF038308  57 RVAADIeevspETEVRLvpVVLRDPWDFEEVYGALLDFARAYPFDTENEDYLVhittgthvaqicWFLLVEARYLPA-RL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 103 VIKPFDLDELN---LIVQRAL----QLQSMKKEIRHLHQALSTSWqwghILTNSPAMMDICKDTAKIAL-SQASVLISGE 174
Cdd:NF038308 136 LQTSPPRDKEEgtyEIIDLDLsrydALAQRFAREQAEAVSFLKSG----IATRNAAFNRLIEQIERVALrSRAPILLTGP 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 175 SGTGKELIARAIHYNSRRA---KGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGEMPL 251
Cdd:NF038308 212 TGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGL 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 252 VLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFL 331
Cdd:NF038308 292 DEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYEL 371

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 332 QKFSSENQRDI-----IDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI--------RQPVCNAG 398
Cdd:NF038308 372 DRFARELGRQVrfnkeARFRYLAFATSPEALWPGNFRELSASVTRMATLADGGRITEELVEEEIarlraawqSAPAAADD 451

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446047443 399 EAKTAPVGERNLKE--EIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRAL-----MYKLQEYGID 457
Cdd:NF038308 452 DALADLLGGEQLAEldLFDRVQLAAVLRVCRQSRSLSAAGRRLFGVSRQQKaspndADRLRKYLAR 517
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-311 7.81e-114

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 331.67  E-value: 7.81e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  145 ILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  225 AQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*..
gi 446047443  305 RLNVIHL 311
Cdd:pfam00158 161 RLNVIPI 167
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 7-121 1.82e-35

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: 127.45  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAF--ALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
resp_reg_YycF NF040534
response regulator YycF;
6-112 3.61e-18

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 83.23  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsNETRTPVILMTAY 85
Cdd:NF040534   2 KILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVR-KKYDMPIIMLTAK 80

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:NF040534  81 DSEIDKVLGLELGADDYVTKPFSTREL 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 6-59 4.16e-14

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: 66.44  E-value: 4.16e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446047443     6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMP 59
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-457 0e+00

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 925.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVI 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEA 400
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEV 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446047443 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 6-455 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: 595.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQalstswqwghILTNSPAMMDICKDTAKIALS 165
Cdd:COG2204   84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKVAPS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
Cdd:COG2204  154 DATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
Cdd:COG2204  234 IGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPL 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 326 LANHFLQKFSSENQRDIIdIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPpqirqpvcnageaktapv 405
Cdd:COG2204  314 LARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP------------------ 374

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 446047443 406 gernlkEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYG 455
Cdd:COG2204  375 ------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 115-457 0e+00

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: 513.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 115 IVQRALQLQSMKKEIR--HLHQALSTSWQWGHILTNSPAMMDIcKDTA-KIALSQASVLISGESGTGKELIARAIHYNSR 191
Cdd:COG3829  108 TFRDITELKRLERKLReeELERGLSAKYTFDDIIGKSPAMKEL-LELAkRVAKSDSTVLILGESGTGKELFARAIHNASP 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 192 RAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTL-RQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIG 270
Cdd:COG3829  187 RRDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 271 GHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAM 350
Cdd:COG3829  267 GTKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEAL 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 351 SLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPvcnagEAKTAPVGERNLKEEIKRVEKRIIMEVLEQQE 430
Cdd:COG3829  347 ELLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEE-----AEAASAAEEGSLKEALEEVEKELIEEALEKTG 421

                        330       340
                 ....*....|....*....|....*..
gi 446047443 431 GNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:COG3829  422 GNKSKAAKALGISRSTLYRKLKKYGIK 448
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
 7-453 2.34e-154

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: 446.11  E-value: 2.34e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQwghILTNSPAMMDICKDTAKIALSQ 166
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEAEDSAE---LIGEAPAMQEVFRAIGRLSRSD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEI 246
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  247 GEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI-------RQPVCNAGE 399
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELaltgrpaSAPDSDGQD 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446047443  400 AKTAPV----------GERNLKEEI-KRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQE 453
Cdd:TIGR01818 398 SWDEALeawakqalsrGEQGLLDRAlPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
7-451 1.06e-150

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 436.00  E-value: 1.06e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNlivqralqlQSMKKEIRHLHQA-----LSTSWQWGHIlTNSPAMMDICKDTAK 161
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQ---------ATLEKALAHTHSIdaetpAVTASQFGMV-GKSPAMQHLLSEIAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 162 IALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTL 241
Cdd:PRK10365 158 VAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 242 LLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRRE 321
Cdd:PRK10365 238 FLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRRE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 322 DISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI-RQPVCNAGEA 400
Cdd:PRK10365 318 DIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIaSTPIPLGQSQ 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446047443 401 KTAPVGErnlkeeikrVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKL 451
Cdd:PRK10365 398 DIQPLVE---------VEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 7-456 3.18e-143

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: 417.23  E-value: 3.18e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443    7 ILIVDDEDNVRRMLSTAFAlqGFETHCANNGRTALHLFADIHPDVVLMDIRMPE-----MDGIKALKEMRSNETRTPVIL 81
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPPdadgaSEGLAALQQILAIAPDTKVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGhILTNSPAMMDICKDTAK 161
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG-LITSSPGMQKICRTIEK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  162 IALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTL 241
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  242 LLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRRE 321
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  322 DISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQirqpvcnAGEAK 401
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLGLD-------ARERA 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446047443  402 TAPVgERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Cdd:TIGR02915 391 ETPL-EVNLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 7-457 1.06e-137

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 403.87  E-value: 1.06e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSwqwgHILTNSPAMMDICKDTAKIALSQ 166
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTT----DIIGEAPAMQDVFRIIGRLSRSS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEI 246
Cdd:PRK10923 162 ISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 247 GEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326
Cdd:PRK10923 242 GDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEAKTAP-- 404
Cdd:PRK10923 322 ARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQPds 401

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446047443 405 --------------VGERN-LKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK10923 402 watllaqwadralrSGHQNlLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
120-455 1.71e-127

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 383.10  E-value: 1.71e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 120 LQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIK 199
Cdd:COG3284  298 LRLRPARRAARAAPAGAPAPAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 200 VNCAALPESLLESELFGHEKGAFTGAQT-LRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVD 278
Cdd:COG3284  378 VNCAAIPEELIESELFGYEPGAFTGARRkGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVD 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 279 IRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDrREDISLLANHFLQKFSSEnqRDIIDIDPMAMSLLTAWSW 358
Cdd:COG3284  458 VRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRE-REDLPALIEHLLRELAAG--RGPLRLSPEALALLAAYPW 534

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 359 PGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEAKTAPVGernlkeEIKRVEKRIIMEVLEQQEGNRTRTAL 438
Cdd:COG3284  535 PGNVRELRNVLRTALALADGGVITVEDLPDELRAELAAAAPAAAAPLT------SLEEAERDAILRALRACGGNVSAAAR 608

                        330
                 ....*....|....*..
gi 446047443 439 MLGISRRALMYKLQEYG 455
Cdd:COG3284  609 ALGISRSTLYRKLKRYG 625
PRK15115 PRK15115
response regulator GlrR; Provisional
 6-460 3.14e-125

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 371.09  E-value: 3.14e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQlqsmkkeirhlHQALSTSWQW-GHILTNSPAMMDICKDTAKIAL 164
Cdd:PRK15115  87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALE-----------QSAPATDERWrEAIVTRSPLMLRLLEQARMVAQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLD 244
Cdd:PRK15115 156 SDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 245 EIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324
Cdd:PRK15115 236 EIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIP 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 325 LLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIfSEDLPPQIRQpvcnaGEAKTAP 404
Cdd:PRK15115 316 LLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVI-SDALVEQALE-----GENTALP 389

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446047443 405 --VGERNlkeeikRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGIDPAD 460
Cdd:PRK15115 390 tfVEARN------QFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDAND 441
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
 145-457 2.84e-124

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: 371.74  E-value: 2.84e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  145 ILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTG 224
Cdd:TIGR01817 198 IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTG 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  225 AQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFY 304
Cdd:TIGR01817 278 AIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYY 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  305 RLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDiIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSE 384
Cdd:TIGR01817 358 RINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRP-LTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRS 436

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  385 DL-------------PPQIRQPVCNAGEAKTAPVGERNLKEEIKRV--------EKRIIMEVLEQQEGNRTRTALMLGIS 443
Cdd:TIGR01817 437 DFscqsgqclspmlaKTCPHGHISIDPLAGTTPPHSPASAALPGEPglsgptlsERERLIAALEQAGWVQAKAARLLGMT 516

                         330
                  ....*....|....
gi 446047443  444 RRALMYKLQEYGID 457
Cdd:TIGR01817 517 PRQVGYALRKLNIE 530
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
94-444 2.50e-116

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 350.63  E-value: 2.50e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  94 ALRCGAFDyvikPFDLDELNLI-------VQRALQLQSMKKEIRHLHQALST----SWQWGHILTNSPAMMDICKDTAKI 162
Cdd:PRK05022 131 ALDPGQFD----AFSDEELRALaalaaatLRNALLIEQLESQAELPQDVAEFlrqeALKEGEMIGQSPAMQQLKKEIEVV 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 163 ALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLL 242
Cdd:PRK05022 207 AASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLF 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 243 LDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRRED 322
Cdd:PRK05022 287 LDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDD 366

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 323 ISLLANHFL----QKFSSENQRdiidIDPMAMSLLTAWSWPGNIRELSNVIERAVVM----NSGPIIFSE----DLPPQI 390
Cdd:PRK05022 367 VLLLAGYFLeqnrARLGLRSLR----LSPAAQAALLAYDWPGNVRELEHVISRAALLararGAGRIVTLEaqhlDLPAEV 442

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446047443 391 RQPVCNAGEAKTAPVGeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISR 444
Cdd:PRK05022 443 ALPPPEAAAAPAAVVS-QNLREATEAFQRQLIRQALAQHQGNWAAAARALELDR 495
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
42-457 1.11e-115

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 349.56  E-value: 1.11e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  42 HLFADI-----HPDVVL--MDIRMPEMDGIKALKEMRSNETRTPVILMTAYAE------------VETAVEALRCGAfDY 102
Cdd:NF038308  57 RVAADIeevspETEVRLvpVVLRDPWDFEEVYGALLDFARAYPFDTENEDYLVhittgthvaqicWFLLVEARYLPA-RL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 103 VIKPFDLDELN---LIVQRAL----QLQSMKKEIRHLHQALSTSWqwghILTNSPAMMDICKDTAKIAL-SQASVLISGE 174
Cdd:NF038308 136 LQTSPPRDKEEgtyEIIDLDLsrydALAQRFAREQAEAVSFLKSG----IATRNAAFNRLIEQIERVALrSRAPILLTGP 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 175 SGTGKELIARAIHYNSRRA---KGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGEMPL 251
Cdd:NF038308 212 TGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAADGGTLFLDEIGELGL 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 252 VLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFL 331
Cdd:NF038308 292 DEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGLRERREDIEPNLDYEL 371

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 332 QKFSSENQRDI-----IDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQI--------RQPVCNAG 398
Cdd:NF038308 372 DRFARELGRQVrfnkeARFRYLAFATSPEALWPGNFRELSASVTRMATLADGGRITEELVEEEIarlraawqSAPAAADD 451

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446047443 399 EAKTAPVGERNLKE--EIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRAL-----MYKLQEYGID 457
Cdd:NF038308 452 DALADLLGGEQLAEldLFDRVQLAAVLRVCRQSRSLSAAGRRLFGVSRQQKaspndADRLRKYLAR 517
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-311 7.81e-114

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 331.67  E-value: 7.81e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  145 ILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  225 AQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160


                  ....*..
gi 446047443  305 RLNVIHL 311
Cdd:pfam00158 161 RLNVIPI 167
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
 120-456 1.21e-111

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 338.70  E-value: 1.21e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 120 LQLQS---MKKEIRHLHQALSTSWqwGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGP 196
Cdd:COG3283  180 VTLKSaarLGEQLQALQVNDDSGF--DHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKP 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 197 FIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIK 276
Cdd:COG3283  258 FLALNCAALPDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVK 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 277 VDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAW 356
Cdd:COG3283  338 VDVRVICATQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSY 417

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 357 SWPGNIRELSNVIERAVVMNSGPIIFSEDlppqIRQPVCNAGEAKTAPVGERNLKEEIKRVEKriimEVLEQ--QEGNRT 434
Cdd:COG3283  418 PWPGNVRQLENALYRAVSLLEGDELTPED----LQLPEYAASAGLLDDLLEGSLDEIVKRFER----SLLRRlyPSYPST 489

                        330       340
                 ....*....|....*....|...
gi 446047443 435 RT-ALMLGISRRALMYKLQEYGI 456
Cdd:COG3283  490 RKlAKRLGVSHTAIANKLREYGI 512
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
 145-450 4.88e-104

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: 312.69  E-value: 4.88e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  145 ILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTG 224
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  225 AQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFY 304
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  305 RL--NVIHliLPPLRDRREDISLLANHFLQKFSSENQRDII-DIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGP-- 379
Cdd:TIGR02974 161 RLafDVIT--LPPLRERQEDIMLLAEHFAIRMARELGLPLFpGFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEea 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  380 ----IIF----SEDLPPQIRQPVCNAGEAKTAPVGER--------NLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGIS 443
Cdd:TIGR02974 239 pideIIIdpfaSPWRPKQAAPAVDEVNSTPTDLPSPSsiaaafplDLKQAQQDYEIELLQQALAEAQFNQRKAAELLGLT 318

                         330
                  ....*....|
gi 446047443  444 R---RALMYK 450
Cdd:TIGR02974 319 YhqlRGLLRK 328
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 165-457 1.01e-97

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: 297.14  E-value: 1.01e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESelfghekgaftgaqtlrqglferanegtllld 244
Cdd:COG3604  114 SLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 245 eigemplvlqakllriLQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDIS 324
Cdd:COG3604  162 ----------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIP 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 325 LLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRqpvcnageaktap 404
Cdd:COG3604  226 LLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSR------------- 292

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446047443 405 vgernlkEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:COG3604  293 -------EALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
 134-458 6.43e-97

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 301.64  E-value: 6.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 134 QALSTSWQWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIH--------YNSRRAKGPFIKVNCAAL 205
Cdd:PRK15424 210 NALRTRYVLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfarhdARQGKKSHPFVAVNCGAI 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 206 PESLLESELFGHEKGAFTGAQTL-RQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAA 284
Cdd:PRK15424 290 AESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISA 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 285 TNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQK--------FSSENQRDIIdidpMAMSLLTAW 356
Cdd:PRK15424 370 THCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQslaalsapFSAALRQGLQ----QCETLLLHY 445

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 357 SWPGNIRELSNVIER-AVVMNSGPiifSEDLPPQIRQPVcnAGEAKTAPVGERNLKEEIKRVEkriimEVLEQQEGNRTR 435
Cdd:PRK15424 446 DWPGNVRELRNLMERlALFLSVEP---TPDLTPQFLQLL--LPELARESAKTPAPRLLAATLQ-----QALERFNGDKTA 515

                        330       340
                 ....*....|....*....|...
gi 446047443 436 TALMLGISRRALMYKLQEYGIDP 458
Cdd:PRK15424 516 AANYLGISRTTLWRRLKAEAKAQ 538
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
141-457 3.68e-95

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 301.36  E-value: 3.68e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 141 QWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKG 220
Cdd:PRK15429 374 EFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERG 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 221 AFTGAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFRE 300
Cdd:PRK15429 454 AFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRS 533

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 301 DLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPI 380
Cdd:PRK15429 534 DLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNV 613

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 381 IfsedlppQIRQPVCNAGEAKTAPVGERNLKEeiKRVEKRIIMEVLEQQEG---NRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK15429 614 L-------QLSLPDITLPEPETPPAATVVAQE--GEDEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTLLSRMKRLGID 684
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
 135-452 5.64e-91

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: 285.99  E-value: 5.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  135 ALSTSWQWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESEL 214
Cdd:TIGR02329 204 QLRTRYRLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  215 FGHEKGAFTGAQTL-RQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMV 293
Cdd:TIGR02329 284 FGYEEGAFTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAV 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  294 KEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQrdiIDIDPMAM-------SLLTAWSWPGNIRELS 366
Cdd:TIGR02329 364 QQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALR---LPDSEAAAqvlagvaDPLQRYPWPGNVRELR 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  367 NVIERAVVMNSG---PIIFSEDL----PPQIRQpvcnAGEAKTAPVGERnlkeEIKRVEKRIIMEVLEQQEGNRTRTALM 439
Cdd:TIGR02329 441 NLVERLALELSAmpaGALTPDVLralaPELAEA----SGKGKTSALSLR----ERSRVEALAVRAALERFGGDRDAAAKA 512

                         330
                  ....*....|...
gi 446047443  440 LGISRRALMYKLQ 452
Cdd:TIGR02329 513 LGISRTTLWRRLK 525
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
 169-452 4.12e-88

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 271.93  E-value: 4.12e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEIGE 248
Cdd:PRK11608  32 VLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELAT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 249 MPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRL--NVIHliLPPLRDRREDISLL 326
Cdd:PRK11608 112 APMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLafDVVQ--LPPLRERQSDIMLM 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 327 ANHFLQKFSSENQRDIID-IDPMAMSLLTAWSWPGNIRELSNVIERAVVM---NSGP---II---FSEDLPPQIRQPVCN 396
Cdd:PRK11608 190 AEHFAIQMCRELGLPLFPgFTERARETLLNYRWPGNIRELKNVVERSVYRhgtSEYPldnIIidpFKRRPAEEAIAVSET 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446047443 397 aGEAKTAPVgerNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISR---RALMYKLQ 452
Cdd:PRK11608 270 -TSLPTLPL---DLREWQHQQEKELLQRSLQQAKFNQKRAAELLGLTYhqlRALLKKHQ 324
PRK10820 PRK10820
transcriptional regulator TyrR;
144-456 2.02e-84

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 268.86  E-value: 2.02e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 144 HILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFT 223
Cdd:PRK10820 205 QIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYP 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 224 GAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLF 303
Cdd:PRK10820 285 NALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLY 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 304 YRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPiifs 383
Cdd:PRK10820 365 YRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGY---- 440

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446047443 384 eDLPPQ-IRQPVCNAGEAKTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRtRTALMLGISRRALMYKLQEYGI 456
Cdd:PRK10820 441 -ELRPQdILLPDYDAAVAVGEDAMEGSLDEITSRFERSVLTRLYRNYPSTR-KLAKRLGVSHTAIANKLREYGL 512
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 127-460 2.49e-67

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 226.87  E-value: 2.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 127 KEIRHL--HQALSTSWQWGHILTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAA 204
Cdd:PRK11388 307 EQMRQLmtSQLGKVSHTFDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQL 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 205 LPESLLESELFGhekGAFTGAQTLRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAA 284
Cdd:PRK11388 387 YPDEALAEEFLG---SDRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIAT 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 285 TNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLLANHFLQKFSSENQRDiIDIDPMAMSLLTAWSWPGNIRE 364
Cdd:PRK11388 464 TTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTR-LKIDDDALARLVSYRWPGNDFE 542

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 365 LSNVIERAVVMNSGPIIFSEDLPPQIRQPvcNAGEAKTAPVGERNLKeeIKRVEKRIIMEVLEQQEGNRTRTALMLGISR 444
Cdd:PRK11388 543 LRSVIENLALSSDNGRIRLSDLPEHLFTE--QATDDVSATRLSTSLS--LAELEKEAIINAAQVCGGRIQEMAALLGIGR 618

                        330
                 ....*....|....*.
gi 446047443 445 RALMYKLQEYGIDPAD 460
Cdd:PRK11388 619 TTLWRKMKQHGIDAGQ 634
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
 161-371 9.66e-53

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: 185.42  E-value: 9.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 161 KIAL-SQASVLISGESGTGKELIARAIhYNSRRA----KGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFER 235
Cdd:COG4650  202 RVAIrSRAPILLTGPTGAGKSQLARRI-YELKKArhqvSGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRS 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 236 ANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPP 315
Cdd:COG4650  281 ADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPG 360

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446047443 316 LRDRREDISLLANHFLQKFSSENQRDI-IDIDPMAMSLLTA----WSWPGNIRELSNVIER 371
Cdd:COG4650  361 LAERREDIEPNLDYELARFAREQGRRVrFNKEARARYLAFAtspeALWSGNFRDLNASVTR 421
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
 5-120 1.17e-39

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: 138.77  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA 84
Cdd:COG5803    3 KKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTA 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:COG5803   83 YGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 6-121 2.16e-37

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: 135.47  E-value: 2.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTAR 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:COG0745   83 DDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 6-124 2.45e-37

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: 133.05  E-value: 2.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILMT 83
Cdd:COG0784    7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRlpDIPIIALT 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQS 124
Cdd:COG0784   87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 6-136 1.25e-35

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: 131.44  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILMT 83
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIPVIFLT 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQAL 136
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYL 140
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 7-121 1.82e-35

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: 127.45  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAF--ALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 6-112 5.33e-35

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: 128.49  E-value: 5.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILMT 83
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRtaDIPIIFLT 82

                         90       100
                 ....*....|....*....|....*....
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:COG3706   83 ALDDEEDRARALEAGADDYLTKPFDPEEL 111
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 6-106 1.18e-34

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: 124.89  E-value: 1.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAF-ALQGFET-HCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILeWEAGFEVvGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80

                         90       100
                 ....*....|....*....|...
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKP 106
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLKP 103
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 8-106 1.24e-34

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: 124.65  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   8 LIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYAE 87
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80

                         90
                 ....*....|....*....
gi 446047443  88 VETAVEALRCGAFDYVIKP 106
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 7-121 3.69e-33

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: 121.06  E-value: 3.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 7-136 8.14e-33

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: 120.67  E-value: 8.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQAL 136
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 8-106 1.14e-32

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: 119.43  E-value: 1.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   8 LIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYAE 87
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                         90
                 ....*....|....*....
gi 446047443  88 VETAVEALRCGAFDYVIKP 106
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 7-112 2.88e-32

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: 118.79  E-value: 2.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100
                  ....*....|....*....|....*.
gi 446047443   87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDEL 106
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 6-128 3.41e-32

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 119.30  E-value: 3.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFA-LQGFET-HCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:COG4565    5 RVLIVEDDPMVAELLRRYLErLPGFEVvGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVIT 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKE 128
Cdd:COG4565   85 AARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 5-120 1.78e-31

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: 116.60  E-value: 1.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA 84
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 7-127 2.11e-31

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: 116.53  E-value: 2.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKK 127
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 7-141 2.19e-29

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 113.66  E-value: 2.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQ 141
Cdd:COG4566   82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLA 136
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 6-119 2.75e-29

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: 110.77  E-value: 2.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446047443  86 AEVETAVEALRCGAfdYVIKPFDLDELNLIVQRA 119
Cdd:cd17554   82 SEYKSDFSSWAADA--YVVKSSDLTELKETIKRL 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 6-119 2.86e-29

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: 110.75  E-value: 2.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446047443  86 AEVETAVEALRCGAFDYVIKPF-DLDELNLIVQRA 119
Cdd:cd17555   82 GVMSDAVEALRLGAWDYLTKPIeDLAVLEHAVRRA 116
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 169-392 3.78e-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: 120.98  E-value: 3.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIH----YNSRRAKG-PFIKVNCAAL---PEsLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
Cdd:COG1221  133 TLILGPTGVGKSFFAELMYeyaiEIGVLPEDaPFVVFNCADYannPQ-LLMSQLFGYVKGAFTGADKDKEGLIEKADGGI 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 241 LLLDEIGEMPLVLQAKLLRILQEREFERIG-GHQTIKVDIRIIAATNRDLQ-AMVKegTFREdlfyRLNVIhlI-LPPLR 317
Cdd:COG1221  212 LFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPEsSLLK--TFLR----RIPMV--IkLPSLE 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 318 DR--REDISLLaNHFLQKFSSENQRDIIdIDPMAMSLLTAWSWPGNIRELSNVIE----RA----VVMNSGPI-IFSEDL 386
Cdd:COG1221  284 ERslEERLELI-KHFFKEEAKRLNKPIK-VSKEVLKALLLYDCPGNIGQLKSDIQlacaKAflnyITNKKEEIeITLSDL 361


                 ....*.
gi 446047443 387 PPQIRQ 392
Cdd:COG1221  362 PENVKK 367
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 6-128 8.25e-28

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 110.68  E-value: 8.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLstAFALQGFETH----CANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVIL 81
Cdd:COG3279    3 KILIVDDEPLARERL--ERLLEKYPDLevvgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446047443  82 MTAYAEVetAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKE 128
Cdd:COG3279   81 TTAYDEY--ALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAA 125
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 6-112 1.76e-27

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: 105.90  E-value: 1.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17615   81 DSVEDRIAGLTAGGDDYVTKPFSLEEV 107
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 1-112 6.38e-27

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: 106.54  E-value: 6.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVI 80
Cdd:COG4567    1 SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:COG4567   81 VLTGYASIATAVEAIKLGADDYLAKPADADDL 112
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 7-120 1.62e-25

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: 100.54  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELnLIVQRAL 120
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEEL-LARVRAL 113
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 7-112 2.11e-25

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: 100.24  E-value: 2.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET---RTPVILMT 83
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGggrRTPIIALT 80

                         90       100
                 ....*....|....*....|....*....
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQL 109
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 6-138 2.44e-25

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: 102.73  E-value: 2.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMrSNETRTPVILMTA 84
Cdd:COG3707    5 RVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI-SEERPAPVILLTA 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDEL----NLIVQRALQLQSMKKEIRHLHQALST 138
Cdd:COG3707   84 YSDPELIERALEAGVSAYLVKPLDPEDLlpalELALARFRELRALRRELAKLREALEE 141
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 165-312 1.13e-24

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 99.53  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 165 SQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEkgaftgAQTLRQGLFERANEGTLLLD 244
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLLFELAEKAKPGVLFID 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446047443 245 EIGEMPLVLQAKLLRILQEREFERIgghqtIKVDIRIIAATNRDLqamvkEGTFREDLFYRLNVIHLI 312
Cdd:cd00009   92 EIDSLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPL-----LGDLDRALYDRLDIRIVI 149
orf27 CHL00148
Ycf27; Reviewed
 6-112 1.97e-24

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 101.33  E-value: 1.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAY 85
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK-ESDVPIIMLTAL 86

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:CHL00148  87 GDVSDRITGLELGADDYVVKPFSPKEL 113
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 6-112 2.45e-24

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: 97.13  E-value: 2.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFA-LQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDG---IKALKEMRSNETrTPVIL 81
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRsAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGlefIRRLRALPGLED-VPIVM 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446047443  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFDPVEL 111
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 7-112 2.60e-24

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: 97.14  E-value: 2.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILMTA 84
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80

                         90       100
                 ....*....|....*....|....*....
gi 446047443  85 YAEVETAVEALRCGaFD-YVIKPFDLDEL 112
Cdd:cd17580   81 YGQPEDRERALEAG-FDaHLVKPVDPDEL 108
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 5-120 2.65e-24

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: 97.35  E-value: 2.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHC-ANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 6-121 3.10e-24

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 97.09  E-value: 3.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGY 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446047443  86 AEVETAVEAL-RCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd17569   82 ADLDAAIEAInEGEIYRFLTKPWDDEELKETIRQALE 118
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 7-107 3.29e-24

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: 96.43  E-value: 3.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE-TR-TPVILMTA 84
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPaTRhIPVIFLTA 80

                         90       100
                 ....*....|....*....|...
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPF 107
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 6-121 4.77e-24

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: 96.47  E-value: 4.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd17553   82 GELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 8-112 6.60e-24

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: 96.14  E-value: 6.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   8 LIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYAE 87
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80

                         90       100
                 ....*....|....*....|....*
gi 446047443  88 VETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAEL 105
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 7-112 6.90e-24

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: 96.01  E-value: 6.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEEL 106
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 5-112 1.81e-23

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: 94.82  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA 84
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80

                         90       100
                 ....*....|....*....|....*...
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17563   81 YASIATAVEAIKLGADDYLAKPADADEI 108
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 7-112 2.01e-23

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: 94.89  E-value: 2.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVR----RMLSTAFALQGFEThcANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILM 82
Cdd:cd17535    1 VLIVDDHPLVReglrRLLESEPDIEVVGE--AADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVL 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 6-114 3.01e-23

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: 94.38  E-value: 3.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQ-GFE---ThcANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKE-MRsnETRTPVI 80
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDpDIEvvgT--ARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRiMA--ERPTPVV 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446047443  81 LMTAYAE--VETAVEALRCGAFDYVIKPFDLDELNL 114
Cdd:cd17541   78 MVSSLTEegAEITLEALELGAVDFIAKPSGGISLDL 113
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 7-106 3.19e-23

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: 93.38  E-value: 3.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNeTRTPVILMTAYA 86
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW-SAVPVIVLSARD 79

                         90       100
                 ....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKP 106
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 7-120 6.75e-23

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: 93.43  E-value: 6.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 6-107 7.22e-23

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: 92.56  E-value: 7.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSN-ETRT-PVILMT 83
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDpETRHiPVIMIT 80

                         90       100
                 ....*....|....*....|....
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPF 107
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 5-112 1.24e-22

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: 92.70  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE--TRTPVILM 82
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEmtRDIPIIML 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPREL 110
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 6-120 6.98e-22

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: 90.54  E-value: 6.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMP-EMDGIKALKEMRSNeTRTPVILMT 83
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK-FDIPVIFLT 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd17534   81 AYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 6-112 2.09e-21

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: 89.23  E-value: 2.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLsTAF--ALQGFET-HCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILM 82
Cdd:cd19925    2 NVLIVEDDPMVAEIH-RAYveQVPGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19925   81 TAANDVETVREALRLGVVDYLIKPFTFERL 110
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 8-120 2.24e-21

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: 88.87  E-value: 2.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   8 LIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE--TRTPVILMTAY 85
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPktSSIPIIMLTAK 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
146-316 3.60e-21

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 89.32  E-value: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  146 LTNSPAMMDICKDTAKIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESelfghekgaftga 225
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  226 qtlrqglferANEGTLLLDEIGEMPLVLQAKLLRILQEREferigghqtiKVDIRIIAATNRDLQAMVKEGTFREDLFYR 305
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127

                         170
                  ....*....|.
gi 446047443  306 LNVIHLILPPL 316
Cdd:pfam14532 128 LSALRLHVPPL 138
fixJ PRK09390
response regulator FixJ; Provisional
 9-121 6.28e-21

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 90.45  E-value: 6.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   9 IVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYAEV 88
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDV 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  89 ETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:PRK09390  88 PLAVEAMKLGAVDFIEKPFEDERLIGAIERALA 120
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 7-112 1.44e-20

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: 86.71  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsNETRTPVILMTAYA 86
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR-KTSNVPIIMLTAKD 79

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKPFSNREL 105
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
 1-122 3.09e-20

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: 89.86  E-value: 3.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAInRILIVDDEDNVRRMLSTAFALQG-FE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSN--ETR 76
Cdd:COG5801    2 MEKI-KVLIADDNREFCELLEEYLSSQPdMEvVGVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMnlEKR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446047443  77 TPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELnliVQRALQL 122
Cdd:COG5801   81 PKVIMLTAFGQEDITQRAVELGADYYILKPFDLDVL---AERIRQL 123
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 6-112 3.57e-20

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: 85.54  E-value: 3.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHC-ANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETrTPVILMTA 84
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVLLTA 80

                         90       100
                 ....*....|....*....|....*...
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19932   81 YSQQDLVERAKEAGAMAYLVKPFSESDL 108
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 6-112 3.60e-20

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: 85.60  E-value: 3.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAY 85
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTAK 80

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17626   81 SDTVDVVLGLESGADDYVAKPFKPKEL 107
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 7-106 3.75e-20

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: 85.18  E-value: 3.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLfADIHP-DVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHL-ALTNEyDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTAR 79

                         90       100
                 ....*....|....*....|.
gi 446047443  86 AEVETAVEALRCGAFDYVIKP 106
Cdd:cd19935   80 DSVEDRVKGLDLGADDYLVKP 100
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 6-118 1.48e-19

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: 83.74  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILMT 83
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPAtrDIPVIALT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 7-106 1.82e-19

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: 82.97  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80

                         90       100
                 ....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKP 106
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 7-112 1.83e-19

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: 83.87  E-value: 1.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEEL 106
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 7-112 1.88e-19

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 83.51  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAYA 86
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTARG 79

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFNPREL 105
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 6-118 2.75e-19

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: 83.62  E-value: 2.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGF--ETHCANNGRTALHL------FADI-HPDVVLMDIRMPEMDGIKALKEMRSNET- 75
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVRDGEEALDFlrgegeYADApRPDLILLDLNMPRMDGFEVLREIKADPDl 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446047443  76 -RTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
Cdd:cd17557   81 rRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 6-121 1.27e-18

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: 81.44  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMlsTAFALQ---GFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSN-ETRT-PVI 80
Cdd:cd17552    3 RILVIDDEEDIREV--VQACLEklaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANpETQSiPVI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd17552   81 LLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
pleD PRK09581
response regulator PleD; Reviewed
 1-130 3.49e-18

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 86.49  E-value: 3.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAinRILIVDD-EDNVRrMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRT-- 77
Cdd:PRK09581   1 MTA--RILVVDDiPANVK-LLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATThi 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446047443  78 PVILMTAYAEVETAVEALRCGAFDYVIKPfdLDELNLIVQ-RAL-QLQSMKKEIR 130
Cdd:PRK09581  78 PVVMVTALDDPEDRVRGLEAGADDFLTKP--INDVALFARvKSLtRLKMVIDELR 130
resp_reg_YycF NF040534
response regulator YycF;
6-112 3.61e-18

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 83.23  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsNETRTPVILMTAY 85
Cdd:NF040534   2 KILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVR-KKYDMPIIMLTAK 80

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:NF040534  81 DSEIDKVLGLELGADDYVTKPFSTREL 107
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-118 3.82e-18

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 85.59  E-value: 3.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAInRILIVDDEDNVRRMLSTAFalqgfETH-------CANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKE-MRs 72
Cdd:PRK00742   1 MMKI-RVLVVDDSAFMRRLISEIL-----NSDpdievvgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKiMR- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446047443  73 nETRTPVILMTAYAE--VETAVEALRCGAFDYVIKPF-----DLDEL-NLIVQR 118
Cdd:PRK00742  74 -LRPTPVVMVSSLTErgAEITLRALELGAVDFVTKPFlgislGMDEYkEELAEK 126
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 6-112 8.66e-18

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: 78.97  E-value: 8.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAY 85
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE-QSEVGIILVTGR 80

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17619   81 DDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 7-108 8.83e-18

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: 78.91  E-value: 8.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDG------IKALKEMRSnetrTPVI 80
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGyelcrkIKSDPDLKD----IPVI 76

                         90       100
                 ....*....|....*....|....*...
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFD 108
Cdd:cd17598   77 LLTTLSDPRDVIRGLECGADNFITKPYD 104
PRK15479 PRK15479
transcriptional regulator TctD;
6-125 1.57e-17

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 81.31  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVqRALQLQSM 125
Cdd:PRK15479  82 SAVADRVKGLNVGADDYLPKPFELEELDARL-RALLRRSA 120
PRK10643 PRK10643
two-component system response regulator PmrA;
6-142 1.64e-17

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 81.24  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVqRALqlqsmkkeIRHlHQALSTSWQW 142
Cdd:PRK10643  82 DTLEDRVAGLDVGADDYLVKPFALEELHARI-RAL--------IRR-HQGQGENELQ 128
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 6-112 1.86e-17

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: 78.15  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILM 82
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGAlsHLPVLMV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
4-112 7.64e-17

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 79.46  E-value: 7.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   4 INRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFaDIHPDVVLMDIRMPEMDGIKALKEMRSNEtRTPVILMT 83
Cdd:PRK10955   1 MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLT 78

                         90       100
                 ....*....|....*....|....*....
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDREL 107
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
 6-122 8.15e-17

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 80.22  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443    6 RILIVDDEDNVRRMLSTAFALQG--FETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTP--VIL 81
Cdd:TIGR02875   4 RIVIADDNKEFCNLLKEYLAAQPdmEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARprVIM 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446047443   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELnliVQRALQL 122
Cdd:TIGR02875  84 LSAFGQEKITQRAVALGADYYVLKPFDLEIL---AARIRQL 121
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 7-120 9.60e-17

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 75.74  E-value: 9.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADiHP---DVVLMDIRMPEMDGIKALKEMRSnETRTPVILMT 83
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRE-NKdefDLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMS 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd17584   79 ADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 6-120 1.66e-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: 75.41  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILMT 83
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILMLT 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 7-122 1.73e-16

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: 75.27  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDE----DNVRRMLSTAFALQGFEThcANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILM 82
Cdd:cd17532    1 ALIVDDEplarEELRYLLEEHPDIEIVGE--AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446047443  83 TAYAEVetAVEALRCGAFDYVIKPFDLDELNLIVQRALQL 122
Cdd:cd17532   79 TAYDEY--AVEAFELNAVDYLLKPFSEERLAEALAKLRKR 116
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 7-106 2.87e-16

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: 74.02  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAYA 86
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQ-KSTLPVIFLTSKD 79

                         90       100
                 ....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKP 106
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 6-107 6.23e-16

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: 73.41  E-value: 6.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQ-GFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSN--ETRTPVIL 81
Cdd:cd17561    3 KVLIADDNREFVQLLEEYLNSQpDMEvVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMrlEKRPKIIM 82

                         90       100
                 ....*....|....*....|....*.
gi 446047443  82 MTAYAEVETAVEALRCGAFDYVIKPF 107
Cdd:cd17561   83 LTAFGQEDITQRAVELGASYYILKPF 108
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 6-112 1.36e-15

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: 72.94  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADiHPDV--VLMDIRMPEMDGIKALKEMRSNETRT--PVIL 81
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQ-HPDIklVITDYNMPEMDGFELVREIRKKYSRDqlAIIG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446047443  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17544   81 ISASGDNALSARFIKAGANDFLTKPFLPEEF 111
PRK10693 PRK10693
two-component system response regulator RssB;
32-112 1.62e-15

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 76.95  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  32 HCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYAEVETAVEALRCGAFDYVIKPF-DLD 110
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVkDLN 80


                 ..
gi 446047443 111 EL 112
Cdd:PRK10693  81 RL 82
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 6-112 1.87e-15

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 75.35  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAEL 108
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 6-138 2.51e-15

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: 72.40  E-value: 2.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFAlQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446047443  86 AEVETAVEALR-CGAFDYVIKPFDLDELNLIVQRALQLQSMKKEirhlHQALST 138
Cdd:cd17596   81 TDSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAARLFELQRE----NERLSL 130
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 7-120 2.92e-15

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: 71.54  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETrTPVILMTAYA 86
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 6-107 3.27e-15

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 71.38  E-value: 3.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLF---ADIhpDVVLMDIRMPEMDGIKALKEMRSNETRTPVILM 82
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqqgKDI--DIVVTDIVMPEMDGIELAREARKIDPDVKILFI 78

                         90       100
                 ....*....|....*....|....*
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKPF 107
Cdd:cd18160   79 SGGAAAAPELLSDAVGDNATLKKPF 103
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 6-112 8.53e-15

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: 70.48  E-value: 8.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAY 85
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR-FSDVPIIMVTAR 79

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19938   80 VEEIDRLLGLELGADDYICKPYSPREV 106
PRK10816 PRK10816
two-component system response regulator PhoP;
6-117 1.00e-14

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 73.23  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQ 117
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 7-112 1.15e-14

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: 70.13  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 6-152 1.23e-14

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 73.07  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA- 84
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTAr 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446047443  85 YAEVETAVeALRCGAFDYVIKPFDLDELNLIVqRALqLQSMKKeirhlHQALSTSWQWGHILTNSPAM 152
Cdd:PRK11083  85 SDEVDRLV-GLEIGADDYVAKPFSPREVAARV-RTI-LRRVKK-----FAAPSPVIRIGHFELDEPAA 144
PRK10336 PRK10336
two-component system response regulator QseB;
6-131 1.43e-14

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 72.62  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDE----LNLIVQRALQLQSmkKEIRH 131
Cdd:PRK10336  82 DALAERVEGLRLGADDYLCKPFALIEvaarLEALMRRTNGQAS--NELRH 129
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-106 1.92e-14

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 74.15  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQgfETH----CANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKE-MRsnETRTPVI 80
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARD--PDHevvwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRiMA--ERPCPIL 77

                         90       100
                 ....*....|....*....|....*...
gi 446047443  81 LMTAYAE--VETAVEALRCGAFDYVIKP 106
Cdd:PRK12555  78 IVTSLTErnASRVFEAMGAGALDAVDTP 105
PRK11517 PRK11517
DNA-binding response regulator HprR;
6-138 2.23e-14

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 72.24  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNEtRTPVILMTAY 85
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK-QTPVICLTAR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDELnlivqralqLQSMKKEIRHLHQALST 138
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVKPFSFSEL---------LARVRAQLRQHHALNST 124
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 7-106 2.44e-14

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 68.56  E-value: 2.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSN-ETRT-PVILMTA 84
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNaDFDTiPVIFLTA 80

                         90       100
                 ....*....|....*....|..
gi 446047443  85 YAEVETAVEALRCGAFDYVIKP 106
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
ompR PRK09468
osmolarity response regulator; Provisional
 5-112 2.92e-14

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 72.31  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA 84
Cdd:PRK09468   6 YKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTA 85

                         90       100
                 ....*....|....*....|....*...
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK09468  86 KGEEVDRIVGLEIGADDYLPKPFNPREL 113
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 6-59 4.16e-14

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: 66.44  E-value: 4.16e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446047443     6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMP 59
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 6-112 4.72e-14

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 68.17  E-value: 4.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsNETRTPVILMTAY 85
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR-EHSHVPILMLTAR 79

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCKPFSPREL 106
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 6-113 1.07e-13

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: 67.18  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAF-ALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA 84
Cdd:cd17593    2 KVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446047443  85 YAEVEtAVEalRC---GAFDYVIKPFDLDELN 113
Cdd:cd17593   82 DVQPE-AKE--RVlelGALAFLKKPFDPEKLA 110
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 6-70 1.89e-13

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: 67.22  E-value: 1.89e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQ-GFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEM 70
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEpDIEvVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 7-112 2.42e-13

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: 66.30  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVL 106
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 7-106 2.73e-13

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: 65.86  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI---------HPDVVLMDIRMPEMDGIKALKEMRSNE--T 75
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPrlA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446047443  76 RTPVILMTAYAEVETAVEALRCGAFDYVIKP 106
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 168-288 4.90e-13

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: 66.63  E-value: 4.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   168 SVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLES---ELFGHEKGAFTGAQTLRQgLFERANE---GTL 241
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRL-ALALARKlkpDVL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 446047443   242 LLDEIGEMPLVLQAKLLRILqerEFERIGGHQTIKVDIRIIAATNRD 288
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLL---EELRLLLLLKSEKNLTVILTTNDE 126
dpiA PRK10046
two-component response regulator DpiA; Provisional
 1-125 4.95e-13

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 68.12  E-value: 4.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAINRILIVDDEDNVRRMLSTAFA-LQGF-ETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsnETRTP 78
Cdd:PRK10046   1 MTAPLTLLIVEDETPLAEMHAEYIRhIPGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELV--QAHYP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446047443  79 --VILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSM 125
Cdd:PRK10046  79 gdVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHM 127
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 5-124 5.85e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 67.91  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsNETRTPVILMTA 84
Cdd:PRK10529   2 TNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR-QWSAIPVIVLSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQS 124
Cdd:PRK10529  81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHS 120
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 7-106 5.99e-13

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 64.53  E-value: 5.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAYA 86
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA-RSNVPVIMVTAKD 79

                         90       100
                 ....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKP 106
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 7-106 6.07e-13

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: 64.83  E-value: 6.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80

                         90       100
                 ....*....|....*....|
gi 446047443  87 EVETAVEALRCGAFDYVIKP 106
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
PRK10766 PRK10766
two-component system response regulator TorR;
6-112 9.96e-13

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 67.37  E-value: 9.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETrTPVILMTAY 85
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRST-VGIILVTGR 82

                         90       100
                 ....*....|....*....|....*..
gi 446047443  86 AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK10766  83 TDSIDRIVGLEMGADDYVTKPLELREL 109
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
6-112 1.18e-12

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 67.44  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEM-RSNETR-TPVILMT 83
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLkRESMTRdIPVVMLT 83

                         90       100
                 ....*....|....*....|....*....
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKEL 112
PRK10610 PRK10610
chemotaxis protein CheY;
6-107 1.84e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 64.23  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFET-HCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE--TRTPVILM 82
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGFNNvEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLMV 86

                         90       100
                 ....*....|....*....|....*
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKPF 107
Cdd:PRK10610  87 TAEAKKENIIAAAQAGASGYVVKPF 111
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
7-132 2.48e-12

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 69.38  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446047443   87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHL 132
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHL 1086
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 7-106 3.61e-12

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: 62.42  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI--HPDVVLMDIRMPEMDGIKALKEMRSNET--RTPVILM 82
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEqnEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMM 80

                         90       100
                 ....*....|....*....|....
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKP 106
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
PRK15347 PRK15347
two component system sensor kinase;
6-123 8.21e-12

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 67.74  E-value: 8.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVR----RMLSTafalQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE----TRT 77
Cdd:PRK15347 692 QILLVDDVETNRdiigMMLVE----LGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPnnldPDC 767

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446047443  78 PVILMTAYA---EVETAVEAlrcGAFDYVIKPFDLDELNLIVQRALQLQ 123
Cdd:PRK15347 768 MIVALTANAapeEIHRCKKA---GMNHYLTKPVTLAQLARALELAAEYQ 813
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 5-108 1.13e-11

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 61.63  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTA 84
Cdd:cd17622    1 TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP-KYQGPILLLTA 79

                         90       100
                 ....*....|....*....|....
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFD 108
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVE 103
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 6-112 2.97e-11

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 60.88  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDE----DNVRRMLSTAfalQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSN-ETR-TPV 79
Cdd:cd17575    2 MVLLVDDQaiigEAVRRALADE---EDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANpATRdIPI 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17575   79 IVLSTKEEPEVKSEAFALGANDYLVKLPDKIEL 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 7-107 4.74e-11

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 59.28  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTAL-HLFADIHPDVVLMDIRMP-EMDGIKALKEMRSNETRTPVILMTA 84
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALdLLESGPDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80

                         90       100
                 ....*....|....*....|...
gi 446047443  85 YAEVETAVEALRCGaFDYVIKPF 107
Cdd:cd18161   81 YAENAIEGGDLAPG-VDVLSKPF 102
PRK11173 PRK11173
two-component response regulator; Provisional
 6-140 5.13e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 62.73  E-value: 5.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNeTRTPVILMTAY 85
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ-ANVALMFLTGR 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446047443  86 -AEVETaVEALRCGAFDYVIKPFDLDEL-----NLIvQRALQLQSMKKEIRHLHQALSTSW 140
Cdd:PRK11173  84 dNEVDK-ILGLEIGADDYITKPFNPRELtirarNLL-SRTMNLGTVSEERRSVESYKFNGW 142
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 7-112 5.60e-11

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 59.38  E-value: 5.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSnETRTPVILMTAYA 86
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA-RSDVPIIIISGDR 80

                         90       100
                 ....*....|....*....|....*..
gi 446047443  87 EVETA-VEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17594   81 RDEIDrVVGLELGADDYLAKPFGLREL 107
PRK13557 PRK13557
histidine kinase; Provisional
 6-120 1.44e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 63.15  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFAD-IHPDVVLMDIRMP-EMDGIKALKEMRSNETRTPVILMT 83
Cdd:PRK13557 417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDShPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTT 496

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446047443  84 AYAevETAVEalRCGA----FDYVIKPFDLDELNLIVQRAL 120
Cdd:PRK13557 497 GYA--EASIE--RTDAggseFDILNKPYRRAELARRVRMVL 533
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 7-112 2.13e-10

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: 58.05  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQG--FETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTA 84
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80

                         90       100
                 ....*....|....*....|....*...
gi 446047443  85 YAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEEL 108
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
 2-107 2.27e-10

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 60.85  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   2 TAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNeTRTPVIL 81
Cdd:PRK10710   8 ENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF-SDIPIVM 86

                         90       100
                 ....*....|....*....|....*.
gi 446047443  82 MTAYAEVETAVEALRCGAFDYVIKPF 107
Cdd:PRK10710  87 VTAKIEEIDRLLGLEIGADDYICKPY 112
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
414-453 2.48e-10

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 55.48  E-value: 2.48e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 446047443  414 IKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQE 453
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 7-121 4.30e-10

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: 56.97  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDE----DNVRRMLSTA--FALQGFethcANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVI 80
Cdd:cd19931    1 VLLIDDHpllrKGIKQLIELDpdFTVVGE----ASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
Cdd:cd19931   77 ILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
PRK11697 PRK11697
two-component system response regulator BtsR;
6-118 4.39e-10

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 59.86  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDE----DNVRRMLSTAfalQGFET--HCANngrtALHLFADIH---PDVVLMDIRMPEMDGIKALKeMRSNETR 76
Cdd:PRK11697   3 KVLIVDDEplarEELRELLQEE---GDIEIvgECSN----AIEAIGAIHrlkPDVVFLDIQMPRISGLELVG-MLDPEHM 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446047443  77 TPVILMTAYAEVetAVEALRCGAFDYVIKPFDLDELNLIVQR 118
Cdd:PRK11697  75 PYIVFVTAFDEY--AIKAFEEHAFDYLLKPIDPARLAKTLAR 114
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 30-108 4.50e-10

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 62.17  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  30 ETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMR--SNETRTPVILMTAYAEVETAVEALRCGAFDYVIKPF 107
Cdd:PRK11107 693 HVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRqlPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPI 772


                 .
gi 446047443 108 D 108
Cdd:PRK11107 773 D 773
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
6-112 4.67e-10

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 61.91  E-value: 4.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAY 85
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTAN 882

                         90       100       110
                 ....*....|....*....|....*....|
gi 446047443  86 AEVEtavEALRC---GAFDYVIKPFDLDEL 112
Cdd:PRK10841 883 ALAE---EKQRCleaGMDSCLSKPVTLDVL 909
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 6-119 5.46e-10

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 59.27  E-value: 5.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDE----DNVRRMLSTAFALQGFEThcANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVIL 81
Cdd:PRK10651   8 TILLIDDHpmlrTGVKQLISMAPDITVVGE--ASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVV 85

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446047443  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRA 119
Cdd:PRK10651  86 FSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQA 123
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 7-106 1.42e-09

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: 55.07  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMR-SNETR-TPVILMTA 84
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRkSSALKdTPIIMLTG 80

                         90       100
                 ....*....|....*....|..
gi 446047443  85 YAEVETAVEALRCGAFDYVIKP 106
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 5-112 1.84e-09

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: 55.53  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFA-LQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEdLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446047443  84 AY-----AEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17530   81 GLdggilESAETLAGANGLNLLGTLSKPFSPEEL 114
PRK15369 PRK15369
two component system response regulator;
6-105 1.98e-09

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 57.40  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDE----DNVRRMLST--AFALQGFethcANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPV 79
Cdd:PRK15369   5 KILLVDDHeliiNGIKNMLAPypRYKIVGQ----VDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI 80

                         90       100
                 ....*....|....*....|....*.
gi 446047443  80 ILMTAYAEVETAVEALRCGAFDYVIK 105
Cdd:PRK15369  81 LVLTARQEEHMASRTLAAGALGYVLK 106
PRK10430 PRK10430
two-component system response regulator DcuR;
4-107 1.60e-08

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 55.11  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   4 INrILIVDDEDNV----RRMLSTafaLQGFetHCANNGRT-----ALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE 74
Cdd:PRK10430   2 IN-VLIVDDDAMVaelnRRYVAQ---IPGF--QCCGTASTleqakEIIFNSDTPIDLILLDIYMQQENGLDLLPVLHEAG 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  75 TRTPVILMTAYAEVETAVEALRCGAFDYVIKPF 107
Cdd:PRK10430  76 CKSDVIVISSAADAATIKDSLHYGVVDYLIKPF 108
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
414-457 1.68e-08

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


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 51.35  E-value: 1.68e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446047443 414 IKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:COG2901   40 LAEVEKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGLL 83
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
 5-105 5.44e-07

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 50.41  E-value: 5.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETrTPVILMTA 84
Cdd:PRK10701   2 NKIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQ-GPIVLLTS 80

                         90       100
                 ....*....|....*....|.
gi 446047443  85 YAEVETAVEALRCGAFDYVIK 105
Cdd:PRK10701  81 LDSDMNHILALEMGACDYILK 101
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
 7-108 6.63e-07

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 48.49  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQ---GFETHCANNGRTALHLFADI---HPDVVLM--DIRMPEMDGIKALKEMRSNETRTP 78
Cdd:cd17595    3 ILTVDDDPQVLRAVARDLRRQygkDYRVLRADSGAEALDALKELklrGEAVALFlvDQRMPEMDGVEFLEKAMELFPEAK 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446047443  79 VILMTAYAEVETAVEALRCGAFD-YVIKPFD 108
Cdd:cd17595   83 RVLLTAYADTDAAIRAINDVQLDyYLLKPWD 113
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 169-319 8.66e-07

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 47.97  E-value: 8.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  169 VLISGESGTGKELIARAIhynSRRAKGPFIKVNCaalpeslleSELFGHEKGAftGAQTLRQgLFERANEGT---LLLDE 245
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV---AKELGAPFIEISG---------SELVSKYVGE--SEKRLRE-LFEAAKKLApcvIFIDE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  246 I-----------GEMPLVLQAKLLRILQereferigGHQTIKVDIRIIAATNRdlqamvkegtfredlfyrlnvIHLILP 314
Cdd:pfam00004  66 IdalagsrgsggDSESRRVVNQLLTELD--------GFTSSNSKVIVIAATNR---------------------PDKLDP 116


                  ....*
gi 446047443  315 PLRDR 319
Cdd:pfam00004 117 ALLGR 121
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 7-106 1.57e-06

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: 46.50  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQ--GFETHCANNGRTALH--LFADihPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILM 82
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDeiLFLQ--PDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMI 78

                         90       100
                 ....*....|....*....|....
gi 446047443  83 TAYAEVETAVEALRCGAFDYVIKP 106
Cdd:cd17565   79 SQVSDKEMIGKAYQAGIEFFINKP 102
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 6-112 2.42e-06

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 46.24  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDnVRRMLSTAFALQ-GFETHCANNGRTALHLFADIHPD--VVLMDIRMPEMDGIK---ALKEMRSNETRTPV 79
Cdd:cd19933    2 KVLLVDDNA-VNRMVTKGLLEKlGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEvalRIRKLFGRRERPLI 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19933   81 VALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 169-386 7.18e-06

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 47.69  E-value: 7.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIhynSRRAKGPFIKVNcaaLPESLleSELFGhekgafTGAQTLRQgLFERANEGT---LLLDE 245
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAV---AGELGAPFIRVR---GSELV--SKYIG------EGARNVRE-VFELAREKApsiIFIDE 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 246 I-------------GEM-PLVLQakllrILQE-REFERIGghqtikvDIRIIAATNR-DL--QAMVKEGTFreDLfyrln 307
Cdd:COG1222  180 IdaiaarrtddgtsGEVqRTVNQ-----LLAElDGFESRG-------DVLIIAATNRpDLldPALLRPGRF--DR----- 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 308 VIHLILPPLRDRREdisLLANHfLQKFSSENqrdiiDIDPMAMSLLTA-WSwpGniRELSNVIERA---VVMNSGPIIFS 383
Cdd:COG1222  241 VIEVPLPDEEAREE---ILKIH-LRDMPLAD-----DVDLDKLAKLTEgFS--G--ADLKAIVTEAgmfAIREGRDTVTM 307


                 ...
gi 446047443 384 EDL 386
Cdd:COG1222  308 EDL 310
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 168-319 7.51e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 45.36  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443  168 SVLISGESGTGKELIARaiHYNSRRAKGPFIKVNCaalPESLLESELFGHEKGAFTGAQTLRQGLFERANEG-TLLLDEI 246
Cdd:pfam07728   1 GVLLVGPPGTGKTELAE--RLAAALSNRPVFYVQL---TRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446047443  247 GEMPLVLQAKLLRILQEREFERIGGHQTIKV---DIRIIAATNrdlqamvkegtfreDLFYRLNVihlILPPLRDR 319
Cdd:pfam07728  76 NRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMN--------------PLDRGLNE---LSPALRSR 134
fis PRK00430
DNA-binding transcriptional regulator Fis;
417-456 1.09e-05

DNA-binding transcriptional regulator Fis;


Pssm-ID: 179020 [Multi-domain]  Cd Length: 95  Bit Score: 43.90  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446047443 417 VEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Cdd:PRK00430  55 VEAPLLDMVMQYTRGNQTRAALMLGINRGTLRKKLKKYGM 94
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
169-340 1.18e-05

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 46.42  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIhynSRRAKGPFIKVNCAALPESLLEselfghekgafTGAQTLRQgLFERANE--GTLLLDEI 246
Cdd:COG1223   38 ILFYGPPGTGKTMLAEAL---AGELKLPLLTVRLDSLIGSYLG-----------ETARNLRK-LFDFARRapCVIFFDEF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 247 -------------GEMPLVLQAkllrILQEREFerigghqtIKVDIRIIAATNRdlQAMVKEGTFR--EDlfyrlnVIHL 311
Cdd:COG1223  103 daiakdrgdqndvGEVKRVVNA----LLQELDG--------LPSGSVVIAATNH--PELLDSALWRrfDE------VIEF 162

                        170       180
                 ....*....|....*....|....*....
gi 446047443 312 ILPPLRDRREDISLLANHFLQKFSSENQR 340
Cdd:COG1223  163 PLPDKEERKEILELNLKKFPLPFELDLKK 191
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
 7-112 2.85e-05

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 43.40  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGF---EThcANNGRTALHLFADIHPDVVLMDIRMPE-MDGIKALKEMRSNETRTP---V 79
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVtriDT--ASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPstvF 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17589   79 IMVTGESSRAMVLSALELEPDDYLLKPFTVSEL 111
PRK09483 PRK09483
response regulator; Provisional
 7-105 3.37e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.10  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVR----RMLSTafaLQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVIL 81
Cdd:PRK09483   4 VLLVDDHELVRagirRILED---IKGIKvVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIM 80

                         90       100
                 ....*....|....*....|....
gi 446047443  82 MTAYAEVETAVEALRCGAFDYVIK 105
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSK 104
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 169-299 3.79e-05

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 45.54  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIhynSRRAKGPFIKVNCAalpESLLESELFGHEK-GAFTGAQTLRQG-LFeranEGTLLLDEI 246
Cdd:COG0714   34 LLLEGVPGVGKTTLAKAL---ARALGLPFIRIQFT---PDLLPSDILGTYIyDQQTGEFEFRPGpLF----ANVLLADEI 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446047443 247 GEMPLVLQAKLLRILQEREFErIGGhQTIKVD--IRIIAATNRDLQamvkEGTFR 299
Cdd:COG0714  104 NRAPPKTQSALLEAMEERQVT-IPG-GTYKLPepFLVIATQNPIEQ----EGTYP 152
PRK01905 PRK01905
Fis family transcriptional regulator;
414-456 6.61e-05

Fis family transcriptional regulator;


Pssm-ID: 179348 [Multi-domain]  Cd Length: 77  Bit Score: 41.33  E-value: 6.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446047443 414 IKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Cdd:PRK01905  34 LSCVEKPLLEVVMEQAGGNQSLAAEYLGINRNTLRKKLQQHGL 76
PRK13856 PRK13856
two-component response regulator VirG; Provisional
 7-124 7.88e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 44.03  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMrSNETRTPVILMTAYA 86
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSL-ATKSDVPIIIISGDR 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446047443  87 EVET-AVEALRCGAFDYVIKPFDLDELNLIVQRALQLQS 124
Cdd:PRK13856  83 LEEAdKVVALELGATDFIAKPFGTREFLARIRVALRVRP 121
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 168-287 7.98e-05

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 43.04  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 168 SVLISGESGTGKELIARAIhynSRRAKGPFIKVNCaalpeslleSELFGHEKGAftGAQTLRQgLFERANE---GTLLLD 244
Cdd:cd19481   28 GILLYGPPGTGKTLLAKAL---AGELGLPLIVVKL---------SSLLSKYVGE--SEKNLRK-IFERARRlapCILFID 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446047443 245 EI---------GEMPLVLQAKLLRILQEreferIGGhQTIKVDIRIIAATNR 287
Cdd:cd19481   93 EIdaigrkrdsSGESGELRRVLNQLLTE-----LDG-VNSRSKVLVIAATNR 138
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
50-120 1.90e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.56  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446047443  50 DVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
Cdd:PRK09935  51 DLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMIL 121
pleD PRK09581
response regulator PleD; Reviewed
 6-112 2.01e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 43.74  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDED----NVRRMLSTAFALQgFETHCAnngrTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE-TR-TPV 79
Cdd:PRK09581 157 RILLVDDDVsqaeRIANILKEEFRVV-VVSDPS----EALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKErTRyVPI 231

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK09581 232 LLLVDEDDDPRLVKALELGVNDYLMRPIDKNEL 264
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
 6-121 2.08e-04

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 40.69  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQGFE-THCANNGRTALHLFADIHPDVVLMDIRMPE-MDGIKALKEMRSNETrTPVILMT 83
Cdd:cd17540    2 RVLIIEDEPLIAMDLEQIVEDLGHQvVGIARTRDEAVALARRERPDLILADIQLADgSSGIDAVNEILTTHD-VPVIFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446047443  84 AYAevetavEALRCGAF---DYVI-KPFDLDELNLIVQRALQ 121
Cdd:cd17540   81 AYP------ERLLTGERpepTFLItKPFDPEMVKAAISQALF 116
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
6-112 2.15e-04

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 42.53  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAFALQ-GFE-THCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMT 83
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDpGFEvVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87

                         90       100
                 ....*....|....*....|....*....
gi 446047443  84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK10403  88 VSDASSDVFALIDAGADGYLLKDSDPEVL 116
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
1-112 3.39e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.80  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   1 MTAInrilIVDDEDNVRRMLSTAFALQGFETHCA-NNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPV 79
Cdd:PRK09958   1 MNAI----IIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGII 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:PRK09958  77 IIVSAKNDHFYGKHCADAGANGFVSKKEGMNNI 109
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
 7-112 4.31e-04

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 39.77  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNETRTPVILMTAYA 86
Cdd:cd19922    1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHWE 80

                         90       100
                 ....*....|....*....|....*.
gi 446047443  87 EVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd19922   81 DLQEELEEVQRFAVSYVVKPVLISNL 106
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
 7-112 8.03e-04

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 39.22  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDN----VRRMLSTAFALQgfethCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSNE-TR-TPVI 80
Cdd:cd17539    1 VLLVDDRPSsaerIAAMLSSEHEVV-----VEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLErTRqLPIL 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446047443  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
Cdd:cd17539   76 AVADPGDRGRLIRALEIGVNDYLVRPIDPNEL 107
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 7-106 1.63e-03

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 38.50  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHL-----------FADIHPDVVLMDIRMPEMDGIKALKEMR--SN 73
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFlgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKesSA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446047443  74 ETRTPVILMTAYAEVETAVEALRCGAFDYVIKP 106
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
PRK14084 PRK14084
DNA-binding response regulator;
6-132 2.55e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 39.35  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDEDNVRRMLSTAF-ALQGFET--HCANNGRTALHLFADIHpDVVLMDIRMPEMDGI---KALKEMRsnetRTPV 79
Cdd:PRK14084   2 KALIVDDEPLARNELTYLLnEIGGFEEinEAENVKETLEALLINQY-DIIFLDINLMDESGIelaAKIQKMK----EPPA 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446047443  80 ILMtAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHL 132
Cdd:PRK14084  77 IIF-ATAHDQFAVKAFELNATDYILKPFEQKRIEQAVNKVRATKAKDDNNASA 128
PRK13435 PRK13435
response regulator; Provisional
 6-120 3.16e-03

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 38.11  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443   6 RILIVDDE----DNVRRMLSTAfalqGFET-HCANNGRTALHLFADIHPDVVLMDIRMpeMDGIKALKEMR--SNETRTP 78
Cdd:PRK13435   7 KVLIVEDEaliaLELEKLVEEA----GHEVvGIAMSSEQAIALGRRRQPDVALVDVHL--ADGPTGVEVARrlSADGGVE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446047443  79 VILMTAYAEVetaVEALRCGAFDYVIKPFDLDElnliVQRAL 120
Cdd:PRK13435  81 VVFMTGNPER---VPHDFAGALGVIAKPYSPRG----VARAL 115
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 169-287 4.07e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 38.04  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIhynSRRAKGPFIKVNCAALPESLL-ESElfghekgaftgaQTLRqGLFERANEGT---LLLD 244
Cdd:cd19503   37 VLLHGPPGTGKTLLARAV---ANEAGANFLSISGPSIVSKYLgESE------------KNLR-EIFEEARSHApsiIFID 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446047443 245 EI-----------GEMPLVLQAKLLRILQEREFERigghqtikvDIRIIAATNR 287
Cdd:cd19503  101 EIdalapkreedqREVERRVVAQLLTLMDGMSSRG---------KVVVIAATNR 145
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 169-287 7.20e-03

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 38.74  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446047443 169 VLISGESGTGKELIARAIhynSRRAKGPFIKVNCAAlpeslLESELFGHekgaftGAQTLRQgLFERA---NEGTLLLDE 245
Cdd:COG0464  194 LLLYGPPGTGKTLLARAL---AGELGLPLIEVDLSD-----LVSKYVGE------TEKNLRE-VFDKArglAPCVLFIDE 258

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446047443 246 I--------GEMPLVLQ---AKLLRILQEREFERIgghqtikvdirIIAATNR 287
Cdd:COG0464  259 AdalagkrgEVGDGVGRrvvNTLLTEMEELRSDVV-----------VIAATNR 300
 
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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