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Conserved domains on  [gi|16131834|ref|NP_418432|]
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DNA-binding transcriptional activator ZraR [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

two-component system response regulator ZraR( domain architecture ID 11484678)

two-component system response regulator ZraR is a sigma 54-dependent transcriptional regulator that regulates the expression of zraP when activated via phosphorylation by ZraS and positively autoregulates the expression of the zraSR operon

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-441 0e+00

sigma-54-dependent response regulator transcription factor ZraR;


:

Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 907.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
Cdd:PRK10365 161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  241 EIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
Cdd:PRK10365 241 EIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQ 400
Cdd:PRK10365 321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQ 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 16131834  401 PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:PRK10365 401 PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
 
Name Accession Description Interval E-value
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-441 0e+00

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 907.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
Cdd:PRK10365 161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  241 EIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
Cdd:PRK10365 241 EIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQ 400
Cdd:PRK10365 321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQ 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 16131834  401 PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:PRK10365 401 PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
8-441 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: 587.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHthsidAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVLI 167
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALER-----RRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 168 HGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISP 247
Cdd:COG2204 160 TGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 248 MMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFL 327
Cdd:COG2204 240 ALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 328 QRFAERNRKAVKgFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIAstpiplgqsqdiqplvEVEK 407
Cdd:COG2204 320 ARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEALE----------------EVER 382
                       410       420       430
                ....*....|....*....|....*....|....
gi 16131834 408 EVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:COG2204 383 ELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-439 2.57e-145

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: 422.22  E-value: 2.57e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834     8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSiDAETPAVTASQFG---MVGKSPAMQHLLSEIALVAPSEAT 164
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQE-QVALPADAGEAEDsaeLIGEAPAMQEVFRAIGRLSRSDIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   165 VLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGD 244
Cdd:TIGR01818 160 VLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   245 ISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAG 324
Cdd:TIGR01818 240 MPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLAR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   325 HFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQP--- 401
Cdd:TIGR01818 320 HFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQdsw 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131834   402 -----------------------LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:TIGR01818 400 dealeawakqalsrgeqglldraLPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKL 460
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
140-435 1.13e-112

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 341.08  E-value: 1.13e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  140 GMVGKSPAMQHLLSEIALVAP-SEATVLIHGDSGTGKELVARAIHASSARS---EKPLVTLNCAALNESLLESELFGHEK 215
Cdd:NF038308 180 GIATRNAAFNRLIEQIERVALrSRAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVK 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  216 GAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFR 295
Cdd:NF038308 260 GAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFR 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  296 QDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNR-----KAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVV 370
Cdd:NF038308 340 EDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGrqvrfNKEARFRYLAFATSPEALWPGNFRELSASVTRMAT 419
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  371 LLTGEYISERELPLAIA-------STPIPLGQSQDIQPLVE-----------VEKEVILAALEKTGGNKTEAARQLGITR 432
Cdd:NF038308 420 LADGGRITEELVEEEIArlraawqSAPAAADDDALADLLGGeqlaeldlfdrVQLAAVLRVCRQSRSLSAAGRRLFGVSR 499

                 ...
gi 16131834  433 KTL 435
Cdd:NF038308 500 QQK 502
Sigma54_activat pfam00158
Sigma-54 interaction domain;
141-308 3.85e-108

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 316.27  E-value: 3.85e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTG 220
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   221 ADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYY 300
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 16131834   301 RLNVVAIE 308
Cdd:pfam00158 161 RLNVIPIE 168
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
8-122 1.08e-35

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: 127.61  E-value: 1.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
Cdd:cd17550  81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
8-59 1.85e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.82  E-value: 1.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 16131834      8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRM 59
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMM 54
 
Name Accession Description Interval E-value
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-441 0e+00

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 907.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
Cdd:PRK10365 161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  241 EIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
Cdd:PRK10365 241 EIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQ 400
Cdd:PRK10365 321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQ 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 16131834  401 PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:PRK10365 401 PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
8-441 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: 587.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHthsidAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVLI 167
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALER-----RRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDATVLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 168 HGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISP 247
Cdd:COG2204 160 TGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 248 MMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFL 327
Cdd:COG2204 240 ALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHFL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 328 QRFAERNRKAVKgFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIAstpiplgqsqdiqplvEVEK 407
Cdd:COG2204 320 ARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPEALE----------------EVER 382
                       410       420       430
                ....*....|....*....|....*....|....
gi 16131834 408 EVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:COG2204 383 ELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
140-441 4.60e-176

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: 499.68  E-value: 4.60e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 140 GMVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFT 219
Cdd:COG3829 139 DIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFT 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 220 GADKR-REGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDL 298
Cdd:COG3829 219 GAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDL 298
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 299 YYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYIS 378
Cdd:COG3829 299 YYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIERAVVLSEGDVIT 378
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131834 379 ERELPLAIASTPIPLGQSQDI---QPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:COG3829 379 PEHLPEYLLEEAEAASAAEEGslkEALEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKK 444
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
8-439 5.19e-167

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 477.42  E-value: 5.19e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL---AHTHSIDAETPAVTAS-QFG-MVGKSPAMQHLLSEIALVAPSE 162
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALqlqSMKKEIRHLHQALSTSwQWGhILTNSPAMMDICKDTAKIALSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  163 ATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEI 242
Cdd:PRK11361 167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  243 GDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLL 322
Cdd:PRK11361 247 GEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  323 AGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQP- 401
Cdd:PRK11361 327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEVKTAPVg 406
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 16131834  402 -------LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:PRK11361 407 ernlkeeIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKL 451
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-439 2.57e-145

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: 422.22  E-value: 2.57e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834     8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSiDAETPAVTASQFG---MVGKSPAMQHLLSEIALVAPSEAT 164
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQE-QVALPADAGEAEDsaeLIGEAPAMQEVFRAIGRLSRSDIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   165 VLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGD 244
Cdd:TIGR01818 160 VLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   245 ISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAG 324
Cdd:TIGR01818 240 MPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLAR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   325 HFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQP--- 401
Cdd:TIGR01818 320 HFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQdsw 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131834   402 -----------------------LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:TIGR01818 400 dealeawakqalsrgeqglldraLPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKL 460
PRK15115 PRK15115
response regulator GlrR; Provisional
1-441 2.02e-137

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 401.52  E-value: 2.02e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAEtpavtASQFGMVGKSPAMQHLLSEIALVAP 160
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDE-----RWREAIVTRSPLMLRLLEQARMVAQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
Cdd:PRK15115 156 SDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  241 EIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
Cdd:PRK15115 236 EIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIAstpiplGQSQDIQ 400
Cdd:PRK15115 316 LLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALE------GENTALP 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 16131834  401 PLVEVEKEVILAALEK----TGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:PRK15115 390 TFVEARNQFELNYLRKllqiTKGNVTHAARMAGRNRTEFYKLLSR 434
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
74-441 4.12e-131

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 391.57  E-value: 4.12e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  74 LNPAIPVLIMTAYSSV-ETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQF------GMVGKSP 146
Cdd:COG3284 249 LGLADAALLGRPLEELfGLDLEALPDGARRAPASPRPLRLRDGRRLGALLRLRPARRAARAAPAGAPapaalaALAGGDP 328
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 147 AMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKR-R 225
Cdd:COG3284 329 AMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKgR 408
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 226 EGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVV 305
Cdd:COG3284 409 PGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGL 488
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 306 AIEVPSLRQrREDIPLLAGHFLQRFAERNRKAvkGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLA 385
Cdd:COG3284 489 TLTLPPLRE-REDLPALIEHLLRELAAGRGPL--RLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITVEDLPDE 565
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131834 386 IASTPIPLGQSQDIQ--PLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:COG3284 566 LRAELAAAAPAAAAPltSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKR 623
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
117-438 1.59e-130

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 386.06  E-value: 1.59e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  117 LEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTL 196
Cdd:PRK05022 165 LESQAELPQDVAEFLRQEALKEGEMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYL 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  197 NCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVR 276
Cdd:PRK05022 245 NCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVR 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  277 LIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLqrfaERNR-----KAVKgFTPQAMDLLIH 351
Cdd:PRK05022 325 VIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFL----EQNRarlglRSLR-LSPAAQAALLA 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  352 YDWPGNIRELENAVERAVVLLTGE--------------YISERELPLAIASTPIPLGQSQDIQPLVE-VEKEVILAALEK 416
Cdd:PRK05022 400 YDWPGNVRELEHVISRAALLARARgagrivtleaqhldLPAEVALPPPEAAAAPAAVVSQNLREATEaFQRQLIRQALAQ 479
                        330       340
                 ....*....|....*....|....
gi 16131834  417 TGGNKTEAARQLGITRKTL--LAK 438
Cdd:PRK05022 480 HQGNWAAAARALELDRANLhrLAK 503
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
8-441 1.14e-128

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: 379.09  E-value: 1.14e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834     8 ILVVDDDIShctiLQALLRgWG---YNVALANSGRQALEQVREQVFDLVLCDVRM-----AEMDGIATLKEIKALNPAIP 79
Cdd:TIGR02915   1 LLIVEDDLG----LQKQLK-WSfadYELAVAADRESAIALVRRHEPAVVTLDLGLppdadGASEGLAALQQILAIAPDTK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALaHTHSIDAETPAVTASQF-----GMVGKSPAMQHLLSE 154
Cdd:TIGR02915  76 VIVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAF-HLYTLETENRRLQSALGgtalrGLITSSPGMQKICRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   155 IALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADG 234
Cdd:TIGR02915 155 IEKIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   235 GTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQ 314
Cdd:TIGR02915 235 GTLFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRS 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   315 RREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISEREL---PLAIASTP- 390
Cdd:TIGR02915 315 RDGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLgldARERAETPl 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131834   391 -IPLGQSQDiqplvEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:TIGR02915 395 eVNLREVRE-----RAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKK 441
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
8-439 4.72e-126

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 373.44  E-value: 4.72e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSID-AETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVL 166
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQqPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  167 IHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDIS 246
Cdd:PRK10923 166 INGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  247 PMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHF 326
Cdd:PRK10923 246 LDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHF 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  327 LQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQS---------- 396
Cdd:PRK10923 326 LQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSqmqpdswatl 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131834  397 -------------QDI--QPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:PRK10923 406 laqwadralrsghQNLlsEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKL 463
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
140-431 4.66e-122

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: 365.58  E-value: 4.66e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   140 GMVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFT 219
Cdd:TIGR01817 197 GIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFT 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   220 GADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLY 299
Cdd:TIGR01817 277 GAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLY 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   300 YRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKgFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISE 379
Cdd:TIGR01817 357 YRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPLT-ITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITR 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   380 RE--------LPLAIAST----PIPLGQSQDIQPLVEV-----------------EKEVILAALEKTGGNKTEAARQLGI 430
Cdd:TIGR01817 436 SDfscqsgqcLSPMLAKTcphgHISIDPLAGTTPPHSPasaalpgepglsgptlsERERLIAALEQAGWVQAKAARLLGM 515

                  .
gi 16131834   431 T 431
Cdd:TIGR01817 516 T 516
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
140-435 1.13e-112

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 341.08  E-value: 1.13e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  140 GMVGKSPAMQHLLSEIALVAP-SEATVLIHGDSGTGKELVARAIHASSARS---EKPLVTLNCAALNESLLESELFGHEK 215
Cdd:NF038308 180 GIATRNAAFNRLIEQIERVALrSRAPILLTGPTGAGKSFLARRIYELKKRRhqvSGPFVEVNCATLRGDLAMSELFGHVK 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  216 GAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFR 295
Cdd:NF038308 260 GAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFR 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  296 QDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNR-----KAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVV 370
Cdd:NF038308 340 EDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGrqvrfNKEARFRYLAFATSPEALWPGNFRELSASVTRMAT 419
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  371 LLTGEYISERELPLAIA-------STPIPLGQSQDIQPLVE-----------VEKEVILAALEKTGGNKTEAARQLGITR 432
Cdd:NF038308 420 LADGGRITEELVEEEIArlraawqSAPAAADDDALADLLGGeqlaeldlfdrVQLAAVLRVCRQSRSLSAAGRRLFGVSR 499

                 ...
gi 16131834  433 KTL 435
Cdd:NF038308 500 QQK 502
Sigma54_activat pfam00158
Sigma-54 interaction domain;
141-308 3.85e-108

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 316.27  E-value: 3.85e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTG 220
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   221 ADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYY 300
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 16131834   301 RLNVVAIE 308
Cdd:pfam00158 161 RLNVIPIE 168
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
142-431 7.42e-102

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: 306.53  E-value: 7.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   142 VGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGA 221
Cdd:TIGR02974   2 IGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   222 DKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYR 301
Cdd:TIGR02974  82 QKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   302 LNVVAIEVPSLRQRREDIPLLAGHFLQRFA-ERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYI--- 377
Cdd:TIGR02974 162 LAFDVITLPPLRERQEDIMLLAEHFAIRMArELGLPLFPGFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEEApid 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131834   378 ---------SERELPLAIASTPIPLG-------------QSQDIQPLV-EVEKEVILAALEKTGGNKTEAARQLGIT 431
Cdd:TIGR02974 242 eiiidpfasPWRPKQAAPAVDEVNSTptdlpspssiaaaFPLDLKQAQqDYEIELLQQALAEAQFNQRKAAELLGLT 318
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
141-394 2.50e-101

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 311.35  E-value: 2.50e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTG 220
Cdd:COG3283 206 IVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFGN 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 221 ADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYY 300
Cdd:COG3283 286 AREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYY 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 301 RLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISER 380
Cdd:COG3283 366 RLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDELTPE 445
                       250
                ....*....|....
gi 16131834 381 ELPLAIASTPIPLG 394
Cdd:COG3283 446 DLQLPEYAASAGLL 459
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
141-439 2.32e-96

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 299.33  E-value: 2.32e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHA--------SSARSEKPLVTLNCAALNESLLESELFG 212
Cdd:PRK15424 221 LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHReyfarhdaRQGKKSHPFVAVNCGAIAESLLEAELFG 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  213 HEKGAFTGAdkRREGR---FVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEV 289
Cdd:PRK15424 301 YEEGAFTGS--RRGGRaglFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDV 378
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  290 NAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQR-FAERN----RKAVKGFTpQAMDLLIHYDWPGNIRELENA 364
Cdd:PRK15424 379 RQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQsLAALSapfsAALRQGLQ-QCETLLLHYDWPGNVRELRNL 457
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  365 VERAVVL--------LTGEYISER--ELPLAIASTPIPLGQSQDIQplvevekevilAALEKTGGNKTEAARQLGITRKT 434
Cdd:PRK15424 458 MERLALFlsveptpdLTPQFLQLLlpELARESAKTPAPRLLAATLQ-----------QALERFNGDKTAAANYLGISRTT 526

                 ....*
gi 16131834  435 LLAKL 439
Cdd:PRK15424 527 LWRRL 531
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
145-441 1.35e-93

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: 285.97  E-value: 1.35e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 145 SPAMQHLLSEIAlvapSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESelfghekgaftgadkr 224
Cdd:COG3604 102 SEEDLRLLETLA----SLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES---------------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 225 regrfveadggtlfldeigdispmmqvrllraIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNV 304
Cdd:COG3604 162 --------------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNV 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 305 VAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPl 384
Cdd:COG3604 210 FPIRLPPLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLA- 288
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131834 385 aiastpiplgqSQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:COG3604 289 -----------PGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKK 334
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
137-441 4.92e-93

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 295.20  E-value: 4.92e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  137 SQFG-MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEK 215
Cdd:PRK15429 373 SEFGeIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHER 452
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  216 GAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFR 295
Cdd:PRK15429 453 GAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFR 532
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  296 QDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAvVLLTGE 375
Cdd:PRK15429 533 SDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERA-VLLTRG 611
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  376 YISERELP-LAIASTPIPLGQSQDIQPlVEVEKEVILAALEKTGG---NKTEAARQLGITRKTLLAKLSR 441
Cdd:PRK15429 612 NVLQLSLPdITLPEPETPPAATVVAQE-GEDEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTLLSRMKR 680
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
141-439 2.89e-89

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: 280.98  E-value: 2.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTG 220
Cdd:TIGR02329 214 LLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTG 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   221 AdkRREGR---FVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQD 297
Cdd:TIGR02329 294 A--RRGGRtglIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRD 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   298 LYYRLNVVAIEVPSLRQRREDIPLLAGHFLQR-FAERN----RKAVKGFTPQAmDLLIHYDWPGNIRELENAVERAVVLL 372
Cdd:TIGR02329 372 LFYRLSILRIALPPLRERPGDILPLAAEYLVQaAAALRlpdsEAAAQVLAGVA-DPLQRYPWPGNVRELRNLVERLALEL 450
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131834   373 --------TGEYISERELPLAIASTPIPLGQSQdIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:TIGR02329 451 sampagalTPDVLRALAPELAEASGKGKTSALS-LRERSRVEALAVRAALERFGGDRDAAAKALGISRTTLWRRL 524
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
141-439 8.26e-88

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 270.39  E-value: 8.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTG 220
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  221 ADKRREGRFVEADGGTLFLDEIGdISPMM-QVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLY 299
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELA-TAPMLvQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  300 YRLNVVAIEVPSLRQRREDIPLLAGHF-LQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVvlltgeY-- 376
Cdd:PRK11608 167 DRLAFDVVQLPPLRERQSDIMLMAEHFaIQMCRELGLPLFPGFTERARETLLNYRWPGNIRELKNVVERSV------Yrh 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  377 -ISEREL------PLAIASTPIPLGQSQDIQ----PL------VEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:PRK11608 241 gTSEYPLdniiidPFKRRPAEEAIAVSETTSlptlPLdlrewqHQQEKELLQRSLQQAKFNQKRAAELLGLTYHQLRALL 320
PRK10820 PRK10820
transcriptional regulator TyrR;
141-395 3.99e-72

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 236.12  E-value: 3.99e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTG 220
Cdd:PRK10820 206 IVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPN 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  221 ADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYY 300
Cdd:PRK10820 286 ALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYY 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  301 RLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISER 380
Cdd:PRK10820 366 RLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYELRPQ 445
                        250
                 ....*....|....*
gi 16131834  381 ELPLAIASTPIPLGQ 395
Cdd:PRK10820 446 DILLPDYDAAVAVGE 460
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
141-439 3.18e-69

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 231.11  E-value: 3.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  141 MVGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGhekGAFTG 220
Cdd:PRK11388 327 MPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTD 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  221 ADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLYY 300
Cdd:PRK11388 404 SENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYY 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  301 RLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKgFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISER 380
Cdd:PRK11388 484 ALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLK-IDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIRLS 562
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131834  381 ELPLAIASTpIPLGQSqDIQP------LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:PRK11388 563 DLPEHLFTE-QATDDV-SATRlstslsLAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKM 625
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
144-379 5.68e-48

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


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 171.94  E-value: 5.68e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 144 KSPAMQHLLSEIALVA-PSEATVLIHGDSGTGKELVARAIHA---SSARSEKPLVTLNCAALNESLLESELFGHEKGAFT 219
Cdd:COG4650 189 RNAAFNRLIEQIERVAiRSRAPILLTGPTGAGKSQLARRIYElkkARHQVSGRFVEVNCATLRGDGAMSALFGHVKGAFT 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 220 GADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQIISVDVRLIAATHRDLAAEVNAGRFRQDLY 299
Cdd:COG4650 269 GAVSDRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLL 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 300 YRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERNRKAVKgFTPQAMDLLIHYD------WPGNIRELENAVERAVVLLT 373
Cdd:COG4650 349 ARINLWTFRLPGLAERREDIEPNLDYELARFAREQGRRVR-FNKEARARYLAFAtspealWSGNFRDLNASVTRMATLAE 427

                ....*.
gi 16131834 374 GEYISE 379
Cdd:COG4650 428 GGRITV 433
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-126 1.03e-36

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: 130.74  E-value: 1.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAI 78
Cdd:COG0784   1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16131834  79 PVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHS 126
Cdd:COG0784  81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
8-118 6.98e-36

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: 128.04  E-value: 6.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834     8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 16131834    88 SVETAVEALKTGALDYLIKPLDFDNLQATLE 118
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
8-122 1.08e-35

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: 127.61  E-value: 1.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
Cdd:cd17550  81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
9-107 7.84e-35

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: 125.03  E-value: 7.84e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   9 LVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSS 88
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                        90
                ....*....|....*....
gi 16131834  89 VETAVEALKTGALDYLIKP 107
Cdd:cd00156  81 EEDAVRALELGADDYLVKP 99
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
8-130 1.81e-33

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: 125.28  E-value: 1.81e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA--IPVLIMTA 85
Cdd:COG3437   9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLTA 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 16131834  86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAE 130
Cdd:COG3437  89 LADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQREL 133
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
8-126 1.82e-33

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: 124.68  E-value: 1.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:COG0745   4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHS 126
Cdd:COG0745  84 DEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAA 122
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
8-118 5.31e-32

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: 120.01  E-value: 5.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN--PAIPVLIMTA 85
Cdd:COG3706   4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPrtADIPIIFLTA 83
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131834  86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLE 118
Cdd:COG3706  84 LDDEEDRARALEAGADDYLTKPFDPEELLARVD 116
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
165-365 1.79e-31

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: 127.53  E-value: 1.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 165 VLIHGDSGTGKELVARAIH----ASSARSEK-PLVTLNCA--ALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTL 237
Cdd:COG1221 133 TLILGPTGVGKSFFAELMYeyaiEIGVLPEDaPFVVFNCAdyANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGIL 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 238 FLDEIGDISPMMQVRLLRAIQEREVQRVG-SNQIISVDVRLIAATHRDLAAevnagrfrqdlyYRLNV------VAIEVP 310
Cdd:COG1221 213 FLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPES------------SLLKTflrripMVIKLP 280
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131834 311 SLRQR----REDIPLlagHFLQRFAERNRKAVKgFTPQAMDLLIHYDWPGNIRELENAV 365
Cdd:COG1221 281 SLEERsleeRLELIK---HFFKEEAKRLNKPIK-VSKEVLKALLLYDCPGNIGQLKSDI 335
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
4-125 4.00e-31

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 116.22  E-value: 4.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   4 DNIDILVVDDDISHCTILQALLR---GWGyNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
Cdd:COG4565   2 KMIRVLIVEDDPMVAELLRRYLErlpGFE-VVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 16131834  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTH 125
Cdd:COG4565  81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRR 125
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
7-122 1.36e-30

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: 114.12  E-value: 1.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
Cdd:COG5803   4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAY 83
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131834  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
Cdd:COG5803  84 GELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
8-117 9.87e-30

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: 111.79  E-value: 9.87e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL---NPAIPVLIMT 84
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeggGRRTPIIALT 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
Cdd:cd17546  81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
8-107 1.18e-29

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: 111.02  E-value: 1.18e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWG--YNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                        90       100
                ....*....|....*....|..
gi 16131834  86 YSSVETAVEALKTGALDYLIKP 107
Cdd:COG4753  82 YSDFEYAQEAIKLGADDYLLKP 103
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
8-123 1.47e-29

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: 111.28  E-value: 1.47e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYN---VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMT 84
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH 123
Cdd:cd17536  81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
9-107 4.07e-29

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: 109.42  E-value: 4.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   9 LVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSS 88
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                        90
                ....*....|....*....
gi 16131834  89 VETAVEALKTGALDYLIKP 107
Cdd:cd17574  81 EEDKVLGLELGADDYITKP 99
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
8-123 8.84e-29

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: 109.21  E-value: 8.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH 123
Cdd:cd17572  81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKH 116
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
8-124 3.18e-28

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: 109.62  E-value: 3.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:COG4567   7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGYA 86
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHT 124
Cdd:COG4567  87 SIATAVEAIKLGADDYLAKPADADDLLAALERAEGDA 123
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
8-122 1.08e-27

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: 106.33  E-value: 1.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGYA 82
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131834  88 SVETAVEALKTGALD-YLIKPLDFDNLQATLEKALA 122
Cdd:cd17569  83 DLDAAIEAINEGEIYrFLTKPWDDEELKETIRQALE 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
8-120 1.44e-27

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: 105.75  E-value: 1.44e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17555   3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  88 SVETAVEALKTGALDYLIKPL-DFDNLQATLEKA 120
Cdd:cd17555  83 VMSDAVEALRLGAWDYLTKPIeDLAVLEHAVRRA 116
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
8-130 2.65e-27

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: 107.88  E-value: 2.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:COG4566   2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAE 130
Cdd:COG4566  82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAE 124
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
8-123 5.10e-27

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 104.88  E-value: 5.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH 123
Cdd:cd17549  81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEK 116
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
6-139 6.21e-27

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 107.98  E-value: 6.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDISHCTILQALLRGW-GYN-VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
Cdd:COG3279   2 MKILIVDDEPLARERLERLLEKYpDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFT 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131834  84 TAYSsvETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQF 139
Cdd:COG3279  82 TAYD--EYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDR 135
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
8-107 2.39e-26

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: 102.19  E-value: 2.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMT 84
Cdd:cd17538   2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKE-DPEtrhIPVIMIT 80
                        90       100
                ....*....|....*....|...
gi 16131834  85 AYSSVETAVEALKTGALDYLIKP 107
Cdd:cd17538  81 ALDDREDRIRGLEAGADDFLSKP 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
8-120 2.25e-25

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: 99.60  E-value: 2.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17554   3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYS 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131834  88 SVETAVEALKTGAldYLIKPLDFDNLQATLEKA 120
Cdd:cd17554  83 EYKSDFSSWAADA--YVVKSSDLTELKETIKRL 113
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
6-121 2.46e-25

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: 99.79  E-value: 2.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDISHCTILQALLRGWGYNV-ALANSGRQALEQVREQVFDLVLCDVRMA-EMDGIATLKEIKALNPaIPVLIM 83
Cdd:cd17534   1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD-IPVIFL 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16131834  84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd17534  80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
8-115 2.47e-25

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: 99.82  E-value: 2.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGY-NVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP--AIPVLIMT 84
Cdd:cd17551   3 ILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGleDVPIVMIT 82
                        90       100       110
                ....*....|....*....|....*....|.
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd17551  83 ADTDREVRLRALEAGATDFLTKPFDPVELLA 113
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
8-107 3.12e-25

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: 99.12  E-value: 3.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMT 84
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKA-DPAtrhIPVIFLT 79
                        90       100
                ....*....|....*....|...
gi 16131834  85 AYSSVETAVEALKTGALDYLIKP 107
Cdd:cd19920  80 ALTDTEDKVKGFELGAVDYITKP 102
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
8-117 3.18e-25

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: 99.44  E-value: 3.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17563   3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGYA 82
                        90       100       110
                ....*....|....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATL 117
Cdd:cd17563  83 SIATAVEAIKLGADDYLAKPADADEILAAL 112
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
7-121 1.80e-24

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: 97.34  E-value: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
Cdd:cd19919   2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd19919  82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
8-115 1.92e-24

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: 97.31  E-value: 1.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV--FDLVLCDVRMAEMDGIATLKEIKaLNPAIPVLIMTA 85
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKdeFDLVITDVHMPDMDGFEFLELIR-LEMDLPVIMMSA 79
                        90       100       110
                ....*....|....*....|....*....|
gi 16131834  86 YSSVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd17584  80 DGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
146-305 9.78e-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: 96.45  E-value: 9.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 146 PAMQHLLSEIALVA--PSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEkgaftgADK 223
Cdd:cd00009   1 VGQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834 224 RREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRvgsnqIISVDVRLIAATHRDLaaevnAGRFRQDLYYRLN 303
Cdd:cd00009  75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLR-----IDRENVRVIGATNRPL-----LGDLDRALYDRLD 144

                ..
gi 16131834 304 VV 305
Cdd:cd00009 145 IR 146
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
8-121 6.10e-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: 93.04  E-value: 6.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17537   3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd17537  83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
9-115 1.25e-22

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: 92.28  E-value: 1.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   9 LVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSS 88
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                        90       100
                ....*....|....*....|....*..
gi 16131834  89 VETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd17625  81 VEDRVKGLDLGADDYLPKPFSLAELLA 107
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
8-121 2.99e-22

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: 91.19  E-value: 2.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVAL-ANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
Cdd:cd17542   3 VLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd17542  83 GQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
142-312 6.09e-22

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 91.25  E-value: 6.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   142 VGKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESelfghekgaftga 221
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   222 dkrregrfveADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRvgsnqiisvdVRLIAATHRDLAAEVNAGRFRQDLYYR 301
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAEGYR----------VRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 16131834   302 LNVVAIEVPSL 312
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
6-121 2.08e-21

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: 88.93  E-value: 2.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDISHCTILQALLRGWGY-NVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN--PAIPVLI 82
Cdd:cd19923   1 MKVLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGalSHLPVLM 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131834  83 MTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd19923  81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
8-129 4.59e-21

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: 90.40  E-value: 4.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNV-ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAiPVLIMTAY 86
Cdd:COG3707   6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA-PVILLTAY 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 16131834  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDA 129
Cdd:COG3707  85 SDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRA 127
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
8-121 1.09e-20

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: 86.84  E-value: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd17553  83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
8-119 2.73e-20

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: 85.67  E-value: 2.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMT 84
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPAtrdIPVIALT 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:cd17548  81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
fixJ PRK09390
response regulator FixJ; Provisional
10-136 4.42e-20

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 87.75  E-value: 4.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   10 VVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSV 89
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDV 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 16131834   90 ETAVEALKTGALDYLIKPLDFDNLQATLEKALAH---THSIDAETPAVTA 136
Cdd:PRK09390  88 PLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQapeAAKSEAVAADIRA 137
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
8-117 5.03e-20

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 84.82  E-value: 5.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP--AIPVLIMTA 85
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 16131834  86 YSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
Cdd:cd17580  81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
8-107 1.75e-19

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: 82.87  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd19935  81 SVEDRVKGLDLGADDYLVKP 100
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
8-122 2.66e-19

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: 82.95  E-value: 2.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGW-GYN-VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEpDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16131834  86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
Cdd:cd17535  81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
8-123 6.76e-19

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 81.76  E-value: 6.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLeKALAH 123
Cdd:cd17624  81 GVDDRVAGLDAGADDYLVKPFALEELLARL-RALLR 115
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
6-107 1.08e-18

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: 81.67  E-value: 1.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDISHCTILQALLRGWGY--NVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPaIPVLIM 83
Cdd:cd17541   1 IRVLIVDDSAVMRKLLSRILESDPDieVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMV 79
                        90       100
                ....*....|....*....|....*.
gi 16131834  84 TAYSS--VETAVEALKTGALDYLIKP 107
Cdd:cd17541  80 SSLTEegAEITLEALELGAVDFIAKP 105
pleD PRK09581
response regulator PleD; Reviewed
8-109 1.33e-18

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 87.65  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMT 84
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKS-DPAtthIPVVMVT 83
                         90       100
                 ....*....|....*....|....*
gi 16131834   85 AYSSVETAVEALKTGALDYLIKPLD 109
Cdd:PRK09581  84 ALDDPEDRVRGLEAGADDFLTKPIN 108
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
8-109 1.40e-18

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: 81.20  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTARG 79
                        90       100
                ....*....|....*....|..
gi 16131834  88 SVETAVEALKTGALDYLIKPLD 109
Cdd:cd17623  80 DDIDRILGLELGADDYLPKPFN 101
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
8-121 3.44e-18

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: 80.12  E-value: 3.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLeKAL 121
Cdd:cd17627  81 SVSDRVAGLDAGADDYLVKPFALEELLARV-RAL 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
8-121 2.23e-17

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: 77.73  E-value: 2.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALnPA---IPVLIMT 84
Cdd:cd17562   3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKL-PAykfTPILMLT 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd17562  82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
8-118 2.31e-17

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: 77.71  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLE 118
Cdd:cd19934  81 SWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
8-117 2.89e-17

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 77.39  E-value: 2.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                        90       100       110
                ....*....|....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATL 117
Cdd:cd17615  82 SVEDRIAGLTAGGDDYVTKPFSLEEVVARL 111
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
6-119 5.04e-17

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 76.90  E-value: 5.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDishcTILQALLRGW-----GYNV-ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIP 79
Cdd:cd19925   1 INVLIVEDD----PMVAEIHRAYveqvpGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVD 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 16131834  80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:cd19925  77 VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
8-114 1.02e-16

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: 76.05  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALL-RGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIM 83
Cdd:cd17552   4 ILVIDDEEDIREVVQACLeKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPEtqsIPVILL 82
                        90       100       110
                ....*....|....*....|....*....|.
gi 16131834  84 TAYSSVETAVEALKTGALDYLIKPldFDNLQ 114
Cdd:cd17552  83 TAKAQPSDRQRFASLGVAGVIAKP--FDPLT 111
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
8-107 1.81e-16

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: 74.51  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLRE-WSAVPVIVLSARD 79
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd17620  80 EESDKIAALDAGADDYLTKP 99
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
8-107 1.83e-16

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: 74.74  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVF--DLVLCDVRMAEMDGIATLKEI---KALNpAIPVLI 82
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYImrhKICK-NIPVIM 79
                        90       100
                ....*....|....*....|....*
gi 16131834  83 MTAYSSVETAVEALKTGALDYLIKP 107
Cdd:cd17582  80 MSSQDSVGVVFKCLSKGAADYLVKP 104
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
8-113 2.58e-16

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: 74.67  E-value: 2.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNP---AIPVLIMT 84
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKS-DPdlkDIPVILLT 79
                        90       100
                ....*....|....*....|....*....
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNL 113
Cdd:cd17598  80 TLSDPRDVIRGLECGADNFITKPYDEKYL 108
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
8-125 3.55e-16

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 77.54  E-value: 3.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVfDLVLCDVRMAEMDGIATLKEIKaLNPAIPVLIMTAYS 87
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDTLKELR-QTHQTPVIMLTARG 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTH 125
Cdd:PRK10955  82 SELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSH 119
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
8-122 6.51e-16

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: 73.60  E-value: 6.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNV-ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAiPVLIMTAY 86
Cdd:cd19932   3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLTAY 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131834  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
Cdd:cd19932  82 SQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIA 117
orf27 CHL00148
Ycf27; Reviewed
1-139 8.60e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 76.68  E-value: 8.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPV 80
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK-ESDVPI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131834   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQF 139
Cdd:CHL00148  81 IMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIPNSSII 139
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
7-118 1.11e-15

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: 73.22  E-value: 1.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   7 DILVVDDDISHCTILQALLRGWGYNVAL--ANSGRQALEQVREQ-------VFDLVLCDVRMAEMDGIATLKEIKAlNPA 77
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAGVPNELhvVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKA-DPD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16131834  78 ---IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLE 118
Cdd:cd17557  80 lrrIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123
PRK15347 PRK15347
two component system sensor kinase;
8-184 1.39e-15

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 79.30  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLK----EIKALNPAIPVLIM 83
Cdd:PRK15347 693 ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQlwrdDPNNLDPDCMIVAL 772
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVG-KSPAMQHLLSEIALVAPSE 162
Cdd:PRK15347 773 TANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAEYQLLRGIELSPQDSSCSPLLDtDDMALNSKLYQSLLLLLAQ 852
                        170       180
                 ....*....|....*....|..
gi 16131834  163 ATVLIHgdsgtGKELVARAIHA 184
Cdd:PRK15347 853 IEQAVE-----NQEVLSQLLHT 869
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
8-107 5.71e-15

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: 70.26  E-value: 5.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd19926   1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd19926  81 SLDTAIEALKAGAFDFLTKP 100
PRK10610 PRK10610
chemotaxis protein CheY;
1-119 7.68e-15

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 70.77  E-value: 7.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGY-NVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN--PA 77
Cdd:PRK10610   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 16131834   78 IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:PRK10610  81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
8-107 8.51e-15

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: 70.10  E-value: 8.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALE---------QVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA- 77
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNklenlakegNDLSKELDLIITDIEMPKMDGYELTFELRD-DPRl 79
                        90       100       110
                ....*....|....*....|....*....|..
gi 16131834  78 --IPVLIMTAYSSVETAVEALKTGALDYLIKP 107
Cdd:cd19924  80 anIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
8-107 1.09e-14

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 70.19  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd17626   3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTAKS 81
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd17626  82 DTVDVVLGLESGADDYVAKP 101
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
8-121 1.76e-14

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: 69.37  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNpAIPVLIMTAYS 87
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd17614  80 SEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
8-107 2.57e-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: 2.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKaLNPA---IPVLIMT 84
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLR-KNADfdtIPVIFLT 79
                        90       100
                ....*....|....*....|...
gi 16131834  85 AYSSVETAVEALKTGALDYLIKP 107
Cdd:cd19927  80 AKGMTSDRIKGYNAGCDGYLSKP 102
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
6-119 6.47e-14

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: 67.95  E-value: 6.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDD-ISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMT 84
Cdd:cd17593   1 MKVLICDDSsMARKQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:cd17593  81 GDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEE 115
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
8-109 1.12e-13

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: 67.75  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDIShctILQALLR------GWGYNVALANSGRQALEQVRE-----QVFDLVLCDVRMAEMDGIATLKEIKALNP 76
Cdd:cd17595   3 ILTVDDDPQ---VLRAVARdlrrqyGKDYRVLRADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMELFP 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  77 AIPVLIMTAYSSVETAVEALKTGALD-YLIKPLD 109
Cdd:cd17595  80 EAKRVLLTAYADTDAAIRAINDVQLDyYLLKPWD 113
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
8-121 2.30e-13

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: 66.15  E-value: 2.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPaIPVLIMTAYS 87
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:cd18159  80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
8-107 2.64e-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: 65.60  E-value: 2.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTIL-QALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
Cdd:cd19928   1 ILVADDDRAIRTVLtQALGRA-GYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQ 79
                        90       100
                ....*....|....*....|.
gi 16131834  87 SSVETAVEALKTGALDYLIKP 107
Cdd:cd19928  80 NTLMTAVKAAERGAFEYLPKP 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
9-115 2.98e-13

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: 66.14  E-value: 2.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   9 LVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP--AIPVLIMTAY 86
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKtsSIPIIMLTAK 80
                        90       100
                ....*....|....*....|....*....
gi 16131834  87 SSVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd19937  81 GEEFDKVLGLELGADDYITKPFSPRELLA 109
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
8-107 3.21e-13

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 65.60  E-value: 3.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVR-EQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQqGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                        90       100
                ....*....|....*....|.
gi 16131834  87 SSVETAVEALKTGALDYLIKP 107
Cdd:cd18160  82 AAAAPELLSDAVGDNATLKKP 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
32-120 3.68e-13

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 65.64  E-value: 3.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  32 VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSsvETAVEALKTGALDYLIKPLDFD 111
Cdd:cd17532  27 VGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTAYD--EYAVEAFELNAVDYLLKPFSEE 104

                ....*....
gi 16131834 112 NLQATLEKA 120
Cdd:cd17532 105 RLAEALAKL 113
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
8-121 6.19e-13

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: 65.47  E-value: 6.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17596   3 ILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  88 SVETAVEALKTGAL-DYLIKPLDFDNLQATLEKAL 121
Cdd:cd17596  82 DSEDIIAGINEAGIyQYLTKPWHPDQLLLTVRNAA 116
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
5-139 1.11e-12

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 70.26  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK--ALNPAIPVLI 82
Cdd:PRK11107 667 PLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRqlPHNQNTPIIA 746
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131834   83 MTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQF 139
Cdd:PRK11107 747 VTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEPV 803
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
8-59 1.85e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 61.82  E-value: 1.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 16131834      8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRM 59
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMM 54
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
402-441 3.16e-12

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 60.48  E-value: 3.16e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 16131834   402 LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
8-107 3.95e-12

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: 62.65  E-value: 3.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK--ALNPAIPVLIMTA 85
Cdd:cd17618   3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIMLTA 82
                        90       100
                ....*....|....*....|..
gi 16131834  86 YSSVETAVEALKTGALDYLIKP 107
Cdd:cd17618  83 RGEEEDKVRGLEAGADDYITKP 104
PRK15479 PRK15479
transcriptional regulator TctD;
8-121 4.34e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 65.51  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDD--DISHCtiLQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:PRK15479   3 LLLAEDnrELAHW--LEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16131834   86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:PRK15479  81 RSAVADRVKGLNVGADDYLPKPFELEELDARLRALL 116
PRK10336 PRK10336
two-component system response regulator QseB;
8-125 4.39e-12

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 65.30  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTH 125
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPFALIEVAARLEALMRRTN 120
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
6-107 4.45e-12

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 62.92  E-value: 4.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV-FDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMT 84
Cdd:cd17544   1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIG 80
                        90       100
                ....*....|....*....|....*
gi 16131834  85 AYSSVETAVEA--LKTGALDYLIKP 107
Cdd:cd17544  81 ISASGDNALSArfIKAGANDFLTKP 105
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
8-115 8.10e-12

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: 61.68  E-value: 8.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17573   1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                        90       100
                ....*....|....*....|....*...
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd17573  81 KTEQEIEAFKEGADDYIAKPFDFKVLVA 108
PRK10643 PRK10643
two-component system response regulator PmrA;
8-115 1.04e-11

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 64.29  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDIshcTILQAL---LRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMT 84
Cdd:PRK10643   3 ILIVEDDT---LLLQGLilaLQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILT 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16131834   85 AYSSVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:PRK10643  80 ARDTLEDRVAGLDVGADDYLVKPFALEELHA 110
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
8-115 1.42e-11

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: 61.27  E-value: 1.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                        90       100
                ....*....|....*....|....*...
gi 16131834  88 SVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd17616  81 DIEDKVKGLGFGADDYMTKPFHKDELVA 108
PRK10693 PRK10693
two-component system response regulator RssB;
33-117 1.65e-11

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 65.01  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   33 ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPL-DFD 111
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVkDLN 80

                 ....*.
gi 16131834  112 NLQATL 117
Cdd:PRK10693  81 RLREMV 86
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
8-119 2.13e-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: 60.54  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd17594   2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA-RSDVPIIIISGDR 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131834  88 SVETA-VEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:cd17594  81 RDEIDrVVGLELGADDYLAKPFGLRELLARVRA 113
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
8-108 3.12e-11

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 60.46  E-value: 3.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALE-----------QVREQVFDLVLCDVRMAEMDGIATLKEIKALNP 76
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEflgledeedssNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 16131834  77 --AIPVLIMTAYSSVETAVEALKTGALDYLIKPL 108
Cdd:cd17581  81 lkEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
8-139 3.64e-11

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 62.67  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:PRK11083   6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTARS 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQF 139
Cdd:PRK11083  86 DEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRRVKKFAAPSPVIRIGHF 137
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
8-131 4.11e-11

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 62.63  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAET 131
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIES 126
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
8-107 4.70e-11

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 59.70  E-value: 4.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALnPAIPVLIMTAYS 87
Cdd:cd19938   2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRF-SDVPIIMVTARV 80
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd19938  81 EEIDRLLGLELGADDYICKP 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
8-109 5.12e-11

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 59.71  E-value: 5.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd17619   3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE-QSEVGIILVTGRD 81
                        90       100
                ....*....|....*....|..
gi 16131834  88 SVETAVEALKTGALDYLIKPLD 109
Cdd:cd17619  82 DEVDRIVGLEIGADDYVTKPFN 103
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
8-107 7.29e-11

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: 58.75  E-value: 7.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA-RSNVPVIMVTAKD 79
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd17621  80 SEIDKVVGLELGADDYVTKP 99
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
8-107 1.23e-10

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: 57.84  E-value: 1.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNpAIPVLIMTAYS 87
Cdd:cd19936   1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd19936  80 DEIDEVFGLRMGADDYITKP 99
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-302 1.47e-10

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.31  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    164 TVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEA-----DGGTLF 238
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAlarklKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131834    239 LDEIGDISPMMQVRLLRAIQERevqRVGSNQIISVDVRLIAATHR--DLAAEVNAGRFRQDLYYRL 302
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEEL---RLLLLLKSEKNLTVILTTNDekDLGPALLRRRFDRRIVLLL 146
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-119 1.98e-10

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 63.21  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834     4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
Cdd:PRK09959  957 EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGL 1036
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16131834    84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:PRK09959 1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQ 1072
PRK11517 PRK11517
DNA-binding response regulator HprR;
8-129 2.23e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 60.30  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNpAIPVLIMTAYS 87
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK-QTPVICLTARD 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDA 129
Cdd:PRK11517  82 SVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNS 123
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-107 2.23e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 61.70  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    6 IDILVVDDdishctilQALLRGW---------GYNV-ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN 75
Cdd:PRK00742   4 IRVLVVDD--------SAFMRRLiseilnsdpDIEVvGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLR 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131834   76 PaIPVLImtaYSSV-----ETAVEALKTGALDYLIKP 107
Cdd:PRK00742  76 P-TPVVM---VSSLtergaEITLRALELGAVDFVTKP 108
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
4-117 2.40e-10

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 62.68  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
Cdd:PRK10841 800 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGV 879
                         90       100       110
                 ....*....|....*....|....*....|....
gi 16131834   84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
Cdd:PRK10841 880 TANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTL 913
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
5-137 2.77e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 60.20  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNpAIPVLIMT 84
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS-AIPVIVLS 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16131834   85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTAS 137
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPAPDPLVKFS 132
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
8-114 2.86e-10

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: 57.27  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGY-NVALANSGRQALEQVREQVFDLVLCDVRMAE-MDGIATLKEIKaLNPAIP---VLI 82
Cdd:cd17589   1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELR-HKKLISpstVFI 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 16131834  83 M-TAYSSVETAVEALKTGALDYLIKPLDFDNLQ 114
Cdd:cd17589  80 MvTGESSRAMVLSALELEPDDYLLKPFTVSELR 112
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
5-107 3.07e-10

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: 57.23  E-value: 3.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   5 NIDILVVDDDISHCTILQALLrgwgyN-------VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN-- 75
Cdd:cd17561   1 KIKVLIADDNREFVQLLEEYL-----NsqpdmevVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRle 75
                        90       100       110
                ....*....|....*....|....*....|..
gi 16131834  76 PAIPVLIMTAYSSVETAVEALKTGALDYLIKP 107
Cdd:cd17561  76 KRPKIIMLTAFGQEDITQRAVELGASYYILKP 107
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
8-109 1.42e-09

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 55.46  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAiPVLIMTAYS 87
Cdd:cd17622   3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-PILLLTALD 81
                        90       100
                ....*....|....*....|..
gi 16131834  88 SVETAVEALKTGALDYLIKPLD 109
Cdd:cd17622  82 SDIDHILGLELGADDYVVKPVE 103
ompR PRK09468
osmolarity response regulator; Provisional
1-115 1.47e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 58.06  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
Cdd:PRK09468   1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPI 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 16131834   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:PRK09468  81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLA 115
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
32-122 4.67e-09

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: 53.89  E-value: 4.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  32 VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFD 111
Cdd:cd19931  27 VGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVTALRAGADGYLLKDMEPE 106
                        90
                ....*....|.
gi 16131834 112 NLQATLEKALA 122
Cdd:cd19931 107 DLLEALKQAAS 117
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
8-108 7.25e-09

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: 53.05  E-value: 7.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVAL--ANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:cd17565   1 FYIVDDDKNIIKILSDIIEDDDLGEVVgeADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80
                        90       100
                ....*....|....*....|...
gi 16131834  86 YSSVETAVEALKTGALDYLIKPL 108
Cdd:cd17565  81 VSDKEMIGKAYQAGIEFFINKPI 103
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-107 1.00e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 56.43  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    6 IDILVVDDDISHCTIL-QALLRGWGYNVA-LANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAiPVLIM 83
Cdd:PRK12555   1 MRIGIVNDSPLAVEALrRALARDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPC-PILIV 79
                         90       100
                 ....*....|....*....|....*...
gi 16131834   84 TaySSVETAV----EALKTGALDYLIKP 107
Cdd:PRK12555  80 T--SLTERNAsrvfEAMGAGALDAVDTP 105
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
8-107 1.00e-08

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 52.73  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQ-VFDLVLCDVRMA-EMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80
                        90       100
                ....*....|....*....|..
gi 16131834  86 YSSVETAVEALKTGaLDYLIKP 107
Cdd:cd18161  81 YAENAIEGGDLAPG-VDVLSKP 101
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
8-120 1.35e-08

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: 52.83  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGY-NVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
Cdd:cd17530   3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131834  87 -----SSVETAVEALKTGALDYLIKPLDFDNLQATLEKA 120
Cdd:cd17530  83 dggilESAETLAGANGLNLLGTLSKPFSPEELTELLTKY 121
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
6-71 2.01e-08

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 52.59  E-value: 2.01e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131834   6 IDILVVDDDISHCTILQALLRG-WGYNV-ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEI 71
Cdd:COG2197   2 IRVLIVDDHPLVREGLRALLEAePDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
8-107 3.00e-08

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: 51.61  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:cd19939   2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-HSHVPILMLTART 80
                        90       100
                ....*....|....*....|
gi 16131834  88 SVETAVEALKTGALDYLIKP 107
Cdd:cd19939  81 EEMDRVLGLEMGADDYLCKP 100
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
165-283 5.99e-08

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: 51.52  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   165 VLIHGDSGTGKELVARaiHASSARSEKPLVTLNCaalNESLLESELFGHEKGAfTGADKRREGRFVEA--DGGTLFLDEI 242
Cdd:pfam07728   2 VLLVGPPGTGKTELAE--RLAAALSNRPVFYVQL---TRDTTEEDLFGRRNID-PGGASWVDGPLVRAarEGEIAVLDEI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 16131834   243 GDISPMMQVRLLRAIQEREVQRVGSNQIISV---DVRLIAATHR 283
Cdd:pfam07728  76 NRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMNP 119
PRK10430 PRK10430
two-component system response regulator DcuR;
6-121 7.31e-08

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 53.19  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    6 IDILVVDDD-----ISHCTILQALlrgwGYN-VALANSGRQALEQV--REQVFDLVLCDVRMAEMDGIATLKEIKALNPA 77
Cdd:PRK10430   2 INVLIVDDDamvaeLNRRYVAQIP----GFQcCGTASTLEQAKEIIfnSDTPIDLILLDIYMQQENGLDLLPVLHEAGCK 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 16131834   78 IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFdnlqATLEKAL 121
Cdd:PRK10430  78 SDVIVISSAADAATIKDSLHYGVVDYLIKPFQA----SRFEEAL 117
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
8-117 8.78e-08

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: 50.48  E-value: 8.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALE--QVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAI--PVLI- 82
Cdd:cd19933   3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNllASAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRerPLIVa 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16131834  83 MTAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
Cdd:cd19933  83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
32-122 9.05e-08

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 52.34  E-value: 9.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   32 VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFD 111
Cdd:PRK10651  35 VGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPE 114
                         90
                 ....*....|.
gi 16131834  112 NLQATLEKALA 122
Cdd:PRK10651 115 DLLKALQQAAA 125
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
32-122 1.04e-07

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: 50.35  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  32 VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFD 111
Cdd:cd19930  27 VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIE 106
                        90
                ....*....|.
gi 16131834 112 NLQATLEKALA 122
Cdd:cd19930 107 ELADAIRTVHA 117
PRK13557 PRK13557
histidine kinase; Provisional
8-107 1.62e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 53.52  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV-FDLVLCDVRM-AEMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:PRK13557 418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPeVDLLFTDLIMpGGMNGVMLAREARRRQPKIKVLLTTG 497
                         90       100
                 ....*....|....*....|....*.
gi 16131834   86 YSsvETAVEalKTGA----LDYLIKP 107
Cdd:PRK13557 498 YA--EASIE--RTDAggseFDILNKP 519
dpiA PRK10046
two-component response regulator DpiA; Provisional
6-119 1.85e-07

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 51.56  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    6 IDILVVDDDISHCTILQALLRGW-GYN-VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
Cdd:PRK10046   5 LTLLIVEDETPLAEMHAEYIRHIpGFSqILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFT 84
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16131834   84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
Cdd:PRK10046  85 TAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTR 120
PRK10816 PRK10816
two-component system response regulator PhoP;
8-126 2.80e-07

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 51.28  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16131834   88 SVETAVEALKTGALDYLIKPLDFDNLQATLEkALAHTHS 126
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVMARMQ-ALMRRNS 120
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
404-439 4.53e-07

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


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 47.50  E-value: 4.53e-07
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16131834 404 EVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:COG2901  42 EVEKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKL 77
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
6-126 6.16e-07

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; 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 AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 48.39  E-value: 6.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   6 IDILVVDDDISH----CTILQALLRGWG--YNVALANSGRQALEQV----REQVFDLVLcDVRMAEMDGIATLKEIKALN 75
Cdd:cd17533   1 MNIFILEDDKIQrvrlEEIIENILKIENieYVIELTGKTEELLEKIkergKNGIYFLDI-DIKMEEKNGLEVAQKIRKYD 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131834  76 PAIPVLIMTAYSsvETAVEAL--KTGALDYLIKPLDFDNLQATLEKALAHTHS 126
Cdd:cd17533  80 PYAIIIFVTTHS--EFAPLTFeyKVAALDFILKPLKLEEFKKRIEECIKYAQK 130
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
8-121 9.46e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 49.72  E-value: 9.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK--ALNPAIPVLIMTA 85
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKreSMTRDIPVVMLTA 84
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16131834   86 YSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
PRK15369 PRK15369
two component system response regulator;
5-138 9.95e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 49.31  E-value: 9.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    5 NIDILVVDDdisHCTI---LQALLRGWG-YN-VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIP 79
Cdd:PRK15369   3 NYKILLVDD---HELIingIKNMLAPYPrYKiVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMN 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131834   80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDaetPAVTASQ 138
Cdd:PRK15369  80 ILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYID---PALNREA 135
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
8-115 1.88e-06

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: 46.92  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP--AIPVLIMTA 85
Cdd:cd17539   1 VLLVDDRPSSAERIAAMLSS-EHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERtrQLPILAVAD 79
                        90       100       110
                ....*....|....*....|....*....|
gi 16131834  86 YSSVETAVEALKTGALDYLIKPLDFDNLQA 115
Cdd:cd17539  80 PGDRGRLIRALEIGVNDYLVRPIDPNELLA 109
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
2-107 3.19e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 48.14  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    2 THDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNpAIPVL 81
Cdd:PRK10710   7 DENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-DIPIV 85
                         90       100
                 ....*....|....*....|....*.
gi 16131834   82 IMTAYSSVETAVEALKTGALDYLIKP 107
Cdd:PRK10710  86 MVTAKIEEIDRLLGLEIGADDYICKP 111
PLN03029 PLN03029
type-a response regulator protein; Provisional
8-113 5.52e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 47.34  E-value: 5.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQV--------------------REQVFDLVLCDVRMAEMDGIAT 67
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspnshQEVEVNLIITDYCMPGMTGYDL 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 16131834   68 LKEIKALNPA--IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNL 113
Cdd:PLN03029  91 LKKIKESSSLrnIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
PRK10766 PRK10766
two-component system response regulator TorR;
1-113 9.31e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 46.57  E-value: 9.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    1 MTHDnidILVVDDDIshctILQALLRGW----GYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP 76
Cdd:PRK10766   1 MSYH---ILVVEDEP----VTRARLQGYfeqeGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRST 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131834   77 AIPVLIMTAYSSVETAVeALKTGALDYLIKPLDFDNL 113
Cdd:PRK10766  74 VGIILVTGRTDSIDRIV-GLEMGADDYVTKPLELREL 109
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
7-138 1.98e-05

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 46.86  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGI---ATLKEIKALNPAIPVLIM 83
Cdd:PRK11091 527 NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLdiaRELRERYPREDLPPLVAL 606
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16131834   84 TAySSVETAVEALKTGALDYLIKPLDFDNLQATLEKaLAHTHSIDAETPAVTASQ 138
Cdd:PRK11091 607 TA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKK-FWDTQDDEESTVTTEESS 659
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
29-113 3.80e-05

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: 42.85  E-value: 3.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  29 GYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPL 108
Cdd:cd19922  22 GYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHWEDLQEELEEVQRFAVSYVVKPV 101

                ....*
gi 16131834 109 DFDNL 113
Cdd:cd19922 102 LISNL 106
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
8-107 4.49e-05

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 42.36  E-value: 4.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN--PAIPVLIMTA 85
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTG 80
                        90       100
                ....*....|....*....|..
gi 16131834  86 YSSVETAVEALKTGALDYLIKP 107
Cdd:cd17602  81 KDGLVDRIRAKMAGASGYLTKP 102
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
21-122 4.86e-05

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: 42.62  E-value: 4.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  21 LQALLRGWGYNVA-LANSGRQALEQVREQVFDLVLCDVRMAE-MDGIATLKEIKALNpAIPVLIMTAYSsvetavEALKT 98
Cdd:cd17540  16 LEQIVEDLGHQVVgIARTRDEAVALARRERPDLILADIQLADgSSGIDAVNEILTTH-DVPVIFVTAYP------ERLLT 88
                        90       100
                ....*....|....*....|....*...
gi 16131834  99 GA---LDYLI-KPLDFDNLQATLEKALA 122
Cdd:cd17540  89 GErpePTFLItKPFDPEMVKAAISQALF 116
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
39-131 1.04e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 43.33  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   39 RQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLE 118
Cdd:PRK09935  39 RITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQ 118
                         90
                 ....*....|...
gi 16131834  119 KALAHTHSIDAET 131
Cdd:PRK09935 119 MILSGYTFFPSET 131
PRK09191 PRK09191
two-component response regulator; Provisional
7-121 5.26e-04

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 41.76  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    7 DILVVDDDishcTI----LQALLRGWGYNVA-LANSGRQALEQVREQVFDLVLCDVRMAE-MDGIATLKEIKALNPaIPV 80
Cdd:PRK09191 139 RVLIIEDE----PIiamdLEQLVESLGHRVTgIARTRAEAVALAKKTRPGLILADIQLADgSSGIDAVNDILKTFD-VPV 213
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16131834   81 LIMTAYSsvetavEALKTGA---LDYLI-KPLDFDNLQATLEKAL 121
Cdd:PRK09191 214 IFITAFP------ERLLTGErpePAFLItKPFQPDTVKAAISQAL 252
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
8-137 9.96e-04

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 41.59  E-value: 9.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVRE--QVFDLVLCDVRMAEMDGIATLkeIKALNPAIPVLIMTA 85
Cdd:PRK13837 700 VLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKgpERFDLVLVDDRLLDEEQAAAA--LHAAAPTLPIILGGN 777
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16131834   86 ySSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTAS 137
Cdd:PRK13837 778 -SKTMALSPDLLASVAEILAKPISSRTLAYALRTALATARAAAARAEGTPAL 828
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
395-441 1.52e-03

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: 39.51  E-value: 1.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 16131834 395 QSQDIQPLVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
Cdd:COG4567 126 PPENPMSLDRLEWEHIQRVLAECDGNISATARALGMHRRTLQRKLAK 172
PRK14084 PRK14084
DNA-binding response regulator;
8-122 1.63e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 40.12  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGY--NVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTA 85
Cdd:PRK14084   3 ALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFATA 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16131834   86 YSSVetAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
Cdd:PRK14084  83 HDQF--AVKAFELNATDYILKPFEQKRIEQAVNKVRA 117
PRK11173 PRK11173
two-component response regulator; Provisional
8-107 1.77e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 39.61  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAIPVLIMTAYS 87
Cdd:PRK11173   6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE-QANVALMFLTGRD 84
                         90       100
                 ....*....|....*....|
gi 16131834   88 SVETAVEALKTGALDYLIKP 107
Cdd:PRK11173  85 NEVDKILGLEIGADDYITKP 104
PRK01905 PRK01905
Fis family transcriptional regulator;
402-439 3.45e-03

Fis family transcriptional regulator;


Pssm-ID: 179348 [Multi-domain]  Cd Length: 77  Bit Score: 36.32  E-value: 3.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 16131834  402 LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
Cdd:PRK01905  34 LSCVEKPLLEVVMEQAGGNQSLAAEYLGINRNTLRKKL 71
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
40-106 6.16e-03

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: 36.62  E-value: 6.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834  40 QALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMTAYSSVETAVEALKTGALDYLIK 106
Cdd:cd17575  36 EAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRA-NPAtrdIPIIVLSTKEEPEVKSEAFALGANDYLVK 104
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
8-106 8.09e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 37.69  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAiPVLIMTAYS 87
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG-PIVLLTSLD 82
                         90
                 ....*....|....*....
gi 16131834   88 SVETAVEALKTGALDYLIK 106
Cdd:PRK10701  83 SDMNHILALEMGACDYILK 101
PRK11697 PRK11697
two-component system response regulator BtsR;
41-119 8.88e-03

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 37.52  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131834   41 ALEQVREQVFDLVLCDVRMAEMDGiatLKEIKALNPA-IP-VLIMTAYSsvETAVEALKTGALDYLIKPLDFDNLQATLE 118
Cdd:PRK11697  39 AIGAIHRLKPDVVFLDIQMPRISG---LELVGMLDPEhMPyIVFVTAFD--EYAIKAFEEHAFDYLLKPIDPARLAKTLA 113

                 .
gi 16131834  119 K 119
Cdd:PRK11697 114 R 114
 
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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