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Conserved domains on  [gi|15600704|ref|NP_254198|]
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DNA-binding response regulator MifR [Pseudomonas aeruginosa PAO1]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-435 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: 526.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRlkeqaslkdqvDARLLGVSKPMEALRRQVLALAPT 164
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-----------DSGLIGRSPAMQEVRRLIEKVAPS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:COG2204 154 DATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDE 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:COG2204 234 IGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPL 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 325 LFEHFASVASQRLGREPqPAAPAELARLMAHDWPGNVRELANAAERHVLGLERGDAEEgggltSGLAERMEAFEAECLRQ 404
Cdd:COG2204 314 LARHFLARFAAELGKPV-KLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITA-----EDLPEALEEVERELIER 387
                       410       420       430
                ....*....|....*....|....*....|.
gi 15600704 405 ALGQCRGDIKAVMELLQLPRRTLNEKMLRHG 435
Cdd:COG2204 388 ALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-435 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: 526.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRlkeqaslkdqvDARLLGVSKPMEALRRQVLALAPT 164
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-----------DSGLIGRSPAMQEVRRLIEKVAPS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:COG2204 154 DATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDE 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:COG2204 234 IGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPL 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 325 LFEHFASVASQRLGREPqPAAPAELARLMAHDWPGNVRELANAAERHVLGLERGDAEEgggltSGLAERMEAFEAECLRQ 404
Cdd:COG2204 314 LARHFLARFAAELGKPV-KLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITA-----EDLPEALEEVERELIER 387
                       410       420       430
                ....*....|....*....|....*....|.
gi 15600704 405 ALGQCRGDIKAVMELLQLPRRTLNEKMLRHG 435
Cdd:COG2204 388 ALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
5-370 1.86e-124

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: 369.45  E-value: 1.86e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704     5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRlvlENRRLKEQASLKDQvDARLLGVSKPMEALRRQVLALAPT 164
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ---EQVALPADAGEAED-SAELIGEAPAMQEVFRAIGRLSRS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 15600704   325 LFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAER 370
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRW 362
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-436 1.60e-119

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 356.47  E-value: 1.60e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQASLKDQVdARLLGVSKPMEALRRQVLALAPT 164
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQW-GHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  325 LFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAERHVL--------------GLERGDAEEGGGLTS-- 388
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVmnsgpiifsedlppQIRQPVCNAGEVKTApv 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15600704  389 ---GLAERMEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHGL 436
Cdd:PRK11361 406 gerNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Sigma54_activat pfam00158
Sigma-54 interaction domain;
144-311 4.82e-101

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 298.55  E-value: 4.82e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTG 223
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   224 AQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVY 303
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 15600704   304 RLNVAELR 311
Cdd:pfam00158 161 RLNVIPIE 168
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
86-370 1.62e-84

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 268.67  E-value: 1.62e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   86 VPMAVEAMRQGAyDFIEKPFTPERLLGSLR---RALEKRRLVLENRRLKEQAS---LKDQVDARllgvSKPMEALRRQVL 159
Cdd:NF038308 122 WFLLVEARYLPA-RLLQTSPPRDKEEGTYEiidLDLSRYDALAQRFAREQAEAvsfLKSGIATR----NAAFNRLIEQIE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  160 ALAP-TPVNVLIRGETGSGKELVARCLHDFGPRADK---PFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHA 235
Cdd:NF038308 197 RVALrSRAPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAA 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  236 HGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPI 315
Cdd:NF038308 277 DGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGL 356
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  316 RERREDIPLLFEHFASVASQRLGR-----EPQPAAPAELARLMAHDWPGNVRELANAAER 370
Cdd:NF038308 357 RERREDIEPNLDYELDRFARELGRqvrfnKEARFRYLAFATSPEALWPGNFRELSASVTR 416
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
5-134 1.42e-78

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: 239.70  E-value: 1.42e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQA 134
Cdd:cd17549  81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
tetrathio_RR NF040749
tetrathionate respiration response regulator TtrR;
8-131 7.68e-23

tetrathionate respiration response regulator TtrR;


Pssm-ID: 468713 [Multi-domain]  Cd Length: 191  Bit Score: 95.50  E-value: 7.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:NF040749   5 VDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGSTLAVVFLTGHGDVP 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15600704   88 MAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLK 131
Cdd:NF040749  85 MAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIR 128
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-305 2.99e-11

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: 61.24  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    164 TPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFES---ELFGHESGAFTGAQGKRIG--KLEHAHGG 238
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600704    239 TLFLDEIESMPLAQQVKLLRVLQEqqlERLGSNQSIHVDLRVIAAT--KPDLLAEARAGRFREDLVYRL 305
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTndEKDLGPALLRRRFDRRIVLLL 146
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-435 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: 526.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRlkeqaslkdqvDARLLGVSKPMEALRRQVLALAPT 164
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE-----------DSGLIGRSPAMQEVRRLIEKVAPS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:COG2204 154 DATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDE 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:COG2204 234 IGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPL 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 325 LFEHFASVASQRLGREPqPAAPAELARLMAHDWPGNVRELANAAERHVLGLERGDAEEgggltSGLAERMEAFEAECLRQ 404
Cdd:COG2204 314 LARHFLARFAAELGKPV-KLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITA-----EDLPEALEEVERELIER 387
                       410       420       430
                ....*....|....*....|....*....|.
gi 15600704 405 ALGQCRGDIKAVMELLQLPRRTLNEKMLRHG 435
Cdd:COG2204 388 ALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
118-437 2.18e-139

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: 406.85  E-value: 2.18e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 118 LEKRRLVLENRRLKEQASLKDQVDArLLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFV 197
Cdd:COG3829 115 LKRLERKLREEELERGLSAKYTFDD-IIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGPFV 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 198 ALNCAAIPEQLFESELFGHESGAFTGA-QGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHV 276
Cdd:COG3829 194 AVNCAAIPENLLESELFGYEKGAFTGAkKGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPIPV 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 277 DLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPAAPAELARLMAHD 356
Cdd:COG3829 274 DVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLAYD 353
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 357 WPGNVRELANAAER-------HVLGLE-------RGDAEEGGGLTSGLAERMEAFEAECLRQALGQCRGDIKAVMELLQL 422
Cdd:COG3829 354 WPGNVRELENVIERavvlsegDVITPEhlpeyllEEAEAASAAEEGSLKEALEEVEKELIEEALEKTGGNKSKAAKALGI 433
                       330
                ....*....|....*
gi 15600704 423 PRRTLNEKMLRHGLS 437
Cdd:COG3829 434 SRSTLYRKLKKYGIK 448
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
5-370 1.86e-124

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: 369.45  E-value: 1.86e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704     5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRlvlENRRLKEQASLKDQvDARLLGVSKPMEALRRQVLALAPT 164
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQ---EQVALPADAGEAED-SAELIGEAPAMQEVFRAIGRLSRS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:TIGR01818 157 DITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:TIGR01818 237 IGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPR 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 15600704   325 LFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAER 370
Cdd:TIGR01818 317 LARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRW 362
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-436 1.60e-119

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 356.47  E-value: 1.60e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQASLKDQVdARLLGVSKPMEALRRQVLALAPT 164
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQW-GHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  325 LFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAERHVL--------------GLERGDAEEGGGLTS-- 388
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVmnsgpiifsedlppQIRQPVCNAGEVKTApv 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15600704  389 ---GLAERMEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHGL 436
Cdd:PRK11361 406 gerNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
5-437 9.34e-109

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 328.63  E-value: 9.34e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704     5 VIFVDDEATIREAVQqWlELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMP-----GMDGLQLLANLQAVDRDLPVIM 79
Cdd:TIGR02915   1 LLIVEDDLGLQKQLK-W-SFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    80 VTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLkeQASLKDQVDARLLGVSKPMEALRRQVL 159
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRL--QSALGGTALRGLITSSPGMQKICRTIE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   160 ALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGT 239
Cdd:TIGR02915 157 KIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   240 LFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERR 319
Cdd:TIGR02915 237 LFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   320 EDIPLLFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAERHV------------LGLERGDAEEGGGLT 387
Cdd:TIGR02915 317 GDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVimaegnqitaedLGLDARERAETPLEV 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15600704   388 SgLAERMEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHGLS 437
Cdd:TIGR02915 397 N-LREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGIK 445
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-433 6.23e-106

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 321.21  E-value: 6.23e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGH 83
Cdd:PRK10365   7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVlenrrlkeQASLKDQVDAR--LLGVSKPMEALRRQVLAL 161
Cdd:PRK10365  87 SSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSI--------DAETPAVTASQfgMVGKSPAMQHLLSEIALV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  162 APTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLF 241
Cdd:PRK10365 159 APSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  242 LDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERRED 321
Cdd:PRK10365 239 LDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRRED 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  322 IPLLFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAERHVLGL--------ERGDAEEGGGLTSGLAER 393
Cdd:PRK10365 319 IPLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLtgeyiserELPLAIASTPIPLGQSQD 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15600704  394 MEAF---EAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLR 433
Cdd:PRK10365 399 IQPLvevEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
5-366 3.25e-105

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 320.28  E-value: 3.25e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQASLKDqvdarLLGVSKPMEALRRQVLALAPT 164
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTTD-----IIGEAPAMQDVFRIIGRLSRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  165 PVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDE 244
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  245 IESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPL 324
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 15600704  325 LFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELAN 366
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLEN 362
PRK15115 PRK15115
response regulator GlrR; Provisional
2-441 7.27e-102

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 311.00  E-value: 7.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    2 SDQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVT 81
Cdd:PRK15115   5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   82 GHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLEnrrlkeqaslkDQVDARLLGVSKPMEALRRQVLAL 161
Cdd:PRK15115  85 AHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATD-----------ERWREAIVTRSPLMLRLLEQARMV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  162 APTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLF 241
Cdd:PRK15115 154 AQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLF 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  242 LDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERRED 321
Cdd:PRK15115 234 LDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTED 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  322 IPLLFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAERHV----------LGLERGDAEEGGGLTSgLA 391
Cdd:PRK15115 314 IPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCValtsspvisdALVEQALEGENTALPT-FV 392
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 15600704  392 ERMEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHGLSRSDF 441
Cdd:PRK15115 393 EARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDF 442
Sigma54_activat pfam00158
Sigma-54 interaction domain;
144-311 4.82e-101

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 298.55  E-value: 4.82e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTG 223
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   224 AQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVY 303
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 15600704   304 RLNVAELR 311
Cdd:pfam00158 161 RLNVIPIE 168
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
142-435 3.11e-100

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 312.22  E-value: 3.11e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 142 ARLLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAF 221
Cdd:COG3284 321 AALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAF 400
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 222 TGAQGK-RIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFRED 300
Cdd:COG3284 401 TGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFRED 480
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 301 LVYRLNVAELRLPPIRErREDIPLLFEHFAsvasQRLGREPQPA--APAELARLMAHDWPGNVRELANA-------AERH 371
Cdd:COG3284 481 LYYRLNGLTLTLPPLRE-REDLPALIEHLL----RELAAGRGPLrlSPEALALLAAYPWPGNVRELRNVlrtalalADGG 555
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 372 VLGLE------RGDAEEGGGLTSGLAERMEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHG 435
Cdd:COG3284 556 VITVEdlpdelRAELAAAAPAAAAPLTSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKRYG 625
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
112-438 1.70e-97

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 301.71  E-value: 1.70e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  112 GSLRRALEKRRLvlENRRLKEQASLKDQVDAR-----LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLH 186
Cdd:PRK05022 154 ATLRNALLIEQL--ESQAELPQDVAEFLRQEAlkegeMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIH 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  187 DFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLE 266
Cdd:PRK05022 232 AASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQ 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  267 RLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPAAP 346
Cdd:PRK05022 312 RVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSP 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  347 AELARLMAHDWPGNVREL------------ANAAER------HVLGLERGDA--------EEGGGLTSGLAERMEAFEAE 400
Cdd:PRK05022 392 AAQAALLAYDWPGNVRELehvisraallarARGAGRivtleaQHLDLPAEVAlpppeaaaAPAAVVSQNLREATEAFQRQ 471
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 15600704  401 CLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHGLSR 438
Cdd:PRK05022 472 LIRQALAQHQGNWAAAARALELDRANLHRLAKRLGLKD 509
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
119-370 1.15e-89

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: 282.37  E-value: 1.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   119 EKRRLVLENRRLKEQASLKDQVdarLLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVA 198
Cdd:TIGR01817 176 LSKQLRDKAPEIARRRSGKEDG---IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVK 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   199 LNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDL 278
Cdd:TIGR01817 253 VNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDV 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   279 RVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFAsvasQRLGREPQPA---APAELARLMAH 355
Cdd:TIGR01817 333 RLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFL----EKFNRENGRPltiTPSAIRVLMSC 408
                         250
                  ....*....|....*
gi 15600704   356 DWPGNVRELANAAER 370
Cdd:TIGR01817 409 KWPGNVRELENCLER 423
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
144-422 4.19e-88

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: 271.48  E-value: 4.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTG 223
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   224 AQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVY 303
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   304 RLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPA-APAELARLMAHDWPGNVRELANAAERHVLGLERGDA-- 380
Cdd:TIGR02974 161 RLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLFPGfTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEEApi 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600704   381 ---------------------------EEGGGLTSG--------LAERMEAFEAECLRQALGQCRGDIKAVMELLQL 422
Cdd:TIGR02974 241 deiiidpfaspwrpkqaapavdevnstPTDLPSPSSiaaafpldLKQAQQDYEIELLQQALAEAQFNQRKAAELLGL 317
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
129-404 1.18e-85

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 271.29  E-value: 1.18e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 129 RLKEQASLKDQVDAR----LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAI 204
Cdd:COG3283 187 RLGEQLQALQVNDDSgfdhIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAAL 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 205 PEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAAT 284
Cdd:COG3283 267 PDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICAT 346
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 285 KPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPAAPAELARLMAHDWPGNVREL 364
Cdd:COG3283 347 QKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQL 426
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600704 365 ANA-------AERHVLGLE------------RGDAEEGGgltsGLAERMEAFEAECLRQ 404
Cdd:COG3283 427 ENAlyravslLEGDELTPEdlqlpeyaasagLLDDLLEG----SLDEIVKRFERSLLRR 481
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
86-370 1.62e-84

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 268.67  E-value: 1.62e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   86 VPMAVEAMRQGAyDFIEKPFTPERLLGSLR---RALEKRRLVLENRRLKEQAS---LKDQVDARllgvSKPMEALRRQVL 159
Cdd:NF038308 122 WFLLVEARYLPA-RLLQTSPPRDKEEGTYEiidLDLSRYDALAQRFAREQAEAvsfLKSGIATR----NAAFNRLIEQIE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  160 ALAP-TPVNVLIRGETGSGKELVARCLHDFGPRADK---PFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHA 235
Cdd:NF038308 197 RVALrSRAPILLTGPTGAGKSFLARRIYELKKRRHQvsgPFVEVNCATLRGDLAMSELFGHVKGAFTGAQADRAGLLRAA 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  236 HGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPI 315
Cdd:NF038308 277 DGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLYARINLWTFRLPGL 356
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  316 RERREDIPLLFEHFASVASQRLGR-----EPQPAAPAELARLMAHDWPGNVRELANAAER 370
Cdd:NF038308 357 RERREDIEPNLDYELDRFARELGRqvrfnKEARFRYLAFATSPEALWPGNFRELSASVTR 416
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
144-431 4.15e-83

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 265.43  E-value: 4.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLH-----DFGPRADK---PFVALNCAAIPEQLFESELFG 215
Cdd:PRK15424 221 LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfaRHDARQGKkshPFVAVNCGAIAESLLEAELFG 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  216 HESGAFTGAQ-GKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARA 294
Cdd:PRK15424 301 YEEGAFTGSRrGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQ 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  295 GRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPAAPAELAR----LMAHDWPGNVRELANAAER 370
Cdd:PRK15424 381 GRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAPFSAALRQGLQQcetlLLHYDWPGNVRELRNLMER 460
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600704  371 HVLGLergDAEEGGGLT-----SGLAERME--------AFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKM 431
Cdd:PRK15424 461 LALFL---SVEPTPDLTpqflqLLLPELAResaktpapRLLAATLQQALERFNGDKTAAANYLGISRTTLWRRL 531
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
5-134 1.42e-78

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: 239.70  E-value: 1.42e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQA 134
Cdd:cd17549  81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
144-431 2.07e-78

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: 252.86  E-value: 2.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTG 223
Cdd:TIGR02329 214 LLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTG 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   224 A-QGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLV 302
Cdd:TIGR02329 294 ArRGGRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLF 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   303 YRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPAAPAELAR----LMAHDWPGNVRELANAAERHVLGLERG 378
Cdd:TIGR02329 374 YRLSILRIALPPLRERPGDILPLAAEYLVQAAAALRLPDSEAAAQVLAGvadpLQRYPWPGNVRELRNLVERLALELSAM 453
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600704   379 DA-----------------EEGGGLTSGLAERMEA-FEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKM 431
Cdd:TIGR02329 454 PAgaltpdvlralapelaeASGKGKTSALSLRERSrVEALAVRAALERFGGDRDAAAKALGISRTTLWRRL 524
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
120-379 3.79e-78

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 256.30  E-value: 3.79e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  120 KRRLVLENRRLKEQASLKDQVDARLLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVAL 199
Cdd:PRK15429 354 KERLVDENLALTEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKM 433
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  200 NCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLR 279
Cdd:PRK15429 434 NCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVR 513
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  280 VIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQpAAPAELARLMAH-DWP 358
Cdd:PRK15429 514 LIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNID-SIPAETLRTLSNmEWP 592
                        250       260
                 ....*....|....*....|.
gi 15600704  359 GNVRELANAAERHVLgLERGD 379
Cdd:PRK15429 593 GNVRELENVIERAVL-LTRGN 612
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
144-372 1.11e-74

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 236.88  E-value: 1.11e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHESGAFTG 223
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  224 AQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVY 303
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLD 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  304 RLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPA-APAELARLMAHDWPGNVRELANAAERHV 372
Cdd:PRK11608 168 RLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPLFPGfTERARETLLNYRWPGNIRELKNVVERSV 237
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
170-437 6.65e-73

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: 232.82  E-value: 6.65e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 170 IRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESelfghesgaftgaqgkrigklehahggtlfldeiesmp 249
Cdd:COG3604 120 ILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 250 laqqvkllrvLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHF 329
Cdd:COG3604 162 ----------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAEHF 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 330 ASVASQRLGREPQPAAPAELARLMAHDWPGNVRELANAAERHVLgLERGDAEEGGGLTSGLAERMEAFEAECLRQALGQC 409
Cdd:COG3604 232 LEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVI-LAEGGVLDADDLAPGSREALEEVEREHILEALERT 310
                       250       260
                ....*....|....*....|....*...
gi 15600704 410 RGDIKAVMELLQLPRRTLNEKMLRHGLS 437
Cdd:COG3604 311 GGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK10820 PRK10820
transcriptional regulator TyrR;
128-376 2.17e-62

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 210.70  E-value: 2.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  128 RRLKEQASLKDQVDARLLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQ 207
Cdd:PRK10820 190 RQLQNLAVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDD 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  208 LFESELFGHESGAFTGA-QGKRiGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKP 286
Cdd:PRK10820 270 VVESELFGHAPGAYPNAlEGKK-GFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQK 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  287 DLLAEARAGRFREDLVYRLNVAELRLPPIRERREDIPLLFEHFASVASQRLGRePQPAAPAEL-ARLMAHDWPGNVRELA 365
Cdd:PRK10820 349 NLVELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGV-PRPKLAADLnTVLTRYGWPGNVRQLK 427
                        250
                 ....*....|.
gi 15600704  366 NAAERHVLGLE 376
Cdd:PRK10820 428 NAIYRALTQLE 438
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
144-441 3.57e-52

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 185.65  E-value: 3.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  144 LLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGhesGAFTG 223
Cdd:PRK11388 327 MPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTD 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  224 AQGKRIGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVY 303
Cdd:PRK11388 404 SENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYY 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704  304 RLNVAELRLPPIRERREDIPLLFEHFASVASQRLGREPQPaAPAELARLMAHDWPGNVRELANAAER-------HVLGLE 376
Cdd:PRK11388 484 ALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLKI-DDDALARLVSYRWPGNDFELRSVIENlalssdnGRIRLS 562
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600704  377 R----------GDAEEGGGLTSGLAerMEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKMLRHGLSRSDF 441
Cdd:PRK11388 563 DlpehlfteqaTDDVSATRLSTSLS--LAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQF 635
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
5-134 2.06e-43

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: 151.02  E-value: 2.06e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:COG4566   2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQA 134
Cdd:COG4566  82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAEL 131
fixJ PRK09390
response regulator FixJ; Provisional
5-159 1.50e-40

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 143.60  E-value: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:PRK09390   6 VHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHG 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600704   85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRrlvleNRRLKEQASLKDqVDARLLGVSkPMEalrRQVL 159
Cdd:PRK09390  86 DVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQA-----PEAAKSEAVAAD-IRARIASLS-ERE---RQVM 150
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
8-118 8.66e-40

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: 138.88  E-value: 8.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:cd17537   6 VDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHGDVP 85
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  88 MAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17537  86 MAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
8-119 3.16e-38

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: 134.55  E-value: 3.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:cd17550   4 VDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHGTIE 83
                        90       100       110
                ....*....|....*....|....*....|..
gi 15600704  88 MAVEAMRQGAYDFIEKPFTPERLLGSLRRALE 119
Cdd:cd17550  84 TAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
168-368 6.12e-36

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: 139.20  E-value: 6.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 168 VLIRGETGSGKELVARCL-------HDFgpraDKPFVALNCAAIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGTL 240
Cdd:COG4650 211 ILLTGPTGAGKSQLARRIyelkkarHQV----SGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRSADGGVL 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 241 FLDEIESMPLAQQVKLLRVLQEQQLERLGSNQSIHVDLRVIAATKPDLLAEARAGRFREDLVYRLNVAELRLPPIRERRE 320
Cdd:COG4650 287 FLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPGLAERRE 366
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600704 321 DIPLLFEHFASVASQRLGREP---------------QPAAPaelarlmahdWPGNVRELaNAA 368
Cdd:COG4650 367 DIEPNLDYELARFAREQGRRVrfnkeararylafatSPEAL----------WSGNFRDL-NAS 418
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
5-115 3.03e-34

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: 123.80  E-value: 3.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704     5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 15600704    85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLR 115
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
5-133 1.84e-30

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: 117.19  E-value: 1.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVD--RDLPVIMVTG 82
Cdd:COG3437   9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPstRDIPVIFLTA 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQ 133
Cdd:COG3437  89 LADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLY 139
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
8-104 8.76e-30

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: 111.55  E-value: 8.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:cd00156   3 VDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADEE 82
                        90
                ....*....|....*..
gi 15600704  88 MAVEAMRQGAYDFIEKP 104
Cdd:cd00156  83 DAVRALELGADDYLVKP 99
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
5-123 2.14e-28

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: 108.44  E-value: 2.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRL 123
Cdd:cd17572  81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKL 119
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
3-118 5.57e-28

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: 106.97  E-value: 5.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd19919   1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd19919  81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
8-122 3.32e-27

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: 107.73  E-value: 3.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:COG0745   7 VEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARDDEE 86
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600704  88 MAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRR 122
Cdd:COG0745  87 DRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
5-122 5.31e-27

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: 104.93  E-value: 5.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQA--VDRDLPVIMVTG 82
Cdd:COG0784   8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAlpRLPDIPIIALTA 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRR 122
Cdd:COG0784  88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
167-366 1.90e-26

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: 112.51  E-value: 1.90e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 167 NVLIRGETGSGKELVARCLHDFGPR-----ADKPFVALNCA--AIPEQLFESELFGHESGAFTGAQGKRIGKLEHAHGGT 239
Cdd:COG1221 132 HTLILGPTGVGKSFFAELMYEYAIEigvlpEDAPFVVFNCAdyANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGI 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 240 LFLDEIESMPLAQQVKLLRVLQEQQLERLG-SNQSIHVDLRVIAAT--KPD--LLAEaragrFredlvyrlnvaeLR--- 311
Cdd:COG1221 212 LFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATteDPEssLLKT-----F------------LRrip 274
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600704 312 ----LPPIRER----REDiplLFEHFASVASQRLGREPQPAAPAeLARLMAHDWPGNVRELAN 366
Cdd:COG1221 275 mvikLPSLEERsleeRLE---LIKHFFKEEAKRLNKPIKVSKEV-LKALLLYDCPGNIGQLKS 333
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
5-104 9.88e-26

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 100.62  E-value: 9.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLE-LSGFE-VRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEwEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                        90       100
                ....*....|....*....|..
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKP 104
Cdd:COG4753  82 YSDFEYAQEAIKLGADDYLLKP 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
5-129 4.14e-25

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 100.04  E-value: 4.14e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLE-LSGFE-VRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:COG4565   6 VLIVEDDPMVAELLRRYLErLPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITA 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRR 129
Cdd:COG4565  86 ARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
5-120 7.20e-25

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 98.56  E-value: 7.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQ---WLELsGFEVrlCLRA---EECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVI 78
Cdd:cd17536   1 VLIVDDEPLIREGLKKlidWEEL-GFEV--VGEAengEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKII 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15600704  79 MVTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEK 120
Cdd:cd17536  78 ILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
5-111 2.22e-24

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: 99.21  E-value: 2.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDR--DLPVIMVTG 82
Cdd:COG3706   4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRtaDIPIIFLTA 83
                        90       100
                ....*....|....*....|....*....
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLL 111
Cdd:COG3706  84 LDDEEDRARALEAGADDYLTKPFDPEELL 112
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
5-119 3.19e-23

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: 94.01  E-value: 3.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGYA 82
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  85 DVPMAVEAMRQGA-YDFIEKPFTPERLLGSLRRALE 119
Cdd:cd17569  83 DLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
tetrathio_RR NF040749
tetrathionate respiration response regulator TtrR;
8-131 7.68e-23

tetrathionate respiration response regulator TtrR;


Pssm-ID: 468713 [Multi-domain]  Cd Length: 191  Bit Score: 95.50  E-value: 7.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:NF040749   5 VDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGSTLAVVFLTGHGDVP 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15600704   88 MAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLK 131
Cdd:NF040749  85 MAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIR 128
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
145-315 8.74e-22

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 90.86  E-value: 8.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   145 LGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESelfghesgaftga 224
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   225 qgkrigklehAHGGTLFLDEIESMPLAQQVKLLRVLQEQQLERlgsnqsihvdLRVIAATKPDLLAEARAGRFREDLVYR 304
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAEGYR----------VRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 15600704   305 LNVAELRLPPI 315
Cdd:pfam14532 128 LSALRLHVPPL 138
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
151-314 3.35e-21

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: 89.51  E-value: 3.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 151 MEALRRQVLALA--PTPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFESELFGHEsgaftgAQGKR 228
Cdd:cd00009   3 QEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 229 IGKLEHAHGGTLFLDEIESMPLAQQVKLLRVLQEqqlerLGSNQSIHVDLRVIAATKPDLLaearaGRFREDLVYRLNVa 308
Cdd:cd00009  77 FELAEKAKPGVLFIDEIDSLSRGAQNALLRVLET-----LNDLRIDRENVRVIGATNRPLL-----GDLDRALYDRLDI- 145

                ....*.
gi 15600704 309 ELRLPP 314
Cdd:cd00009 146 RIVIPL 151
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
5-117 3.61e-21

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: 88.41  E-value: 3.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17555   3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTP-ERLLGSLRRA 117
Cdd:cd17555  83 VMSDAVEALRLGAWDYLTKPIEDlAVLEHAVRRA 116
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-119 3.73e-21

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 88.31  E-value: 3.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   1 MSDQVIFVDDEATIREAVQQWLELSGFEVRLclrAEECLGALDKSFAG---VVISDVRMPGMDGLQLLANLQAVDRDLPV 77
Cdd:COG5803   1 MMKKILIVDDQAGIRMLLKEVLKKEGYEVFQ---AANGKEALEKVKELkpdLVLLDMKMPGMDGIEILKEIKEIDPDIPV 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15600704  78 IMVTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALE 119
Cdd:COG5803  78 IMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
5-127 4.82e-21

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 89.98  E-value: 4.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:COG4567   7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGYA 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLEN 127
Cdd:COG4567  87 SIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPEN 129
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
5-145 1.01e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 90.65  E-value: 1.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLE-LSGFE-VRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:COG3279   4 ILIVDDEPLARERLERLLEkYPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600704  83 HGDvpMAVEAMRQGAYDFIEKPFTPERllgsLRRALEKrrlVLENRRLKEQASLKDQVDARLL 145
Cdd:COG3279  84 YDE--YALEAFEVNAVDYLLKPIDEER----LAKALEK---AKERLEAKAAAEASPEEKDRIF 137
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
8-104 5.90e-19

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: 81.69  E-value: 5.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVP 87
Cdd:cd17574   3 VEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDEEE 82
                        90
                ....*....|....*..
gi 15600704  88 MAVEAMRQGAYDFIEKP 104
Cdd:cd17574  83 DKVLGLELGADDYITKP 99
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
5-118 2.58e-18

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: 80.42  E-value: 2.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL--QAVDRDLPVIMVTG 82
Cdd:cd17562   3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELrkLPAYKFTPILMLTT 82
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17562  83 ESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
5-114 5.39e-18

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: 79.41  E-value: 5.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDK-SFAGVVIsDVRMPGMDGLQLLANLQAVDRDLPVIMVTGH 83
Cdd:cd17563   3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREeKPDYAVL-DLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSL 114
Cdd:cd17563  82 ASIATAVEAIKLGADDYLAKPADADEILAAL 112
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
5-110 7.18e-18

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: 79.21  E-value: 7.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALD--KSFAGVVISDVRMPGMDGLQLLANLQAVdRDLPVIMVTG 82
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                        90       100
                ....*....|....*....|....*...
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERL 110
Cdd:cd17584  80 DGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
4-118 1.95e-17

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 77.70  E-value: 1.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLELSGFEVrlCLRAEECLGALDKSFA---GVVISDVRMPGMDGLQLLANLQAVDRDLPVIMV 80
Cdd:cd17542   2 KVLIVDDAAFMRMMLKDILTKAGYEV--VGEAANGEEAVEKYKElkpDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMC 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15600704  81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17542  80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
5-110 2.48e-17

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 77.76  E-value: 2.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEvrLCLRAEECLGALDKSFAG---VVISDVRMPGMDGLQLLANLQAVDR--DLPVIM 79
Cdd:cd19923   3 VLVVDDFSTMRRIIKNLLKELGFN--NVEEAEDGVDALEKLKAGgfdFVITDWNMPNMDGLELLKTIRADGAlsHLPVLM 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  80 VTGHGDVPMAVEAMRQGAYDFIEKPFTPERL 110
Cdd:cd19923  81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
5-119 3.15e-17

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: 77.17  E-value: 3.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLEL-SGFE-VRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESePDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALE 119
Cdd:cd17535  81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
4-111 4.79e-17

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: 76.71  E-value: 4.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLE-LSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAV--DRDLPVIMV 80
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRsAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVMI 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLL 111
Cdd:cd17551  82 TADTDREVRLRALEAGATDFLTKPFDPVELL 112
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
5-122 5.05e-17

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: 76.57  E-value: 5.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDrDLPVIMVTGHG 84
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS-QVPVLMLTARG 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALekRR 122
Cdd:cd17623  80 DDIDRILGLELGADDYLPKPFNPRELVARIRAIL--RR 115
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
5-121 1.04e-16

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: 75.88  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLrRALEKR 121
Cdd:cd17627  81 SVSDRVAGLDAGADDYLVKPFALEELLARV-RALLRR 116
orf27 CHL00148
Ycf27; Reviewed
4-117 1.78e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 78.60  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGH 83
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK-ESDVPIIMLTAL 86
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPFTP----ERLLGSLRRA 117
Cdd:CHL00148  87 GDVSDRITGLELGADDYVVKPFSPkeleARIRSVLRRT 124
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
5-104 2.06e-16

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: 74.34  E-value: 2.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL--QAVDRDLPVIMVTG 82
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLrkNADFDTIPVIFLTA 80
                        90       100
                ....*....|....*....|..
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKP 104
Cdd:cd19927  81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
8-121 2.33e-16

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: 74.95  E-value: 2.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEEclgALDKSFAG---VVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17625   3 VEDEKDLSEAITKHLKKEGYTVDVCFDGEE---GLEYALSGiydLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALD 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLrRALEKR 121
Cdd:cd17625  80 AVEDRVKGLDLGADDYLPKPFSLAELLARI-RALLRR 115
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
5-117 2.74e-16

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: 74.70  E-value: 2.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPE----RLLGSLRRA 117
Cdd:cd17615  82 SVEDRIAGLTAGGDDYVTKPFSLEevvaRLRALLRRS 118
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
3-130 3.76e-16

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: 74.71  E-value: 3.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   3 DQVIFVDDEATIREAVQQWLElSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd17596   1 PTILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15600704  83 HGDVPMAVEAMRQ-GAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRL 130
Cdd:cd17596  80 YTDSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERL 128
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
3-115 1.81e-15

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 72.28  E-value: 1.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL--QAVDRDLPVIMV 80
Cdd:cd17618   1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLkrDEMTRDIPIIML 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600704  81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLR 115
Cdd:cd17618  81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-143 1.88e-15

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 74.61  E-value: 1.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   1 MSDQVIFVDDEATIREAVQQWLELSGFEVrlCLRAEECLGALDKSFA---GVVISDVRMPGMDGLQLLANLQAvDRDLPV 77
Cdd:COG3707   2 RGLRVLVVDDEPLRRADLREGLREAGYEV--VAEAADGEDAVELVRElkpDLVIVDIDMPDRDGLEAARQISE-ERPAPV 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600704  78 IMVTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRlvlENRRL-KEQASLKDQVDAR 143
Cdd:COG3707  79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFR---ELRALrRELAKLREALEER 142
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-152 5.07e-15

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 73.98  E-value: 5.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    1 MSDQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL--QAVDRDLPVI 78
Cdd:PRK10161   1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLkrESMTRDIPVV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600704   79 MVTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQASLKDQVDARLLGVSKPME 152
Cdd:PRK10161  81 MLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLDPTSHRVMAGEEPLE 154
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
8-111 7.12e-15

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: 70.77  E-value: 7.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL--QAVDRDLPVIMVTGHGD 85
Cdd:cd19937   3 VDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILrsDPKTSSIPIIMLTAKGE 82
                        90       100
                ....*....|....*....|....*.
gi 15600704  86 VPMAVEAMRQGAYDFIEKPFTPERLL 111
Cdd:cd19937  83 EFDKVLGLELGADDYITKPFSPRELL 108
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
8-85 9.89e-15

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: 69.94  E-value: 9.89e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGD 85
Cdd:cd17554   6 VDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYSE 83
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
8-111 2.35e-14

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: 69.04  E-value: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGAL-DKSFAgVVISDVRMPGMDGLQL---LANLQAVDRDLPVIMVTGH 83
Cdd:cd17546   4 VDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLkEEPFD-LVLMDLQMPVMDGLEAtrrIRELEGGGRRTPIIALTAN 82
                        90       100
                ....*....|....*....|....*...
gi 15600704  84 GDVPMAVEAMRQGAYDFIEKPFTPERLL 111
Cdd:cd17546  83 ALEEDREKCLEAGMDDYLSKPVKLDQLK 110
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
8-104 4.14e-14

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 67.86  E-value: 4.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDrDLPVIMVTGHGDVP 87
Cdd:cd19936   4 VDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKDDEI 82
                        90
                ....*....|....*..
gi 15600704  88 MAVEAMRQGAYDFIEKP 104
Cdd:cd19936  83 DEVFGLRMGADDYITKP 99
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
5-118 5.65e-14

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 68.12  E-value: 5.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVD--RDLPVIMVTG 82
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPdlKDIPVILLTT 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17598  81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
8-114 6.12e-14

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: 67.87  E-value: 6.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL--QAVDRDLPVIMVTGHGD 85
Cdd:cd17580   4 VDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLreLPWLANTPAIALTGYGQ 83
                        90       100
                ....*....|....*....|....*....
gi 15600704  86 VPMAVEAMRQGAYDFIEKPFTPERLLGSL 114
Cdd:cd17580  84 PEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
4-118 8.66e-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: 67.49  E-value: 8.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGH 83
Cdd:cd17626   2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTAK 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600704  84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17626  81 SDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
5-121 8.71e-14

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: 67.69  E-value: 8.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLrRALEKR 121
Cdd:cd19934  81 SWQDKVEGLDAGADDYLTKPFHIEELLARL-RALIRR 116
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
8-124 1.12e-13

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 67.42  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLE-LSGFEVRLCLR-AEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVdRDLPVIMVTGH-- 83
Cdd:cd17541   6 VDDSAVMRKLLSRILEsDPDIEVVGTARdGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE-RPTPVVMVSSLte 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15600704  84 GDVPMAVEAMRQGAYDFIEKPftpeRLLGSLRRALEKRRLV 124
Cdd:cd17541  85 EGAEITLEALELGAVDFIAKP----SGGISLDLEEIAEELI 121
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
5-105 2.44e-13

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: 65.98  E-value: 2.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVD--RDLPVIMVTG 82
Cdd:cd17538   2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPetRHIPVIMITA 81
                        90       100
                ....*....|....*....|...
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPF 105
Cdd:cd17538  82 LDDREDRIRGLEAGADDFLSKPI 104
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
5-110 2.46e-13

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 66.39  E-value: 2.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFA-GVVISDVRMPGMDGLQLLANL-QAVDRD-LPVIMVT 81
Cdd:cd17544   3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDiKLVITDYNMPEMDGFELVREIrKKYSRDqLAIIGIS 82
                        90       100
                ....*....|....*....|....*....
gi 15600704  82 GHGDVPMAVEAMRQGAYDFIEKPFTPERL 110
Cdd:cd17544  83 ASGDNALSARFIKAGANDFLTKPFLPEEF 111
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
4-118 2.93e-13

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 66.04  E-value: 2.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLE-LSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQA--VDRDLPVIMV 80
Cdd:cd17552   3 RILVIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQAnpETQSIPVILL 82
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15600704  81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17552  83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
5-122 4.01e-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: 4.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLE-LSGFE-VRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEeHPDIEiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15600704  83 HGDvpMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRR 122
Cdd:cd17532  81 YDE--YAVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
5-115 5.42e-13

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: 65.20  E-value: 5.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLR 115
Cdd:cd17624  81 GVDDRVAGLDAGADDYLVKPFALEELLARLR 111
ompR PRK09468
osmolarity response regulator; Provisional
3-121 6.94e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 68.08  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:PRK09468   6 YKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTA 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15600704   83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKR 121
Cdd:PRK09468  86 KGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQ 124
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
3-120 8.71e-13

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 64.88  E-value: 8.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd17553   1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTperlLGSLRRALEK 120
Cdd:cd17553  81 YGELDMIQESKELGALTHFAKPFD----IDEIRDAVKK 114
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
8-105 8.89e-13

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: 64.07  E-value: 8.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVD--RDLPVIMVTGHGD 85
Cdd:cd19920   4 VDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPatRHIPVIFLTALTD 83
                        90       100
                ....*....|....*....|
gi 15600704  86 VPMAVEAMRQGAYDFIEKPF 105
Cdd:cd19920  84 TEDKVKGFELGAVDYITKPF 103
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
5-104 2.52e-12

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: 62.94  E-value: 2.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd19926   1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                        90       100
                ....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKP 104
Cdd:cd19926  81 SLDTAIEALKAGAFDFLTKP 100
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
5-122 2.73e-12

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: 63.42  E-value: 2.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLE-LSGFEV-RLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd19925   3 VLIVEDDPMVAEIHRAYVEqVPGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERllgsLRRALEKRR 122
Cdd:cd19925  83 ANDVETVREALRLGVVDYLIKPFTFER----LRQRLERYR 118
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
5-104 3.07e-12

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: 62.52  E-value: 3.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                        90       100
                ....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKP 104
Cdd:cd19928  81 TLMTAVKAAERGAFEYLPKP 100
PRK10610 PRK10610
chemotaxis protein CheY;
6-120 3.39e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 63.45  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    6 IFVDDEATIREAVQQWLELSGFEVrlCLRAEECLGALDKSFAG---VVISDVRMPGMDGLQLLANLQAVDR--DLPVIMV 80
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLKELGFNN--VEEAEDGVDALNKLQAGgfgFVISDWNMPNMDGLELLKTIRADGAmsALPVLMV 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15600704   81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEK 120
Cdd:PRK10610  87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
5-104 3.55e-12

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: 62.46  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEEclgALDKSFAG---VVISDVRMPGMDGLQLLANLQAVDRDLPVIMVT 81
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGED---GLHLALTNeydLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLT 77
                        90       100
                ....*....|....*....|...
gi 15600704  82 GHGDVPMAVEAMRQGAYDFIEKP 104
Cdd:cd19935  78 ARDSVEDRVKGLDLGADDYLVKP 100
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-305 2.99e-11

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: 61.24  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    164 TPVNVLIRGETGSGKELVARCLHDFGPRADKPFVALNCAAIPEQLFES---ELFGHESGAFTGAQGKRIG--KLEHAHGG 238
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600704    239 TLFLDEIESMPLAQQVKLLRVLQEqqlERLGSNQSIHVDLRVIAAT--KPDLLAEARAGRFREDLVYRL 305
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEE---LRLLLLLKSEKNLTVILTTndEKDLGPALLRRRFDRRIVLLL 146
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
5-115 4.90e-11

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 59.77  E-value: 4.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCL-RAEECLGALDKSfAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGH 83
Cdd:cd17594   2 VLVVDDDAAMRHLLILYLRERGFDVTAAAdGAEEARLMLHRR-VDLVLLDLRLGQESGLDLLRTIRA-RSDVPIIIISGD 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15600704  84 GDVPMA-VEAMRQGAYDFIEKPFTPERLLGSLR 115
Cdd:cd17594  80 RRDEIDrVVGLELGADDYLAKPFGLRELLARVR 112
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
5-105 8.17e-11

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: 58.67  E-value: 8.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRlclRAEECLGALDKSFAG----VVISDVRMPGMDGLQLLANLQAVDRDLPVIMV 80
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVT---EAESGAEALEKLQQGkdidIVVTDIVMPEMDGIELAREARKIDPDVKILFI 78
                        90       100
                ....*....|....*....|....*
gi 15600704  81 TGHGDVPMAVEAMRQGAYDFIEKPF 105
Cdd:cd18160  79 SGGAAAAPELLSDAVGDNATLKKPF 103
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-121 9.25e-11

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 61.52  E-value: 9.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    1 MSDQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMV 80
Cdd:PRK11083   2 QQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15600704   81 TGHGDVPMAVEAMRQGAYDFIEKPFTPeRLLGSLRRALEKR 121
Cdd:PRK11083  82 TARSDEVDRLVGLEIGADDYVAKPFSP-REVAARVRTILRR 121
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
3-111 1.09e-10

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: 58.55  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRdLPVIMVTG 82
Cdd:cd17619   1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE-VGIILVTG 79
                        90       100
                ....*....|....*....|....*....
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLL 111
Cdd:cd17619  80 RDDEVDRIVGLEIGADDYVTKPFNPRELL 108
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
3-118 2.26e-10

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: 57.77  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVdRDLPVIMVTG 82
Cdd:cd17622   1 TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTA 79
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17622  80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
3-169 3.70e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 59.82  E-value: 3.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    3 DQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFaGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTG 82
Cdd:PRK10955   2 NKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDTLKELRQ-THQTPVIMLTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLrRALEKRRLVLENRRLKEQASLKDQVDARLLGVSKPMEALRRQVLALA 162
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELVARI-RAILRRSHWSEQQQNNDNGSPTLEVDALSLNPGRQEASFDGQTLELT 158

                 ....*..
gi 15600704  163 PTPVNVL 169
Cdd:PRK10955 159 GTEFTLL 165
PRK15479 PRK15479
transcriptional regulator TctD;
4-132 6.71e-10

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 58.96  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLC---LRAEECLgaLDKSFAgVVISDVRMPGMDGLQLLANLQAVDRDLPVIMV 80
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVfdgLAADHLL--QSEMYA-LAVLDINMPGMDGLEVLQRLRKRGQTLPVLLL 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15600704   81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLrRALEKRR--LVLENRRLKE 132
Cdd:PRK15479  79 TARSAVADRVKGLNVGADDYLPKPFELEELDARL-RALLRRSagQVQEVQQLGE 131
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
4-110 2.45e-09

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 54.85  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWL-ELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTg 82
Cdd:cd17593   2 KVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS- 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15600704  83 hGDV-PMAVE-AMRQGAYDFIEKPFTPERL 110
Cdd:cd17593  81 -GDVqPEAKErVLELGALAFLKKPFDPEKL 109
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
5-104 4.39e-09

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 53.74  E-value: 4.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDrDLPVIMVTGHG 84
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTAKD 79
                        90       100
                ....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKP 104
Cdd:cd17621  80 SEIDKVVGLELGADDYVTKP 99
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
5-116 1.00e-08

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: 52.93  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVD--RDLPVIMVTG 82
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPatRDIPVIALTA 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  83 H---GDVPMAVEAmrqGAYDFIEKPFTPERLLGSLRR 116
Cdd:cd17548  82 YamkGDREKILEA---GCDGYISKPIDTREFLETVAK 115
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
5-104 1.26e-08

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: 52.77  E-value: 1.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAG---------VVISDVRMPGMDGLQLLANLQAVDR-- 73
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEgndlskeldLIITDIEMPKMDGYELTFELRDDPRla 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  74 DLPVIMVTGHGDVPMAVEAMRQGAYDFIEKP 104
Cdd:cd19924  81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
4-118 1.62e-08

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 52.38  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDrDLPVIMVTGH 83
Cdd:cd19938   1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-DVPIIMVTAR 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600704  84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd19938  80 VEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
5-120 1.79e-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: 52.38  E-value: 1.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGHG 84
Cdd:cd19939   2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-HSHVPILMLTART 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEK 120
Cdd:cd19939  81 EEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
4-120 2.07e-08

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: 52.42  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLELSGFEVRLCLR-AEECLGALDKSFAGVVISDVRMPGMDGLQLlANLQAVDRDLPVIMVTG 82
Cdd:cd19932   2 RVLIAEDEALIRMDLREMLEEAGYEVVGEASdGEEAVELAKKHKPDLVIMDVKMPRLDGIEA-AKIITSENIAPIVLLTA 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEK 120
Cdd:cd19932  81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
PRK11517 PRK11517
DNA-binding response regulator HprR;
4-131 3.27e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 54.13  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLG-ALDKSFAgVVISDVRMPGMDGLQLLANLQAVDRDlPVIMVTG 82
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYlALKDDYA-LIILDIMLPGMDGWQILQTLRTAKQT-PVICLTA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15600704   83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALekRRLVLENRRLK 131
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL--RQHHALNSTLE 126
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-110 3.50e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 55.16  E-value: 3.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLEL-SGFEVrlCLRAEECLGALDKSFA---GVVISDVRMPGMDGLQLLANLQAVdRDLPVIM 79
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEILNSdPDIEV--VGTAPDGLEAREKIKKlnpDVITLDVEMPVMDGLDALEKIMRL-RPTPVVM 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15600704   80 V---TGHG-DVPMavEAMRQGAYDFIEKPFTPERL 110
Cdd:PRK00742  82 VsslTERGaEITL--RALELGAVDFVTKPFLGISL 114
PRK10766 PRK10766
two-component system response regulator TorR;
1-140 3.68e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 53.89  E-value: 3.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    1 MSDQVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMV 80
Cdd:PRK10766   1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS-RSTVGIILV 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVlenRRLKEQASLKDQV 140
Cdd:PRK10766  80 TGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLLWRISLA---RQAQPHAQEEDNC 136
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
8-118 4.14e-08

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 51.25  E-value: 4.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEV-RLCLRAEECLGALDKSFAGVVISDVRMPG-MDGLQLLANLQAvDRDLPVIMVTGHGD 85
Cdd:cd17534   6 VEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIRE-KFDIPVIFLTAYSD 84
                        90       100       110
                ....*....|....*....|....*....|...
gi 15600704  86 VPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd17534  85 EETLERAKETNPYGYLVKPFNERELKAAIELAL 117
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
5-117 8.80e-08

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 52.72  E-value: 8.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELsgfEVRLCLRAEECLGALDKSFAG-----VVISDVRMPGMDGLQLLANLQAVDRDLPVIM 79
Cdd:PRK10651   9 ILLIDDHPMLRTGVKQLISM---APDITVVGEASNGEQGIELAEsldpdLILLDLNMPGMNGLETLDKLREKSLSGRIVV 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15600704   80 VT---GHGDVpmaVEAMRQGAYDFIEKPFTPERLLGSLRRA 117
Cdd:PRK10651  86 FSvsnHEEDV---VTALKRGADGYLLKDMEPEDLLKALQQA 123
PRK10336 PRK10336
two-component system response regulator QseB;
4-117 1.04e-07

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 52.59  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGH 83
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPF----TPERLLGSLRRA 117
Cdd:PRK10336  82 DALAERVEGLRLGADDYLCKPFalieVAARLEALMRRT 119
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
5-103 1.53e-07

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: 50.10  E-value: 1.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWL-ELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQA--VDRDLPVIMVT 81
Cdd:cd17575   3 VLLVDDQAIIGEAVRRALaDEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRAnpATRDIPIIVLS 82
                        90       100
                ....*....|....*....|..
gi 15600704  82 GHGDVPMAVEAMRQGAYDFIEK 103
Cdd:cd17575  83 TKEEPEVKSEAFALGANDYLVK 104
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
5-115 3.35e-07

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 48.56  E-value: 3.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLR 115
Cdd:cd17616  81 DIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK11697 PRK11697
two-component system response regulator BtsR;
5-125 3.85e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 51.00  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGfEVRL---CLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLqavDRD-LP-VIM 79
Cdd:PRK11697   4 VLIVDDEPLAREELRELLQEEG-DIEIvgeCSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML---DPEhMPyIVF 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15600704   80 VTGHGDvpMAVEAMRQGAYDFIEKPFTPERL---LGSLRRALEKRRLVL 125
Cdd:PRK11697  80 VTAFDE--YAIKAFEEHAFDYLLKPIDPARLaktLARLRQERSPQDVLL 126
dpiA PRK10046
two-component response regulator DpiA; Provisional
5-141 3.90e-07

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 50.79  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLE-LSGF-EVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:PRK10046   7 LLIVEDETPLAEMHAEYIRhIPGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTA 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600704   83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENrrlkEQASLKdQVD 141
Cdd:PRK10046  87 ASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESI----DSASQK-QID 140
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
5-104 5.15e-07

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 47.78  E-value: 5.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLC---LRAEECLGALDKSFaGVVISDVRMPGMDGLQLLANLQAVD--RDLPVIM 79
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAAsdgLQAWDVLEDEQNEI-DLILTEVDLPVSSGFKLLSYIMRHKicKNIPVIM 79
                        90       100
                ....*....|....*....|....*
gi 15600704  80 VTGHGDVPMAVEAMRQGAYDFIEKP 104
Cdd:cd17582  80 MSSQDSVGVVFKCLSKGAADYLVKP 104
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
5-104 5.65e-07

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: 47.75  E-value: 5.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVrLCLR-AEECLGALDKSFAGVVISDVRMPGMDGLQL---LANLQAVdRDLPVIMV 80
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRV-VVIDdPLRALTTLLNSKPDLILIDIDMPDLDGYELcslLRKSSAL-KDTPIIML 78
                        90       100
                ....*....|....*....|....
gi 15600704  81 TGHGDVPMAVEAMRQGAYDFIEKP 104
Cdd:cd17602  79 TGKDGLVDRIRAKMAGASGYLTKP 102
PRK10360 PRK10360
transcriptional regulator UhpA;
5-117 6.15e-07

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 49.59  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLelsGFEVRLCLRAE-----ECLGALDKSFAGVVISDVRMPGMDGLQLLANLQavdRDLPVIM 79
Cdd:PRK10360   4 VALIDDHLIVRSGFAQLL---GLEPDLQVVAEfgsgrEALAGLPGRGVQVCICDISMPDISGLELLSQLP---KGMATIM 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15600704   80 VTGHgDVPMAVE-AMRQGAYDFIEKPFTPERLLGSLRRA 117
Cdd:PRK10360  78 LSVH-DSPALVEqALNAGARGFLSKRCSPDELIAAVHTV 115
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
8-118 6.16e-07

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 48.05  E-value: 6.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRdLPVIMVTGHgDVP 87
Cdd:cd18159   4 VEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSR-DDN 81
                        90       100       110
                ....*....|....*....|....*....|..
gi 15600704  88 M-AVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd18159  82 MdQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
4-136 6.51e-07

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 50.45  E-value: 6.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGH 83
Cdd:PRK10710  12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR-FSDIPIVMVTAK 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQASL 136
Cdd:PRK10710  91 IEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPL 143
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-57 6.62e-07

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: 46.02  E-value: 6.62e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15600704      5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMP 57
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK13856 PRK13856
two-component response regulator VirG; Provisional
5-135 8.69e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 49.81  E-value: 8.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLqAVDRDLPVIMVTGHG 84
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSL-ATKSDVPIIIISGDR 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600704   85 -DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLenrRLKEQAS 135
Cdd:PRK13856  83 lEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVV---RTKDRRS 131
PRK10643 PRK10643
two-component system response regulator PmrA;
4-171 8.82e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 49.65  E-value: 8.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGH 83
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALekrrlvlenRRLKEQASLKDQVDARLLGVSKPMEALRRQVLALAP 163
Cdd:PRK10643  82 DTLEDRVAGLDVGADDYLVKPFALEELHARIRALI---------RRHQGQGENELQVGNLTLNLGRQQVWLDGQELILTP 152

                 ....*...
gi 15600704  164 TPVNVLIR 171
Cdd:PRK10643 153 KEFALLSR 160
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
5-116 1.06e-06

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 47.42  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVdRDLPVIMVTGHG 84
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT-SNVPIIMLTAKD 79
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPFTPERLL----GSLRR 116
Cdd:cd17614  80 SEVDKVLGLELGADDYVTKPFSNRELLarvkANLRR 115
PRK10430 PRK10430
two-component system response regulator DcuR;
5-156 1.16e-06

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 49.34  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWL-ELSGFE----VRLCLRAEECLGALDKSFaGVVISDVRMPGMDGLQLLANLQAVDRDLPVIM 79
Cdd:PRK10430   4 VLIVDDDAMVAELNRRYVaQIPGFQccgtASTLEQAKEIIFNSDTPI-DLILLDIYMQQENGLDLLPVLHEAGCKSDVIV 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600704   80 VTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLvLENRRLKEQAslkdQVDARLLGVSKPMEALRR 156
Cdd:PRK10430  83 ISSAADAATIKDSLHYGVVDYLIKPFQASRFEEALTGWRQKKMA-LEKHQYYDQA----ELDQLIHGSSSNEQDPRR 154
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
4-106 1.20e-06

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 47.01  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAG--VVISDVRMPGMDGLQLLANLQAV--DRDLPVIM 79
Cdd:cd19933   2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLfgRRERPLIV 81
                        90       100
                ....*....|....*....|....*...
gi 15600704  80 -VTGHGDVPMAVEAMRQGAYDFIEKPFT 106
Cdd:cd19933  82 aLTANTDDSTREKCLSLGMNGVITKPVS 109
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
5-119 1.36e-06

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 46.88  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLEL-SGFEVRL-CLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd19930   1 VLIAEDQEMVRGALAALLELeDDLEVVAqASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15600704  83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALE 119
Cdd:cd19930  81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
5-118 2.14e-06

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: 46.57  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFevrLCLRAEECLGALDKSFA-----GVVISDVRMPGMDGLQLLANLQAVDRDLPVIM 79
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPD---FTVVGEASSGEEGIELAerldpDLILLDLNMKGMSGLDTLKALREEGVSARIVI 77
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15600704  80 VTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRAL 118
Cdd:cd19931  78 LTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAA 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
5-104 2.59e-06

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: 45.62  E-value: 2.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDrDLPVIMVTGHG 84
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                        90       100
                ....*....|....*....|
gi 15600704  85 DVPMAVEAMRQGAYDFIEKP 104
Cdd:cd17620  80 EESDKIAALDAGADDYLTKP 99
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
4-120 5.24e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 47.61  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLclrAEECLGALDKSFAG---VVISDVRMPGMDGLQLLANLQAVDRDLPVIMV 80
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDL---ADNGLNGYHLAMTGdydLIILDIMLPDVNGWDIVRMLRSANKGMPILLL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15600704   81 TGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEK 120
Cdd:PRK09836  79 TALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
PRK09483 PRK09483
response regulator; Provisional
5-115 7.73e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 46.64  E-value: 7.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLE-LSGFEVR-LCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:PRK09483   4 VLLVDDHELVRAGIRRILEdIKGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTV 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15600704   83 HGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLR 115
Cdd:PRK09483  84 HTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
8-104 7.99e-06

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 44.57  E-value: 7.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   8 VDDEATIREAVQQWLElSGFEVRLCLRAEECLGALDK-SFAGV--VISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17565   4 VDDDKNIIKILSDIIE-DDDLGEVVGEADNGAQAYDEiLFLQPdiVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVS 82
                        90       100
                ....*....|....*....|....*
gi 15600704  85 DvpmavEAMRQGAYD-----FIEKP 104
Cdd:cd17565  83 D-----KEMIGKAYQagiefFINKP 102
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
5-68 9.46e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 44.88  E-value: 9.46e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600704   5 VIFVDDEATIREAVQQWLELS-GFEV-RLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANL 68
Cdd:COG2197   4 VLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
5-122 9.52e-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: 44.61  E-value: 9.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLElSGFEVRLCLRAEECL-GALDKSFAGVVISdVRMPGMDGLQLLANLQAVD--RDLPVIMVT 81
Cdd:cd17539   1 VLLVDDRPSSAERIAAMLS-SEHEVVVEADPDEALfRAAEGPFDLVIVS-LALEDFDGLRLCSQLRSLErtRQLPILAVA 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15600704  82 GHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRR 122
Cdd:cd17539  79 DPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRRKR 119
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
5-110 1.23e-05

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 44.17  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGF-EVRLCLRAEECLGALDKSFAGVVISDVRM-PGMDGLQLLANL---QAVDRDLPVIM 79
Cdd:cd17589   1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELrhkKLISPSTVFIM 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15600704  80 VTGHGDVPMAVEAMRQGAYDFIEKPFTPERL 110
Cdd:cd17589  81 VTGESSRAMVLSALELEPDDYLLKPFTVSEL 111
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
5-105 2.02e-05

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 43.57  E-value: 2.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:cd17573   1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                        90       100
                ....*....|....*....|.
gi 15600704  85 DVPMAVEAMRQGAYDFIEKPF 105
Cdd:cd17573  81 KTEQEIEAFKEGADDYIAKPF 101
PRK15369 PRK15369
two component system response regulator;
49-161 3.29e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 44.68  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   49 VVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENR 128
Cdd:PRK15369  52 IVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYIDPAL 131
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15600704  129 RLkeqaslkDQVDARLLGVSKPMEAL---RRQVLAL 161
Cdd:PRK15369 132 NR-------EAILALLNADDTNPPLLtprERQILKL 160
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
36-105 4.05e-05

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: 42.60  E-value: 4.05e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600704  36 EECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDR--DLPVIMVTGHGDVPMAVEAMRQGAYDFIEKPF 105
Cdd:cd17561  37 QEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLekRPKIIMLTAFGQEDITQRAVELGASYYILKPF 108
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
5-104 5.97e-05

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 42.35  E-value: 5.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVR-----------LCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVD- 72
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTavdsgkralefLGLEDEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSa 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15600704  73 -RDLPVIMVTGHGDVPMAVEAMRQGAYDFIEKP 104
Cdd:cd17581  81 lKEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
PRK11173 PRK11173
two-component response regulator; Provisional
4-142 8.34e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 43.85  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGH 83
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE-QANVALMFLTGR 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPFTPERLlgslrrALEKRRLVLENRRLKEQASLKDQVDA 142
Cdd:PRK11173  84 DNEVDKILGLEIGADDYITKPFNPREL------TIRARNLLSRTMNLGTVSEERRSVES 136
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
5-105 9.89e-05

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: 41.18  E-value: 9.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFA-GVVISDVRMPG-MDGLQLLANLQAVDRDLPVIMVTG 82
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDiDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                        90       100
                ....*....|....*....|....
gi 15600704  83 HGDVpmAVEAMRQGA-YDFIEKPF 105
Cdd:cd18161  81 YAEN--AIEGGDLAPgVDVLSKPF 102
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
4-116 1.13e-04

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: 41.63  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   4 QVIFVDDEATIREAVQQWLELSGFEVRLC-----------LRAEEclGALDKSFAGVVISDVRMPGMDGLQLLANLQAvD 72
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAGVPNELHvvrdgeealdfLRGEG--EYADAPRPDLILLDLNMPRMDGFEVLREIKA-D 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600704  73 ---RDLPVIMVT---GHGDVpmaVEAMRQGAYDFIEKPFTPERLLGSLRR 116
Cdd:cd17557  78 pdlRRIPVVVLTtsdAEEDI---ERAYELGANSYIVKPVDFEEFVEAIRS 124
pleD PRK09581
response regulator PleD; Reviewed
1-104 1.14e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 44.51  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    1 MSDQVIFVDD-EATIR--EAVqqwLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQA--VDRDL 75
Cdd:PRK09581   1 MTARILVVDDiPANVKllEAK---LLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSdpATTHI 77
                         90       100
                 ....*....|....*....|....*....
gi 15600704   76 PVIMVTGHGDVPMAVEAMRQGAYDFIEKP 104
Cdd:PRK09581  78 PVVMVTALDDPEDRVRGLEAGADDFLTKP 106
PRK10816 PRK10816
two-component system response regulator PhoP;
4-121 1.68e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 42.80  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGH 83
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15600704   84 GDVPMAVEAMRQGAYDFIEKPFTPERLLGSLrRALEKR 121
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTKPFHIEEVMARM-QALMRR 118
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
5-120 1.72e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 42.87  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRdLPVIMVTGHG 84
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVLSARS 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15600704   85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEK 120
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKPFGIGELQARLRVALRR 118
PRK15347 PRK15347
two component system sensor kinase;
4-119 1.74e-04

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 44.25  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    4 QVIFVDDEATIREAVQQWLELSGFEVRLCLRAEEclgALDKSFAGV---VISDVRMPGMDGLQLLA----NLQAVDRDLP 76
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTE---ALELGRQHRfdlVLMDIRMPGLDGLETTQlwrdDPNNLDPDCM 768
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15600704   77 VIMVTGHGdVPMAVEAMRQ-GAYDFIEKPFTperlLGSLRRALE 119
Cdd:PRK15347 769 IVALTANA-APEEIHRCKKaGMNHYLTKPVT----LAQLARALE 807
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
5-134 1.90e-04

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 43.95  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704     5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15600704    85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRALEKRRLVLENRRLKEQA 134
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEA 1090
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
8-104 3.06e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 42.56  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    8 VDDEATIREAVQQWLELSGfEVRLCLRAEECLGALDKSFA---GVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTG-- 82
Cdd:PRK12555   6 VNDSPLAVEALRRALARDP-DHEVVWVATDGAQAVERCAAqppDVILMDLEMPRMDGVEATRRIMA-ERPCPILIVTSlt 83
                         90       100
                 ....*....|....*....|..
gi 15600704   83 HGDVPMAVEAMRQGAYDFIEKP 104
Cdd:PRK12555  84 ERNASRVFEAMGAGALDAVDTP 105
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
5-117 5.02e-04

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: 39.73  E-value: 5.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   5 VIFVDDEATIREAVQQWLE-LSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGH 83
Cdd:cd17530   3 VLVLDDDPFQCMMAATILEdLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15600704  84 -GDVPMAVEAMrQGAYDF-----IEKPFTPERLLGSLRRA 117
Cdd:cd17530  83 dGGILESAETL-AGANGLnllgtLSKPFSPEELTELLTKY 121
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
5-103 5.12e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 41.40  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGfEVRLCLRAEECLGALD--KSFA-GVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVT 81
Cdd:PRK09935   6 VIIMDTHPIIRMSIEVLLQKNS-ELQIVLKTDDYRITIDylRTRPvDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLS 84
                         90       100
                 ....*....|....*....|..
gi 15600704   82 GHGDVPMAVEAMRQGAYDFIEK 103
Cdd:PRK09935  85 SKSECFYAGRAIQAGANGFVSK 106
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
394-431 5.48e-04

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 37.37  E-value: 5.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 15600704   394 MEAFEAECLRQALGQCRGDIKAVMELLQLPRRTLNEKM 431
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKL 38
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
5-174 6.86e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 41.16  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    5 VIFVDDEATIREAVQQWLELSGFEVRLCLRAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAvDRDLPVIMVTGHg 84
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRP-KWQGPIVLLTSL- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   85 DVPM-AVEAMRQGAYDFIEKPFTPERLLGSLRRALekrrlvlenrRLKEQASLKDQVDARLLgvsKPMEALRRQVLALAP 163
Cdd:PRK10701  82 DSDMnHILALEMGACDYILKTTPPAVLLARLRLHL----------RQNEQATQTKGLQETSL---TPYKALHFGTLTIDP 148
                        170
                 ....*....|.
gi 15600704  164 TPVNVLIRGET 174
Cdd:PRK10701 149 VNRQVTLAGEE 159
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
39-81 7.44e-04

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 41.88  E-value: 7.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15600704   39 LGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVT 81
Cdd:PRK10841 838 LNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVT 880
PRK10693 PRK10693
two-component system response regulator RssB;
50-160 9.50e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.13  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704   50 VISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHGDVPMAVEAMRQGAYDFIEKPFTP-----ERLLGSLRRALEKRRLV 124
Cdd:PRK10693  21 IICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKDlnrlrEMVFACLYPSMFNSRVE 100
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15600704  125 LENRRLKEQASLKDQVDA--RLLgvsKPMEALRRQVLA 160
Cdd:PRK10693 101 EEERLFRDWDALVDNPAAaaKLL---KQLQPPVQQVIA 135
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
6-117 1.12e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 40.26  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704    6 IFVDDEATIREAVQQWLELSGFEVRLCL-RAEECLGALDKSFAGVVISDVRMPGMDGLQLLANLQAVDRDLPVIMVTGHG 84
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILAELtEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKN 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15600704   85 DVPMAVEAMRQGAYDFIEKPFTPERLLGSLRRA 117
Cdd:PRK09958  84 DHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
140-299 2.86e-03

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 38.42  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 140 VDARLLGVSKPMEALRRQVLALAPTPVNVLIRGETGSGKELVARCLhdfGPRADKPFVALNCaaipeqlfeSELFghesG 219
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKAL---AGELGLPLIVVKL---------SSLL----S 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600704 220 AFTGAQGKRIGKL-EHAH---GGTLFLDEIESM-----PLAQQVKLLRVLQeQQLERLgSNQSIHVDLRVIAAT-KPDLL 289
Cdd:cd19481  65 KYVGESEKNLRKIfERARrlaPCILFIDEIDAIgrkrdSSGESGELRRVLN-QLLTEL-DGVNSRSKVLVIAATnRPDLL 142
                       170
                ....*....|..
gi 15600704 290 AEA--RAGRFRE 299
Cdd:cd19481 143 DPAllRPGRFDE 154
 
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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