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Conserved domains on  [gi|26111063|gb|AAN83246|]
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Nitrogen regulation protein NR(I) [Escherichia coli CFT073]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 11485099)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
21-489 0e+00

nitrogen regulation protein NR(I); Provisional


:

Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 979.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 100
Cdd:PRK10923   1 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRS 180
Cdd:PRK10923  81 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  181 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 260
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  261 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPR 340
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  341 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESNVPESTSHMQPD 420
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQPD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26111063  421 SWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:PRK10923 401 SWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
 
Name Accession Description Interval E-value
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
21-489 0e+00

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 979.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 100
Cdd:PRK10923   1 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRS 180
Cdd:PRK10923  81 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  181 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 260
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  261 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPR 340
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  341 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESNVPESTSHMQPD 420
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQPD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26111063  421 SWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:PRK10923 401 SWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
26-486 0e+00

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: 845.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQ-LNGPTTDIIGEAPAMQDVFRIIGRLSRSSISV 184
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAgEAEDSAELIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   185 LINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDM 264
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   265 PLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARH 344
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   345 FLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGEL-FESNVPESTSHMQPDSWA 423
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELaLTGRPASAPDSDGQDSWD 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26111063   424 TLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKEL 486
Cdd:TIGR01818 401 EALEAWAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKEL 463
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
26-487 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: 585.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRnvqlngPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 185
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENA------EDSGLIGRSPAMQEVRRLIEKVAPSDATVL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 186 INGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMP 265
Cdd:COG2204 159 ITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 266 LDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHF 345
Cdd:COG2204 239 LALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 346 LQVAARELGVEAKlLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPgelfesnvpestshmqpdswatl 425
Cdd:COG2204 319 LARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP----------------------- 374
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26111063 426 laqwadralrsghqnllsEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELG 487
Cdd:COG2204 375 ------------------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
Sigma54_activat pfam00158
Sigma-54 interaction domain;
160-327 5.55e-110

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 322.81  E-value: 5.55e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   160 IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTG 239
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   240 ANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFH 319
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 26111063   320 RLNVIRVH 327
Cdd:pfam00158 161 RLNVIPIE 168
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
24-139 1.49e-78

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: 240.64  E-value: 1.49e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  24 GIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:cd19919   1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd19919  81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
183-321 6.11e-13

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 66.24  E-value: 6.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    183 SVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIES---ELFGHEKGAFTGANTIRQG--RFEQADGGTLF 257
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26111063    258 LDEIGDMPLDVQTRLLRVLadgQFYRVGGYAPVKVDVRIIAATH--QNLEQRVLEGKFREDLFHRL 321
Cdd:smart00382  84 LDEITSLLDAEQEALLLLL---EELRLLLLLKSEKNLTVILTTNdeKDLGPALLRRRFDRRIVLLL 146
 
Name Accession Description Interval E-value
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
21-489 0e+00

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 979.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 100
Cdd:PRK10923   1 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRS 180
Cdd:PRK10923  81 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  181 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 260
Cdd:PRK10923 161 SISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  261 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPR 340
Cdd:PRK10923 241 IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  341 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESNVPESTSHMQPD 420
Cdd:PRK10923 321 LARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQPD 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26111063  421 SWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:PRK10923 401 SWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
26-486 0e+00

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: 845.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQ-LNGPTTDIIGEAPAMQDVFRIIGRLSRSSISV 184
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAgEAEDSAELIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   185 LINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDM 264
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   265 PLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARH 344
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   345 FLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGEL-FESNVPESTSHMQPDSWA 423
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELaLTGRPASAPDSDGQDSWD 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26111063   424 TLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKEL 486
Cdd:TIGR01818 401 EALEAWAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKEL 463
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
26-487 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: 585.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:COG2204   5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRnvqlngPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 185
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENA------EDSGLIGRSPAMQEVRRLIEKVAPSDATVL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 186 INGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMP 265
Cdd:COG2204 159 ITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 266 LDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHF 345
Cdd:COG2204 239 LALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARHF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 346 LQVAARELGVEAKlLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPgelfesnvpestshmqpdswatl 425
Cdd:COG2204 319 LARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP----------------------- 374
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26111063 426 laqwadralrsghqnllsEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELG 487
Cdd:COG2204 375 ------------------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
127-489 2.47e-162

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: 466.94  E-value: 2.47e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 127 DIDEavalVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSP 206
Cdd:COG3829 111 DITE----LKRLERKLREEELERGLSAKYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASP 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 207 RAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTI-RQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVG 285
Cdd:COG3829 187 RRDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVG 266
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 286 GYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETE 365
Cdd:COG3829 267 GTKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEAL 346
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 366 AALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESNVPESTSHMQPdswatllaqwadralrsghqnlLSEA 445
Cdd:COG3829 347 ELLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAASAAEEGS----------------------LKEA 404
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 26111063 446 QPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:COG3829 405 LEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
23-489 1.16e-148

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 432.74  E-value: 1.16e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   23 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMT 102
Cdd:PRK11361   4 INRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  103 AHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTT----DIIGEAPAMQDVFRIIGRLS 178
Cdd:PRK11361  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSwqwgHILTNSPAMMDICKDTAKIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  179 RSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFL 258
Cdd:PRK11361 164 LSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  259 DEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDI 338
Cdd:PRK11361 244 DEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  339 PRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESNVPESTSHMQ 418
Cdd:PRK11361 324 SLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEVKTA 403
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26111063  419 PDswatllaqwADRALRsghqnllsEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:PRK11361 404 PV---------GERNLK--------EEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
26-483 1.09e-126

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 375.91  E-value: 1.09e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVqLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 185
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPA-VTASQFGMVGKSPAMQHLLSEIALVAPSEATVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  186 INGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMP 265
Cdd:PRK10365 167 IHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDIS 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  266 LDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHF 345
Cdd:PRK10365 247 PMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHF 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  346 LQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESNVPESTShmqpdswatl 425
Cdd:PRK10365 327 LQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQS---------- 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  426 laqwadralrsghqnllSEAQP--ELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKL 483
Cdd:PRK10365 397 -----------------QDIQPlvEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
145-487 1.34e-120

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 366.53  E-value: 1.34e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 145 QQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDL 224
Cdd:COG3284 308 RAAPAGAPAPAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEEL 387
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 225 IESELFGHEKGAFTGANT-IRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQN 303
Cdd:COG3284 388 IESELFGYEPGAFTGARRkGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRD 467
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 304 LEQRVLEGKFREDLFHRLNVIRVHLPPLRErREDIPRLARHFLQVAARELGveAKLLHPETEAALTRLAWPGNVRQLENT 383
Cdd:COG3284 468 LRELVAAGRFREDLYYRLNGLTLTLPPLRE-REDLPALIEHLLRELAAGRG--PLRLSPEALALLAAYPWPGNVRELRNV 544
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 384 CRWLTVMAAGQEVLIQDLPGELFESNVPESTSHMQPdswATLLAqwadralrsghqnllseaqpELERTLLTTALRHTQG 463
Cdd:COG3284 545 LRTALALADGGVITVEDLPDELRAELAAAAPAAAAP---LTSLE--------------------EAERDAILRALRACGG 601
                       330       340
                ....*....|....*....|....
gi 26111063 464 HKQEAARLLGWGRNTLTRKLKELG 487
Cdd:COG3284 602 NVSAAARALGISRSTLYRKLKRYG 625
PRK15115 PRK15115
response regulator GlrR; Provisional
28-476 7.21e-115

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 345.67  E-value: 7.21e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:PRK15115  10 LVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  108 DAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHyqeqqqprnvqlNGPTTD------IIGEAPAMQDVFRIIGRLSRSS 181
Cdd:PRK15115  90 PDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQ------------SAPATDerwreaIVTRSPLMLRLLEQARMVAQSD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  182 ISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEI 261
Cdd:PRK15115 158 VSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  262 GDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRL 341
Cdd:PRK15115 238 GDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  342 ARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENT---CRWLTVMAAGQEVLI-QDLPGElfesnvpestshm 417
Cdd:PRK15115 318 ANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVieqCVALTSSPVISDALVeQALEGE------------- 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26111063  418 qpdswatllaqwaDRALRSghqnlLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGR 476
Cdd:PRK15115 385 -------------NTALPT-----FVEARNQFELNYLRKLLQITKGNVTHAARMAGRNR 425
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
28-488 6.31e-113

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: 340.96  E-value: 6.31e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    28 VVDDDSSIRWVLERALAGagltCTTFENG--AEVLEALASKTPDVLLSDIRMP-----GMDGLALLKQIKQRHPMLPVII 100
Cdd:TIGR02915   3 IVEDDLGLQKQLKWSFAD----YELAVAAdrESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQ-LNGPTTD--IIGEAPAMQDVFRIIGRL 177
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQsALGGTALrgLITSSPGMQKICRTIEKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   178 SRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLF 257
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   258 LDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERRED 337
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   338 IPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLpgELFESNVPESTSHM 417
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDL--GLDARERAETPLEV 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26111063   418 QpdswatllaqwadralrsghqnlLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGM 488
Cdd:TIGR02915 397 N-----------------------LREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
Sigma54_activat pfam00158
Sigma-54 interaction domain;
160-327 5.55e-110

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 322.81  E-value: 5.55e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   160 IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTG 239
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   240 ANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFH 319
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 26111063   320 RLNVIRVH 327
Cdd:pfam00158 161 RLNVIPIE 168
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
132-488 4.18e-108

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 330.60  E-value: 4.18e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  132 VALVERAISHYQEQQQPRNVQLNGPTTD---IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRA 208
Cdd:PRK05022 158 NALLIEQLESQAELPQDVAEFLRQEALKegeMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  209 KAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYA 288
Cdd:PRK05022 238 DKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDR 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  289 PVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAAL 368
Cdd:PRK05022 318 SLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAAL 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  369 TRLAWPGNVRQLENTCRWLTVMA----AGQEVLIQ----DLPGelfESNVPESTSHMQPdswatllAQWADRALRsghqn 440
Cdd:PRK05022 398 LAYDWPGNVRELEHVISRAALLArargAGRIVTLEaqhlDLPA---EVALPPPEAAAAP-------AAVVSQNLR----- 462
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 26111063  441 llsEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGM 488
Cdd:PRK05022 463 ---EATEAFQRQLIRQALAQHQGNWAAAARALELDRANLHRLAKRLGL 507
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
127-473 1.37e-100

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: 312.03  E-value: 1.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   127 DIDEAVALVERAISHYQEQQQPRNVQLNGpttdIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSP 206
Cdd:TIGR01817 169 LIAEAVQLSKQLRDKAPEIARRRSGKEDG----IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSP 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   207 RAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGG 286
Cdd:TIGR01817 245 RAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGG 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   287 YAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGveaKLLHPETEA 366
Cdd:TIGR01817 325 NRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENG---RPLTITPSA 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   367 --ALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLP---GELFESNVPESTSH----MQPDSWATLLAQWADRALrSG 437
Cdd:TIGR01817 402 irVLMSCKWPGNVRELENCLERTATLSRSGTITRSDFScqsGQCLSPMLAKTCPHghisIDPLAGTTPPHSPASAAL-PG 480
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 26111063   438 HQNLLSEAQPELERtlLTTALRHTQGHKQEAARLLG 473
Cdd:TIGR01817 481 EPGLSGPTLSERER--LIAALEQAGWVQAKAARLLG 514
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
160-417 1.96e-100

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 310.97  E-value: 1.96e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 160 IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTG 239
Cdd:COG3283 206 IVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFGN 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 240 ANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFH 319
Cdd:COG3283 286 AREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYY 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 320 RLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTC-RWLTvMAAGQEVLI 398
Cdd:COG3283 366 RLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALyRAVS-LLEGDELTP 444
                       250
                ....*....|....*....
gi 26111063 399 QDLpgelfesNVPESTSHM 417
Cdd:COG3283 445 EDL-------QLPEYAASA 456
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
160-473 1.34e-96

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: 294.59  E-value: 1.34e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   160 IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTG 239
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   240 ANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFH 319
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   320 RLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKL-LHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLI 398
Cdd:TIGR02974 161 RLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLFPgFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEEAPI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26111063   399 QDLPGELFESNVPESTSHMQPDSWATLLAQWADRALRSGHQNL-LSEAQPELERTLLTTALRHTQGHKQEAARLLG 473
Cdd:TIGR02974 241 DEIIIDPFASPWRPKQAAPAVDEVNSTPTDLPSPSSIAAAFPLdLKQAQQDYEIELLQQALAEAQFNQRKAAELLG 316
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
159-485 8.52e-92

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 289.31  E-value: 8.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  159 DIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSP--------RAKAPFIALNMAAIPKDLIESELF 230
Cdd:PRK15424 220 DLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHREYFarhdarqgKKSHPFVAVNCGAIAESLLEAELF 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  231 GHEKGAFTGANtiRQGR---FEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQR 307
Cdd:PRK15424 300 GYEEGAFTGSR--RGGRaglFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEED 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  308 VLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVeakllhPETEAALTRLA----------WPGNV 377
Cdd:PRK15424 378 VRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSA------PFSAALRQGLQqcetlllhydWPGNV 451
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  378 RQLENTCRWLTVMAAGQEvlIQDLPGELFESNVPEstshmqpdswatlLAqwadralrsghQNLLSEAQPELERTLLTTA 457
Cdd:PRK15424 452 RELRNLMERLALFLSVEP--TPDLTPQFLQLLLPE-------------LA-----------RESAKTPAPRLLAATLQQA 505
                        330       340
                 ....*....|....*....|....*...
gi 26111063  458 LRHTQGHKQEAARLLGWGRNTLTRKLKE 485
Cdd:PRK15424 506 LERFNGDKTAAANYLGISRTTLWRRLKA 533
PRK10820 PRK10820
transcriptional regulator TyrR;
145-488 1.27e-81

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 262.32  E-value: 1.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  145 QQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDL 224
Cdd:PRK10820 191 QLQNLAVNDDSAFSQIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDV 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  225 IESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNL 304
Cdd:PRK10820 271 VESELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNL 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  305 EQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTC 384
Cdd:PRK10820 351 VELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAI 430
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  385 -RWLTVMaAGQEVLIQDLPGELFESNVPEStshmqpdswatllaqwaDRALRSGhqnlLSEAQPELERTLLTTALRHTQG 463
Cdd:PRK10820 431 yRALTQL-EGYELRPQDILLPDYDAAVAVG-----------------EDAMEGS----LDEITSRFERSVLTRLYRNYPS 488
                        330       340
                 ....*....|....*....|....*
gi 26111063  464 HKQEAARlLGWGRNTLTRKLKELGM 488
Cdd:PRK10820 489 TRKLAKR-LGVSHTAIANKLREYGL 512
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
160-473 4.57e-81

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 254.60  E-value: 4.57e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  160 IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTG 239
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  240 ANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFH 319
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  320 RLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEaklLHP----ETEAALTRLAWPGNVRQLENTC-----RWLTVM 390
Cdd:PRK11608 168 RLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLP---LFPgfteRARETLLNYRWPGNIRELKNVVersvyRHGTSE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  391 AAGQEVLIQDLPGELFESNVPESTSHMQPdswaTL---LAQWadralrsghqnllseaQPELERTLLTTALRHTQGHKQE 467
Cdd:PRK11608 245 YPLDNIIIDPFKRRPAEEAIAVSETTSLP----TLpldLREW----------------QHQQEKELLQRSLQQAKFNQKR 304

                 ....*.
gi 26111063  468 AARLLG 473
Cdd:PRK11608 305 AAELLG 310
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
128-489 2.40e-80

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 263.23  E-value: 2.40e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  128 IDEAVALVEraISHYQEQQQPRNV----QLNGPTTD---IIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHA 200
Cdd:PRK15429 341 VDNALAYQE--IHRLKERLVDENLalteQLNNVDSEfgeIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARA 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  201 LHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQ 280
Cdd:PRK15429 419 IHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQE 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  281 FYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLL 360
Cdd:PRK15429 499 FERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSI 578
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  361 HPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQeVLIQDLPgELFESNVPESTShmqpdswATLLAQwadralrsghqn 440
Cdd:PRK15429 579 PAETLRTLSNMEWPGNVRELENVIERAVLLTRGN-VLQLSLP-DITLPEPETPPA-------ATVVAQ------------ 637
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 26111063  441 llseaQPELERTLLTTALRHTQG---HKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:PRK15429 638 -----EGEDEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTLLSRMKRLGID 684
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
24-139 1.49e-78

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: 240.64  E-value: 1.49e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  24 GIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:cd19919   1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd19919  81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
168-489 3.20e-72

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: 232.43  E-value: 3.20e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 168 QDVFRIIGRLsrssISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESelfghekgaftgantirqgr 247
Cdd:COG3604 106 LRLLETLASL----AAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 248 feqadggtlfldeigdmpldvqtrllrvLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVH 327
Cdd:COG3604 162 ----------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIR 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 328 LPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPgelfe 407
Cdd:COG3604 214 LPPLRERREDIPLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLA----- 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 408 snvpestshmqpdswatllaqwadralrsghqNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELG 487
Cdd:COG3604 289 --------------------------------PGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLG 336

                ..
gi 26111063 488 ME 489
Cdd:COG3604 337 IK 338
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
145-489 4.31e-57

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 200.29  E-value: 4.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  145 QQQPRNVQlngPT-TDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKD 223
Cdd:PRK11388 314 TSQLGKVS---HTfDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDE 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  224 LIESELFGhekGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQN 303
Cdd:PRK11388 391 ALAEEFLG---SDRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTAD 467
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  304 LEQRVLEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKlLHPETEAALTRLAWPGNVRQLENT 383
Cdd:PRK11388 468 LAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLK-IDDDALARLVSYRWPGNDFELRSV 546
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  384 CRWLTVMAAGQEVLIQDLPGELFeSNVPESTSHMQPDSWATLLAqwadralrsghqnllseaqpELERTLLTTALRHTQG 463
Cdd:PRK11388 547 IENLALSSDNGRIRLSDLPEHLF-TEQATDDVSATRLSTSLSLA--------------------ELEKEAIINAAQVCGG 605
                        330       340
                 ....*....|....*....|....*.
gi 26111063  464 HKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:PRK11388 606 RIQEMAALLGIGRTTLWRKMKQHGID 631
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
178-380 1.27e-44

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: 164.24  E-value: 1.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 178 SRSSISVLINGESGTGKELVA---HALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGG 254
Cdd:COG4650 205 IRSRAPILLTGPTGAGKSQLArriYELKKARHQVSGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRSADGG 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 255 TLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVLEGKFREDLFHRLNVIRVHLPPLRER 334
Cdd:COG4650 285 VLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPGLAER 364
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26111063 335 REDI-PRLArHFLQVAARELGV------EAK---LLHPETEAALtrlaWPGNVRQL 380
Cdd:COG4650 365 REDIePNLD-YELARFAREQGRrvrfnkEARaryLAFATSPEAL----WSGNFRDL 415
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
26-149 6.07e-40

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: 140.32  E-value: 6.07e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPR 149
Cdd:cd17549  81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENR 124
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
25-149 4.53e-39

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: 140.24  E-value: 4.53e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  25 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 104
Cdd:COG4566   1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPR 149
Cdd:COG4566  81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAER 125
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
25-139 2.17e-36

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: 130.41  E-value: 2.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  25 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 104
Cdd:cd17537   2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd17537  82 GDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
26-136 2.84e-36

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 129.96  E-value: 2.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 26111063   106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVE 136
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
21-144 3.16e-36

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 130.36  E-value: 3.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQR--HPMLPV 98
Cdd:COG0784   3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDIPI 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 26111063  99 IIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQE 144
Cdd:COG0784  83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
28-125 1.18e-34

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 125.03  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd00156   2 IVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADE 81
                        90
                ....*....|....*...
gi 26111063 108 DAAVSAYQQGAFDYLPKP 125
Cdd:cd00156  82 EDAVRALELGADDYLVKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
26-139 2.40e-34

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 124.92  E-value: 2.40e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd17550  81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERAL 114
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
184-407 1.10e-33

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: 135.24  E-value: 1.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 184 VLINGESGTGKELVAHALHRHSPRAK-----APFIALNMAaipkD------LIESELFGHEKGAFTGANTIRQGRFEQAD 252
Cdd:COG1221 133 TLILGPTGVGKSFFAELMYEYAIEIGvlpedAPFVVFNCA----DyannpqLLMSQLFGYVKGAFTGADKDKEGLIEKAD 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 253 GGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPV-KVDVRIIAATHQNLEQRVLEGKFRedlfhRLNVIrVHLPPL 331
Cdd:COG1221 209 GGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEKTrKANVRIIFATTEDPESSLLKTFLR-----RIPMV-IKLPSL 282
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 332 RER----REDiprLARHFLQVAARELGVEAKlLHPETEAALTRLAWPGNVRQLEN----TCR--WLTVMAAGQEVL---I 398
Cdd:COG1221 283 EERsleeRLE---LIKHFFKEEAKRLNKPIK-VSKEVLKALLLYDCPGNIGQLKSdiqlACAkaFLNYITNKKEEIeitL 358

                ....*....
gi 26111063 399 QDLPGELFE 407
Cdd:COG1221 359 SDLPENVKK 367
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
28-143 1.57e-33

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 125.84  E-value: 1.57e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:COG0745   6 VVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARDDE 85
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQ 143
Cdd:COG0745  86 EDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
28-136 1.74e-33

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: 124.64  E-value: 1.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHS 105
Cdd:COG3706   6 VVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAdpRTADIPIIFLTALD 85
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVE 136
Cdd:COG3706  86 DEEDRARALEAGADDYLTKPFDPEELLARVD 116
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
22-150 4.39e-33

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 125.28  E-value: 4.39e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  22 QRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVI 99
Cdd:COG3437   5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVI 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 26111063 100 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRN 150
Cdd:COG3437  85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDD 135
fixJ PRK09390
response regulator FixJ; Provisional
21-145 1.37e-32

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 123.19  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 100
Cdd:PRK09390   1 SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 26111063  101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQ 145
Cdd:PRK09390  81 MTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEA 125
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
28-125 6.17e-32

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: 117.95  E-value: 6.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAG--LTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:COG4753   4 IVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSGYS 83
                        90       100
                ....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKP 125
Cdd:COG4753  84 DFEYAQEAIKLGADDYLLKP 103
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
28-139 8.65e-32

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: 118.21  E-value: 8.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCT---TFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 104
Cdd:cd17536   3 IVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSGY 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd17536  83 DDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAK 117
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
28-140 7.04e-31

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: 115.66  E-value: 7.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:COG5803   7 IVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAYGEL 86
                        90       100       110
                ....*....|....*....|....*....|...
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS 140
Cdd:COG5803  87 DMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
26-146 1.35e-29

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 112.29  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQ 146
Cdd:cd17572  81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
28-139 5.96e-29

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: 110.19  E-value: 5.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17569   5 LVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGYADL 84
                        90       100       110
                ....*....|....*....|....*....|...
gi 26111063 108 DAAVSAYQQGA-FDYLPKPFDIDEAVALVERAI 139
Cdd:cd17569  85 DAAIEAINEGEiYRFLTKPWDDEELKETIRQAL 117
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
26-153 6.84e-29

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 110.83  E-value: 6.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALA-GAGLT-CTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:COG4565   6 VLIVEDDPMVAELLRRYLErLPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITA 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQL 153
Cdd:COG4565  86 ARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDL 135
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
28-150 1.19e-27

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 110.29  E-value: 1.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAG-AGLTC-TTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:COG3279   6 IVDDEPLARERLERLLEKyPDLEVvGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTAYD 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 26111063 106 DLdaAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRN 150
Cdd:COG3279  86 EY--ALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEA 128
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
28-138 1.44e-27

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 108.47  E-value: 1.44e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:COG4567   9 LVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGYASI 88
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALVERA 138
Cdd:COG4567  89 ATAVEAIKLGADDYLAKPADADDLLAALERA 119
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
28-125 2.01e-27

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: 105.57  E-value: 2.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17574   2 VVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDEE 81
                        90
                ....*....|....*...
gi 26111063 108 DAAVSAYQQGAFDYLPKP 125
Cdd:cd17574  82 EDKVLGLELGADDYITKP 99
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
161-330 1.51e-26

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: 104.92  E-value: 1.51e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 161 IGEAPAMQDVFRIIGRLSRSSIsvLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEkgaftgA 240
Cdd:cd00009   1 VGQEEAIEALREALELPPPKNL--LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------L 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063 241 NTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRvggyaPVKVDVRIIAATHqnleqRVLEGKFREDLFHR 320
Cdd:cd00009  73 VRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLR-----IDRENVRVIGATN-----RPLLGDLDRALYDR 142
                       170
                ....*....|
gi 26111063 321 LNvIRVHLPP 330
Cdd:cd00009 143 LD-IRIVIPL 151
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
28-130 2.70e-25

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 99.85  E-value: 2.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ---RHPMLPVIIMTAH 104
Cdd:cd17546   3 VVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIALTAN 82
                        90       100
                ....*....|....*....|....*.
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDE 130
Cdd:cd17546  83 ALEEDREKCLEAGMDDYLSKPVKLDQ 108
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
28-125 1.43e-24

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: 98.04  E-value: 1.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17555   5 VIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAGVM 84
                        90
                ....*....|....*...
gi 26111063 108 DAAVSAYQQGAFDYLPKP 125
Cdd:cd17555  85 SDAVEALRLGAWDYLTKP 102
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
28-133 2.33e-24

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


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 97.51  E-value: 2.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAG-LTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTAH 104
Cdd:cd17551   5 IVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedVPIVMITAD 84
                        90       100
                ....*....|....*....|....*....
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVA 133
Cdd:cd17551  85 TDREVRLRALEAGATDFLTKPFDPVELLA 113
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
28-130 5.07e-24

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: 96.52  E-value: 5.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17554   5 VVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYSEY 84
                        90       100
                ....*....|....*....|...
gi 26111063 108 DAAVSAYQQGAfdYLPKPFDIDE 130
Cdd:cd17554  85 KSDFSSWAADA--YVVKSSDLTE 105
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
28-141 7.41e-24

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 96.01  E-value: 7.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17624   3 LVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARDGV 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALVeRAISH 141
Cdd:cd17624  83 DDRVAGLDAGADDYLVKPFALEELLARL-RALLR 115
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
26-139 1.07e-23

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: 95.53  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVeRAI 139
Cdd:cd17627  81 SVSDRVAGLDAGADDYLVKPFALEELLARV-RAL 113
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
161-331 2.03e-23

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 95.49  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   161 IGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLieselfghekgaftga 240
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLEL---------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   241 ntirqgrFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRvggyapvkvdVRIIAATHQNLEQRVLEGKFREDLFHR 320
Cdd:pfam14532  65 -------LEQAKGGTLYLKDIADLSKALQKGLLLLLAKAEGYR----------VRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 26111063   321 LNVIRVHLPPL 331
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
28-133 4.90e-23

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 93.66  E-value: 4.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17563   5 LVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGYASI 84
                        90       100
                ....*....|....*....|....*.
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVA 133
Cdd:cd17563  85 ATAVEAIKLGADDYLAKPADADEILA 110
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
28-140 1.80e-22

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: 92.19  E-value: 1.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGA-GLTCT-TFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17535   3 IVDDHPLVREGLRRLLESEpDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAHD 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS 140
Cdd:cd17535  83 DPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
28-136 5.93e-22

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 90.74  E-value: 5.93e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17625   2 VVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDAV 81
                        90       100
                ....*....|....*....|....*....
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALVE 136
Cdd:cd17625  82 EDRVKGLDLGADDYLPKPFSLAELLARIR 110
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
21-147 6.32e-22

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: 93.10  E-value: 6.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  21 MQRGIVWVVDDDSSIRWVLERALAGAGLT-CTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVI 99
Cdd:COG3707   1 MRGLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA-PVI 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 26111063 100 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQ 147
Cdd:COG3707  80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRA 127
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
26-125 5.87e-21

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: 87.56  E-value: 5.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                        90       100
                ....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKP 125
Cdd:cd19928  81 TLMTAVKAAERGAFEYLPKP 100
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
28-126 1.10e-20

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: 86.78  E-value: 1.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRH--PMLPVIIMTAHS 105
Cdd:cd17538   4 VVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPetRHIPVIMITALD 83
                        90       100
                ....*....|....*....|.
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPF 126
Cdd:cd17538  84 DREDRIRGLEAGADDFLSKPI 104
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
26-130 1.49e-20

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: 86.91  E-value: 1.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASK--TPDVLLSDIRMPGMDGLALLKQIKQRhPMLPVIIMTA 103
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                        90       100
                ....*....|....*....|....*..
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPFDIDE 130
Cdd:cd17584  80 DGSTSTVMKGLAHGACDYLLKPVSIED 106
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
26-135 1.76e-20

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 86.36  E-value: 1.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTA 103
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLanTPAIALTG 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26111063 104 H---SDLDAAVSAyqqgAFD-YLPKPFDIDEAVALV 135
Cdd:cd17580  81 YgqpEDRERALEA----GFDaHLVKPVDPDELIELI 112
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
28-125 1.76e-20

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 87.06  E-value: 1.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAG------AGltctTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIM 101
Cdd:cd17541   5 IVDDSAVMRKLLSRILESdpdievVG----TARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPT-PVVMV 79
                        90       100
                ....*....|....*....|....*.
gi 26111063 102 TAHSDLDAAVS--AYQQGAFDYLPKP 125
Cdd:cd17541  80 SSLTEEGAEITleALELGAVDFIAKP 105
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
28-139 3.86e-20

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 85.68  E-value: 3.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd17553   5 IVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYGEL 84
                        90       100       110
                ....*....|....*....|....*....|..
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd17553  85 DMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
26-125 1.28e-19

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 83.74  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd19926   1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                        90       100
                ....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKP 125
Cdd:cd19926  81 SLDTAIEALKAGAFDFLTKP 100
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
28-126 1.37e-19

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: 83.71  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ----RHpmLPVIIMTA 103
Cdd:cd19920   3 IVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAdpatRH--IPVIFLTA 80
                        90       100
                ....*....|....*....|...
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPF 126
Cdd:cd19920  81 LTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
26-139 1.42e-19

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 83.89  E-value: 1.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTAH- 104
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQV-PVLMLTARg 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 105 SDLDAAVsAYQQGAFDYLPKPFDIDEAVALVeRAI 139
Cdd:cd17623  80 DDIDRIL-GLELGADDYLPKPFNPRELVARI-RAI 112
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
26-139 2.23e-19

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: 83.56  E-value: 2.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVeRAI 139
Cdd:cd17615  82 SVEDRIAGLTAGGDDYVTKPFSLEEVVARL-RAL 114
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
30-142 3.11e-19

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 83.62  E-value: 3.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  30 DDDSSIRWVlERALAGAGLTC--TTFENGAEVLEAL-------ASKTPDVLLSDIRMPGMDGLALLKQIKQ----RHpmL 96
Cdd:cd17557   7 DNPGDAELI-QEAFKEAGVPNelHVVRDGEEALDFLrgegeyaDAPRPDLILLDLNMPRMDGFEVLREIKAdpdlRR--I 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 26111063  97 PVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVeRAISHY 142
Cdd:cd17557  84 PVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAI-RSLGEY 128
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
26-126 4.32e-19

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: 82.16  E-value: 4.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 104
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                        90       100
                ....*....|....*....|..
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPF 126
Cdd:cd18160  82 AAAAPELLSDAVGDNATLKKPF 103
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
26-138 1.05e-18

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: 81.56  E-value: 1.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCT-TFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 104
Cdd:cd17542   3 VLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERA 138
Cdd:cd17542  83 GQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
28-135 4.96e-18

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: 79.62  E-value: 4.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHS 105
Cdd:cd19937   2 VVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSdpKTSSIPIIMLTAKG 81
                        90       100       110
                ....*....|....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALV 135
Cdd:cd19937  82 EEFDKVLGLELGADDYITKPFSPRELLARV 111
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
28-139 6.82e-18

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: 79.37  E-value: 6.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCT-TFENGAEVLEALASKTPDVLLSDIRMPG-MDGLALLKQIKQRHPmLPVIIMTAHS 105
Cdd:cd17534   5 IVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKFD-IPVIFLTAYS 83
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 26111063 106 D---LDAAVSAYQQGafdYLPKPFDIDEAVALVERAI 139
Cdd:cd17534  84 DeetLERAKETNPYG---YLVKPFNERELKAAIELAL 117
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
28-160 9.05e-18

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 82.54  E-value: 9.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASkTPDVLLSDIRMPGMDGLALLKQIKQRHpMLPVIIMTAH-SD 106
Cdd:PRK10955   6 LVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLTARgSE 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 26111063  107 LDaAVSAYQQGAFDYLPKPFDIDEAVALVeRAI---SHYQEQQQprNVQLNGPTTDI 160
Cdd:PRK10955  84 LD-RVLGLELGADDYLPKPFNDRELVARI-RAIlrrSHWSEQQQ--NNDNGSPTLEV 136
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
26-137 1.26e-17

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 78.53  E-value: 1.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTT-FENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMT 102
Cdd:cd19923   3 VLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALshLPVLMVT 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 103 AHSDLDAAVSAYQQGAFDYLPKPFdidEAVALVER 137
Cdd:cd19923  83 AEAKKENVIAAAQAGVNNYIVKPF---TAATLKEK 114
PRK10643 PRK10643
two-component system response regulator PmrA;
28-145 1.39e-17

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 81.62  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:PRK10643   5 IVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARDTL 84
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 26111063  108 DAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQ 145
Cdd:PRK10643  85 EDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQ 122
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
26-139 2.70e-17

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 77.73  E-value: 2.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQrHP---MLPVIIMT 102
Cdd:cd17562   3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRK-LPaykFTPILMLT 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 26111063 103 AHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd17562  82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
28-133 4.60e-17

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: 76.90  E-value: 4.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK--QRHPMLPVIIMTAHS 105
Cdd:cd17618   5 IVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIMLTARG 84
                        90       100
                ....*....|....*....|....*...
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVA 133
Cdd:cd17618  85 EEEDKVRGLEAGADDYITKPFSPRELVA 112
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
26-136 5.36e-17

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: 76.64  E-value: 5.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQrHPMLPVIIMTAHS 105
Cdd:cd19939   2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-HSHVPILMLTART 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVE 136
Cdd:cd19939  81 EEMDRVLGLEMGADDYLCKPFSPRELLARVR 111
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
26-135 7.52e-17

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: 76.33  E-value: 7.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAHS 105
Cdd:cd17594   2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSD-VPIIIISGDR 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063 106 DLDAA-VSAYQQGAFDYLPKPFDIDEAVALV 135
Cdd:cd17594  81 RDEIDrVVGLELGADDYLAKPFGLRELLARV 111
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
26-125 1.16e-16

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 75.28  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTAHS 105
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSAV-PVIVLSARD 79
                        90       100
                ....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKP 125
Cdd:cd17620  80 EESDKIAALDAGADDYLTKP 99
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
21-139 1.58e-16

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 78.47  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 100
Cdd:PRK11083   1 MQQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIF 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 26111063  101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVeRAI 139
Cdd:PRK11083  81 LTARSDEVDRLVGLEIGADDYVAKPFSPREVAARV-RTI 118
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
28-125 1.68e-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: 75.11  E-value: 1.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHS 105
Cdd:cd19927   3 LVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKnaDFDTIPVIFLTAKG 82
                        90       100
                ....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKP 125
Cdd:cd19927  83 MTSDRIKGYNAGCDGYLSKP 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
53-137 2.10e-16

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 75.27  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  53 FENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLdaAVSAYQQGAFDYLPKPFD---ID 129
Cdd:cd17532  30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTAYDEY--AVEAFELNAVDYLLKPFSeerLA 107

                ....*...
gi 26111063 130 EAVALVER 137
Cdd:cd17532 108 EALAKLRK 115
PRK15479 PRK15479
transcriptional regulator TctD;
28-147 3.14e-16

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 77.45  E-value: 3.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWvLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:PRK15479   6 AEDNRELAHW-LEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARSAV 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 26111063  108 DAAVSAYQQGAFDYLPKPFDIDE----AVALVERAISHYQEQQQ 147
Cdd:PRK15479  85 ADRVKGLNVGADDYLPKPFELEEldarLRALLRRSAGQVQEVQQ 128
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
28-125 4.57e-16

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: 73.63  E-value: 4.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEaLASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSD 106
Cdd:cd19935   3 VVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLH-LALTNEyDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARDS 81
                        90
                ....*....|....*....
gi 26111063 107 LDAAVSAYQQGAFDYLPKP 125
Cdd:cd19935  82 VEDRVKGLDLGADDYLVKP 100
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
28-135 5.32e-16

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: 74.04  E-value: 5.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAHSDL 107
Cdd:cd17626   5 VVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG-VPIVMLTAKSDT 83
                        90       100
                ....*....|....*....|....*...
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAVALV 135
Cdd:cd17626  84 VDVVLGLESGADDYVAKPFKPKELVARI 111
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
28-125 1.60e-15

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: 72.09  E-value: 1.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAHSDL 107
Cdd:cd19936   3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST-LPVIFLTSKDDE 81
                        90
                ....*....|....*...
gi 26111063 108 DAAVSAYQQGAFDYLPKP 125
Cdd:cd19936  82 IDEVFGLRMGADDYITKP 99
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
28-127 2.05e-15

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: 72.58  E-value: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALA-GAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIkQRHPM---LPVIIMTA 103
Cdd:cd17552   6 VIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKL-QANPEtqsIPVILLTA 84
                        90       100
                ....*....|....*....|....
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPFD 127
Cdd:cd17552  85 KAQPSDRQRFASLGVAGVIAKPFD 108
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
26-140 2.12e-15

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: 72.45  E-value: 2.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCT-TFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTAH 104
Cdd:cd19932   3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLTAY 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS 140
Cdd:cd19932  82 SQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIA 117
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
28-138 2.77e-15

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 71.93  E-value: 2.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:cd19934   3 LVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARDSW 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 108 DAAVSAYQQGAFDYLPKPFDIDEAV----ALVERA 138
Cdd:cd19934  83 QDKVEGLDAGADDYLTKPFHIEELLarlrALIRRA 117
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
26-130 2.98e-15

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: 71.89  E-value: 2.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAG--LTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:cd19925   3 VLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82
                        90       100
                ....*....|....*....|....*..
gi 26111063 104 HSDLDAAVSAYQQGAFDYLPKPFDIDE 130
Cdd:cd19925  83 ANDVETVREALRLGVVDYLIKPFTFER 109
ompR PRK09468
osmolarity response regulator; Provisional
28-148 4.06e-15

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 74.63  E-value: 4.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDL 107
Cdd:PRK09468  10 VVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAKGEE 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 26111063  108 DAAVSAYQQGAFDYLPKPFDIDEAVALVeRAISHYQEQQQP 148
Cdd:PRK09468  90 VDRIVGLEIGADDYLPKPFNPRELLARI-RAVLRRQAPELP 129
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
26-137 4.54e-15

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 76.34  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAG-AGLT-CTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTA 103
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNSdPDIEvVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPT-PVVMVSS 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 26111063  104 --HSDLDAAVSAYQQGAFDYLPKPF-----DIDEAVA-LVER 137
Cdd:PRK00742  85 ltERGAEITLRALELGAVDFVTKPFlgislGMDEYKEeLAEK 126
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
26-136 5.18e-15

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 71.25  E-value: 5.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKqRHPMLPVIIMTAHS 105
Cdd:cd19938   2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-RFSDVPIIMVTARV 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVE 136
Cdd:cd19938  81 EEIDRLLGLELGADDYICKPYSPREVVARVK 111
orf27 CHL00148
Ycf27; Reviewed
28-130 9.63e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 73.60  E-value: 9.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKqRHPMLPVIIMTAHSDL 107
Cdd:CHL00148  11 VVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR-KESDVPIIMLTALGDV 89
                         90       100
                 ....*....|....*....|...
gi 26111063  108 DAAVSAYQQGAFDYLPKPFDIDE 130
Cdd:CHL00148  90 SDRITGLELGADDYVVKPFSPKE 112
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
26-139 1.67e-14

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: 69.62  E-value: 1.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAHS 105
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:cd18159  80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
cztR_silR_copR TIGR01387
heavy metal response regulator; Members of this family contain a response regulator receiver ...
26-197 5.34e-14

heavy metal response regulator; Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system. [Regulatory functions, DNA interactions]


Pssm-ID: 130454 [Multi-domain]  Cd Length: 218  Bit Score: 70.98  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:TIGR01387   1 ILVVEDEQKTAEYLQQGLSESGYVVDAASNGRDGLHLALKDDYDLIILDVMLPGMDGWQILQTLRRSGKQTPVLFLTARD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRnVQLNGPTTDIIGEapamqdvfriigRLSRSSISVL 185
Cdd:TIGR01387  81 SVADKVKGLDLGADDYLVKPFSFSELLARVRTLLRRSHSLNSTV-LEIADLRMDSVRH------------RVSRGNIRIT 147
                         170
                  ....*....|..
gi 26111063   186 IngesgTGKELV 197
Cdd:TIGR01387 148 L-----TRKEFQ 154
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
26-139 5.71e-14

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 68.20  E-value: 5.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVeRAI 139
Cdd:cd17616  81 DIEDKVKGLGFGADDYMTKPFHKDELVARI-HAI 113
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
28-127 1.08e-13

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: 67.35  E-value: 1.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTAHS 105
Cdd:cd17598   3 IVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLkdIPVILLTTLS 82
                        90       100
                ....*....|....*....|..
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFD 127
Cdd:cd17598  83 DPRDVIRGLECGADNFITKPYD 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
26-125 1.54e-13

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 66.63  E-value: 1.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALA---------SKTPDVLLSDIRMPGMDGLALLKQIKQ--RHP 94
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063  95 MLPVIIMTAHSDLDAAVSAYQQGAFDYLPKP 125
Cdd:cd19924  81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
26-126 1.59e-13

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: 66.60  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKT-PDVLLSDIRMPG-MDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                        90       100
                ....*....|....*....|...
gi 26111063 104 hSDLDAAVSAYQQGAFDYLPKPF 126
Cdd:cd18161  81 -YAENAIEGGDLAPGVDVLSKPF 102
PRK10610 PRK10610
chemotaxis protein CheY;
28-126 1.79e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 67.31  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGL-TCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTAH 104
Cdd:PRK10610  10 VVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMsaLPVLMVTAE 89
                         90       100
                 ....*....|....*....|..
gi 26111063  105 SDLDAAVSAYQQGAFDYLPKPF 126
Cdd:PRK10610  90 AKKENIIAAAQAGASGYVVKPF 111
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
26-161 1.87e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 69.45  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGltCTTFEngAEVL-----EAlASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVII 100
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDG--MRVFE--AETLqrgllEA-ATRKPDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIV 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26111063  101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRN-VQLNGPTTDII 161
Cdd:PRK10529  78 LSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPAPDPlVKFSDVTVDLA 139
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
28-137 3.18e-13

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: 66.02  E-value: 3.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ----RHpmLPVIIMTA 103
Cdd:cd17548   4 IVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEdpatRD--IPVIALTA 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 26111063 104 H---SDLDAAVSAyqqGAFDYLPKPFDIDEAVALVER 137
Cdd:cd17548  82 YamkGDREKILEA---GCDGYISKPIDTREFLETVAK 115
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
31-137 4.81e-13

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 65.64  E-value: 4.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  31 DDSSI-RWVLERAL-AGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAhsdlD 108
Cdd:cd17593   7 DDSSMaRKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG----D 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 26111063 109 AAVSAYQQ----GAFDYLPKPFDIDEAVALVER 137
Cdd:cd17593  83 VQPEAKERvlelGALAFLKKPFDPEKLAQLLEE 115
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
26-137 5.15e-13

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


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 69.06  E-value: 5.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAG------AGLTCttfeNGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK--QRHPMLP 97
Cdd:COG5801   7 VLIADDNREFCELLEEYLSSqpdmevVGVAY----NGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLRemNLEKRPK 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 26111063  98 VIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDeavALVER 137
Cdd:COG5801  83 VIMLTAFGQEDITQRAVELGADYYILKPFDLD---VLAER 119
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
26-130 5.85e-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: 65.62  E-value: 5.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKtPDV--LLSDIRMPGMDGLALLKQIKQRHPM--LPVIIM 101
Cdd:cd17544   3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIklVITDYNMPEMDGFELVREIRKKYSRdqLAIIGI 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 26111063 102 TAHSdlDAAVSAY--QQGAFDYLPKPFDIDE 130
Cdd:cd17544  82 SASG--DNALSARfiKAGANDFLTKPFLPEE 110
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
183-321 6.11e-13

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 66.24  E-value: 6.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063    183 SVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIES---ELFGHEKGAFTGANTIRQG--RFEQADGGTLF 257
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26111063    258 LDEIGDMPLDVQTRLLRVLadgQFYRVGGYAPVKVDVRIIAATH--QNLEQRVLEGKFREDLFHRL 321
Cdd:smart00382  84 LDEITSLLDAEQEALLLLL---EELRLLLLLKSEKNLTVILTTNdeKDLGPALLRRRFDRRIVLLL 146
PRK10336 PRK10336
two-component system response regulator QseB;
26-154 7.72e-13

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 67.61  E-value: 7.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 26111063  106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAI--SHYQEQQQPR--NVQLN 154
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPFALIEVAARLEALMrrTNGQASNELRhgNVMLD 135
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
27-125 9.26e-13

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: 64.22  E-value: 9.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  27 WVVDDDSSIRWVLERALAGA--GLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAH 104
Cdd:cd17565   2 YIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQV 81
                        90       100
                ....*....|....*....|.
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKP 125
Cdd:cd17565  82 SDKEMIGKAYQAGIEFFINKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
26-78 1.20e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.59  E-value: 1.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 26111063     26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMP 78
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
28-136 1.49e-12

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: 63.98  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTAH-SD 106
Cdd:cd17614   3 VVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNV-PIIMLTAKdSE 81
                        90       100       110
                ....*....|....*....|....*....|
gi 26111063 107 LDaAVSAYQQGAFDYLPKPFDIDEAVALVE 136
Cdd:cd17614  82 VD-KVLGLELGADDYVTKPFSNRELLARVK 110
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
26-138 6.24e-12

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: 62.40  E-value: 6.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTAHS 105
Cdd:cd17619   3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEV-GIILVTGRD 81
                        90       100       110
                ....*....|....*....|....*....|...
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEavaLVERA 138
Cdd:cd17619  82 DEVDRIVGLEIGADDYVTKPFNPRE---LLVRA 111
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
26-133 6.95e-12

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 62.06  E-value: 6.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17573   1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                        90       100
                ....*....|....*....|....*...
gi 26111063 106 DLDAAVSAYQQGAFDYLPKPFDIDEAVA 133
Cdd:cd17573  81 KTEQEIEAFKEGADDYIAKPFDFKVLVA 108
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
26-147 1.10e-11

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: 62.00  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAgAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:cd17596   3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 26111063 106 DLDAAVSAYQQ-GAFDYLPKPFDIDEAVALVERAISHYQEQQQ 147
Cdd:cd17596  82 DSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFELQRE 124
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
447-485 1.71e-11

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 58.56  E-value: 1.71e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 26111063   447 PELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKE 485
Cdd:pfam02954   2 EEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
55-126 2.36e-11

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: 60.31  E-value: 2.36e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26111063  55 NGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQR--HPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPF 126
Cdd:cd17561  35 NGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMrlEKRPKIIMLTAFGQEDITQRAVELGASYYILKPF 108
PRK10816 PRK10816
two-component system response regulator PhoP;
26-133 3.18e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 62.83  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                         90       100
                 ....*....|....*....|....*...
gi 26111063  106 DLDAAVSAYQQGAFDYLPKPFDIDEAVA 133
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVMA 110
pleD PRK09581
response regulator PleD; Reviewed
28-137 3.71e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 64.92  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDD-DSSIRwVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK--QRHPMLPVIIMTAH 104
Cdd:PRK09581   7 VVDDiPANVK-LLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKsdPATTHIPVVMVTAL 85
                         90       100       110
                 ....*....|....*....|....*....|...
gi 26111063  105 SDLDAAVSAYQQGAFDYLPKPfdIDEaVALVER 137
Cdd:PRK09581  86 DDPEDRVRGLEAGADDFLTKP--IND-VALFAR 115
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
26-156 4.31e-11

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 62.78  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKqRHPMLPVIIMTAHS 105
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR-RFSDIPIVMVTAKI 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 26111063  106 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGP 156
Cdd:PRK10710  92 EEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESP 142
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
25-127 5.48e-11

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 60.04  E-value: 5.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  25 IVWVVDDDSSIRWVLERALA---GAGLTCTTFENGAEVLEALA-----SKTPDVLLSDIRMPGMDGLALLKQIKQRHPML 96
Cdd:cd17595   2 IILTVDDDPQVLRAVARDLRrqyGKDYRVLRADSGAEALDALKelklrGEAVALFLVDQRMPEMDGVEFLEKAMELFPEA 81
                        90       100       110
                ....*....|....*....|....*....|..
gi 26111063  97 PVIIMTAHSDLDAAVSAYQQGAFD-YLPKPFD 127
Cdd:cd17595  82 KRVLLTAYADTDAAIRAINDVQLDyYLLKPWD 113
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
26-125 8.85e-11

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 59.30  E-value: 8.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTP-----------DVLLSDIRMPGMDGLALLKQIKQRHP 94
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEedssnfnepkvNMIITDYCMPGMTGYDLLKKVKESSA 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 26111063  95 M--LPVIIMTAHSDLDAAVSAYQQGAFDYLPKP 125
Cdd:cd17581  81 LkeIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
51-137 9.50e-11

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 58.82  E-value: 9.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  51 TTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDE 130
Cdd:cd19930  28 AQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEE 107

                ....*..
gi 26111063 131 AVALVER 137
Cdd:cd19930 108 LADAIRT 114
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
26-125 1.25e-10

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 58.18  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTP--DVLLSDIRMPGMDGLALLKQIkQRHPML---PVII 100
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYI-MRHKICkniPVIM 79
                        90       100
                ....*....|....*....|....*
gi 26111063 101 MTAHSDLDAAVSAYQQGAFDYLPKP 125
Cdd:cd17582  80 MSSQDSVGVVFKCLSKGAADYLVKP 104
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
28-89 1.59e-10

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: 58.75  E-value: 1.59e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26111063  28 VVDDDSSIRWVLERALAGAG--LTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQI 89
Cdd:COG2197   6 IVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
51-166 2.18e-10

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 63.33  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   51 TTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQrHPM---LPVIIMTAHsdldaAVSA-----YQQGAFDYL 122
Cdd:PRK11107 695 VLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQ-LPHnqnTPIIAVTAH-----AMAGererlLSAGMDDYL 768
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 26111063  123 PKPfdIDEAValVERAISHYQEQQQPRNVQLNGPTTDIIGEAPA 166
Cdd:PRK11107 769 AKP--IDEAM--LKQVLLRYKPGPKFTSRVVAPEPPEPVHFPNA 808
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
55-129 3.25e-10

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


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 60.58  E-value: 3.25e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26111063    55 NGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK--QRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDID 129
Cdd:TIGR02875  36 NGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNeiELSARPRVIMLSAFGQEKITQRAVALGADYYVLKPFDLE 112
PRK15369 PRK15369
two component system response regulator;
54-124 4.02e-10

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 59.71  E-value: 4.02e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26111063   54 ENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPK 124
Cdd:PRK15369  36 DNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLK 106
PRK10693 PRK10693
two-component system response regulator RssB;
54-125 1.05e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 59.62  E-value: 1.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26111063   54 ENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKP 125
Cdd:PRK10693   4 ANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
28-139 1.15e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 59.89  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAG----LTCTTfeNGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTa 103
Cdd:PRK12555   5 IVNDSPLAVEALRRALARDPdhevVWVAT--DGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPC-PILIVT- 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 26111063  104 hSDLDAAVS----AYQQGAFDYLPKPF-----DIDEAVALVERAI 139
Cdd:PRK12555  81 -SLTERNASrvfeAMGAGALDAVDTPTlgigaGLEEYAAELLAKI 124
PRK11517 PRK11517
DNA-binding response regulator HprR;
25-135 1.84e-09

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 57.99  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   25 IVWVVDDDSSIRWVlERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHpMLPVIIMTAH 104
Cdd:PRK11517   3 ILLIEDNQRTQEWV-TQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK-QTPVICLTAR 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 26111063  105 SDLDAAVSAYQQGAFDYLPKPFDIDEAVALV 135
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVKPFSFSELLARV 111
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
21-165 2.90e-09

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 57.42  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVwVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKqRHPM---LP 97
Cdd:PRK10161   1 MARRIL-VVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLK-RESMtrdIP 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26111063   98 VIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTD------IIGEAP 165
Cdd:PRK10161  79 VVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLDptshrvMAGEEP 152
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
448-489 3.64e-09

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


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 53.28  E-value: 3.64e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 26111063 448 ELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 489
Cdd:COG2901  42 EVEKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGLL 83
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
26-125 1.26e-08

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: 52.59  E-value: 1.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAHS 105
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN-VPVIMVTAKD 79
                        90       100
                ....*....|....*....|
gi 26111063 106 DLDAAVSAYQQGAFDYLPKP 125
Cdd:cd17621  80 SEIDKVVGLELGADDYVTKP 99
PRK10766 PRK10766
two-component system response regulator TorR;
26-145 1.93e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 54.66  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAHS 105
Cdd:PRK10766   5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRST-VGIILVTGRT 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 26111063  106 DLDAAVSAYQQGAFDYLPKPFDIDEAV----------ALVERAISHYQEQ 145
Cdd:PRK10766  84 DSIDRIVGLEMGADDYVTKPLELRELLvrvknllwriSLARQAQPHAQEE 133
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
26-103 3.75e-08

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 56.14  E-value: 3.75e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:PRK10841 804 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTA 881
PRK14084 PRK14084
DNA-binding response regulator;
54-147 7.09e-08

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 53.60  E-value: 7.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   54 ENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQI-KQRHPmlPVIIM-TAHSDLdaAVSAYQQGAFDYLPKPFD---I 128
Cdd:PRK14084  33 ENVKETLEALLINQYDIIFLDINLMDESGIELAAKIqKMKEP--PAIIFaTAHDQF--AVKAFELNATDYILKPFEqkrI 108
                         90
                 ....*....|....*....
gi 26111063  129 DEAVALVERAISHYQEQQQ 147
Cdd:PRK14084 109 EQAVNKVRATKAKDDNNAS 127
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
28-142 7.59e-08

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 52.59  E-value: 7.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   28 VVDDDSSIRWVLERALAGAGLTCTT-FENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSD 106
Cdd:PRK09958   5 IIDDHPLAIAAIRNLLIKNDIEILAeLTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKND 84
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 26111063  107 LDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHY 142
Cdd:PRK09958  85 HFYGKHCADAGANGFVSKKEGMNNIIAAIEAAKNGY 120
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
25-127 7.84e-08

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: 50.84  E-value: 7.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  25 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKqRHPMLPVIIMTAH 104
Cdd:cd17622   2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR-PKYQGPILLLTAL 80
                        90       100
                ....*....|....*....|...
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKPFD 127
Cdd:cd17622  81 DSDIDHILGLELGADDYVVKPVE 103
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
21-140 1.58e-07

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: 49.65  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  21 MQRGIVWVVDDDSSIRWVLERAlagagltcttfeNGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 100
Cdd:cd19931  10 LRKGIKQLIELDPDFTVVGEAS------------SGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVI 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 26111063 101 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS 140
Cdd:cd19931  78 LTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
25-133 1.59e-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: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  25 IVWVVDDDSSIRWVLERALAGAglTCTTFENGAEVLEALASKT---PDVLLSDIRMPGMDGLALLKQIKqRHPM---LPV 98
Cdd:cd17575   2 MVLLVDDQAIIGEAVRRALADE--EDIDFHYCSDPTEAIEVASqikPTVILQDLVMPGVDGLTLVRFFR-ANPAtrdIPI 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063  99 IIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVA 133
Cdd:cd17575  79 IVLSTKEEPEVKSEAFALGANDYLVKLPDKIELVA 113
PLN03029 PLN03029
type-a response regulator protein; Provisional
26-152 1.96e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 51.96  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALA--------SKTPDV------------LLSDIRMPGMDGLAL 85
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnPDTPSVspnshqevevnlIITDYCMPGMTGYDL 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26111063   86 LKQIKQRHPM--LPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVAL---VERAISHYQEQQQPRNVQ 152
Cdd:PLN03029  91 LKKIKESSSLrnIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLkphMMKTKSKNQKQENQEKQE 162
PRK13557 PRK13557
histidine kinase; Provisional
26-139 2.32e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 53.14  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASK-TPDVLLSDIRMPG-MDGLALLKQIKQRHPMLPVIIMTA 103
Cdd:PRK13557 418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTTG 497
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 26111063  104 HSdlDAAVSAYQQGA--FDYLPKPFDIDEAVALVERAI 139
Cdd:PRK13557 498 YA--EASIERTDAGGseFDILNKPYRRAELARRVRMVL 533
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
6-129 2.39e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 53.58  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063     6 RVLGLPAYQEIKVTFMQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLAL 85
Cdd:PRK09959  941 QVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFEL 1020
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 26111063    86 LKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDID 129
Cdd:PRK09959 1021 TRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLD 1064
PRK13856 PRK13856
two-component response regulator VirG; Provisional
26-139 2.46e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 51.74  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMTAhS 105
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKSD-VPIIIISG-D 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 26111063  106 DLDAA--VSAYQQGAFDYLPKPFDIDEAVALVERAI 139
Cdd:PRK13856  82 RLEEAdkVVALELGATDFIAKPFGTREFLARIRVAL 117
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
26-146 3.14e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 51.08  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 105
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 26111063  106 DLDAAVSAYQQGAFDYLPKPFDIDEAVA----LVERAISHYQEQQ 146
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPFAFAELLArvrtLLRRGAAVIIESQ 127
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
26-138 5.06e-07

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: 48.59  E-value: 5.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAG-LTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMtah 104
Cdd:cd17530   3 VLVLDDDPFQCMMAATILEDLGpGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILM--- 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 26111063 105 SDLDAAV--------SAYQQGAFDYLPKPFDIDEAVALVERA 138
Cdd:cd17530  80 SGLDGGIlesaetlaGANGLNLLGTLSKPFSPEELTELLTKY 121
PRK15347 PRK15347
two component system sensor kinase;
26-202 6.19e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 52.34  E-value: 6.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQ----IKQRHPMLPVIIM 101
Cdd:PRK15347 693 ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLwrddPNNLDPDCMIVAL 772
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  102 TAHSDLDAAVSAYQQGAFDYLPKPFDIdeavALVERAISHYQEQQQPRNVQLNgPTTDIigEAP--AMQDVfRIIGRLSR 179
Cdd:PRK15347 773 TANAAPEEIHRCKKAGMNHYLTKPVTL----AQLARALELAAEYQLLRGIELS-PQDSS--CSPllDTDDM-ALNSKLYQ 844
                        170       180
                 ....*....|....*....|....*
gi 26111063  180 sSISVLIN--GESGTGKELVAHALH 202
Cdd:PRK15347 845 -SLLLLLAqiEQAVENQEVLSQLLH 868
PRK13558 PRK13558
bacterio-opsin activator; Provisional
23-164 6.33e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 52.15  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   23 RGIVWVVDDDSSIRWVLERALAGAgLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMT 102
Cdd:PRK13558   8 RGVLFVGDDPEAGPVDCDLDEDGR-LDVTQIRDFVAARDRVEAGEIDCVVADHEPDGFDGLALLEAVRQTTAVPPVVVVP 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26111063  103 AHSDLDAAVSAYQQGAFDYLPKPFDiDEAVALVERAISHYQEQQqpRNVQLNGPTTDIIGEA 164
Cdd:PRK13558  87 TAGDEAVARRAVDADAAAYVPAVSD-DATAAIAERIESAVPEHS--RDTEARMPISDLTVES 145
PRK09483 PRK09483
response regulator; Provisional
26-143 8.52e-07

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 49.72  E-value: 8.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDD----SSIRWVLE--RALAGAGLTCTtfenGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVI 99
Cdd:PRK09483   4 VLLVDDHelvrAGIRRILEdiKGIKVVGEACC----GEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKII 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 26111063  100 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVeRAISHYQ 143
Cdd:PRK09483  80 MLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAI-RSVHSGQ 122
PRK11697 PRK11697
two-component system response regulator BtsR;
55-127 8.56e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 50.23  E-value: 8.56e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26111063   55 NGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHpMLPVIIMTAHSDLdaAVSAYQQGAFDYLPKPFD 127
Cdd:PRK11697  35 NAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEH-MPYIVFVTAFDEY--AIKAFEEHAFDYLLKPID 104
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
53-124 1.18e-06

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 49.45  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   53 FENGAEVLEALASKTPDVLLSDIRMPG---MDGLALLKQIKQRHPMLPVIIMTAHS---------DLDAAVSAYQQGAFD 120
Cdd:PRK10840  35 FEDSTALINNLPKLDAHVLITDLSMPGdkyGDGITLIKYIKRHFPSLSIIVLTMNNnpailsavlDLDIEGIVLKQGAPT 114

                 ....
gi 26111063  121 YLPK 124
Cdd:PRK10840 115 DLPK 118
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
29-125 1.19e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 46.98  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  29 VDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ----RHpmLPVIIMTAH 104
Cdd:cd17602   4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKssalKD--TPIIMLTGK 81
                        90       100
                ....*....|....*....|.
gi 26111063 105 SDLDAAVSAYQQGAFDYLPKP 125
Cdd:cd17602  82 DGLVDRIRAKMAGASGYLTKP 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
183-301 1.57e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 47.29  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   183 SVLINGESGTGK-ELVAHALHRHSPRAkapfiaLNMAAIPKDLIESELFGH-----EKGAFTGANTIRQGRfeqaDGGTL 256
Cdd:pfam07728   1 GVLLVGPPGTGKtELAERLAAALSNRP------VFYVQLTRDTTEEDLFGRrnidpGGASWVDGPLVRAAR----EGEIA 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26111063   257 FLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKV---DVRIIAATH 301
Cdd:pfam07728  71 VLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMN 118
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
55-132 2.38e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 48.49  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   55 NGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPK---PFDIDEA 131
Cdd:PRK10651  40 NGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKdmePEDLLKA 119

                 .
gi 26111063  132 V 132
Cdd:PRK10651 120 L 120
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
58-142 2.55e-06

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 48.33  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   58 EVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVER 137
Cdd:PRK09935  40 ITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQM 119

                 ....*
gi 26111063  138 AISHY 142
Cdd:PRK09935 120 ILSGY 124
PRK11173 PRK11173
two-component response regulator; Provisional
21-160 3.84e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 48.09  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   21 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVII 100
Cdd:PRK11173   1 MQTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANV-ALMF 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26111063  101 MTAH-SDLDaAVSAYQQGAFDYLPKPFDIDE----AVALVERAISHYQEQQQPRNVQ---LNGPTTDI 160
Cdd:PRK11173  80 LTGRdNEVD-KILGLEIGADDYITKPFNPREltirARNLLSRTMNLGTVSEERRSVEsykFNGWELDI 146
dpiA PRK10046
two-component response regulator DpiA; Provisional
68-147 5.92e-06

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 47.32  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   68 PDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFdideAVALVERAISHYQEQQQ 147
Cdd:PRK10046  51 PGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPI----AYERLGQTLTRFRQRKH 126
fis PRK00430
DNA-binding transcriptional regulator Fis;
448-488 6.86e-06

DNA-binding transcriptional regulator Fis;


Pssm-ID: 179020 [Multi-domain]  Cd Length: 95  Bit Score: 44.67  E-value: 6.86e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 26111063  448 ELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGM 488
Cdd:PRK00430  54 EVEAPLLDMVMQYTRGNQTRAALMLGINRGTLRKKLKKYGM 94
PRK10430 PRK10430
two-component system response regulator DcuR;
26-147 7.15e-06

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 47.41  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   26 VWVVDDDSSIRWVLERALAG-AGLTC----TTFENGAEVLeaLASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPMLPVI 99
Cdd:PRK10430   4 VLIVDDDAMVAELNRRYVAQiPGFQCcgtaSTLEQAKEII--FNSDTPiDLILLDIYMQQENGLDLLPVLHEAGCKSDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 26111063  100 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIdeavALVERAISHYQEQQQ 147
Cdd:PRK10430  82 VISSAADAATIKDSLHYGVVDYLIKPFQA----SRFEEALTGWRQKKM 125
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
51-130 9.67e-06

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 44.92  E-value: 9.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  51 TTFENGAEVLEALASKTP---DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFD 127
Cdd:cd17533  34 ELTGKTEELLEKIKERGKngiYFLDIDIKMEEKNGLEVAQKIRKYDPYAIIIFVTTHSEFAPLTFEYKVAALDFILKPLK 113

                ...
gi 26111063 128 IDE 130
Cdd:cd17533 114 LEE 116
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
43-155 1.24e-05

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 47.98  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   43 LAGAGLTCTTFENGAEVLEALASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSdLDAAVSAYQQGAF-D 120
Cdd:PRK11466 701 LNTSGAQVVAVGNAAQALETLQNSEPfAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSAHV-IDETLRQRTSSLFrG 779
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 26111063  121 YLPKPFDIDEAVALVERAISHYQEQQQPRNV-QLNG 155
Cdd:PRK11466 780 IIPKPVPREVLGQLLAHYLQLQVNNDQPLDVsQLNE 815
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
26-106 1.31e-05

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: 44.31  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPD--VLLSDIRMPGMDGLALLKQIKQRHPM---LPVII 100
Cdd:cd19933   3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLFGRrerPLIVA 82

                ....*.
gi 26111063 101 MTAHSD 106
Cdd:cd19933  83 LTANTD 88
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
28-137 5.51e-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: 42.63  E-value: 5.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  28 VVDDDSSIRWVLERALAGAGLT-CTTFENGAEVLEALASKTPDVLLSDIRM-PGMDGLALLKQIKQRHPMLP---VIIMT 102
Cdd:cd17589   3 IVDDQPTFRSMLKSMLRSLGVTrIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELRHKKLISPstvFIMVT 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 103 AHSDLDAAVSAYQQGAFDYLPKPFDIDEavaLVER 137
Cdd:cd17589  83 GESSRAMVLSALELEPDDYLLKPFTVSE---LRER 114
PRK10360 PRK10360
transcriptional regulator UhpA;
53-141 5.92e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 44.20  E-value: 5.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   53 FENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRhpmLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAV 132
Cdd:PRK10360  33 FGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPKG---MATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELI 109

                 ....*....
gi 26111063  133 ALVeRAISH 141
Cdd:PRK10360 110 AAV-HTVAT 117
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
26-139 2.94e-04

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


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 40.14  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGAGLT-CTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHpmLPVIIMTAH 104
Cdd:cd17586   1 VLVLEDEPLIAMNLEDALEDLGGKeVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVADALKRRA--IPFIFATGY 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 26111063 105 SDlDAAVSAYQQGAfDYLPKPFDIDEAVALVERAI 139
Cdd:cd17586  79 GD-SHGIDSRLIDV-PVLRKPFDADSALAALAMLL 111
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
26-137 2.00e-03

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 37.93  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  26 VWVVDDDSSIRWVLERALAGA-GLTCTTFENGAEVLEALASKTPDVL-LSDIRMP-GMDG----LALLKQIkqrhpmlPV 98
Cdd:cd19921   2 VLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLEEGDDYFAaLVDLNLPdAPNGeavdLVLEKGI-------PV 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26111063  99 IIMTAHSDLDAAVSAYQQGAFDYLPK--PFDIDEAVALVER 137
Cdd:cd19921  75 IVLTGSFDEDKRETLLSKGVVDYVLKdsRYSYDYVVKLVRR 115
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
57-139 7.42e-03

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 36.46  E-value: 7.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063  57 AEVLEALASKTPDVLLSDIRMP-GMDGLALLKQIKQRHPMlPVIIMTAHSDlDAAVSAYQQGAFdYLPKPFDIDEAVALV 135
Cdd:cd17540  35 DEAVALARRERPDLILADIQLAdGSSGIDAVNEILTTHDV-PVIFVTAYPE-RLLTGERPEPTF-LITKPFDPEMVKAAI 111

                ....
gi 26111063 136 ERAI 139
Cdd:cd17540 112 SQAL 115
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
184-301 9.69e-03

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 36.42  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26111063   184 VLINGESGTGKELVAHALHRHsprAKAPFIALNMaaipkdlieSELFGHEKGAftGANTIRQgRFEQADGGT---LFLDE 260
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKE---LGAPFIEISG---------SELVSKYVGE--SEKRLRE-LFEAAKKLApcvIFIDE 65
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 26111063   261 I-----------GDMPLDVQTRLLRVLADGQfyrvggyaPVKVDVRIIAATH 301
Cdd:pfam00004  66 IdalagsrgsggDSESRRVVNQLLTELDGFT--------SSNSKVIVIAATN 109
 
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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