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Conserved domains on  [gi|966357534|ref|WP_058405928|]
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MULTISPECIES: nitrogen regulation protein NR(I) [unclassified Pseudoalteromonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ntrC super family cl36982
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-457 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]


The actual alignment was detected with superfamily member TIGR01818:

Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 686.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQAPP--KSAHIIGEAPAMQEVFRAIGKLSASSMSV 161
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEaeDSAELIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  162 LINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDM 241
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  242 PLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQH 321
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  322 FLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTPIQVEGD------WL 395
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDsdgqdsWD 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966357534  396 DAFQQWLNNELKQGKENIWPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:TIGR01818 401 EALEAWAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
 
Name Accession Description Interval E-value
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-457 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: 686.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQAPP--KSAHIIGEAPAMQEVFRAIGKLSASSMSV 161
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEaeDSAELIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  162 LINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDM 241
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  242 PLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQH 321
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  322 FLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTPIQVEGD------WL 395
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDsdgqdsWD 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966357534  396 DAFQQWLNNELKQGKENIWPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:TIGR01818 401 EALEAWAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-457 0e+00

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 671.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF-RANSTKKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMSVL 162
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIsHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 163 INGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDMP 242
Cdd:PRK10923 166 INGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 243 LDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHF 322
Cdd:PRK10923 246 LDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHF 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 323 LHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTP----IQVEGD-WLDA 397
Cdd:PRK10923 326 LQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVpestSQMQPDsWATL 405
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 398 FQQWLNNELKQGKENIWPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:PRK10923 406 LAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKE 465
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-457 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: 553.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRanstkKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMS 160
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE-----RRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 161 VLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGD 240
Cdd:COG2204  157 VLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 241 MPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQ 320
Cdd:COG2204  237 MPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLAR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 321 HFLHKSAKDLQVESKvLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLppeiievtpiqvegdwldafqq 400
Cdd:COG2204  317 HFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDL---------------------- 373
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966357534 401 wlnnelkqgkeniwPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:COG2204  374 --------------PEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
Sigma54_activat pfam00158
Sigma-54 interaction domain;
137-304 4.41e-111

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 324.74  E-value: 4.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  137 IIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTG 216
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  217 ADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFH 296
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 966357534  297 RLNVVRLR 304
Cdd:pfam00158 161 RLNVIPIE 168
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
2-117 6.49e-67

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: 209.82  E-value: 6.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF 117
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
160-278 3.87e-12

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: 63.93  E-value: 3.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   160 SVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVES---ELFGHEKGAFTGADSVRKG--RFEQANGGTLF 234
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 966357534   235 LDEIGDMPLDVQTRLLRVLadgEFYRVGGHQSIKVDVRIIAATH 278
Cdd:smart00382  84 LDEITSLLDAEQEALLLLL---EELRLLLLLKSEKNLTVILTTN 124
 
Name Accession Description Interval E-value
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
4-457 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: 686.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQAPP--KSAHIIGEAPAMQEVFRAIGKLSASSMSV 161
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAHAQEQVALPADAGEaeDSAELIGEAPAMQEVFRAIGRLSRSDITV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  162 LINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDM 241
Cdd:TIGR01818 161 LINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  242 PLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQH 321
Cdd:TIGR01818 241 PLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLARH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  322 FLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTPIQVEGD------WL 395
Cdd:TIGR01818 321 FLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDsdgqdsWD 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966357534  396 DAFQQWLNNELKQGKENIWPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:TIGR01818 401 EALEAWAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLKE 462
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-457 0e+00

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 671.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF-RANSTKKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMSVL 162
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIsHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 163 INGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDMP 242
Cdd:PRK10923 166 INGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 243 LDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHF 322
Cdd:PRK10923 246 LDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHF 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 323 LHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTP----IQVEGD-WLDA 397
Cdd:PRK10923 326 LQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVpestSQMQPDsWATL 405
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 398 FQQWLNNELKQGKENIWPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:PRK10923 406 LAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKE 465
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-457 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: 553.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRanstkKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMS 160
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE-----RRRLRRENAEDSGLIGRSPAMQEVRRLIEKVAPSDAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 161 VLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGD 240
Cdd:COG2204  157 VLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 241 MPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQ 320
Cdd:COG2204  237 MPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLAR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 321 HFLHKSAKDLQVESKvLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLppeiievtpiqvegdwldafqq 400
Cdd:COG2204  317 HFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDL---------------------- 373
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966357534 401 wlnnelkqgkeniwPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:COG2204  374 --------------PEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKK 416
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
105-461 2.38e-155

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: 448.07  E-value: 2.38e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 105 DLNEAVALVEsafRANSTKKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPR 184
Cdd:COG3829  111 DITELKRLER---KLREEELERGLSAKYTFDDIIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPR 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 185 KENQFIALNMAAIPKELVESELFGHEKGAFTGADSV-RKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGG 263
Cdd:COG3829  188 RDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKKGgKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGG 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 264 HQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLQVESKVLSPKATE 343
Cdd:COG3829  268 TKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALE 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 344 QLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTPIQVEGDwldafqqwlNNELKqgkeniwpDIQAQLET 423
Cdd:COG3829  348 LLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAASAAE---------EGSLK--------EALEEVEK 410
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 966357534 424 RLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKERNIS 461
Cdd:COG3829  411 ELIEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
3-460 8.19e-144

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 419.25  E-value: 8.19e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKR--KQAPPKS---AHIIGEAPAMQEVFRAIGKLSAS 157
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRhlHQALSTSwqwGHILTNSPAMMDICKDTAKIALS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 158 SMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDE 237
Cdd:PRK11361 166 QASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 238 IGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIER 317
Cdd:PRK11361 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 318 LAQHFLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIE-VTPIQVegdwld 396
Cdd:PRK11361 326 LANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQpVCNAGE------ 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966357534 397 afqqwlNNELKQGKENIWPDIQaQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKERNI 460
Cdd:PRK11361 400 ------VKTAPVGERNLKEEIK-RVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-455 4.56e-124

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 368.20  E-value: 4.56e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMSVLI 163
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAPSEATVLI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 164 NGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDMPL 243
Cdd:PRK10365 168 HGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 244 DVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHFL 323
Cdd:PRK10365 248 MMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 324 HKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEvTPIQVEgdwldafqqwln 403
Cdd:PRK10365 328 QRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIAS-TPIPLG------------ 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966357534 404 nelkqGKENIWPDIqaQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKL 455
Cdd:PRK10365 395 -----QSQDIQPLV--EVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
127-459 3.20e-122

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 369.61  E-value: 3.20e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 127 RKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESEL 206
Cdd:COG3284  313 GAPAPAALAALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESEL 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 207 FGHEKGAFTGADSV-RKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLV 285
Cdd:COG3284  393 FGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELV 472
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 286 KQGKFRDDLFHRLNVVRLRLPALRERtEDIERLAQHFLHKSAKDLQveSKVLSPKATEQLRLFNWPGNVRQLENTCRWLT 365
Cdd:COG3284  473 AAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAGRG--PLRLSPEALALLAAYPWPGNVRELRNVLRTAL 549
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 366 VMAPGELVTEQDLPPEIIEVTPIQVEGDWLDAfqqwlnNELKqgkeniwpdiqaQLETRLIKTALANCSGHKQDAAIKIG 445
Cdd:COG3284  550 ALADGGVITVEDLPDELRAELAAAAPAAAAPL------TSLE------------EAERDAILRALRACGGNVSAAARALG 611
                        330
                 ....*....|....
gi 966357534 446 WGRNTLTRKLKERN 459
Cdd:COG3284  612 ISRSTLYRKLKRYG 625
PRK15115 PRK15115
response regulator GlrR; Provisional
6-381 9.44e-115

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 344.51  E-value: 9.44e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:PRK15115  10 LVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAF--RANSTKKTKRkqappksAHIIGEAPAMQEVFRAIGKLSASSMSVLI 163
Cdd:PRK15115  90 PDAVAATQQGVFSFLTKPVDRDALYKAIDDALeqSAPATDERWR-------EAIVTRSPLMLRLLEQARMVAQSDVSVLI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 164 NGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDMPL 243
Cdd:PRK15115 163 NGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 244 DVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHFL 323
Cdd:PRK15115 243 PLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLL 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966357534 324 HKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENT---CRWLTVmAP--GELVTEQDLPPE 381
Cdd:PRK15115 323 RQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVieqCVALTS-SPviSDALVEQALEGE 384
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
6-451 1.38e-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: 341.34  E-value: 1.38e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    6 LVDDDASIRFVLEKALErsGFNVESFANAQDVLNALKFSQPAVLVSDVKMP-----GMDGMALLELIAEQNPGLPVIIMT 80
Cdd:TIGR02915   3 IVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANS----TKKTKRKQAPPKSAHIIGEAPAMQEVFRAIGKLSA 156
Cdd:TIGR02915  81 GNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTleteNRRLQSALGGTALRGLITSSPGMQKICRTIEKIAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  157 SSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLD 236
Cdd:TIGR02915 161 SDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLFLD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  237 EIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIE 316
Cdd:TIGR02915 241 EIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGDAV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  317 RLAQHFLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTPIQVEGDwld 396
Cdd:TIGR02915 321 LLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLGLDARERAETPLEVN--- 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966357534  397 afqqwlnneLKQGKENIwpdiqaqlETRLIKTALANCSGHKQDAAIKIGWGRNTL 451
Cdd:TIGR02915 398 ---------LREVRERA--------EREAVRKAIARVDGNIARAAELLGITRPTL 435
Sigma54_activat pfam00158
Sigma-54 interaction domain;
137-304 4.41e-111

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 324.74  E-value: 4.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  137 IIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTG 216
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  217 ADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFH 296
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 966357534  297 RLNVVRLR 304
Cdd:pfam00158 161 RLNVIPIE 168
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
127-377 5.10e-103

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: 317.43  E-value: 5.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  127 RKQAPPKSAHIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESEL 206
Cdd:TIGR01817 188 ARRRSGKEDGIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESEL 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  207 FGHEKGAFTGADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVK 286
Cdd:TIGR01817 268 FGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVA 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  287 QGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHFLHKSAKDlQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTV 366
Cdd:TIGR01817 348 KGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRE-NGRPLTITPSAIRVLMSCKWPGNVRELENCLERTAT 426
                         250
                  ....*....|.
gi 966357534  367 MAPGELVTEQD 377
Cdd:TIGR01817 427 LSRSGTITRSD 437
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
136-378 1.08e-102

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 315.59  E-value: 1.08e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 136 HIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFT 215
Cdd:COG3283  205 HIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFG 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 216 GADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLF 295
Cdd:COG3283  285 NAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLY 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 296 HRLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTC-RWLTvMAPGELVT 374
Cdd:COG3283  365 YRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALyRAVS-LLEGDELT 443

                 ....
gi 966357534 375 EQDL 378
Cdd:COG3283  444 PEDL 447
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
91-399 2.59e-102

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 314.42  E-value: 2.59e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  91 AFQKGAFEYLAkPFDLNEAVALVESAFR--------ANSTKKTKR-----KQAPPKSAHIIGEAPAMQEVFRAIGKLSAS 157
Cdd:PRK05022 131 ALDPGQFDAFS-DEELRALAALAAATLRnallieqlESQAELPQDvaeflRQEALKEGEMIGQSPAMQQLKKEIEVVAAS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 158 SMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQANGGTLFLDE 237
Cdd:PRK05022 210 DLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGTLFLDE 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 238 IGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIER 317
Cdd:PRK05022 290 IGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLL 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 318 LAQHFLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTC-------------RWLTVMAP-GELVTEQDLPPEII 383
Cdd:PRK05022 370 LAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVIsraallarargagRIVTLEAQhLDLPAEVALPPPEA 449
                        330       340
                 ....*....|....*....|
gi 966357534 384 EVTPIQVEGDWL----DAFQ 399
Cdd:PRK05022 450 AAAPAAVVSQNLreatEAFQ 469
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
33-459 3.16e-90

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 284.30  E-value: 3.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  33 NAQDVLNALKFSQPAVLVsdvkmpgmdGMALLELIAEQnPGLP-VIIMTAhsdlDSAVNAFQKgAFEyLAKPFDLNEAVA 111
Cdd:PRK15424 143 DARGQINELKANGIEAVV---------GAGLITDLAEE-AGMTgIFIYSA----ATVRQAFED-ALD-MTRMTLRHNTHY 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 112 LVESAFRANSTKKTkrkqappksahIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSP-------- 183
Cdd:PRK15424 207 ATRNALRTRYVLGD-----------LLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHREYFarhdarqg 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 184 RKENQFIALNMAAIPKELVESELFGHEKGAFTGadSVRKGR---FEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYR 260
Cdd:PRK15424 276 KKSHPFVAVNCGAIAESLLEAELFGYEEGAFTG--SRRGGRaglFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTR 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 261 VGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHFLHKS--AKDLQVESKVLS 338
Cdd:PRK15424 354 VGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSlaALSAPFSAALRQ 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 339 PKATEQ--LRLFNWPGNVRQLENTCRWLTVMAPGElvTEQDLPPEIIevtpiqvegdwldafQQWLNNELKQGKENIWPD 416
Cdd:PRK15424 434 GLQQCEtlLLHYDWPGNVRELRNLMERLALFLSVE--PTPDLTPQFL---------------QLLLPELARESAKTPAPR 496
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 966357534 417 IQAQletrLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKERN 459
Cdd:PRK15424 497 LLAA----TLQQALERFNGDKTAAANYLGISRTTLWRRLKAEA 535
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
137-445 5.14e-89

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: 274.17  E-value: 5.14e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  137 IIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTG 216
Cdd:TIGR02974   1 LIGESNAFLEVLEQVSRLAPLDRPVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  217 ADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFH 296
Cdd:TIGR02974  81 AQKRHQGRFERADGGTLFLDELATASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  297 RLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLQVESKV-LSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGE--LV 373
Cdd:TIGR02974 161 RLAFDVITLPPLRERQEDIMLLAEHFAIRMARELGLPLFPgFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEeaPI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  374 TEQDL---------PPEIIEVTPIQVEGdwldafqqwLNNELKQGKENIWP----DIQAQLETRLIKTALANCSGHKQDA 440
Cdd:TIGR02974 241 DEIIIdpfaspwrpKQAAPAVDEVNSTP---------TDLPSPSSIAAAFPldlkQAQQDYEIELLQQALAEAQFNQRKA 311

                  ....*
gi 966357534  441 AIKIG 445
Cdd:TIGR02974 312 AELLG 316
PRK10820 PRK10820
transcriptional regulator TyrR;
136-386 8.39e-81

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 259.23  E-value: 8.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 136 HIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFT 215
Cdd:PRK10820 205 QIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYP 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 216 GADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLF 295
Cdd:PRK10820 285 NALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLY 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 296 HRLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTC-RWLTVMAPGELvT 374
Cdd:PRK10820 365 YRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIyRALTQLEGYEL-R 443
                        250
                 ....*....|....
gi 966357534 375 EQD--LPPEIIEVT 386
Cdd:PRK10820 444 PQDilLPDYDAAVA 457
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
137-359 1.62e-75

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 239.57  E-value: 1.62e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 137 IIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEKGAFTG 216
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 217 ADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFH 296
Cdd:PRK11608  88 AQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLD 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966357534 297 RLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLQVE-SKVLSPKATEQLRLFNWPGNVRQLEN 359
Cdd:PRK11608 168 RLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPlFPGFTERARETLLNYRWPGNIRELKN 231
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
131-460 5.16e-74

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 245.90  E-value: 5.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 131 PPKSAHIIGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHE 210
Cdd:PRK15429 372 DSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHE 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 211 KGAFTGADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKF 290
Cdd:PRK15429 452 RGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREF 531
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 291 RDDLFHRLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLqveSKVLSPKATEQLRLFN---WPGNVRQLENTCRWLTVM 367
Cdd:PRK15429 532 RSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRM---GRNIDSIPAETLRTLSnmeWPGNVRELENVIERAVLL 608
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 368 APGELVteQDLPPEIIEVTPIQVEGDWLDAfqqwlnnelKQGKEniwpdiQAQLETRLIKTALANCSGHKqDAAIKIGWG 447
Cdd:PRK15429 609 TRGNVL--QLSLPDITLPEPETPPAATVVA---------QEGED------EYQLIVRVLKETNGVVAGPK-GAAQRLGLK 670
                        330
                 ....*....|...
gi 966357534 448 RNTLTRKLKERNI 460
Cdd:PRK15429 671 RTTLLSRMKRLGI 683
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
156-461 1.27e-69

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: 224.73  E-value: 1.27e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 156 ASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESelfghekgaftgadsvrkgrfeqanggtlfl 235
Cdd:COG3604  113 ASLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 236 deigdmpldvqtrllrvLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPALRERTEDI 315
Cdd:COG3604  162 -----------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDI 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 316 ERLAQHFLHKSAKDLQVESKVLSPKATEQLRLFNWPGNVRQLENTCRWLTVMAPGELVTEQDLPPEIIEVTpiqvegdwl 395
Cdd:COG3604  225 PLLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSREAL--------- 295
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966357534 396 dafqqwlnnelkqgkeniwpdiqAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKERNIS 461
Cdd:COG3604  296 -----------------------EEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
2-117 6.49e-67

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: 209.82  E-value: 6.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF 117
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
129-460 3.86e-57

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 199.52  E-value: 3.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 129 QAPPKSAHIIGEAPAMQEVFRaIGKLSASSMS-VLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELF 207
Cdd:PRK11388 319 KVSHTFDHMPQDSPQMRRLIH-FGRQAAKSSFpVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYPDEALAEEFL 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 208 GhekGAFTGADSVRKGRFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQ 287
Cdd:PRK11388 398 G---SDRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTTADLAMLVEQ 474
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 288 GKFRDDLFHRLNVVRLRLPALRERTEDIERLAQHFLHKSAKDLQVESKVlSPKATEQLRLFNWPGNVRQLENTCRWLTVM 367
Cdd:PRK11388 475 NRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTRLKI-DDDALARLVSYRWPGNDFELRSVIENLALS 553
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 368 APGELVTEQDLPPEIIEVTPIqvegdwLDAFQQWLNNELKqgkeniwpdiQAQLETRLIKTALANCSGHKQDAAIKIGWG 447
Cdd:PRK11388 554 SDNGRIRLSDLPEHLFTEQAT------DDVSATRLSTSLS----------LAELEKEAIINAAQVCGGRIQEMAALLGIG 617
                        330
                 ....*....|...
gi 966357534 448 RNTLTRKLKERNI 460
Cdd:PRK11388 618 RTTLWRKMKQHGI 630
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
155-357 2.26e-40

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: 151.91  E-value: 2.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 155 SASSMSVLINGESGTGKELVAS-------ALHNHSPRkenqFIALNMAAIPKELVESELFGHEKGAFTGADSVRKGRFEQ 227
Cdd:COG4650  205 IRSRAPILLTGPTGAGKSQLARriyelkkARHQVSGR----FVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRS 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 228 ANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKVDVRIIAATHQNLEDLVKQGKFRDDLFHRLNVVRLRLPA 307
Cdd:COG4650  281 ADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPG 360
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966357534 308 LRERTEDIERLAQHFLHKSAKDLQV------ESK------VLSPKATeqlrlfnWPGNVRQL 357
Cdd:COG4650  361 LAERREDIEPNLDYELARFAREQGRrvrfnkEARarylafATSPEAL-------WSGNFRDL 415
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
3-156 3.20e-40

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: 142.93  E-value: 3.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRAnstkktkrkqappkSAHIIGEAPAMQEVFRAIGKLSA 156
Cdd:COG4566   81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALAR--------------DRARRAERARRAELRARLASLTP 140
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-116 3.97e-39

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: 137.62  E-value: 3.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRA 113
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
159-382 1.88e-35

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: 139.86  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 159 MSVLINGESGTGKELVASALHNHSprKENQ-------FIALNMA--AIPKELVESELFGHEKGAFTGADSVRKGRFEQAN 229
Cdd:COG1221  131 LHTLILGPTGVGKSFFAELMYEYA--IEIGvlpedapFVVFNCAdyANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKAD 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 230 GGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVG-GHQSIKVDVRIIAATHQNLED-LVKqgKF-RddlfhRLNVVrLRLP 306
Cdd:COG1221  209 GGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPESsLLK--TFlR-----RIPMV-IKLP 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 307 ALRERTEDiERLA--QHFLHKSAKDLQVESKVlSPKATEQLRLFNWPGNVRQLEN----TCR--WLTVMAPGE---LVTE 375
Cdd:COG1221  281 SLEERSLE-ERLEliKHFFKEEAKRLNKPIKV-SKEVLKALLLYDCPGNIGQLKSdiqlACAkaFLNYITNKKeeiEITL 358

                 ....*..
gi 966357534 376 QDLPPEI 382
Cdd:COG1221  359 SDLPENV 365
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
3-116 1.89e-35

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: 127.32  E-value: 1.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:cd17537    2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:cd17537   82 GDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQA 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
4-114 2.09e-34

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 124.57  E-value: 2.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 966357534   84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVE 114
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
6-103 6.12e-33

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: 120.02  E-value: 6.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:cd00156    2 IVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADE 81
                         90
                 ....*....|....*...
gi 966357534  86 DSAVNAFQKGAFEYLAKP 103
Cdd:cd00156   82 EDAVRALELGADDYLVKP 99
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1-118 2.05e-32

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: 122.37  E-value: 2.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-122 1.71e-31

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: 117.26  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELI--AEQNPGLPVII 78
Cdd:COG0784    5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIraLPRLPDIPIIA 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 966357534  79 MTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANST 122
Cdd:COG0784   85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
6-118 5.72e-30

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: 114.62  E-value: 5.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELI--AEQNPGLPVIIMTAHS 83
Cdd:COG3706    6 VVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLraDPRTADIPIIFLTALD 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:COG3706   86 DEEDRARALEAGADDYLTKPFDPEELLARVDLVAR 120
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-156 3.08e-29

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 114.11  E-value: 3.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPG--LPVII 78
Cdd:COG3437    6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVIF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  79 MTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQAPPK----SAHIIGEAPAMQEVFRAIGKL 154
Cdd:COG3437   86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLklaaPLHDIGKIGIPDAILLKPGKL 165

                 ..
gi 966357534 155 SA 156
Cdd:COG3437  166 TP 167
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
4-118 1.72e-28

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 108.74  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
fixJ PRK09390
response regulator FixJ; Provisional
3-184 2.00e-28

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 111.25  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:PRK09390   5 VVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFranstkktkrKQAPPKSAHiigeAPAMQEVFRAIGKLSASSMSVL 162
Cdd:PRK09390  85 GDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERAL----------AQAPEAAKS----EAVAADIRARIASLSERERQVM 150
                        170       180
                 ....*....|....*....|..
gi 966357534 163 INGESGTGKELVASALhNHSPR 184
Cdd:PRK09390 151 DGLVAGLSNKVIARDL-DISPR 171
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
6-103 2.85e-27

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: 104.86  E-value: 2.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALER-SGF-NVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:COG4753    4 IVDDEPLIREGLKRILEWeAGFeVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSGYS 83
                         90       100
                 ....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKP 103
Cdd:COG4753   84 DFEYAQEAIKLGADDYLLKP 103
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-113 4.24e-27

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: 104.88  E-value: 4.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:COG5803    2 MKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMT 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALV 113
Cdd:COG5803   82 AYGELDMVEEAKELGAKGYFTKPFDIDELREAV 114
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-134 7.44e-27

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 105.05  E-value: 7.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGF--NVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVII 78
Cdd:COG4565    3 MIRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIV 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 966357534  79 MTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQAPPKS 134
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDLPEA 138
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
2-116 1.70e-25

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: 102.30  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:COG4567    5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTG 84
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:COG4567   85 YASIATAVEAIKLGADDYLAKPADADDLLAALERA 119
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
4-116 2.24e-25

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: 100.35  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNA 113
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
2-118 1.35e-24

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 97.86  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  82 HSDLDSAVNAFQKGA-FEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17569   81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
6-103 1.47e-24

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 97.09  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:cd17574    2 VVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDEE 81
                         90
                 ....*....|....*...
gi 966357534  86 DSAVNAFQKGAFEYLAKP 103
Cdd:cd17574   82 EDKVLGLELGADDYITKP 99
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
6-116 1.55e-24

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: 97.79  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVE---SFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:cd17536    3 IVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSGY 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:cd17536   83 DDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKA 116
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
3-111 8.30e-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: 95.97  E-value: 8.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGF-NVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPG--LPVIIM 79
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedVPIVMI 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVA 111
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPFDPVELLA 113
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
160-306 1.40e-23

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 96.45  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 160 SVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVESELFGHEkgaftgADSVRKGRFEQANGGTLFLDEIG 239
Cdd:cd00009   21 NLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLLFELAEKAKPGVLFIDEID 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966357534 240 DMPLDVQTRLLRVLADGEFYRVgghqsIKVDVRIIAATHQNLEdlvkqGKFRDDLFHRLNvVRLRLP 306
Cdd:cd00009   95 SLSRGAQNALLRVLETLNDLRI-----DRENVRVIGATNRPLL-----GDLDRALYDRLD-IRIVIP 150
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
138-308 1.03e-22

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 93.56  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  138 IGEAPAMQEVFRAIGKLSASSMSVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELveselfghekgaftga 217
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLEL---------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  218 dsvrkgrFEQANGGTLFLDEIGDMPLDVQTRLLRVLADGEFYRvgghqsikvdVRIIAATHQNLEDLVKQGKFRDDLFHR 297
Cdd:pfam14532  65 -------LEQAKGGTLYLKDIADLSKALQKGLLLLLAKAEGYR----------VRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 966357534  298 LNVVRLRLPAL 308
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
4-103 1.87e-22

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: 91.41  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKP 103
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
6-111 4.60e-22

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: 91.01  E-value: 4.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:cd17624    3 LVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARDGV 82
                         90       100
                 ....*....|....*....|....*.
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVA 111
Cdd:cd17624   83 DDRVAGLDAGADDYLVKPFALEELLA 108
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
2-103 1.51e-21

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 89.57  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80
                         90       100
                 ....*....|....*....|..
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKP 103
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKP 102
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
2-108 4.55e-21

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: 88.05  E-value: 4.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
                         90       100
                 ....*....|....*....|....*..
gi 966357534  82 HSDLDSAVNAFQKGAfeYLAKPFDLNE 108
Cdd:cd17554   81 YSEYKSDFSSWAADA--YVVKSSDLTE 105
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
4-108 5.39e-21

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: 88.07  E-value: 5.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNAL-----KFSqpaVLVSDVKMPGMDGMALLELIAEQnPGLPVII 78
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLrenkdEFD---LVITDVHMPDMDGFEFLELIRLE-MDLPVIM 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 966357534  79 MTAHSDLDSAVNAFQKGAFEYLAKPFDLNE 108
Cdd:cd17584   77 MSADGSTSTVMKGLAHGACDYLLKPVSIED 106
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
2-111 6.74e-21

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: 87.50  E-value: 6.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKPFDLNEAVA 111
Cdd:cd17563   81 YASIATAVEAIKLGADDYLAKPADADEILA 110
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
3-118 1.26e-20

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: 87.02  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17615   81 DSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLR 116
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
6-108 2.54e-20

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: 85.98  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKfSQP--AVLVsDVKMPGMDGMALLELIAEQNPG---LPVIIMT 80
Cdd:cd17546    3 VVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLK-EEPfdLVLM-DLQMPVMDGLEATRRIRELEGGgrrTPIIALT 80
                         90       100
                 ....*....|....*....|....*...
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNE 108
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQ 108
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-138 8.32e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 87.95  E-value: 8.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFN--VESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVII 78
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966357534  79 MTAHSDLdsAVNAFQKGAFEYLAKPFD---LNEAVALVesafRANSTKKTKRKQAPPKSAHII 138
Cdd:COG3279   81 TTAYDEY--ALEAFEVNAVDYLLKPIDeerLAKALEKA----KERLEAKAAAEASPEEKDRIF 137
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
6-118 2.27e-19

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 83.33  E-value: 2.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALER-SGFN-VESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17535    3 IVDDHPLVREGLRRLLESePDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAHD 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17535   83 DPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
4-118 2.63e-19

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: 83.20  E-value: 2.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEELLARVRALLR 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
6-118 4.54e-18

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: 79.57  E-value: 4.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:cd17625    2 VVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDAV 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17625   82 EDRVKGLDLGADDYLPKPFSLAELLARIRALLR 114
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
4-118 5.98e-18

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: 79.34  E-value: 5.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNpGLPVIIMTAHS 83
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTART 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPFSPRELLARVRALLR 115
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
6-103 1.21e-17

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: 77.87  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPgLPVIIMTAHSDL 85
Cdd:cd19936    3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST-LPVIFLTSKDDE 81
                         90
                 ....*....|....*...
gi 966357534  86 DSAVNAFQKGAFEYLAKP 103
Cdd:cd19936   82 IDEVFGLRMGADDYITKP 99
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
2-115 1.99e-17

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: 77.98  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVES 115
Cdd:cd17553   81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKK 114
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
4-113 2.96e-17

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: 77.11  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPG--LPVIIMTA 81
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLanTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  82 H---SDLDSAVNA-FQKgafeYLAKPFDLNEAVALV 113
Cdd:cd17580   81 YgqpEDRERALEAgFDA----HLVKPVDPDELIELI 112
orf27 CHL00148
Ycf27; Reviewed
6-139 5.64e-17

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 80.15  E-value: 5.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNpGLPVIIMTAHSDL 85
Cdd:CHL00148  11 VVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-DVPIIMLTALGDV 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRaNSTKKTKRKQAPPKSAHIIG 139
Cdd:CHL00148  90 SDRITGLELGADDYVVKPFSPKELEARIRSVLR-RTNKKSFSSKIPNSSIIRIG 142
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
2-117 1.06e-16

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: 75.78  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGEAaNGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF 117
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
4-118 1.35e-16

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: 75.42  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPGLPVIIMTAH- 82
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKEL-RKTSQVPVLMLTARg 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  83 SDLDSAVnAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17623   80 DDIDRIL-GLELGADDYLPKPFNPRELVARIRAILR 114
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
6-104 1.93e-16

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: 74.47  E-value: 1.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELI--AEQNPGLPVIIMTAHS 83
Cdd:cd19920    3 IVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLkaDPATRHIPVIFLTALT 82
                         90       100
                 ....*....|....*....|.
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPF 104
Cdd:cd19920   83 DTEDKVKGFELGAVDYITKPF 103
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-135 2.48e-16

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: 76.92  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPgLPVIIM 79
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVVAEAaDGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVILL 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF-RANSTKKTKRKQAPPKSA 135
Cdd:COG3707   82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALaRFRELRALRRELAKLREA 138
PRK15479 PRK15479
transcriptional regulator TctD;
6-118 4.36e-16

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 77.07  E-value: 4.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:PRK15479   5 LAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARSAV 84
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK15479  85 ADRVKGLNVGADDYLPKPFELEELDARLRALLR 117
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-149 9.07e-16

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 76.15  E-value: 9.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:PRK11083   3 QPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLT 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  81 AHSD-LDSAVnAFQKGAFEYLAKPFDLNEAVALVESAFRanSTKKTKRKQAPPKSAHIIGEAPAMQEVFR 149
Cdd:PRK11083  83 ARSDeVDRLV-GLEIGADDYVAKPFSPREVAARVRTILR--RVKKFAAPSPVIRIGHFELDEPAARISYF 149
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
4-103 9.29e-16

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: 72.57  E-value: 9.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKfSQPAVLV-SDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLA-SEPYDLClTDMRLPDGSGLELVQHIQQRLPQTPVAVITAY 79
                         90       100
                 ....*....|....*....|.
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKP 103
Cdd:cd19926   80 GSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
2-111 1.09e-15

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 73.05  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPG--LPVIIM 79
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIML 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVA 111
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPRELVA 112
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
3-104 1.34e-15

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 72.15  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQP-AVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                         90       100
                 ....*....|....*....|...
gi 966357534  82 HSDLDSAVNAFQKGAFEYLAKPF 104
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
7-118 1.72e-15

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 72.31  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   7 VDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNP--GLPVIIMTAHSD 84
Cdd:cd19937    3 VDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKtsSIPIIMLTAKGE 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 966357534  85 LDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd19937   83 EFDKVLGLELGADDYITKPFSPRELLARVKAVLR 116
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
6-103 2.77e-15

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: 71.25  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPGL---PVIIMTAH 82
Cdd:cd19927    3 LVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKL-RKNADFdtiPVIFLTAK 81
                         90       100
                 ....*....|....*....|.
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKP 103
Cdd:cd19927   82 GMTSDRIKGYNAGCDGYLSKP 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
2-117 6.50e-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: 70.91  E-value: 6.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGlPVIIMT 80
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVVGEAsDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF 117
Cdd:cd19932   80 AYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
2-117 6.64e-15

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: 70.90  E-value: 6.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNV-ESFANAQDVLNALKFSQPAVLVSDVKMPG-MDGMALLELIAEQNPgLPVIIM 79
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKFD-IPVIFL 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF 117
Cdd:cd17534   80 TAYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
ompR PRK09468
osmolarity response regulator; Provisional
6-118 1.02e-14

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 73.47  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:PRK09468  10 VVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAKGEE 89
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK09468  90 VDRIVGLEIGADDYLPKPFNPRELLARIRAVLR 122
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
3-115 1.44e-14

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: 69.71  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPGLPVIIMTAH 82
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREI-RRFSDVPIIMVTAR 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVES 115
Cdd:cd19938   80 VEEIDRLLGLELGADDYICKPYSPREVVARVKA 112
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
4-117 2.52e-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: 68.85  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPgLPVIIMTAHS 83
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAF 117
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK10643 PRK10643
two-component system response regulator PmrA;
1-118 3.24e-14

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 71.61  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKtVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:PRK10643   1 MK-ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK10643  80 ARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIR 117
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
3-104 4.89e-14

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: 67.91  E-value: 4.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPG---LPVIIM 79
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRL-KEDPEtrhIPVIMI 79
                         90       100
                 ....*....|....*....|....*
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPF 104
Cdd:cd17538   80 TALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
6-103 5.46e-14

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: 67.47  E-value: 5.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:cd19935    3 VVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARDSV 82
                         90
                 ....*....|....*...
gi 966357534  86 DSAVNAFQKGAFEYLAKP 103
Cdd:cd19935   83 EDRVKGLDLGADDYLVKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
6-118 5.57e-14

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 68.08  E-value: 5.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDL 85
Cdd:cd19934    3 LVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARDSW 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd19934   83 QDKVEGLDAGADDYLTKPFHIEELLARLRALIR 115
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
7-103 7.79e-14

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 67.80  E-value: 7.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   7 VDDDASIRFVLEKALER-SGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPgLPVIIMTAHSD 84
Cdd:cd17541    6 VDDSAVMRKLLSRILESdPDIEVVGTArDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVSSLTE 84
                         90       100
                 ....*....|....*....|.
gi 966357534  85 LDSAV--NAFQKGAFEYLAKP 103
Cdd:cd17541   85 EGAEItlEALELGAVDFIAKP 105
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1-105 1.25e-13

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 67.19  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALER-SGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEqNP---GLPV 76
Cdd:cd17552    1 SKRILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPetqSIPV 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  77 IIMTAHsdldsaVNAFQKGAFEYL------AKPFD 105
Cdd:cd17552   80 ILLTAK------AQPSDRQRFASLgvagviAKPFD 108
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
3-116 1.33e-13

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: 67.47  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGF-NVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMta 81
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILM-- 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966357534  82 hSDLDSAV-NAFQKGAFEY-------LAKPFDLNEAVALVESA 116
Cdd:cd17530   80 -SGLDGGIlESAETLAGANglnllgtLSKPFSPEELTELLTKY 121
PRK10610 PRK10610
chemotaxis protein CheY;
6-104 1.46e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 67.31  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGF-NVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQN--PGLPVIIMTAH 82
Cdd:PRK10610  10 VVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLMVTAE 89
                         90       100
                 ....*....|....*....|..
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPF 104
Cdd:PRK10610  90 AKKENIIAAAQAGASGYVVKPF 111
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
2-113 1.58e-13

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: 66.94  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGmalLELIAE--QNP---GLPV 76
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDG---IELIKElrKLPaykFTPI 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966357534  77 IIMTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALV 113
Cdd:cd17562   78 LMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
6-113 1.65e-13

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: 66.72  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNpGLPVIIMTAHSDL 85
Cdd:cd17626    5 VVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTAKSDT 83
                         90       100
                 ....*....|....*....|....*...
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALV 113
Cdd:cd17626   84 VDVVLGLESGADDYVAKPFKPKELVARI 111
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1-114 3.44e-13

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: 65.82  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKtVWLVDDDASIRFVLEKALERSGF-NVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELI--AEQNPGLPVI 77
Cdd:cd19923    1 MK-VLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIraDGALSHLPVL 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966357534  78 IMTAHSDLDSAVNAFQKGAFEYLAKPFdlnEAVALVE 114
Cdd:cd19923   80 MVTAEAKKENVIAAAQAGVNNYIVKPF---TAATLKE 113
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
3-115 3.96e-13

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: 65.90  E-value: 3.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGF--NVESFANAQDVLNAL-------KFSQPAVLVSDVKMPGMDGMALLELIaEQNPG 73
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVRDGEEALDFLrgegeyaDAPRPDLILLDLNMPRMDGFEVLREI-KADPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 966357534  74 L---PVIIMTAhSDLDSAVN-AFQKGAFEYLAKPFDLNEAVALVES 115
Cdd:cd17557   80 LrriPVVVLTT-SDAEEDIErAYELGANSYIVKPVDFEEFVEAIRS 124
PRK10336 PRK10336
two-component system response regulator QseB;
4-118 4.08e-13

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 68.38  E-value: 4.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPFALIEVAARLEALMR 117
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
4-103 6.01e-13

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 65.09  E-value: 6.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPA---------VLVSDVKMPGMDGMALLELIaEQNPGL 74
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEgndlskeldLIITDIEMPKMDGYELTFEL-RDDPRL 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966357534  75 ---PVIIMTAHSDLDSAVNAFQKGAFEYLAKP 103
Cdd:cd19924   80 aniPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
4-103 1.05e-12

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: 64.11  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNpGLPVIIMTAHS 83
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                         90       100
                 ....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKP 103
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
6-105 1.82e-12

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: 63.88  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQnPGL---PVIIMTAH 82
Cdd:cd17598    3 IVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSD-PDLkdiPVILLTTL 81
                         90       100
                 ....*....|....*....|...
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFD 105
Cdd:cd17598   82 SDPRDVIRGLECGADNFITKPYD 104
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-118 2.66e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 66.36  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVsDVKMPGMDGMALLELIaEQNPGLPVIIMT 80
Cdd:PRK10955   1 MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLL-DVMMPKKNGIDTLKEL-RQTHQTPVIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 966357534  81 AH-SDLDSaVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK10955  79 ARgSELDR-VLGLELGADDYLPKPFNDRELVARIRAILR 116
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
160-278 3.87e-12

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: 63.93  E-value: 3.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   160 SVLINGESGTGKELVASALHNHSPRKENQFIALNMAAIPKELVES---ELFGHEKGAFTGADSVRKG--RFEQANGGTLF 234
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 966357534   235 LDEIGDMPLDVQTRLLRVLadgEFYRVGGHQSIKVDVRIIAATH 278
Cdd:smart00382  84 LDEITSLLDAEQEALLLLL---EELRLLLLLKSEKNLTVILTTN 124
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
6-118 3.89e-12

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 62.94  E-value: 3.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFN--VESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17532    3 IVDDEPLAREELRYLLEEHPDIeiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTAYD 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  84 DLdsAVNAFQKGAFEYLAKPFD---LNEAVALVESAFR 118
Cdd:cd17532   83 EY--AVEAFELNAVDYLLKPFSeerLAEALAKLRKRLS 118
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
3-113 4.93e-12

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: 62.46  E-value: 4.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNpGLPVIIMTAH 82
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISGD 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966357534  83 SDLDSA-VNAFQKGAFEYLAKPFDLNEAVALV 113
Cdd:cd17594   80 RRDEIDrVVGLELGADDYLAKPFGLRELLARV 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
4-104 9.51e-12

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: 61.21  E-value: 9.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALK-FSQPAVLVSDVKMPG-MDGMALLELIAEQNPGLPVIIMTA 81
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLEsGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|...
gi 966357534  82 hSDLDSAVNAFQKGAFEYLAKPF 104
Cdd:cd18161   81 -YAENAIEGGDLAPGVDVLSKPF 102
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-106 2.00e-11

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: 60.72  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALER-SGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQvPGFTVIGTAgTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                         90       100
                 ....*....|....*....|....*.
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDL 106
Cdd:cd19925   82 AANDVETVREALRLGVVDYLIKPFTF 107
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
4-103 3.13e-11

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: 60.11  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAV--LVSDVKMPGMDGMALLELIAEQN--PGLPVIIM 79
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIdlILTEVDLPVSSGFKLLSYIMRHKicKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKP 103
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
3-118 3.37e-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: 60.84  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSgFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGY 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966357534  83 SDLDSAVNAF-QKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17596   81 TDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAAR 117
PRK10816 PRK10816
two-component system response regulator PhoP;
4-121 3.43e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 62.83  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANS 121
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNS 120
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
4-115 1.26e-10

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: 58.57  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVES 115
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDELVARIHA 112
PRK11517 PRK11517
DNA-binding response regulator HprR;
1-121 1.39e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 61.07  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKtVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLN-ALKFSQpAVLVSDVKMPGMDGMALLELI--AEQNPglpVI 77
Cdd:PRK11517   1 MK-ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYlALKDDY-ALIILDIMLPGMDGWQILQTLrtAKQTP---VI 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 966357534  78 IMTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANS 121
Cdd:PRK11517  76 CLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHH 119
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
3-115 1.83e-10

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: 57.94  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEqNPGL---PVIIM 79
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPATrdiPVIAL 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVES 115
Cdd:cd17548   80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1-122 2.05e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 60.59  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPGLPVIIMT 80
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDL-RQWSAIPVIVLS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANST 122
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSA 121
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
4-111 4.60e-10

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: 56.67  E-value: 4.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHS 83
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                         90       100
                 ....*....|....*....|....*...
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVA 111
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVLVA 108
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
4-105 5.20e-10

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: 57.35  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALER---SGFNVESFANAQDVLNALKFSQP-----AVLVSDVKMPGMDGMALLELIAEQNPGLP 75
Cdd:cd17595    3 ILTVDDDPQVLRAVARDLRRqygKDYRVLRADSGAEALDALKELKLrgeavALFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 966357534  76 VIIMTAHSDLDSAVNAFQKGAFE-YLAKPFD 105
Cdd:cd17595   83 RVLLTAYADTDAAIRAINDVQLDyYLLKPWD 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
4-104 1.06e-09

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: 55.99  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKfSQPAV--LVSDVKMPGMDGMALLELIAEQNPG--LPVIIM 79
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE-QHPDIklVITDYNMPEMDGFELVREIRKKYSRdqLAIIGI 81
                         90       100
                 ....*....|....*....|....*..
gi 966357534  80 TAHSdlDSAVNA-FQK-GAFEYLAKPF 104
Cdd:cd17544   82 SASG--DNALSArFIKaGANDFLTKPF 106
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
6-118 1.08e-09

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: 55.89  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNpGLPVIIMTAHSDL 85
Cdd:cd17614    3 VVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKDSE 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  86 DSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:cd17614   82 VDKVLGLELGADDYVTKPFSNRELLARVKANLR 114
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-170 1.26e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 59.78  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALER-SGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPgLPVIIMTA 81
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNSdPDIEVVGTApDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVMVSS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  82 --HSDLDSAVNAFQKGAFEYLAKPF-----DLNEAVALVESAFRANSTKKTKRKQAPPKSAHIIGEAPAmqevfRAIGKL 154
Cdd:PRK00742  85 ltERGAEITLRALELGAVDFVTKPFlgislGMDEYKEELAEKVRAAARARVRALPPRAAAAARAAAAAP-----AALAAA 159
                        170
                 ....*....|....*.
gi 966357534 155 SASSMSVLINGESgTG 170
Cdd:PRK00742 160 PLLSSKLVAIGTS-TG 174
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
2-118 3.40e-09

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 57.04  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQ--NPGLPVIIM 79
Cdd:PRK10161   3 RRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKREsmTRDIPVVML 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK10161  83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
4-105 3.51e-09

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 54.31  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGlPVIIMTAHS 83
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-PILLLTALD 81
                         90       100
                 ....*....|....*....|..
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFD 105
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPVE 103
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1-122 1.29e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 55.32  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKtVWLVDDDASIRFVLEKALERSGFNVESFANAqdvLNALKFSQPA---VLVSDVKMPGMDGMALLELIAEQNPGLPVI 77
Cdd:PRK09836   1 MK-LLIVEDEKKTGEYLTKGLTEAGFVVDLADNG---LNGYHLAMTGdydLIILDIMLPDVNGWDIVRMLRSANKGMPIL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966357534  78 IMTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANST 122
Cdd:PRK09836  77 LLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAA 121
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
21-102 2.47e-08

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 51.89  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  21 LERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDLDSAVNAFQKGAFEYL 100
Cdd:cd19930   20 LEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYV 99

                 ..
gi 966357534 101 AK 102
Cdd:cd19930  100 LK 101
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
7-103 3.24e-08

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: 51.22  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   7 VDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELI--AEQNPGLPVIIMTAHSD 84
Cdd:cd17602    4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLrkSSALKDTPIIMLTGKDG 83
                         90
                 ....*....|....*....
gi 966357534  85 LDSAVNAFQKGAFEYLAKP 103
Cdd:cd17602   84 LVDRIRAKMAGASGYLTKP 102
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
4-110 3.48e-08

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: 51.62  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPgLPVIIMTAHS 83
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE-VGIILVTGRD 81
                         90       100
                 ....*....|....*....|....*..
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAV 110
Cdd:cd17619   82 DEVDRIVGLEIGADDYVTKPFNPRELL 108
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
5-103 5.14e-08

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: 50.73  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   5 WLVDDDASIRFVLEKALERSGFN--VESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:cd17565    2 YIVDDDKNIIKILSDIIEDDDLGevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQV 81
                         90       100
                 ....*....|....*....|.
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKP 103
Cdd:cd17565   82 SDKEMIGKAYQAGIEFFINKP 102
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1-122 9.08e-08

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 52.89  E-value: 9.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGFNVESFANAQDvLNALKFSQPA-VLVSDVKMPGMDGMALLELIAEQNpGLPVIIM 79
Cdd:PRK13856   1 MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQ-FNRVLASETVdVVVVDLNLGREDGLEIVRSLATKS-DVPIIII 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966357534  80 TAhSDLDSA--VNAFQKGAFEYLAKPFDLNEAVALVESAFRANST 122
Cdd:PRK13856  79 SG-DRLEEAdkVVALELGATDFIAKPFGTREFLARIRVALRVRPN 122
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
160-278 1.10e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 50.75  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  160 SVLINGESGTGK----ELVASALHNHSprkenqfiaLNMAAIPKELVESELFGH-----EKGAFTGADSVRKGRfeqaNG 230
Cdd:pfam07728   1 GVLLVGPPGTGKtelaERLAAALSNRP---------VFYVQLTRDTTEEDLFGRrnidpGGASWVDGPLVRAAR----EG 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 966357534  231 GTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHQSIKV---DVRIIAATH 278
Cdd:pfam07728  68 EIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMN 118
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
4-108 2.25e-07

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: 49.29  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNV---ESFANAQDVL------NALKFSQPAV--LVSDVKMPGMDGMALLELIAEQNP 72
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVtavDSGKRALEFLgledeeDSSNFNEPKVnmIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  73 --GLPVIIMTAHSDLDSAVNAFQKGAFEYLAKPFDLNE 108
Cdd:cd17581   81 lkEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLAD 118
PRK09483 PRK09483
response regulator; Provisional
1-118 2.26e-07

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 51.26  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALER-SGFNVesFANAQDVLNALKFS---QPAVLVSDVKMPGMDGMALLELIAEQNPGLPV 76
Cdd:PRK09483   1 MINVLLVDDHELVRAGIRRILEDiKGIKV--VGEACCGEDAVKWCrtnAVDVVLMDMNMPGIGGLEATRKILRYTPDVKI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966357534  77 IIMTAHSDLDSAVNAFQKGAFEYLAK---PFDLNEAVALVESAFR 118
Cdd:PRK09483  79 IMLTVHTENPLPAKVMQAGAAGYLSKgaaPQEVVSAIRSVHSGQR 123
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
3-107 2.53e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 53.20  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:PRK09959  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTAN 1039
                          90       100
                  ....*....|....*....|....*
gi 966357534   83 SDLDSAVNAFQKGAFEYLAKPFDLN 107
Cdd:PRK09959 1040 AQANEREKGLSCGMNLCLFKPLTLD 1064
PRK11697 PRK11697
two-component system response regulator BtsR;
1-105 2.76e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 51.39  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERSGfNVE---SFANAQDVLNALKFSQPAVLVSDVKMPGMDGMallELIAEQNPG-LP- 75
Cdd:PRK11697   1 MIKVLIVDDEPLAREELRELLQEEG-DIEivgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGL---ELVGMLDPEhMPy 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 966357534  76 VIIMTAHSDLdsAVNAFQKGAFEYLAKPFD 105
Cdd:PRK11697  77 IVFVTAFDEY--AIKAFEEHAFDYLLKPID 104
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
419-457 3.41e-07

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 46.62  E-value: 3.41e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 966357534  419 AQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKE 457
Cdd:pfam02954   2 EEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
4-104 4.06e-07

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: 48.37  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKAL-ERSGFNVESFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQN-PGLPVIIM- 79
Cdd:cd17561    4 VLIADDNREFVQLLEEYLnSQPDMEVVGVAhNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRlEKRPKIIMl 83
                         90       100
                 ....*....|....*....|....*
gi 966357534  80 TAHSDLDSAVNAFQKGAFEYLAKPF 104
Cdd:cd17561   84 TAFGQEDITQRAVELGASYYILKPF 108
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1-67 4.84e-07

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: 48.73  E-value: 4.84e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966357534   1 MKTVWLVDDDASIRFVLEKALERS-GFNV-ESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELI 67
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
3-118 1.25e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 49.30  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPGLPVIIMTAH 82
Cdd:PRK10710  12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREI-RRFSDIPIVMVTAK 90
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFR 118
Cdd:PRK10710  91 IEEIDRLLGLEIGADDYICKPYSPREVVARVKTILR 126
pleD PRK09581
response regulator PleD; Reviewed
7-105 2.04e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 49.90  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   7 VDD-DASIRfVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEqNPG---LPVIIMTAH 82
Cdd:PRK09581   8 VDDiPANVK-LLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKS-DPAtthIPVVMVTAL 85
                         90       100
                 ....*....|....*....|...
gi 966357534  83 SDLDSAVNAFQKGAFEYLAKPFD 105
Cdd:PRK09581  86 DDPEDRVRGLEAGADDFLTKPIN 108
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
6-116 4.67e-06

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 47.20  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASIRFVLEKALERSGFNV-ESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLE-LIAEQNPGLpVIIMTAHS 83
Cdd:PRK09958   5 IIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLEtLRKRQYSGI-IIIVSAKN 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  84 DLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:PRK09958  84 DHFYGKHCADAGANGFVSKKEGMNNIIAAIEAA 116
PRK10360 PRK10360
transcriptional regulator UhpA;
1-116 8.26e-06

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 46.51  E-value: 8.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIR--FVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGmalLELIAEQNPGLPVII 78
Cdd:PRK10360   1 MITVALIDDHLIVRsgFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISG---LELLSQLPKGMATIM 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966357534  79 MTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESA 116
Cdd:PRK10360  78 LSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTV 115
PRK15369 PRK15369
two component system response regulator;
28-102 9.39e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.61  E-value: 9.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966357534  28 VESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDLDSAVNAFQKGAFEYLAK 102
Cdd:PRK15369  32 VGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLK 106
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
3-111 1.07e-05

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: 44.71  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKAL-ERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPG---LPVII 78
Cdd:cd17575    2 MVLLVDDQAIIGEAVRRALaDEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFF-RANPAtrdIPIIV 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  79 MTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVA 111
Cdd:cd17575   81 LSTKEEPEVKSEAFALGANDYLVKLPDKIELVA 113
PLN03029 PLN03029
type-a response regulator protein; Provisional
4-129 1.18e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.18  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQ--------PAV------------LVSDVKMPGMDGMAL 63
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEddrsnpdtPSVspnshqevevnlIITDYCMPGMTGYDL 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966357534  64 LELIAEQNP--GLPVIIMTAHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRANSTKKTKRKQ 129
Cdd:PLN03029  91 LKKIKESSSlrNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQ 158
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
6-81 1.33e-05

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 47.66  E-value: 1.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966357534   6 LVDDDASI-RFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTA 81
Cdd:PRK10841 805 LVVDDHPInRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTA 881
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
6-115 2.91e-05

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: 43.29  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   6 LVDDDASirfVLEKALERS---GFNVE-SFA-NAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMT 80
Cdd:cd17593    4 LICDDSS---MARKQLARAlpaDWDVEiTFAeNGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966357534  81 AhsDL-DSAVN-AFQKGAFEYLAKPFDLNEAVALVES 115
Cdd:cd17593   81 G--DVqPEAKErVLELGALAFLKKPFDPEKLAQLLEE 115
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
4-84 3.25e-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: 43.16  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPA--VLVSDVKMPGMDGMALLELIAEQNP---GLPVII 78
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLFGrreRPLIVA 82

                 ....*.
gi 966357534  79 MTAHSD 84
Cdd:cd19933   83 LTANTD 88
dpiA PRK10046
two-component response regulator DpiA; Provisional
45-103 4.02e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 44.62  E-value: 4.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534  45 QPAVLVSDVKMPGMDGMALL-ELIAEQNPGlPVIIMTAHSDLDSAVNAFQKGAFEYLAKP 103
Cdd:PRK10046  50 KPGLILLDNYLPDGRGINLLhELVQAHYPG-DVVFTTAASDMETVSEAVRCGVFDYLIKP 108
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
4-103 1.46e-04

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 40.64  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIaEQNPGLPVIIMTAHS 83
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQL-RARSNVPVIMVTAKD 79
                         90       100
                 ....*....|....*....|
gi 966357534  84 DLDSAVNAFQKGAFEYLAKP 103
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
PRK10430 PRK10430
two-component system response regulator DcuR;
1-104 2.36e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 42.40  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKTVWLVDDDASIRFVLEKALER-SGFN----VESFANAQDVLNALKFSQPAVLVsDVKMPGMDGMALLELIAEQNPGLP 75
Cdd:PRK10430   1 MINVLIVDDDAMVAELNRRYVAQiPGFQccgtASTLEQAKEIIFNSDTPIDLILL-DIYMQQENGLDLLPVLHEAGCKSD 79
                         90       100
                 ....*....|....*....|....*....
gi 966357534  76 VIIMTAHSDLDSAVNAFQKGAFEYLAKPF 104
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIKPF 108
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
4-114 2.62e-04

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 42.13  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   4 VWLVDDDASIRFVLEKALERSGF--NVESFANAQDVLNALKFSQPAVLVSDVKMPG---MDGMALLELIAEQNPGLPVII 78
Cdd:PRK10840   6 VIIADDHPIVLFGIRKSLEQIEWvnVVGEFEDSTALINNLPKLDAHVLITDLSMPGdkyGDGITLIKYIKRHFPSLSIIV 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966357534  79 MTAHS---------DLDSAVNAFQKGAfeylakPFDLNEAVALVE 114
Cdd:PRK10840  86 LTMNNnpailsavlDLDIEGIVLKQGA------PTDLPKALAALQ 124
PRK10766 PRK10766
two-component system response regulator TorR;
2-113 2.64e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 42.33  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   2 KTVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALL-ELIAEQNPGlpVIIMT 80
Cdd:PRK10766   3 YHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTrELRSRSTVG--IILVT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 966357534  81 AHSDLDSAVNAFQKGAFEYLAKPFDLNEAVALV 113
Cdd:PRK10766  81 GRTDSIDRIVGLEMGADDYVTKPLELRELLVRV 113
PRK10693 PRK10693
two-component system response regulator RssB;
32-108 1.09e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 40.74  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966357534  32 ANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDLDSAVNAFQKGAFEYLAKPF-DLNE 108
Cdd:PRK10693   4 ANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVkDLNR 81
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
1-117 1.56e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.86  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MK--TVWLVDDDASIRFVLEKALERSGfNVESFANAQD---VLNALKFSQPAVLVSDVKMPGMDGMALLELIAEQNPGLP 75
Cdd:PRK09935   1 MKpaSVIIMDTHPIIRMSIEVLLQKNS-ELQIVLKTDDyriTIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVK 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966357534  76 VIIMTAHSDLDSAVNAFQKGAFEYLAKPFDLNE---AVALVESAF 117
Cdd:PRK09935  80 VLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDifhAVQMILSGY 124
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
134-301 1.64e-03

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 39.47  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 134 SAHIIGEAPAMQEVFRAI-------GKLSASSMSVLINGESGTGK-ELV---ASALHNhsprKENQFIALNMAAIPKELV 202
Cdd:cd19499   10 HERVVGQDEAVKAVSDAIrraraglSDPNRPIGSFLFLGPTGVGKtELAkalAELLFG----DEDNLIRIDMSEYMEKHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534 203 ESELFG--------HEKGAFTGAdsVRKGRFeqangGTLFLDEIGDMPLDVQTRLLRVLADGEFYRVGGHqsiKVDVR-- 272
Cdd:cd19499   86 VSRLIGappgyvgyTEGGQLTEA--VRRKPY-----SVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGR---TVDFKnt 155
                        170       180
                 ....*....|....*....|....*....
gi 966357534 273 IIAATHQNledlvkqgkFRDDLFHRLNVV 301
Cdd:cd19499  156 IIIMTSNH---------FRPEFLNRIDEI 175
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
52-105 1.97e-03

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 40.60  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966357534  52 DVKMPGMDGMALLELI--AEQNPGLPVIIMTAHsdldsAVNA-----FQKGAFEYLAKPFD 105
Cdd:PRK11107 718 DIQMPGMDGIRACELIrqLPHNQNTPIIAVTAH-----AMAGererlLSAGMDDYLAKPID 773
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
3-135 2.63e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.43  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   3 TVWLVDDDASIRFVLEKAL-----ERSGFNveSFANAQDVLNALKFSQPAVLVSDVKMPGMDGMALLELIAeqnPGLPVI 77
Cdd:PRK13837 699 TVLLVEPDDATLERYEEKLaalgyEPVGFS--TLAAAIAWISKGPERFDLVLVDDRLLDEEQAAAALHAAA---PTLPII 773
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 966357534  78 IMTAhSDLDSAVNAFQKGAFEYLAKPFDLNEAVALVESAFRansTKKTKRKQAPPKSA 135
Cdd:PRK13837 774 LGGN-SKTMALSPDLLASVAEILAKPISSRTLAYALRTALA---TARAAAARAEGTPA 827
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-81 3.01e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 39.48  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534   1 MKtVWLVDDDASIRFVLEKALERSGfNVESFANAQDVLNALKFSQ---PAVLVSDVKMPGMDGMALLELIAEQNPgLPVI 77
Cdd:PRK12555   1 MR-IGIVNDSPLAVEALRRALARDP-DHEVVWVATDGAQAVERCAaqpPDVILMDLEMPRMDGVEATRRIMAERP-CPIL 77

                 ....
gi 966357534  78 IMTA 81
Cdd:PRK12555  78 IVTS 81
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
46-110 4.09e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 38.47  E-value: 4.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966357534  46 PAVLVSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDLDSAVNAFQKGAFEYLAK---PFDLNEAV 110
Cdd:PRK10651  53 PDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKdmePEDLLKAL 120
PRK13558 PRK13558
bacterio-opsin activator; Provisional
50-99 5.39e-03

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 39.44  E-value: 5.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 966357534  50 VSDVKMPGMDGMALLELIAEQNPGLPVIIMTAHSDLDSAVNAFQKGAFEY 99
Cdd:PRK13558  56 VADHEPDGFDGLALLEAVRQTTAVPPVVVVPTAGDEAVARRAVDADAAAY 105
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
412-460 6.02e-03

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


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 35.56  E-value: 6.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 966357534 412 NIWPDIQAQLETRLIKTALANCSGHKQDAAIKIGWGRNTLTRKLKERNI 460
Cdd:COG2901   34 DLYDMVLAEVEKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGL 82
FleQ pfam06490
Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of ...
3-90 6.06e-03

Flagellar regulatory protein FleQ; This domain is found at the N terminus of a subset of sigma54-dependent transcriptional activators that are involved in regulation of flagellar motility e.g. FleQ in Pseudomonas aeruginosa. It is clearly related to pfam00072, but lacks the conserved aspartate residue that undergoes phosphorylation in the classic two-component system response regulator (pfam00072).


Pssm-ID: 428975 [Multi-domain]  Cd Length: 108  Bit Score: 36.40  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966357534    3 TVWLVDDDASIRFVLEKALERSGFNVESFANAQDVLNALKFSQPAVLVSDVKmpgMDGMALLELIAEQNPGLPVIIMTAH 82
Cdd:pfam06490   1 KILVIDDDAERRHDLSTILEFLGEQCEAISSEDLSAALWSSRWEALAVILGS---VSAAELLKALAKWDPHLPVLLLGET 77

                  ....*...
gi 966357534   83 SDLDSAVN 90
Cdd:pfam06490  78 DDALELAN 85
 
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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