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Conserved domains on  [gi|612671434|gb|EZS87530|]
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LexA repressor [Staphylococcus aureus VET0159R]

Protein Classification

LexA family protein( domain architecture ID 11449429)

LexA family protein may function as a transcriptional regulator involved in the repression of one or more genes involved in the response to DNA damage (SOS response), including recA and lexA and/or may contain a S24 peptidase domain such as in the translesion error-prone DNA polymerase V autoproteolytic subunit

Gene Ontology:  GO:0003677|GO:0045892
PubMed:  10679470|10908318

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-207 6.41e-91

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 264.85  E-value: 6.41e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   1 MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQtndninmE 80
Cdd:COG1974    1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGL-SSSAVHRHLKALEKKGYLRRDPGKSRAIELLPAS-------P 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434  81 ETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTStHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMT 160
Cdd:COG1974   73 EVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVK-NPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 612671434 161 eEDEATVKRFYKEKNRYRLQPENSTMEPIYL--DNVAVIGKVIGLYREM 207
Cdd:COG1974  152 -DGEATVKRLYKEGGRVRLQPENPAYPPIIIegDDVEILGVVVGVIRRL 199
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-207 6.41e-91

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 264.85  E-value: 6.41e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   1 MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQtndninmE 80
Cdd:COG1974    1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGL-SSSAVHRHLKALEKKGYLRRDPGKSRAIELLPAS-------P 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434  81 ETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTStHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMT 160
Cdd:COG1974   73 EVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVK-NPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 612671434 161 eEDEATVKRFYKEKNRYRLQPENSTMEPIYL--DNVAVIGKVIGLYREM 207
Cdd:COG1974  152 -DGEATVKRLYKEGGRVRLQPENPAYPPIIIegDDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-205 1.01e-81

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 241.54  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434    1 MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDninme 80
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPKG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   81 etihVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDiFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMT 160
Cdd:TIGR00498  76 ----VPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAV-FLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMI 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 612671434  161 eEDEATVKRFYKEKNRYRLQPENSTMEPIYLD--NVAVIGKVIGLYR 205
Cdd:TIGR00498 151 -DGEVTVKRFYKDGTKVELKPENPEFDPIVLNaeDVTILGKVVGVIR 196
Peptidase_S24 pfam00717
Peptidase S24-like;
86-201 3.11e-39

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 130.79  E-value: 3.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   86 PVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDiFILNVVGDSMiEAGILDGDKVIVRSQTIAENGDIIVAMTEeDEA 165
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLSPPGNL-FALRVKGDSM-EPGIPDGDLVLVDPSREARNGDIVVARLD-GEA 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 612671434  166 TVKRFYKEKNRYRLQPENSTMEPIYL---DNVAVIGKVI 201
Cdd:pfam00717  78 TVKRLYRDGGGIRLISLNPEYPPIELpaeDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 122-201 1.18e-17

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 74.13  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434 122 FILNVVGDSMIEAgILDGDKVIVRSQTIAENGDIIVAMTeEDEATVKRFYKEK-NRYRLQPENSTMEPIYL--DNVAVIG 198
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARL-DGELTVKRLQRRGgGRLRLISDNPAYPPIEIdeEELEIVG 78


                 ...
gi 612671434 199 KVI 201
Cdd:cd06529   79 VVG 81
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
91-201 1.81e-16

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 72.52  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434  91 VTAGVPITAVENIEEYFPLPEhLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTeEDEATVKRF 170
Cdd:PRK10276  22 VQCGFPSPAADYVEQRIDLNE-LLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAV-DGEFTVKKL 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 612671434 171 YKeKNRYRLQPENSTMEPIYL---DNVAVIGKVI 201
Cdd:PRK10276 100 QL-RPTVQLIPMNSAYSPITIsseDTLDVFGVVT 132
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
25-60 4.89e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 37.96  E-value: 4.89e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 612671434    25 PPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDP 60
Cdd:smart00347  24 PLSVSELAKRLGV-SPSTVTRVLDRLEKKGLVRREP 58
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 1-207 6.41e-91

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 264.85  E-value: 6.41e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   1 MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQtndninmE 80
Cdd:COG1974    1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGL-SSSAVHRHLKALEKKGYLRRDPGKSRAIELLPAS-------P 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434  81 ETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTStHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMT 160
Cdd:COG1974   73 EVVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVK-NPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 612671434 161 eEDEATVKRFYKEKNRYRLQPENSTMEPIYL--DNVAVIGKVIGLYREM 207
Cdd:COG1974  152 -DGEATVKRLYKEGGRVRLQPENPAYPPIIIegDDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-205 1.01e-81

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 241.54  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434    1 MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDninme 80
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPKG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   81 etihVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDiFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMT 160
Cdd:TIGR00498  76 ----VPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAV-FLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMI 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 612671434  161 eEDEATVKRFYKEKNRYRLQPENSTMEPIYLD--NVAVIGKVIGLYR 205
Cdd:TIGR00498 151 -DGEVTVKRFYKDGTKVELKPENPEFDPIVLNaeDVTILGKVVGVIR 196
Peptidase_S24 pfam00717
Peptidase S24-like;
86-201 3.11e-39

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 130.79  E-value: 3.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434   86 PVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDiFILNVVGDSMiEAGILDGDKVIVRSQTIAENGDIIVAMTEeDEA 165
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLSPPGNL-FALRVKGDSM-EPGIPDGDLVLVDPSREARNGDIVVARLD-GEA 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 612671434  166 TVKRFYKEKNRYRLQPENSTMEPIYL---DNVAVIGKVI 201
Cdd:pfam00717  78 TVKRLYRDGGGIRLISLNPEYPPIELpaeDDVEIIGRVV 116
LexA_DNA_bind pfam01726
LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ...
 4-65 1.01e-26

LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor which prevents expression of DNA repair proteins. The aligned region contains a variant form of the helix-turn-helix DNA binding motif. This domain is found associated with pfam00717 the auto-proteolytic domain of LexA EC:3.4.21.88.


Pssm-ID: 396335 [Multi-domain]  Cd Length: 63  Bit Score: 97.07  E-value: 1.01e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612671434    4 LTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRA 65
Cdd:pfam01726   2 LTERQREVLDFIKASIEETGYPPSRREIARALGLRSPNAAEEHLKALERKGYIERDPGKPRA 63
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 122-201 1.18e-17

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 74.13  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434 122 FILNVVGDSMIEAgILDGDKVIVRSQTIAENGDIIVAMTeEDEATVKRFYKEK-NRYRLQPENSTMEPIYL--DNVAVIG 198
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARL-DGELTVKRLQRRGgGRLRLISDNPAYPPIEIdeEELEIVG 78


                 ...
gi 612671434 199 KVI 201
Cdd:cd06529   79 VVG 81
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
91-201 1.81e-16

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 72.52  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434  91 VTAGVPITAVENIEEYFPLPEhLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTeEDEATVKRF 170
Cdd:PRK10276  22 VQCGFPSPAADYVEQRIDLNE-LLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAV-DGEFTVKKL 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 612671434 171 YKeKNRYRLQPENSTMEPIYL---DNVAVIGKVI 201
Cdd:PRK10276 100 QL-RPTVQLIPMNSAYSPITIsseDTLDVFGVVT 132
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 85-202 1.00e-14

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 67.68  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434  85 VPVI-GKVTAGVP-ITAVENIEEYFPLPehltSTHNSDIFILNVVGDSMiEAGILDGDKVIV-RSQTIAENGDIIVAMTe 161
Cdd:COG2932    1 VPLYdGEASAGGGaFNEVEEPVDKLEFP----GLPPDNLFAVRVSGDSM-EPTIRDGDIVLVdPSDTEIRDGGIYVVRT- 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 612671434 162 EDEATVKRFYKEK-NRYRLQPENSTMEPIYL-----DNVAVIGKVIG 202
Cdd:COG2932   75 DGELLVKRLQRRPdGKLRLISDNPAYPPIEIppedaDEIEIIGRVVW 121
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 122-200 1.58e-14

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 66.13  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671434 122 FILNVVGDSMIEAgILDGDKVIV-RSQTIAENGDIIVAMTEEDEATVKRFYK--EKNRYRLQPENSTMEPIYL---DNVA 195
Cdd:cd06462    1 FALRVEGDSMEPT-IPDGDLVLVdKSSYEPKRGDIVVFRLPGGELTVKRVIGlpGEGHYFLLGDNPNSPDSRIdgpPELD 79


                 ....*
gi 612671434 196 VIGKV 200
Cdd:cd06462   80 IVGVV 84
HTH_IclR pfam09339
IclR helix-turn-helix domain;
25-60 2.31e-05

IclR helix-turn-helix domain;


Pssm-ID: 430539 [Multi-domain]  Cd Length: 52  Bit Score: 40.47  E-value: 2.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 612671434   25 PPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDP 60
Cdd:pfam09339  18 PLTLTEIARRTGL-PKSTAHRLLQTLVELGYVEQDP 52
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
25-69 2.80e-05

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 42.26  E-value: 2.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 612671434  25 PPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRR--DPTKPRAIEIV 69
Cdd:COG1846   52 GLTQSELAERLGL-TKSTVSRLLDRLEEKGLVERepDPEDRRAVLVR 97
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 27-64 2.96e-05

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 40.74  E-value: 2.96e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 612671434  27 SVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPR 64
Cdd:cd00090   22 TVSELAERLGL-SQSTVSRHLKKLEEAGLVESRREGRR 58
IclR COG1414
DNA-binding transcriptional regulator, IclR family [Transcription];
25-68 6.70e-05

DNA-binding transcriptional regulator, IclR family [Transcription];


Pssm-ID: 441024 [Multi-domain]  Cd Length: 253  Bit Score: 42.50  E-value: 6.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 612671434  25 PPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDPTK------PRAIEI 68
Cdd:COG1414   24 GLSLSELARRLGL-PKSTVHRLLATLEEEGYVERDPEGgryrlgPRLLEL 72
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
27-58 1.00e-04

DNA-binding transcriptional regulator, Lrp family [Transcription];


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 40.92  E-value: 1.00e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 612671434  27 SVREIGEAVGLaSSSTVHGHLSRLEEKGYIRR 58
Cdd:COG1522   21 SFAELAERVGL-SESTVLRRVRRLEEAGVIRG 51
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
27-56 2.00e-04

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 37.80  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 612671434   27 SVREIGEAVGLaSSSTVHGHLSRLEEKGYI 56
Cdd:pfam13412  17 SQRELAERLGL-SPSTVNRRLKRLEEEGVI 45
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
5-62 4.62e-04

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 39.91  E-value: 4.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612671434   5 TKRQseIYNYIKQvvqmKGyPPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDPTK 62
Cdd:COG2345   14 TRRR--ILELLKR----AG-PVTAAELAEALGL-TPNAVRRHLDALEEEGLVERETER 63
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
25-60 4.89e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 37.96  E-value: 4.89e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 612671434    25 PPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDP 60
Cdd:smart00347  24 PLSVSELAKRLGV-SPSTVTRVLDRLEKKGLVRREP 58
COG2512 COG2512
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ...
 3-58 5.48e-04

Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only];


Pssm-ID: 442002 [Multi-domain]  Cd Length: 80  Bit Score: 37.59  E-value: 5.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612671434   3 ELTKRQSEIYNYIKQvvqmKGYPPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRR 58
Cdd:COG2512   12 ELLEDERRVLELLRE----NGGRMTQSEIVKETGW-SKSKVSRLLSRLEERGLIEK 62
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 25-58 8.89e-04

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 36.41  E-value: 8.89e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 612671434   25 PPSVREIGEAVGLaSSSTVHGHLSRLEEKGYIRR 58
Cdd:pfam12802  19 GLTVAELARRLGI-SKQTVSRLVKRLEAKGLVER 51
HTH_ARSR smart00418
helix_turn_helix, Arsenical Resistance Operon Repressor;
27-62 7.25e-03

helix_turn_helix, Arsenical Resistance Operon Repressor;


Pssm-ID: 197713 [Multi-domain]  Cd Length: 66  Bit Score: 34.11  E-value: 7.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 612671434    27 SVREIGEAVGLaSSSTVHGHLSRLEEKGYI--RRDPTK 62
Cdd:smart00418  12 CVCELAEILGL-SQSTVSHHLKKLREAGLVesRREGKR 48
HTH_ICLR smart00346
helix_turn_helix isocitrate lyase regulation;
27-60 9.54e-03

helix_turn_helix isocitrate lyase regulation;


Pssm-ID: 214629 [Multi-domain]  Cd Length: 91  Bit Score: 34.10  E-value: 9.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 612671434    27 SVREIGEAVGLaSSSTVHGHLSRLEEKGYIRRDP 60
Cdd:smart00346  22 TLAELAERLGL-SKSTAHRLLNTLQELGYVEQDG 54
 
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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