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Conserved domains on  [gi|1262881925|gb|PFU91207|]
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transcriptional repressor LexA [Bacillus anthracis]

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, ...
 5-209 9.09e-95

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


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 274.48  E-value: 9.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925   5 MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEdrmdteTQS 84
Cdd:COG1974     1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGL-SSSAVHRHLKALEKKGYLRRDPGKSRAIELLPA------SPE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  85 VIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTeD 164
Cdd:COG1974    74 VVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI-D 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1262881925 165 NEATVKRFYKEKDHFRLQPENSSLEPIILK--QVSVIGKVIGVYRDL 209
Cdd:COG1974   153 GEATVKRLYKEGGRVRLQPENPAYPPIIIEgdDVEILGVVVGVIRRL 199
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 5-209 9.09e-95

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 274.48  E-value: 9.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925   5 MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEdrmdteTQS 84
Cdd:COG1974     1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGL-SSSAVHRHLKALEKKGYLRRDPGKSRAIELLPA------SPE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  85 VIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTeD 164
Cdd:COG1974    74 VVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI-D 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1262881925 165 NEATVKRFYKEKDHFRLQPENSSLEPIILK--QVSVIGKVIGVYRDL 209
Cdd:COG1974   153 GEATVKRLYKEGGRVRLQPENPAYPPIIIEgdDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 5-210 9.52e-87

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: 254.25  E-value: 9.52e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925   5 MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMdtetqs 84
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPK------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  85 viQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTED 164
Cdd:TIGR00498  75 --GVPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1262881925 165 nEATVKRFYKEKDHFRLQPENSSLEPIILK--QVSVIGKVIGVYRDLH 210
Cdd:TIGR00498 153 -EVTVKRFYKDGTKVELKPENPEFDPIVLNaeDVTILGKVVGVIRNFQ 199
Peptidase_S24 pfam00717
Peptidase S24-like;
89-203 9.36e-42

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 137.34  E-value: 9.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  89 PIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMiEAGIFDGDLVVVRQQQSAYNGEIVVALTEDnEAT 168
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSM-EPGIPDGDLVLVDPSREARNGDIVVARLDG-EAT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1262881925 169 VKRFYKEKDHFRLQPENSSLEPIILK---QVSVIGKVI 203
Cdd:pfam00717  79 VKRLYRDGGGIRLISLNPEYPPIELPaedDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 124-203 9.93e-20

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: 79.53  E-value: 9.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925 124 FMLRISGDSMIEAgIFDGDLVVVRQQQSAYNGEIVVALTeDNEATVKRFYKEKD-HFRLQPENSSLEPIILK--QVSVIG 200
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARL-DGELTVKRLQRRGGgRLRLISDNPAYPPIEIDeeELEIVG 78


                  ...
gi 1262881925 201 KVI 203
Cdd:cd06529    79 VVG 81
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
80-193 8.07e-17

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 73.68  E-value: 8.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  80 TETQSVIQVPIVGK-VTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIV 158
Cdd:PRK10276    7 AELREIVTFPLFSDlVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIV 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1262881925 159 VALTeDNEATVKRFYKeKDHFRLQPENSSLEPIIL 193
Cdd:PRK10276   87 IAAV-DGEFTVKKLQL-RPTVQLIPMNSAYSPITI 119
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
6-64 1.11e-03

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 37.19  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1262881925    6 EKLTKRQQDILDFIKlkvqEKGyPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDP 64
Cdd:smart00347   6 LGLTPTQFLVLRILY----EEG-PLSVSELAKRLGV-SPSTVTRVLDRLEKKGLVRREP 58
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 5-209 9.09e-95

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 274.48  E-value: 9.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925   5 MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEdrmdteTQS 84
Cdd:COG1974     1 MKKLTKRQREILDFIKEYIRERGYPPSQREIAEALGL-SSSAVHRHLKALEKKGYLRRDPGKSRAIELLPA------SPE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  85 VIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTeD 164
Cdd:COG1974    74 VVGLPLLGRVAAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALI-D 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1262881925 165 NEATVKRFYKEKDHFRLQPENSSLEPIILK--QVSVIGKVIGVYRDL 209
Cdd:COG1974   153 GEATVKRLYKEGGRVRLQPENPAYPPIIIEgdDVEILGVVVGVIRRL 199
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 5-210 9.52e-87

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: 254.25  E-value: 9.52e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925   5 MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMdtetqs 84
Cdd:TIGR00498   1 MKPLTARQQEVLDLIRAHIESTGYPPSIREIARAVGLRSPSAAEEHLKALERKGYIERDPGKPRAIRILDDEPK------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  85 viQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTED 164
Cdd:TIGR00498  75 --GVPLIGRVAAGEPILAEQHIEEYFPIDFSLLKKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1262881925 165 nEATVKRFYKEKDHFRLQPENSSLEPIILK--QVSVIGKVIGVYRDLH 210
Cdd:TIGR00498 153 -EVTVKRFYKDGTKVELKPENPEFDPIVLNaeDVTILGKVVGVIRNFQ 199
Peptidase_S24 pfam00717
Peptidase S24-like;
89-203 9.36e-42

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 137.34  E-value: 9.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  89 PIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMiEAGIFDGDLVVVRQQQSAYNGEIVVALTEDnEAT 168
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSM-EPGIPDGDLVLVDPSREARNGDIVVARLDG-EAT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1262881925 169 VKRFYKEKDHFRLQPENSSLEPIILK---QVSVIGKVI 203
Cdd:pfam00717  79 VKRLYRDGGGIRLISLNPEYPPIELPaedDVEIIGRVV 116
LexA_DNA_bind pfam01726
LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ...
 7-69 9.59e-30

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: 104.77  E-value: 9.59e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1262881925   7 KLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRA 69
Cdd:pfam01726   1 PLTERQREVLDFIKASIEETGYPPSRREIARALGLRSPNAAEEHLKALERKGYIERDPGKPRA 63
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 124-203 9.93e-20

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: 79.53  E-value: 9.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925 124 FMLRISGDSMIEAgIFDGDLVVVRQQQSAYNGEIVVALTeDNEATVKRFYKEKD-HFRLQPENSSLEPIILK--QVSVIG 200
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARL-DGELTVKRLQRRGGgRLRLISDNPAYPPIEIDeeELEIVG 78


                  ...
gi 1262881925 201 KVI 203
Cdd:cd06529    79 VVG 81
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
80-193 8.07e-17

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 73.68  E-value: 8.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  80 TETQSVIQVPIVGK-VTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIV 158
Cdd:PRK10276    7 AELREIVTFPLFSDlVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIV 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1262881925 159 VALTeDNEATVKRFYKeKDHFRLQPENSSLEPIIL 193
Cdd:PRK10276   87 IAAV-DGEFTVKKLQL-RPTVQLIPMNSAYSPITI 119
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 88-204 3.89e-15

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 68.84  E-value: 3.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925  88 VPIV-GKVTAGLP-ITAVESVEEHFPLPAsivAGADQVFMLRISGDSMiEAGIFDGDLVVVRQQQSAY-NGEIVVALTeD 164
Cdd:COG2932     1 VPLYdGEASAGGGaFNEVEEPVDKLEFPG---LPPDNLFAVRVSGDSM-EPTIRDGDIVLVDPSDTEIrDGGIYVVRT-D 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1262881925 165 NEATVKRFYKEKDH-FRLQPENSSLEPIILK-----QVSVIGKVIG 204
Cdd:COG2932    76 GELLVKRLQRRPDGkLRLISDNPAYPPIEIPpedadEIEIIGRVVW 121
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 124-202 6.94e-15

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: 66.90  E-value: 6.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925 124 FMLRISGDSMIEAgIFDGDLVVV-RQQQSAYNGEIVVALTEDNEATVKRFYK--EKDHFRLQPENSSLEPIIL---KQVS 197
Cdd:cd06462     1 FALRVEGDSMEPT-IPDGDLVLVdKSSYEPKRGDIVVFRLPGGELTVKRVIGlpGEGHYFLLGDNPNSPDSRIdgpPELD 79


                  ....*
gi 1262881925 198 VIGKV 202
Cdd:cd06462    80 IVGVV 84
HTH_IclR pfam09339
IclR helix-turn-helix domain;
14-64 2.20e-05

IclR helix-turn-helix domain;


Pssm-ID: 430539 [Multi-domain]  Cd Length: 52  Bit Score: 40.47  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1262881925  14 DILDFIKlkvqEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDP 64
Cdd:pfam09339   7 AILDALA----EAPGPLTLTEIARRTGL-PKSTAHRLLQTLVELGYVEQDP 52
COG2512 COG2512
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ...
 6-62 9.49e-05

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: 39.51  E-value: 9.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1262881925   6 EKLTKRQQDILDFIKlkvqEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRR 62
Cdd:COG2512    11 PELLEDERRVLELLR----ENGGRMTQSEIVKETGW-SKSKVSRLLSRLEERGLIEK 62
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
8-64 1.09e-04

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 40.72  E-value: 1.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1262881925   8 LTKRQQDILDFIklkvQEKGyPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDP 64
Cdd:COG1846    36 LTPAQFRVLAAL----AEAG-GLTQSELAERLGL-TKSTVSRLLDRLEEKGLVEREP 86
IclR COG1414
DNA-binding transcriptional regulator, IclR family [Transcription];
14-64 1.37e-04

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


Pssm-ID: 441024 [Multi-domain]  Cd Length: 253  Bit Score: 41.34  E-value: 1.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1262881925  14 DILDFiklkVQEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDP 64
Cdd:COG1414    13 AILEA----LAEAGGGLSLSELARRLGL-PKSTVHRLLATLEEEGYVERDP 58
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 31-68 2.34e-04

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: 38.43  E-value: 2.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1262881925  31 SVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDPTKPR 68
Cdd:cd00090    22 TVSELAERLGL-SQSTVSRHLKKLEEAGLVESRREGRR 58
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
31-60 3.44e-04

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 37.03  E-value: 3.44e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1262881925  31 SVREIGQAVGLaSSSTVHGHLSRLEEKGYI 60
Cdd:pfam13412  17 SQRELAERLGL-SPSTVNRRLKRLEEEGVI 45
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
11-66 3.47e-04

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 40.29  E-value: 3.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1262881925  11 RQQDILDFIKlkvqEKGyPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDPTK 66
Cdd:COG2345    14 TRRRILELLK----RAG-PVTAAELAEALGL-TPNAVRRHLDALEEEGLVERETER 63
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
31-62 4.04e-04

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


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 38.99  E-value: 4.04e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1262881925  31 SVREIGQAVGLaSSSTVHGHLSRLEEKGYIRR 62
Cdd:COG1522    21 SFAELAERVGL-SESTVLRRVRRLEEAGVIRG 51
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
6-64 1.11e-03

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 37.19  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1262881925    6 EKLTKRQQDILDFIKlkvqEKGyPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDP 64
Cdd:smart00347   6 LGLTPTQFLVLRILY----EEG-PLSVSELAKRLGV-SPSTVTRVLDRLEKKGLVRREP 58
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
5-64 2.41e-03

Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 36.72  E-value: 2.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262881925   5 MEKLTKRQQDILDFIkLKVQEKGYPPSVREIGQAVGLaSSSTVHGHLSRLEEKGYIRRDP 64
Cdd:COG1321     1 MMMLSESEEDYLKAI-YELSEEGGPVRTSDIAERLGV-SPPSVTEMLKKLEEKGLVEYEP 58
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 8-62 3.62e-03

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: 34.49  E-value: 3.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1262881925   8 LTKRQQDILDFIKlkvqekGYPP-SVREIGQAVGLaSSSTVHGHLSRLEEKGYIRR 62
Cdd:pfam12802   3 LTPAQFRVLLALA------RNPGlTVAELARRLGI-SKQTVSRLVKRLEAKGLVER 51
 
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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