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MULTISPECIES: LexA family transcriptional regulator [Gammaproteobacteria]

Protein Classification

LexA family transcriptional regulator( domain architecture ID 13394083)

LexA family transcriptional regulator containing an XRE family helix-turn-helix (HTH) domain and a S24 family peptidase domain which catalyzes an autocatalytic cleavage that disrupts the DNA-binding and represses a number of genes involved in the response to DNA damage (SOS response)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 154-234 8.39e-13

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: 62.19  E-value: 8.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397 154 YGIKGTGDSMFPAIRNGWYVVCDPDADLVPNEFVqVCLKDGRCTIKEFVGINGGVLSLLSVNGG-ERFFFEMDEVESITA 232
Cdd:cd06529    1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGDIV-VARLDGELTVKRLQRRGGGRLRLISDNPAyPPIEIDEEELEIVGV 79


                 ..
gi 445974397 233 IT 234
Cdd:cd06529   80 VG 81
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
6-61 2.28e-10

Helix-turn-helix XRE-family like proteins;


:

Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 54.83  E-value: 2.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 445974397     6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
PRK13355 super family cl36239
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 5-124 5.03e-08

bifunctional HTH-domain containing protein/aminotransferase; Provisional


The actual alignment was detected with superfamily member PRK13355:

Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 53.20  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397   5 TRIRQKLEEKKLRAADLARATKKSPVAAKK-----WLDGTSVPTAENLKVIAKFLGVSDDWLLYGGSDEQESSNNLAqln 79
Cdd:PRK13355   6 ERLKQAMKARGLKQEDLVHAAEARGVKLGKshisqYVSGKTGPRRDVLPFLAAILGVSEDWLLGGESPADQESDASA--- 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445974397  80 viDIEAFKQKYNIPDSEDAVKFVQAPAKPFPIQKRyvPVKAYSKM 124
Cdd:PRK13355  83 --VVESAPNSHLADPSAPTTPISQTSSEISIGNRR--TFKKSHKL 123
 
Name Accession Description Interval E-value
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 154-234 8.39e-13

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: 62.19  E-value: 8.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397 154 YGIKGTGDSMFPAIRNGWYVVCDPDADLVPNEFVqVCLKDGRCTIKEFVGINGGVLSLLSVNGG-ERFFFEMDEVESITA 232
Cdd:cd06529    1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGDIV-VARLDGELTVKRLQRRGGGRLRLISDNPAyPPIEIDEEELEIVGV 79


                 ..
gi 445974397 233 IT 234
Cdd:cd06529   80 VG 81
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 139-238 1.03e-10

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 57.66  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397 139 AGDGYVPTHT-----------AGPRAYGIKGTGDSMFPAIRNGWYVVCDPDA-DLVPNEFVqVCLKDGRCTIKEFVGING 206
Cdd:COG2932   10 AGGGAFNEVEepvdklefpglPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDtEIRDGGIY-VVRTDGELLVKRLQRRPD 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 445974397 207 GVLSLLSVN-GGERFFFEMDEVESITAITDIVP 238
Cdd:COG2932   89 GKLRLISDNpAYPPIEIPPEDADEIEIIGRVVW 121
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
6-61 2.28e-10

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 54.83  E-value: 2.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 445974397     6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-77 8.60e-10

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 53.85  E-value: 8.60e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445974397   1 MSLHTRIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWLLyGGSDEQESSNNLAQ 77
Cdd:COG1396    6 KALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDELL-GGADEELPEALLSE 81
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 6-61 2.40e-09

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 52.17  E-value: 2.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445974397   6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:cd00093    3 RLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
PRK09706 PRK09706
transcriptional repressor DicA; Reviewed
 6-69 3.19e-09

transcriptional repressor DicA; Reviewed


Pssm-ID: 182039 [Multi-domain]  Cd Length: 135  Bit Score: 53.70  E-value: 3.19e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445974397   6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWLLYGGSDEQ 69
Cdd:PRK09706   9 RIRYRRKQLKLSQRSLAKAVKVSHVSISQWERDETEPTGKNLFALAKALQCSPTWLLFGDEDKQ 72
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 7-61 5.55e-09

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 51.00  E-value: 5.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 445974397    7 IRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
Peptidase_S24 pfam00717
Peptidase S24-like;
148-215 1.24e-08

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 51.82  E-value: 1.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445974397  148 TAGPRAYGIKGTGDSMFPAIRNGWYVVCDPDADLVPNEFVqVCLKDGRCTIKEFVgINGGVLSLLSVN 215
Cdd:pfam00717  30 SPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREARNGDIV-VARLDGEATVKRLY-RDGGGIRLISLN 95
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 5-124 5.03e-08

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 53.20  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397   5 TRIRQKLEEKKLRAADLARATKKSPVAAKK-----WLDGTSVPTAENLKVIAKFLGVSDDWLLYGGSDEQESSNNLAqln 79
Cdd:PRK13355   6 ERLKQAMKARGLKQEDLVHAAEARGVKLGKshisqYVSGKTGPRRDVLPFLAAILGVSEDWLLGGESPADQESDASA--- 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445974397  80 viDIEAFKQKYNIPDSEDAVKFVQAPAKPFPIQKRyvPVKAYSKM 124
Cdd:PRK13355  83 --VVESAPNSHLADPSAPTTPISQTSSEISIGNRR--TFKKSHKL 123
 
Name Accession Description Interval E-value
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 154-234 8.39e-13

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: 62.19  E-value: 8.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397 154 YGIKGTGDSMFPAIRNGWYVVCDPDADLVPNEFVqVCLKDGRCTIKEFVGINGGVLSLLSVNGG-ERFFFEMDEVESITA 232
Cdd:cd06529    1 FALRVKGDSMEPTIPDGDLVLVDPSDTPRDGDIV-VARLDGELTVKRLQRRGGGRLRLISDNPAyPPIEIDEEELEIVGV 79


                 ..
gi 445974397 233 IT 234
Cdd:cd06529   80 VG 81
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 139-238 1.03e-10

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 57.66  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397 139 AGDGYVPTHT-----------AGPRAYGIKGTGDSMFPAIRNGWYVVCDPDA-DLVPNEFVqVCLKDGRCTIKEFVGING 206
Cdd:COG2932   10 AGGGAFNEVEepvdklefpglPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDtEIRDGGIY-VVRTDGELLVKRLQRRPD 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 445974397 207 GVLSLLSVN-GGERFFFEMDEVESITAITDIVP 238
Cdd:COG2932   89 GKLRLISDNpAYPPIEIPPEDADEIEIIGRVVW 121
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
6-61 2.28e-10

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 54.83  E-value: 2.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 445974397     6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-77 8.60e-10

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 53.85  E-value: 8.60e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445974397   1 MSLHTRIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWLLyGGSDEQESSNNLAQ 77
Cdd:COG1396    6 KALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDELL-GGADEELPEALLSE 81
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 6-61 2.40e-09

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 52.17  E-value: 2.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445974397   6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:cd00093    3 RLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
PRK09706 PRK09706
transcriptional repressor DicA; Reviewed
 6-69 3.19e-09

transcriptional repressor DicA; Reviewed


Pssm-ID: 182039 [Multi-domain]  Cd Length: 135  Bit Score: 53.70  E-value: 3.19e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445974397   6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWLLYGGSDEQ 69
Cdd:PRK09706   9 RIRYRRKQLKLSQRSLAKAVKVSHVSISQWERDETEPTGKNLFALAKALQCSPTWLLFGDEDKQ 72
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 7-61 5.55e-09

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 51.00  E-value: 5.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 445974397    7 IRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWL 61
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
Peptidase_S24 pfam00717
Peptidase S24-like;
148-215 1.24e-08

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 51.82  E-value: 1.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445974397  148 TAGPRAYGIKGTGDSMFPAIRNGWYVVCDPDADLVPNEFVqVCLKDGRCTIKEFVgINGGVLSLLSVN 215
Cdd:pfam00717  30 SPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREARNGDIV-VARLDGEATVKRLY-RDGGGIRLISLN 95
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 5-124 5.03e-08

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 53.20  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974397   5 TRIRQKLEEKKLRAADLARATKKSPVAAKK-----WLDGTSVPTAENLKVIAKFLGVSDDWLLYGGSDEQESSNNLAqln 79
Cdd:PRK13355   6 ERLKQAMKARGLKQEDLVHAAEARGVKLGKshisqYVSGKTGPRRDVLPFLAAILGVSEDWLLGGESPADQESDASA--- 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445974397  80 viDIEAFKQKYNIPDSEDAVKFVQAPAKPFPIQKRyvPVKAYSKM 124
Cdd:PRK13355  83 --VVESAPNSHLADPSAPTTPISQTSSEISIGNRR--TFKKSHKL 123
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 6-62 1.87e-07

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.


Pssm-ID: 463728 [Multi-domain]  Cd Length: 64  Bit Score: 46.90  E-value: 1.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 445974397    6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWLL 62
Cdd:pfam12844   3 RLRKAREERGLTQEELAERLGISRSQLSAIENGKSVPPAETLYKIAELLGVPANWLL 59
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 154-215 7.38e-07

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: 46.10  E-value: 7.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445974397 154 YGIKGTGDSMFPAIRNGWYVVCDPDA-DLVPNEFVQVCLKDGRCTIKEFVGING-GVLSLLSVN 215
Cdd:cd06462    1 FALRVEGDSMEPTIPDGDLVLVDKSSyEPKRGDIVVFRLPGGELTVKRVIGLPGeGHYFLLGDN 64
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 3-60 4.07e-06

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 43.39  E-value: 4.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445974397   3 LHTRIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDW 60
Cdd:COG1813   13 YGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISLAE 70
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
1-64 7.20e-06

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 42.53  E-value: 7.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445974397   1 MSLHTRIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDDWLLYG 64
Cdd:COG1476    3 KKLGNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSL 66
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 149-215 9.24e-04

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 39.13  E-value: 9.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445974397 149 AGPRAYGIKGTGDSMF-PAIRNGWYVVCDPDADLVPNEFVqVCLKDGRCTIKEFVgINGGVLSLLSVN 215
Cdd:COG1974  108 NPGATFALRVKGDSMIdAGILDGDLVIVDRQLEAENGDIV-VALIDGEATVKRLY-KEGGRVRLQPEN 173
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
 6-57 1.33e-03

Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433211 [Multi-domain]  Cd Length: 63  Bit Score: 36.36  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 445974397    6 RIRQKLEEKKLRAADLARATKKSPVAAKKWLDGTSV-PTAENLKVIAKFLGVS 57
Cdd:pfam13443   1 KLRKLMADRGISKSDLARATGISRATLSRLRKGKPKrVSLDTLDKICDALGCQ 53
VapI COG3093
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ...
 11-61 3.90e-03

Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];


Pssm-ID: 442327 [Multi-domain]  Cd Length: 87  Bit Score: 35.56  E-value: 3.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445974397  11 LEEKKLRAADLARATKKSPVAAKKWLDGTSVPTAENLKVIAKFLGVSDD-WL 61
Cdd:COG3093   18 LEPLGLSQTELAKALGVSRQRISEILNGKRAITADTALRLARAFGTSAEfWL 69
 
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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