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Conserved domains on  [gi|2214417305|ref|WP_242821393|]
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LexA family transcriptional regulator [Candidatus Arthromitus sp. SFB-rat-Yit]

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, ...
 2-55 1.90e-10

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


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 1.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2214417305   2 IVKKQNDINSANIAIIRVNGDdATCKKIIKHKDCINLVSLNPKYDPIYYDRNDI 55
Cdd:COG1974   134 IVDRQLEAENGDIVVALIDGE-ATVKRLYKEGGRVRLQPENPAYPPIIIEGDDV 186
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 2-55 1.90e-10

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 1.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2214417305   2 IVKKQNDINSANIAIIRVNGDdATCKKIIKHKDCINLVSLNPKYDPIYYDRNDI 55
Cdd:COG1974   134 IVDRQLEAENGDIVVALIDGE-ATVKRLYKEGGRVRLQPENPAYPPIIIEGDDV 186
Peptidase_S24 pfam00717
Peptidase S24-like;
1-56 5.49e-10

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 51.05  E-value: 5.49e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2214417305   1 MIVKKQNDINSANIAIIRVNGDdATCKKIIKHKDCINLVSLNPKYDPIYYDRNDIV 56
Cdd:pfam00717  55 VLVDPSREARNGDIVVARLDGE-ATVKRLYRDGGGIRLISLNPEYPPIELPAEDDV 109
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 1-55 1.20e-05

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: 39.08  E-value: 1.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2214417305  1 MIVKKQNDINSANIAIIRVNGDdATCKKIIKHKD-CINLVSLNPKYDPIYYDRNDI 55
Cdd:cd06529   20 VLVDPSDTPRDGDIVVARLDGE-LTVKRLQRRGGgRLRLISDNPAYPPIEIDEEEL 74
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-55 5.08e-04

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: 36.23  E-value: 5.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2214417305   1 MIVKKQNDINSANIAIIRVnGDDATCKKIIKHKDCINLVSLNPKYDPIYYDRNDI 55
Cdd:TIGR00498 132 LIVRSQKDARNGEIVAAMI-DGEVTVKRFYKDGTKVELKPENPEFDPIVLNAEDV 185
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 2-55 1.90e-10

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 1.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2214417305   2 IVKKQNDINSANIAIIRVNGDdATCKKIIKHKDCINLVSLNPKYDPIYYDRNDI 55
Cdd:COG1974   134 IVDRQLEAENGDIVVALIDGE-ATVKRLYKEGGRVRLQPENPAYPPIIIEGDDV 186
Peptidase_S24 pfam00717
Peptidase S24-like;
1-56 5.49e-10

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 51.05  E-value: 5.49e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2214417305   1 MIVKKQNDINSANIAIIRVNGDdATCKKIIKHKDCINLVSLNPKYDPIYYDRNDIV 56
Cdd:pfam00717  55 VLVDPSREARNGDIVVARLDGE-ATVKRLYRDGGGIRLISLNPEYPPIELPAEDDV 109
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 1-55 1.20e-05

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: 39.08  E-value: 1.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2214417305  1 MIVKKQNDINSANIAIIRVNGDdATCKKIIKHKD-CINLVSLNPKYDPIYYDRNDI 55
Cdd:cd06529   20 VLVDPSDTPRDGDIVVARLDGE-LTVKRLQRRGGgRLRLISDNPAYPPIEIDEEEL 74
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 6-55 3.36e-04

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 36.09  E-value: 3.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2214417305   6 QNDINSANIAIIRVNGDdATCKKIIKHKD-CINLVSLNPKYDPIYYDRNDI 55
Cdd:COG2932    61 DTEIRDGGIYVVRTDGE-LLVKRLQRRPDgKLRLISDNPAYPPIEIPPEDA 110
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 1-55 5.08e-04

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: 36.23  E-value: 5.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2214417305   1 MIVKKQNDINSANIAIIRVnGDDATCKKIIKHKDCINLVSLNPKYDPIYYDRNDI 55
Cdd:TIGR00498 132 LIVRSQKDARNGEIVAAMI-DGEVTVKRFYKDGTKVELKPENPEFDPIVLNAEDV 185
 
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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