hypothetical protein [Enterococcus malodoratus]
Protein Classification
transcriptional repressor LexA( domain architecture ID 1008439)
transcriptional repressor LexA represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| lexA super family | cl36676 | SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ... |
7-77 | 1.18e-10 | ||
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] The actual alignment was detected with superfamily member TIGR00498: Pssm-ID: 273106 [Multi-domain] Cd Length: 199 Bit Score: 54.72 E-value: 1.18e-10
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| Name | Accession | Description | Interval | E-value | ||
| lexA | TIGR00498 | SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ... |
7-77 | 1.18e-10 | ||
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: 54.72 E-value: 1.18e-10
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| LexA | COG1974 | SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ... |
1-78 | 4.91e-10 | ||
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms]; Pssm-ID: 441577 [Multi-domain] Cd Length: 199 Bit Score: 52.99 E-value: 4.91e-10
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| LexA_DNA_bind | pfam01726 | LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ... |
8-66 | 6.28e-09 | ||
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: 47.38 E-value: 6.28e-09
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| Name | Accession | Description | Interval | E-value | ||
| lexA | TIGR00498 | SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ... |
7-77 | 1.18e-10 | ||
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: 54.72 E-value: 1.18e-10
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| LexA | COG1974 | SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ... |
1-78 | 4.91e-10 | ||
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms]; Pssm-ID: 441577 [Multi-domain] Cd Length: 199 Bit Score: 52.99 E-value: 4.91e-10
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| LexA_DNA_bind | pfam01726 | LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ... |
8-66 | 6.28e-09 | ||
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: 47.38 E-value: 6.28e-09
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| TFIIE_beta | pfam02186 | TFIIE beta subunit core domain; General transcription factor TFIIE consists of two subunits, ... |
11-58 | 6.45e-03 | ||
TFIIE beta subunit core domain; General transcription factor TFIIE consists of two subunits, TFIIE alpha pfam02002 and TFIIE beta. TFIIE beta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. The structure of the DNA binding core region has been solved and has a winged helix fold. Pssm-ID: 460479 Cd Length: 66 Bit Score: 32.12 E-value: 6.45e-03
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