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Conserved domains on  [gi|1272197937|ref|WP_099369141|]
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translesion error-prone DNA polymerase V autoproteolytic subunit [Aeromonas salmonicida]

Protein Classification

S24/S26 family peptidase( domain architecture ID 586)

S24/S26 family peptidase similar to human signal peptidase complex catalytic subunit SEC11C, a component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum

EC:  3.4.21.-
Gene Ontology:  GO:0017171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S24_S26 super family cl10465
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 10-134 1.76e-58

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.


The actual alignment was detected with superfamily member PRK10276:

Pssm-ID: 447902  Cd Length: 139  Bit Score: 177.68  E-value: 1.76e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  10 ITELPLFLTPAVCGFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIVLACLD 89
Cdd:PRK10276   12 IVTFPLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1272197937  90 GEFTIKILQTNP-PALLPANPDFPPIILQEGQELDIFGVVTFVLHK 134
Cdd:PRK10276   92 GEFTVKKLQLRPtVQLIPMNSAYSPITISSEDTLDVFGVVTHIVKA 137
 
Name Accession Description Interval E-value
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
10-134 1.76e-58

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 177.68  E-value: 1.76e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  10 ITELPLFLTPAVCGFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIVLACLD 89
Cdd:PRK10276   12 IVTFPLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1272197937  90 GEFTIKILQTNP-PALLPANPDFPPIILQEGQELDIFGVVTFVLHK 134
Cdd:PRK10276   92 GEFTVKKLQLRPtVQLIPMNSAYSPITISSEDTLDVFGVVTHIVKA 137
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 5-134 1.03e-50

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 160.08  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937   5 NTDAPITELPLFlTPAVCGFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIV 84
Cdd:COG1974    69 PASPEVVGLPLL-GRVAAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIV 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1272197937  85 LACLDGEFTIKILQTNP--PALLPANPDFPPIILqEGQELDIFGVVTFVLHK 134
Cdd:COG1974   148 VALIDGEATVKRLYKEGgrVRLQPENPAYPPIII-EGDDVEILGVVVGVIRR 198
Peptidase_S24 pfam00717
Peptidase S24-like;
23-128 7.02e-31

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 106.91  E-value: 7.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  23 GFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMiEAGINDGDLLVIDRAVTARHGDIVLACLDGEFTIKILQTNPP 102
Cdd:pfam00717   9 GAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSM-EPGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLYRDGG 87

                          90       100
                  ....*....|....*....|....*...
gi 1272197937 103 --ALLPANPDFPPIILQEGQELDIFGVV 128
Cdd:pfam00717  88 giRLISLNPEYPPIELPAEDDVEIIGRV 115
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 50-129 2.76e-24

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: 88.77  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  50 FYVWAGGYSMIEAgINDGDLLVIDRAVTARHGDIVLACLDGEFTIKILQTNPPA---LLPANPDFPPIILQEgQELDIFG 126
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGGrlrLISDNPAYPPIEIDE-EELEIVG 78


                  ...
gi 1272197937 127 VVT 129
Cdd:cd06529    79 VVG 81
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 23-134 2.40e-19

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: 79.37  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  23 GFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIVLACLDGEFTIKIL--QTN 100
Cdd:TIGR00498  85 GEPILAEQHIEEYFPIDFSLLKKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFykDGT 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1272197937 101 PPALLPANPDFPPIILQEgQELDIFGVVTFVLHK 134
Cdd:TIGR00498 165 KVELKPENPEFDPIVLNA-EDVTILGKVVGVIRN 197
 
Name Accession Description Interval E-value
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
10-134 1.76e-58

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 177.68  E-value: 1.76e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  10 ITELPLFLTPAVCGFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIVLACLD 89
Cdd:PRK10276   12 IVTFPLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1272197937  90 GEFTIKILQTNP-PALLPANPDFPPIILQEGQELDIFGVVTFVLHK 134
Cdd:PRK10276   92 GEFTVKKLQLRPtVQLIPMNSAYSPITISSEDTLDVFGVVTHIVKA 137
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 5-134 1.03e-50

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 160.08  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937   5 NTDAPITELPLFlTPAVCGFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIV 84
Cdd:COG1974    69 PASPEVVGLPLL-GRVAAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIV 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1272197937  85 LACLDGEFTIKILQTNP--PALLPANPDFPPIILqEGQELDIFGVVTFVLHK 134
Cdd:COG1974   148 VALIDGEATVKRLYKEGgrVRLQPENPAYPPIII-EGDDVEILGVVVGVIRR 198
Peptidase_S24 pfam00717
Peptidase S24-like;
23-128 7.02e-31

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 106.91  E-value: 7.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  23 GFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMiEAGINDGDLLVIDRAVTARHGDIVLACLDGEFTIKILQTNPP 102
Cdd:pfam00717   9 GAPILAEEEIEGYLPLPESLLSPPGNLFALRVKGDSM-EPGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLYRDGG 87

                          90       100
                  ....*....|....*....|....*...
gi 1272197937 103 --ALLPANPDFPPIILQEGQELDIFGVV 128
Cdd:pfam00717  88 giRLISLNPEYPPIELPAEDDVEIIGRV 115
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 50-129 2.76e-24

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: 88.77  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  50 FYVWAGGYSMIEAgINDGDLLVIDRAVTARHGDIVLACLDGEFTIKILQTNPPA---LLPANPDFPPIILQEgQELDIFG 126
Cdd:cd06529     1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGGrlrLISDNPAYPPIEIDE-EELEIVG 78


                  ...
gi 1272197937 127 VVT 129
Cdd:cd06529    79 VVG 81
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 23-134 2.40e-19

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: 79.37  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  23 GFPSPAQDYVEQTIDLNQHCVSHPAATFYVWAGGYSMIEAGINDGDLLVIDRAVTARHGDIVLACLDGEFTIKIL--QTN 100
Cdd:TIGR00498  85 GEPILAEQHIEEYFPIDFSLLKKPSAVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRFykDGT 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1272197937 101 PPALLPANPDFPPIILQEgQELDIFGVVTFVLHK 134
Cdd:TIGR00498 165 KVELKPENPEFDPIVLNA-EDVTILGKVVGVIRN 197
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 50-128 9.99e-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: 64.59  E-value: 9.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  50 FYVWAGGYSMIEAgINDGDLLVIDRAVT-ARHGDIVLACLDG-EFTIKILQTNPPA----LLPANPDFPPIILQEGQELD 123
Cdd:cd06462     1 FALRVEGDSMEPT-IPDGDLVLVDKSSYePKRGDIVVFRLPGgELTVKRVIGLPGEghyfLLGDNPNSPDSRIDGPPELD 79


                  ....*
gi 1272197937 124 IFGVV 128
Cdd:cd06462    80 IVGVV 84
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 13-128 3.46e-13

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 61.52  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272197937  13 LPLFLTPAVCGFPS-PAQDYVEQTIDLNQhcvSHPAATFYVWAGGYSMiEAGINDGDLLVIDRAVTA-RHGDIVLACLDG 90
Cdd:COG2932     1 VPLYDGEASAGGGAfNEVEEPVDKLEFPG---LPPDNLFAVRVSGDSM-EPTIRDGDIVLVDPSDTEiRDGGIYVVRTDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1272197937  91 EFTIKILQTNPPA---LLPANPDFPPIIL--QEGQELDIFGVV 128
Cdd:COG2932    77 ELLVKRLQRRPDGklrLISDNPAYPPIEIppEDADEIEIIGRV 119
 
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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