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Conserved domains on  [gi|446033435|ref|WP_000111290|]
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MULTISPECIES: translesion error-prone DNA polymerase V autoproteolytic subunit [Enterobacterales]

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 ...
 17-133 5.05e-45

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: 143.79  E-value: 5.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  17 PFFSDLLSCGVMSPCAGHEDNELNLHEYVVRNRPSTFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFT 96
Cdd:PRK10276  16 PLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFT 95

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446033435  97 VKILHTYPELLLMPSNPAYKPIRVNPES-LEIWGVVTF 133
Cdd:PRK10276  96 VKKLQLRPTVQLIPMNSAYSPITISSEDtLDVFGVVTH 133
 
Name Accession Description Interval E-value
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
17-133 5.05e-45

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 143.79  E-value: 5.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  17 PFFSDLLSCGVMSPCAGHEDNELNLHEYVVRNRPSTFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFT 96
Cdd:PRK10276  16 PLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFT 95

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446033435  97 VKILHTYPELLLMPSNPAYKPIRVNPES-LEIWGVVTF 133
Cdd:PRK10276  96 VKKLQLRPTVQLIPMNSAYSPITISSEDtLDVFGVVTH 133
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 24-138 2.23e-42

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 138.89  E-value: 2.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  24 SCGVMSPCAGHEDNELNLHEYVVRNRPSTFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFTVKILHTY 103
Cdd:COG1974   84 AAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKRLYKE 163

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446033435 104 P-ELLLMPSNPAYKPIRVNPESLEIWGVVTFALNQF 138
Cdd:COG1974  164 GgRVRLQPENPAYPPIIIEGDDVEILGVVVGVIRRL 199
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 53-132 9.01e-27

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: 95.32  E-value: 9.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  53 FFVRAAGLSMINAgINDGAILVVDRSLTARHGSIVVALVDGEFTVKILHTYPE--LLLMPSNPAYKPIRVNPESLEIWGV 130
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGgrLRLISDNPAYPPIEIDEEELEIVGV 79


                 ..
gi 446033435 131 VT 132
Cdd:cd06529   80 VG 81
Peptidase_S24 pfam00717
Peptidase S24-like;
34-131 4.86e-25

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 92.27  E-value: 4.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435   34 HEDNELNLHEYVVRNRPSTFFVRAAGLSMInAGINDGAILVVDRSLTARHGSIVVALVDGEFTVKILHTYP-ELLLMPSN 112
Cdd:pfam00717  17 EIEGYLPLPESLLSPPGNLFALRVKGDSME-PGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLYRDGgGIRLISLN 95

                          90       100
                  ....*....|....*....|
gi 446033435  113 PAYKPIRVNPE-SLEIWGVV 131
Cdd:pfam00717  96 PEYPPIELPAEdDVEIIGRV 115
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 51-131 4.08e-17

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: 73.98  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435   51 STFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFTVKILhtYPE---LLLMPSNPAYKPIRVNPESLEI 127
Cdd:TIGR00498 110 AVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRF--YKDgtkVELKPENPEFDPIVLNAEDVTI 187


                  ....
gi 446033435  128 WGVV 131
Cdd:TIGR00498 188 LGKV 191
 
Name Accession Description Interval E-value
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
17-133 5.05e-45

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 143.79  E-value: 5.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  17 PFFSDLLSCGVMSPCAGHEDNELNLHEYVVRNRPSTFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFT 96
Cdd:PRK10276  16 PLFSDLVQCGFPSPAADYVEQRIDLNELLIQHPSATYFVKASGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFT 95

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446033435  97 VKILHTYPELLLMPSNPAYKPIRVNPES-LEIWGVVTF 133
Cdd:PRK10276  96 VKKLQLRPTVQLIPMNSAYSPITISSEDtLDVFGVVTH 133
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 24-138 2.23e-42

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 138.89  E-value: 2.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  24 SCGVMSPCAGHEDNELNLHEYVVRNRPSTFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFTVKILHTY 103
Cdd:COG1974   84 AAGFPIPAEENIEEYLDLPEELVKNPGATFALRVKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKRLYKE 163

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446033435 104 P-ELLLMPSNPAYKPIRVNPESLEIWGVVTFALNQF 138
Cdd:COG1974  164 GgRVRLQPENPAYPPIIIEGDDVEILGVVVGVIRRL 199
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 53-132 9.01e-27

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: 95.32  E-value: 9.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  53 FFVRAAGLSMINAgINDGAILVVDRSLTARHGSIVVALVDGEFTVKILHTYPE--LLLMPSNPAYKPIRVNPESLEIWGV 130
Cdd:cd06529    1 FALRVKGDSMEPT-IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGgrLRLISDNPAYPPIEIDEEELEIVGV 79


                 ..
gi 446033435 131 VT 132
Cdd:cd06529   80 VG 81
Peptidase_S24 pfam00717
Peptidase S24-like;
34-131 4.86e-25

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 92.27  E-value: 4.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435   34 HEDNELNLHEYVVRNRPSTFFVRAAGLSMInAGINDGAILVVDRSLTARHGSIVVALVDGEFTVKILHTYP-ELLLMPSN 112
Cdd:pfam00717  17 EIEGYLPLPESLLSPPGNLFALRVKGDSME-PGIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLYRDGgGIRLISLN 95

                          90       100
                  ....*....|....*....|
gi 446033435  113 PAYKPIRVNPE-SLEIWGVV 131
Cdd:pfam00717  96 PEYPPIELPAEdDVEIIGRV 115
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 51-131 4.08e-17

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: 73.98  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435   51 STFFVRAAGLSMINAGINDGAILVVDRSLTARHGSIVVALVDGEFTVKILhtYPE---LLLMPSNPAYKPIRVNPESLEI 127
Cdd:TIGR00498 110 AVFLLKVMGDSMVDAGICDGDLLIVRSQKDARNGEIVAAMIDGEVTVKRF--YKDgtkVELKPENPEFDPIVLNAEDVTI 187


                  ....
gi 446033435  128 WGVV 131
Cdd:TIGR00498 188 LGKV 191
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 53-131 1.06e-14

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: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  53 FFVRAAGLSMINAgINDGAILVVDRSLT-ARHGSIVVALVDG-EFTVKILHTYPE---LLLMPSNPAYKPIRVN-PESLE 126
Cdd:cd06462    1 FALRVEGDSMEPT-IPDGDLVLVDKSSYePKRGDIVVFRLPGgELTVKRVIGLPGeghYFLLGDNPNSPDSRIDgPPELD 79


                 ....*
gi 446033435 127 IWGVV 131
Cdd:cd06462   80 IVGVV 84
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 17-131 3.84e-11

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 56.51  E-value: 3.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446033435  17 PFFSDLLSCGvmspcAGHEDNELNLHEYVV---RNRPSTFFVRAAGLSMINAgINDGAILVVDRSLTA-RHGSIVVALVD 92
Cdd:COG2932    2 PLYDGEASAG-----GGAFNEVEEPVDKLEfpgLPPDNLFAVRVSGDSMEPT-IRDGDIVLVDPSDTEiRDGGIYVVRTD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446033435  93 GEFTVKILHTYPE--LLLMPSNPAYKPIRVNPE---SLEIWGVV 131
Cdd:COG2932   76 GELLVKRLQRRPDgkLRLISDNPAYPPIEIPPEdadEIEIIGRV 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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