NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1240939184|ref|WP_095708331|]
View 

S24 family peptidase [Pantoea vagans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 3-109 1.78e-19

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: 77.92  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   3 FQSPAQNYTEARLSLGDLVHLSPSSTYLMR-SDSSFPDTGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDPVP 81
Cdd:PRK10276   26 FPSPAADYVEQRIDLNELLIQHPSATYFVKaSGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTV 105

                          90       100
                  ....*....|....*....|....*...
gi 1240939184  82 ALQAPDSDETITLLDVSQGLPIWGVVAY 109
Cdd:PRK10276  106 QLIPMNSAYSPITISSEDTLDVFGVVTH 133
 
Name Accession Description Interval E-value
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
3-109 1.78e-19

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 77.92  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   3 FQSPAQNYTEARLSLGDLVHLSPSSTYLMR-SDSSFPDTGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDPVP 81
Cdd:PRK10276   26 FPSPAADYVEQRIDLNELLIQHPSATYFVKaSGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTV 105

                          90       100
                  ....*....|....*....|....*...
gi 1240939184  82 ALQAPDSDETITLLDVSQGLPIWGVVAY 109
Cdd:PRK10276  106 QLIPMNSAYSPITISSEDTLDVFGVVTH 133
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 5-107 4.46e-14

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 65.32  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   5 SPAQNYTEARLSLGDLVHLSPSSTYLMR-SDSSFPDTGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDP-VPA 82
Cdd:COG1974    89 IPAEENIEEYLDLPEELVKNPGATFALRvKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKRLYKEGgRVR 168

                          90       100
                  ....*....|....*....|....*.
gi 1240939184  83 LQAPDSD-ETITLldVSQGLPIWGVV 107
Cdd:COG1974   169 LQPENPAyPPIII--EGDDVEILGVV 192
Peptidase_S24 pfam00717
Peptidase S24-like;
1-107 1.11e-07

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 46.81  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   1 MAFQSPAQNYTEARLSLGDLVHLSPSSTYLMR--SDSSFPdtGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLD 78
Cdd:pfam00717   8 AGAPILAEEEIEGYLPLPESLLSPPGNLFALRvkGDSMEP--GIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLYRD 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1240939184  79 P-VPALQAPDSD-ETITlLDVSQGLPIWGVV 107
Cdd:pfam00717  86 GgGIRLISLNPEyPPIE-LPAEDDVEIIGRV 115
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 42-107 1.05e-06

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: 43.32  E-value: 1.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240939184  42 IVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDPVPALQA-PD----SDETITLLDVSqglpIWGVV 107
Cdd:cd06529    14 IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGGRLRLiSDnpayPPIEIDEEELE----IVGVV 80
 
Name Accession Description Interval E-value
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
3-109 1.78e-19

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 77.92  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   3 FQSPAQNYTEARLSLGDLVHLSPSSTYLMR-SDSSFPDTGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDPVP 81
Cdd:PRK10276   26 FPSPAADYVEQRIDLNELLIQHPSATYFVKaSGDSMIDAGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTV 105

                          90       100
                  ....*....|....*....|....*...
gi 1240939184  82 ALQAPDSDETITLLDVSQGLPIWGVVAY 109
Cdd:PRK10276  106 QLIPMNSAYSPITISSEDTLDVFGVVTH 133
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 5-107 4.46e-14

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 65.32  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   5 SPAQNYTEARLSLGDLVHLSPSSTYLMR-SDSSFPDTGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDP-VPA 82
Cdd:COG1974    89 IPAEENIEEYLDLPEELVKNPGATFALRvKGDSMIDAGILDGDLVIVDRQLEAENGDIVVALIDGEATVKRLYKEGgRVR 168

                          90       100
                  ....*....|....*....|....*.
gi 1240939184  83 LQAPDSD-ETITLldVSQGLPIWGVV 107
Cdd:COG1974   169 LQPENPAyPPIII--EGDDVEILGVV 192
Peptidase_S24 pfam00717
Peptidase S24-like;
1-107 1.11e-07

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 46.81  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240939184   1 MAFQSPAQNYTEARLSLGDLVHLSPSSTYLMR--SDSSFPdtGIVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLD 78
Cdd:pfam00717   8 AGAPILAEEEIEGYLPLPESLLSPPGNLFALRvkGDSMEP--GIPDGDLVLVDPSREARNGDIVVARLDGEATVKRLYRD 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1240939184  79 P-VPALQAPDSD-ETITlLDVSQGLPIWGVV 107
Cdd:pfam00717  86 GgGIRLISLNPEyPPIE-LPAEDDVEIIGRV 115
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 42-107 1.05e-06

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: 43.32  E-value: 1.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240939184  42 IVKGSVLAIDRALVPAHGQLIVAEFDGELTLRRLLLDPVPALQA-PD----SDETITLLDVSqglpIWGVV 107
Cdd:cd06529    14 IPDGDLVLVDPSDTPRDGDIVVARLDGELTVKRLQRRGGGRLRLiSDnpayPPIEIDEEELE----IVGVV 80
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH