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Conserved domains on  [gi|2294385085|ref|WP_259296617|]
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S24 family peptidase [Bacteroides uniformis]

Protein Classification

helix-turn-helix transcriptional regulator( domain architecture ID 11459250)

helix-turn-helix (HTH) transcriptional regulator similar to phage repressor protein CI and Pseudomonas aeruginosa HTH-type transcriptional regulator PrtR, which represses the expression of various pyocin genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 104-230 6.79e-12

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


:

Pssm-ID: 442176  Cd Length: 121  Bit Score: 60.36  E-value: 6.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294385085 104 PYYNVDFIGGFEFVSNDQTqlPDYYINYPPYNKPGVMWCNLTGHSMEPEISNGDVIALKEVRSPIEylpAGEIYGIITDD 183
Cdd:COG2932     2 PLYDGEASAGGGAFNEVEE--PVDKLEFPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIR---DGGIYVVRTDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2294385085 184 YRTVKRIRPGAqKGFVRLIPANksPEFCEQEIPVEMIRRVfAVLGSI 230
Cdd:COG2932    77 ELLVKRLQRRP-DGKLRLISDN--PAYPPIEIPPEDADEI-EIIGRV 119
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 104-230 6.79e-12

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 60.36  E-value: 6.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294385085 104 PYYNVDFIGGFEFVSNDQTqlPDYYINYPPYNKPGVMWCNLTGHSMEPEISNGDVIALKEVRSPIEylpAGEIYGIITDD 183
Cdd:COG2932     2 PLYDGEASAGGGAFNEVEE--PVDKLEFPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIR---DGGIYVVRTDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2294385085 184 YRTVKRIRPGAqKGFVRLIPANksPEFCEQEIPVEMIRRVfAVLGSI 230
Cdd:COG2932    77 ELLVKRLQRRP-DGKLRLISDN--PAYPPIEIPPEDADEI-EIIGRV 119
Peptidase_S24 pfam00717
Peptidase S24-like;
115-224 1.35e-10

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 56.83  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294385085 115 EFVSNDQTQLPdyYINYPPYNKPGVMWCNLTGHSMEPEISNGDVIALKEVRSPIeylpAGEIYGIITDDYRTVKRI-RPG 193
Cdd:pfam00717  13 LAEEEIEGYLP--LPESLLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREAR----NGDIVVARLDGEATVKRLyRDG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2294385085 194 aqkGFVRLIPANKS--PEFCEQEIPVEMIRRVF 224
Cdd:pfam00717  87 ---GGIRLISLNPEypPIELPAEDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 145-223 3.69e-08

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: 49.09  E-value: 3.69e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294385085 145 TGHSMEPEISNGDVIALKEVRSPIEylpaGEIYGIITDDYRTVKRIRPGAQKGfVRLIPANKSPEfcEQEIPVEMIRRV 223
Cdd:cd06529     6 KGDSMEPTIPDGDLVLVDPSDTPRD----GDIVVARLDGELTVKRLQRRGGGR-LRLISDNPAYP--PIEIDEEELEIV 77
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 104-230 6.79e-12

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 60.36  E-value: 6.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294385085 104 PYYNVDFIGGFEFVSNDQTqlPDYYINYPPYNKPGVMWCNLTGHSMEPEISNGDVIALKEVRSPIEylpAGEIYGIITDD 183
Cdd:COG2932     2 PLYDGEASAGGGAFNEVEE--PVDKLEFPGLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIR---DGGIYVVRTDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2294385085 184 YRTVKRIRPGAqKGFVRLIPANksPEFCEQEIPVEMIRRVfAVLGSI 230
Cdd:COG2932    77 ELLVKRLQRRP-DGKLRLISDN--PAYPPIEIPPEDADEI-EIIGRV 119
Peptidase_S24 pfam00717
Peptidase S24-like;
115-224 1.35e-10

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 56.83  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294385085 115 EFVSNDQTQLPdyYINYPPYNKPGVMWCNLTGHSMEPEISNGDVIALKEVRSPIeylpAGEIYGIITDDYRTVKRI-RPG 193
Cdd:pfam00717  13 LAEEEIEGYLP--LPESLLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPSREAR----NGDIVVARLDGEATVKRLyRDG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2294385085 194 aqkGFVRLIPANKS--PEFCEQEIPVEMIRRVF 224
Cdd:pfam00717  87 ---GGIRLISLNPEypPIELPAEDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 145-223 3.69e-08

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: 49.09  E-value: 3.69e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294385085 145 TGHSMEPEISNGDVIALKEVRSPIEylpaGEIYGIITDDYRTVKRIRPGAQKGfVRLIPANKSPEfcEQEIPVEMIRRV 223
Cdd:cd06529     6 KGDSMEPTIPDGDLVLVDPSDTPRD----GDIVVARLDGELTVKRLQRRGGGR-LRLISDNPAYP--PIEIDEEELEIV 77
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 146-206 6.12e-06

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: 43.41  E-value: 6.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2294385085 146 GHSMEPEISNGDVIALKEVRSPIEYlpaGEIYGIITDDYR-TVKRIRPGAQKGFVRLIPANK 206
Cdd:cd06462     7 GDSMEPTIPDGDLVLVDKSSYEPKR---GDIVVFRLPGGElTVKRVIGLPGEGHYFLLGDNP 65
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 146-233 2.64e-05

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294385085 146 GHSM-EPEISNGDVIAlkeVRSPIEYLPaGEIYGIITDDYRTVKRIRPgaQKGFVRLIPANksPEFCEQEIPVEMIrRVF 224
Cdd:COG1974   119 GDSMiDAGILDGDLVI---VDRQLEAEN-GDIVVALIDGEATVKRLYK--EGGRVRLQPEN--PAYPPIIIEGDDV-EIL 189

                          90
                  ....*....|
gi 2294385085 225 AVL-GSIRKF 233
Cdd:COG1974   190 GVVvGVIRRL 199
 
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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