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Conserved domains on  [gi|496774673|ref|WP_009368566|]
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MULTISPECIES: S24 family peptidase [Bilophila]

Protein Classification

HTH_XRE and S24_LexA-like domain-containing protein( domain architecture ID 11715193)

HTH_XRE and S24_LexA-like domain-containing protein

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: ...
 96-210 5.21e-19

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


:

Pssm-ID: 442176  Cd Length: 121  Bit Score: 78.85  E-value: 5.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673  96 LPYYD-----SDRVQDGVWEPSGTIMLPePYAGKELRILRITGDSFSPTVRQGAFVGVDTSSVRPSSGSIFAVSVPfEGV 170
Cdd:COG2932    1 VPLYDgeasaGGGAFNEVEEPVDKLEFP-GLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIYVVRTD-GEL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496774673 171 VIKRVFCDSD-TLLLRTDNPLHPSMSIPLAEAGRL--IGRVAW 210
Cdd:COG2932   79 LVKRLQRRPDgKLRLISDNPAYPPIEIPPEDADEIeiIGRVVW 121
HTH_XRE super family cl22854
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 8-72 1.94e-10

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


The actual alignment was detected with superfamily member pfam07022:

Pssm-ID: 473980  Cd Length: 65  Bit Score: 54.64  E-value: 1.94e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496774673    8 EIFRRFQSVTGTSTQQELADVLGIKQSTISESKKRGTVPPGWFLVLFEMRGVNPDWLKQGKGPIY 72
Cdd:pfam07022   1 AVIERLMKAYGFKSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGDGELY 65
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 96-210 5.21e-19

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 78.85  E-value: 5.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673  96 LPYYD-----SDRVQDGVWEPSGTIMLPePYAGKELRILRITGDSFSPTVRQGAFVGVDTSSVRPSSGSIFAVSVPfEGV 170
Cdd:COG2932    1 VPLYDgeasaGGGAFNEVEEPVDKLEFP-GLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIYVVRTD-GEL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496774673 171 VIKRVFCDSD-TLLLRTDNPLHPSMSIPLAEAGRL--IGRVAW 210
Cdd:COG2932   79 LVKRLQRRPDgKLRLISDNPAYPPIEIPPEDADEIeiIGRVVW 121
Peptidase_S24 pfam00717
Peptidase S24-like;
102-208 5.09e-13

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 62.99  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673  102 DRVQDGVWEP-----SGTIMLPE--PYAGKELRILRITGDSFSPTVRQGAFVGVDTSsVRPSSGSIFAVSVPfEGVVIKR 174
Cdd:pfam00717   4 GRVAAGAPILaeeeiEGYLPLPEslLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPS-REARNGDIVVARLD-GEATVKR 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 496774673  175 VFCDSDTLLLRTDNPLHPSMSIPLAEAGRLIGRV 208
Cdd:pfam00717  82 LYRDGGGIRLISLNPEYPPIELPAEDDVEIIGRV 115
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 127-208 4.11e-11

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: 57.27  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673 127 RILRITGDSFSPTVRQGAFVGVDTSSVRPSSGSIFAVSVPFEGVVIKRVF--CDSDTLLLRTDNPLHPSMSIPLAEAGRL 204
Cdd:cd06462    1 FALRVEGDSMEPTIPDGDLVLVDKSSYEPKRGDIVVFRLPGGELTVKRVIglPGEGHYFLLGDNPNSPDSRIDGPPELDI 80


                 ....
gi 496774673 205 IGRV 208
Cdd:cd06462   81 VGVV 84
Phage_CI_repr pfam07022
Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI ...
 8-72 1.94e-10

Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI repressor proteins and related bacterial sequences. The CI repressor is known to function as a transcriptional switch, determining whether transcription is lytic or lysogenic.


Pssm-ID: 311152  Cd Length: 65  Bit Score: 54.64  E-value: 1.94e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496774673    8 EIFRRFQSVTGTSTQQELADVLGIKQSTISESKKRGTVPPGWFLVLFEMRGVNPDWLKQGKGPIY 72
Cdd:pfam07022   1 AVIERLMKAYGFKSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGDGELY 65
PRK08301 PRK08301
RNA polymerase sporulation sigma factor SigE;
21-42 7.56e-03

RNA polymerase sporulation sigma factor SigE;


Pssm-ID: 236228 [Multi-domain]  Cd Length: 234  Bit Score: 36.37  E-value: 7.56e-03
                         10        20
                 ....*....|....*....|..
gi 496774673  21 TQQELADVLGIKQSTISESKKR 42
Cdd:PRK08301 200 TQKEVADMLGISQSYISRLEKR 221
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 96-210 5.21e-19

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 78.85  E-value: 5.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673  96 LPYYD-----SDRVQDGVWEPSGTIMLPePYAGKELRILRITGDSFSPTVRQGAFVGVDTSSVRPSSGSIFAVSVPfEGV 170
Cdd:COG2932    1 VPLYDgeasaGGGAFNEVEEPVDKLEFP-GLPPDNLFAVRVSGDSMEPTIRDGDIVLVDPSDTEIRDGGIYVVRTD-GEL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496774673 171 VIKRVFCDSD-TLLLRTDNPLHPSMSIPLAEAGRL--IGRVAW 210
Cdd:COG2932   79 LVKRLQRRPDgKLRLISDNPAYPPIEIPPEDADEIeiIGRVVW 121
Peptidase_S24 pfam00717
Peptidase S24-like;
102-208 5.09e-13

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 62.99  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673  102 DRVQDGVWEP-----SGTIMLPE--PYAGKELRILRITGDSFSPTVRQGAFVGVDTSsVRPSSGSIFAVSVPfEGVVIKR 174
Cdd:pfam00717   4 GRVAAGAPILaeeeiEGYLPLPEslLSPPGNLFALRVKGDSMEPGIPDGDLVLVDPS-REARNGDIVVARLD-GEATVKR 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 496774673  175 VFCDSDTLLLRTDNPLHPSMSIPLAEAGRLIGRV 208
Cdd:pfam00717  82 LYRDGGGIRLISLNPEYPPIELPAEDDVEIIGRV 115
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 127-208 4.11e-11

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: 57.27  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673 127 RILRITGDSFSPTVRQGAFVGVDTSSVRPSSGSIFAVSVPFEGVVIKRVF--CDSDTLLLRTDNPLHPSMSIPLAEAGRL 204
Cdd:cd06462    1 FALRVEGDSMEPTIPDGDLVLVDKSSYEPKRGDIVVFRLPGGELTVKRVIglPGEGHYFLLGDNPNSPDSRIDGPPELDI 80


                 ....
gi 496774673 205 IGRV 208
Cdd:cd06462   81 VGVV 84
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 127-208 1.47e-10

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: 55.64  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673 127 RILRITGDSFSPTVRQGAFVGVDTsSVRPSSGSIFAVSVPFEgVVIKRVF-CDSDTLLLRTDNPLHPSMSIPLAEAgRLI 205
Cdd:cd06529    1 FALRVKGDSMEPTIPDGDLVLVDP-SDTPRDGDIVVARLDGE-LTVKRLQrRGGGRLRLISDNPAYPPIEIDEEEL-EIV 77


                 ...
gi 496774673 206 GRV 208
Cdd:cd06529   78 GVV 80
Phage_CI_repr pfam07022
Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI ...
 8-72 1.94e-10

Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI repressor proteins and related bacterial sequences. The CI repressor is known to function as a transcriptional switch, determining whether transcription is lytic or lysogenic.


Pssm-ID: 311152  Cd Length: 65  Bit Score: 54.64  E-value: 1.94e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496774673    8 EIFRRFQSVTGTSTQQELADVLGIKQSTISESKKRGTVPPGWFLVLFEMRGVNPDWLKQGKGPIY 72
Cdd:pfam07022   1 AVIERLMKAYGFKSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGDGELY 65
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 8-212 4.42e-10

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 56.85  E-value: 4.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673   8 EIFRRFQSVTGTS-TQQELADVLGIKQSTISESkkrgtvppgwfLVLFEMRGvnpdwlkqgkgpiYLRTEDG--RYMEPE 84
Cdd:COG1974   13 DFIKEYIRERGYPpSQREIAEALGLSSSAVHRH-----------LKALEKKG-------------YLRRDPGksRAIELL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496774673  85 PAATPLgrgVSLPYYdsDRVQDGVW-----EPSGTIMLPEPYAG--KELRILRITGDSF-SPTVRQGAFVGVDTSSVrPS 156
Cdd:COG1974   69 PASPEV---VGLPLL--GRVAAGFPipaeeNIEEYLDLPEELVKnpGATFALRVKGDSMiDAGILDGDLVIVDRQLE-AE 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496774673 157 SGSIFAVSVPfEGVVIKRVFCDSDTLLLRTDNPLHPSMSIPLAEAgRLIGRVAWVF 212
Cdd:COG1974  143 NGDIVVALID-GEATVKRLYKEGGRVRLQPENPAYPPIIIEGDDV-EILGVVVGVI 196
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 21-69 7.46e-04

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.


Pssm-ID: 463728 [Multi-domain]  Cd Length: 64  Bit Score: 36.88  E-value: 7.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 496774673   21 TQQELADVLGIKQSTIS--ESKKRGTvPPGWFLVLFEMRGVNPDWLKQGKG 69
Cdd:pfam12844  14 TQEELAERLGISRSQLSaiENGKSVP-PAETLYKIAELLGVPANWLLQGEG 63
PRK08301 PRK08301
RNA polymerase sporulation sigma factor SigE;
21-42 7.56e-03

RNA polymerase sporulation sigma factor SigE;


Pssm-ID: 236228 [Multi-domain]  Cd Length: 234  Bit Score: 36.37  E-value: 7.56e-03
                         10        20
                 ....*....|....*....|..
gi 496774673  21 TQQELADVLGIKQSTISESKKR 42
Cdd:PRK08301 200 TQKEVADMLGISQSYISRLEKR 221
 
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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