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Conserved domains on  [gi|1080263887|gb|OFK56948|]
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hypothetical protein HMPREF2811_06890 [Globicatella sp. HMSC072A10]

Protein Classification

C39 family peptidase( domain architecture ID 10609171)

uncharacterized C39 family peptidase; C39 mostly contains bacteriocin-processing endopeptidases that cleaves the double-glycine leader peptide from the precursors of various bacteriocins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
163-273 3.69e-18

Peptidase_C39 like family;


:

Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 79.03  E-value: 3.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080263887 163 GENGCALVSLSMIESYYqNRIVEPNEILNWSQ-------------NDYYVHNEGTSWQIFYDFAIEHDYQFEN-FGSNFY 228
Cdd:pfam13529  11 LPNGCGPTSLAMVLSYL-GITVTQDELAKEIGtnpdgnpntgfvgNPYDKSGYGVYNPPIVALAEKYGLKVTDiTGSSFD 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080263887 229 DAMDALNQNHIVIVSVQ-----PGHFTEVGHILLIRGYDSKNRKVYVNDP 273
Cdd:pfam13529  90 EVIRLLDAGIPVVVSTTtfgplNYYFTSSGHLVVIVGYDDKGDYVYVNDP 139
 
Name Accession Description Interval E-value
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
163-273 3.69e-18

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 79.03  E-value: 3.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080263887 163 GENGCALVSLSMIESYYqNRIVEPNEILNWSQ-------------NDYYVHNEGTSWQIFYDFAIEHDYQFEN-FGSNFY 228
Cdd:pfam13529  11 LPNGCGPTSLAMVLSYL-GITVTQDELAKEIGtnpdgnpntgfvgNPYDKSGYGVYNPPIVALAEKYGLKVTDiTGSSFD 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080263887 229 DAMDALNQNHIVIVSVQ-----PGHFTEVGHILLIRGYDSKNRKVYVNDP 273
Cdd:pfam13529  90 EVIRLLDAGIPVVVSTTtfgplNYYFTSSGHLVVIVGYDDKGDYVYVNDP 139
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 163-279 4.82e-15

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 70.90  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080263887 163 GENGCALVSLSMIESYYQNRIVEPNEILNWSQNDYYVHNEGTSW-QIFYDFAIEHDYQFENFGSNfYDAMDALNQNHIVI 241
Cdd:cd02549     3 LENGCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGTYPkPIVSAAARKYGLVVRPLTGL-LALLRQLAAGHPVI 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1080263887 242 VSVQPGHF-TEVGHILLIRGYDSKNRkVYVNDPNDNAEK 279
Cdd:cd02549    82 VSVNLGVSiTPSGHAMVVIGYDRKGN-VYVNDPGGGRRL 119
 
Name Accession Description Interval E-value
Peptidase_C39_2 pfam13529
Peptidase_C39 like family;
163-273 3.69e-18

Peptidase_C39 like family;


Pssm-ID: 379241 [Multi-domain]  Cd Length: 139  Bit Score: 79.03  E-value: 3.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080263887 163 GENGCALVSLSMIESYYqNRIVEPNEILNWSQ-------------NDYYVHNEGTSWQIFYDFAIEHDYQFEN-FGSNFY 228
Cdd:pfam13529  11 LPNGCGPTSLAMVLSYL-GITVTQDELAKEIGtnpdgnpntgfvgNPYDKSGYGVYNPPIVALAEKYGLKVTDiTGSSFD 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080263887 229 DAMDALNQNHIVIVSVQ-----PGHFTEVGHILLIRGYDSKNRKVYVNDP 273
Cdd:pfam13529  90 EVIRLLDAGIPVVVSTTtfgplNYYFTSSGHLVVIVGYDDKGDYVYVNDP 139
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 163-279 4.82e-15

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 70.90  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080263887 163 GENGCALVSLSMIESYYQNRIVEPNEILNWSQNDYYVHNEGTSW-QIFYDFAIEHDYQFENFGSNfYDAMDALNQNHIVI 241
Cdd:cd02549     3 LENGCGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGTYPkPIVSAAARKYGLVVRPLTGL-LALLRQLAAGHPVI 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1080263887 242 VSVQPGHF-TEVGHILLIRGYDSKNRkVYVNDPNDNAEK 279
Cdd:cd02549    82 VSVNLGVSiTPSGHAMVVIGYDRKGN-VYVNDPGGGRRL 119
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 161-284 1.32e-04

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 41.29  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080263887 161 ELGENGCALVSLSMIESYYQNRIVEPNEIlNWSQNDYYVHNEGTSWQIFYDFAiehdyQFENFGS-----NFYDA---MD 232
Cdd:pfam12385  12 QQAAMGCWAASASMIAGYRGQKPIDPSEI-AALVPGWSQYDTGLNGPEDIALA-----EKWGLGNvpeppQSYSIdalVK 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1080263887 233 ALNQNHIVIVSVQ-PGHFteVGHILLIRGYDSKNRKVYVNDPNDNAEKMFSIQ 284
Cdd:pfam12385  86 LLRAYGPLWCAIAwPGGF--VGHAIVLTGIDEDGTPVYYHDPWSGPRREVSLA 136
 
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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