conserved hypothetical protein [Nocardioides sp. JS614]
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
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Peptidase_C39_2 | pfam13529 | Peptidase_C39 like family; |
201-351 | 9.75e-30 | |||
Peptidase_C39 like family; : Pssm-ID: 379241 [Multi-domain] Cd Length: 139 Bit Score: 111.77 E-value: 9.75e-30
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Name | Accession | Description | Interval | E-value | ||||
Peptidase_C39_2 | pfam13529 | Peptidase_C39 like family; |
201-351 | 9.75e-30 | ||||
Peptidase_C39 like family; Pssm-ID: 379241 [Multi-domain] Cd Length: 139 Bit Score: 111.77 E-value: 9.75e-30
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Peptidase_C39A | cd02549 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
220-383 | 1.31e-25 | ||||
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: 100.95 E-value: 1.31e-25
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Name | Accession | Description | Interval | E-value | ||||
Peptidase_C39_2 | pfam13529 | Peptidase_C39 like family; |
201-351 | 9.75e-30 | ||||
Peptidase_C39 like family; Pssm-ID: 379241 [Multi-domain] Cd Length: 139 Bit Score: 111.77 E-value: 9.75e-30
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Peptidase_C39A | cd02549 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
220-383 | 1.31e-25 | ||||
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: 100.95 E-value: 1.31e-25
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Peptidase_C70 | pfam12385 | Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ... |
224-362 | 3.73e-05 | ||||
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: 43.22 E-value: 3.73e-05
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Blast search parameters | ||||
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