MULTISPECIES: GBS Bsp-like repeat-containing protein [Streptococcus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Peptidase_C39A | cd02549 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
703-832 | 1.93e-29 | |||
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: 114.04 E-value: 1.93e-29
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GBS_Bsp-like | pfam08481 | GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins ... |
590-673 | 5.25e-21 | |||
GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology. : Pssm-ID: 400671 Cd Length: 89 Bit Score: 88.13 E-value: 5.25e-21
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
548-581 | 1.36e-13 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 65.07 E-value: 1.36e-13
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
396-429 | 1.34e-12 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 62.38 E-value: 1.34e-12
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
249-282 | 6.89e-11 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 57.37 E-value: 6.89e-11
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
155-188 | 5.61e-09 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 51.98 E-value: 5.61e-09
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
202-236 | 9.15e-09 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 51.59 E-value: 9.15e-09
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KxYKxGKxW_sig | pfam19258 | KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as ... |
5-40 | 3.36e-05 | |||
KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK signal peptide. : Pssm-ID: 466014 [Multi-domain] Cd Length: 41 Bit Score: 41.71 E-value: 3.36e-05
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
351-383 | 3.46e-04 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 38.50 E-value: 3.46e-04
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
309-339 | 8.89e-03 | |||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. : Pssm-ID: 429523 Cd Length: 35 Bit Score: 34.64 E-value: 8.89e-03
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Name | Accession | Description | Interval | E-value | ||||
Peptidase_C39A | cd02549 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
703-832 | 1.93e-29 | ||||
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: 114.04 E-value: 1.93e-29
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GBS_Bsp-like | pfam08481 | GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins ... |
590-673 | 5.25e-21 | ||||
GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology. Pssm-ID: 400671 Cd Length: 89 Bit Score: 88.13 E-value: 5.25e-21
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
548-581 | 1.36e-13 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 65.07 E-value: 1.36e-13
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
396-429 | 1.34e-12 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 62.38 E-value: 1.34e-12
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
249-282 | 6.89e-11 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 57.37 E-value: 6.89e-11
|
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
547-595 | 5.57e-10 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 55.34 E-value: 5.57e-10
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
155-188 | 5.61e-09 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 51.98 E-value: 5.61e-09
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
202-236 | 9.15e-09 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 51.59 E-value: 9.15e-09
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
395-438 | 9.25e-09 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 51.88 E-value: 9.25e-09
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Peptidase_C39_2 | pfam13529 | Peptidase_C39 like family; |
683-816 | 1.57e-08 | ||||
Peptidase_C39 like family; Pssm-ID: 379241 [Multi-domain] Cd Length: 139 Bit Score: 53.99 E-value: 1.57e-08
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
201-247 | 1.80e-08 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 51.10 E-value: 1.80e-08
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
154-192 | 3.15e-07 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 47.64 E-value: 3.15e-07
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
248-280 | 5.84e-07 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 46.87 E-value: 5.84e-07
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KxYKxGKxW_sig | pfam19258 | KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as ... |
5-40 | 3.36e-05 | ||||
KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK signal peptide. Pssm-ID: 466014 [Multi-domain] Cd Length: 41 Bit Score: 41.71 E-value: 3.36e-05
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YvpB | COG4990 | Predicted cysteine peptidase, C39 family [General function prediction only]; |
653-841 | 1.54e-04 | ||||
Predicted cysteine peptidase, C39 family [General function prediction only]; Pssm-ID: 444014 [Multi-domain] Cd Length: 303 Bit Score: 44.80 E-value: 1.54e-04
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KxYKxGKxW | TIGR03715 | KxYKxGKxW signal peptide; This model describes a novel form of signal peptide that occurs as ... |
5-25 | 1.69e-04 | ||||
KxYKxGKxW signal peptide; This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus. Pssm-ID: 274741 [Multi-domain] Cd Length: 23 Bit Score: 39.29 E-value: 1.69e-04
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
351-383 | 3.46e-04 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 38.50 E-value: 3.46e-04
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
309-339 | 8.89e-03 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 34.64 E-value: 8.89e-03
|
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Name | Accession | Description | Interval | E-value | ||||
Peptidase_C39A | cd02549 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
703-832 | 1.93e-29 | ||||
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: 114.04 E-value: 1.93e-29
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GBS_Bsp-like | pfam08481 | GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins ... |
590-673 | 5.25e-21 | ||||
GBS Bsp-like repeat; This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology. Pssm-ID: 400671 Cd Length: 89 Bit Score: 88.13 E-value: 5.25e-21
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
548-581 | 1.36e-13 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 65.07 E-value: 1.36e-13
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
396-429 | 1.34e-12 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 62.38 E-value: 1.34e-12
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
249-282 | 6.89e-11 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 57.37 E-value: 6.89e-11
|
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
547-595 | 5.57e-10 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 55.34 E-value: 5.57e-10
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
155-188 | 5.61e-09 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 51.98 E-value: 5.61e-09
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
202-236 | 9.15e-09 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 51.59 E-value: 9.15e-09
|
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
395-438 | 9.25e-09 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 51.88 E-value: 9.25e-09
|
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Peptidase_C39_2 | pfam13529 | Peptidase_C39 like family; |
683-816 | 1.57e-08 | ||||
Peptidase_C39 like family; Pssm-ID: 379241 [Multi-domain] Cd Length: 139 Bit Score: 53.99 E-value: 1.57e-08
|
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
201-247 | 1.80e-08 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 51.10 E-value: 1.80e-08
|
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
154-192 | 3.15e-07 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 47.64 E-value: 3.15e-07
|
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ChW | smart00728 | Clostridial hydrophobic, with a conserved W residue, domain; |
248-280 | 5.84e-07 | ||||
Clostridial hydrophobic, with a conserved W residue, domain; Pssm-ID: 214791 Cd Length: 46 Bit Score: 46.87 E-value: 5.84e-07
|
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Peptidase_C39 | pfam03412 | Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
706-816 | 7.18e-06 | ||||
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family. Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 46.06 E-value: 7.18e-06
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KxYKxGKxW_sig | pfam19258 | KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as ... |
5-40 | 3.36e-05 | ||||
KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK signal peptide. Pssm-ID: 466014 [Multi-domain] Cd Length: 41 Bit Score: 41.71 E-value: 3.36e-05
|
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YvpB | COG4990 | Predicted cysteine peptidase, C39 family [General function prediction only]; |
653-841 | 1.54e-04 | ||||
Predicted cysteine peptidase, C39 family [General function prediction only]; Pssm-ID: 444014 [Multi-domain] Cd Length: 303 Bit Score: 44.80 E-value: 1.54e-04
|
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KxYKxGKxW | TIGR03715 | KxYKxGKxW signal peptide; This model describes a novel form of signal peptide that occurs as ... |
5-25 | 1.69e-04 | ||||
KxYKxGKxW signal peptide; This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus. Pssm-ID: 274741 [Multi-domain] Cd Length: 23 Bit Score: 39.29 E-value: 1.69e-04
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
351-383 | 3.46e-04 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 38.50 E-value: 3.46e-04
|
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ChW | pfam07538 | Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based ... |
309-339 | 8.89e-03 | ||||
Clostridial hydrophobic W; A novel extracellular macromolecular system has been proposed based on the proteins containing ChW repeats. ChW stands for Clostridial hydrophobic with conserved W (tryptophan). This repeat was originally described in Clostridium acetobutylicum but is also found in other Gram-positive bacteria including Enterococcus faecalis, Streptococcus agalactiae and Streptomyces coelicolor. Pssm-ID: 429523 Cd Length: 35 Bit Score: 34.64 E-value: 8.89e-03
|
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Blast search parameters | ||||
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