dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Clostridium beijerinckii

Lineage

Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium beijerinckii

CAZyme ID

MGYG000004667_00548

CAZy Family

GH0

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1061	MGYG000004667_34\|CGC1	117231.38	5.5457

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004667	6180974	Isolate	United States	North America

Gene Location

Start: 88377; End: 91562 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000004667_00548.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07478	Peptidases_S8_CspA-like	4.54e-177	124	555	3	455	Peptidase S8 family domain in CspA-like proteins. GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07487	Peptidases_S8_1	7.63e-36	124	539	1	264	Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07474	Peptidases_S8_subtilisin_Vpr-like	1.29e-28	124	514	1	251	Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
pfam00082	Peptidase_S8	1.63e-26	124	555	1	287	Subtilase family. Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
cd00306	Peptidases_S8_S53	4.39e-26	127	514	1	224	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QES76183.1	9.27e-257	618	1061	1	443
QGH20837.1	1.56e-227	617	1061	3	441
QSX02883.1	1.56e-227	617	1061	3	441
QMW92695.1	1.56e-227	617	1061	3	441
AXB86494.1	1.56e-227	617	1061	3	441

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4I0W_B	7.04e-165	106	568	3	467	Structureof the Clostridium Perfringens CspB protease [Clostridium perfringens],4I0W_D Structure of the Clostridium Perfringens CspB protease [Clostridium perfringens]
6MW4_A	8.59e-49	68	570	28	557	ChainA, Putative germination-specific protease [Clostridioides difficile R20291]
4I0W_A	1.78e-11	8	101	1	94	Structureof the Clostridium Perfringens CspB protease [Clostridium perfringens],4I0W_C Structure of the Clostridium Perfringens CspB protease [Clostridium perfringens]
3AFG_A	1.16e-09	124	372	138	356	ChainA, Subtilisin-like serine protease [Thermococcus kodakarensis],3AFG_B Chain B, Subtilisin-like serine protease [Thermococcus kodakarensis]
6PAK_A	1.54e-09	355	513	67	236	Insightinto subtilisin E-S7 cleavage pattern based on crystal structure and hydrolysates peptide analysis [Bacillus subtilis subsp. subtilis str. 168],6PAK_B Insight into subtilisin E-S7 cleavage pattern based on crystal structure and hydrolysates peptide analysis [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P16271	4.08e-20	59	617	148	751	PI-type proteinase OS=Lactococcus lactis subsp. cremoris OX=1359 GN=prtP PE=3 SV=1
P15292	1.60e-19	59	617	148	751	PIII-type proteinase OS=Lactococcus lactis subsp. cremoris (strain SK11) OX=272622 GN=prtP PE=1 SV=2
P15293	2.08e-19	59	617	148	751	PII-type proteinase OS=Lactococcus lactis subsp. cremoris OX=1359 GN=prt PE=3 SV=1
Q02470	6.17e-17	59	617	148	751	PII-type proteinase OS=Lacticaseibacillus paracasei OX=1597 GN=prtP PE=1 SV=1
P29141	2.69e-11	119	565	175	596	Minor extracellular protease vpr OS=Bacillus subtilis (strain 168) OX=224308 GN=vpr PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000048	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004667_00548.

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