dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Saprolegnia parasitica

Lineage

Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica

CAZyme ID

SPRG_15000-t26_1-p1

CAZy Family

GT69

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
750		81087.95	6.6127

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65	20435	695850	314	20121

Gene Location

Enzyme Prediction help

EC	-	-

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	8.82e-101	164	426	1	264	Peptidase S8 family domain in BacillopeptidaseF-like proteins. Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a 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 these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity.
173787	Peptidases_S8_S53	1.20e-40	167	424	1	241	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.
173803	Peptidases_S8_Subtilisin_subset	1.23e-40	166	424	1	229	Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. 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.
395035	Peptidase_S8	3.05e-40	164	426	1	273	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.
173812	Peptidases_S8_1	1.25e-39	164	426	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
0.0	1	750	1	748
0.0	1	750	1	751
5.88e-297	1	750	1	748
4.29e-296	1	750	1	745
1.00e-65	58	470	35	427

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.14e-26	146	407	17	270	Chain A, Tk-subtilisin [Thermococcus kodakarensis]
8.56e-26	146	407	6	259	Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1],2Z57_A Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1],2Z58_A Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1]
8.89e-26	146	407	8	261	Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1]
1.05e-25	146	407	17	270	Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1],3A3N_A Chain A, Tk-subtilisin [Thermococcus kodakarensis],3A3O_A Chain A, Tk-subtilisin [Thermococcus kodakarensis],3VV2_A Crystal structure of complex form between S324A-subtilisin and mutant Tkpro [Thermococcus kodakarensis KOD1]
1.57e-25	146	407	6	259	Crystal structure of mature form of Tk-subtilisin [Thermococcus kodakarensis KOD1]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.08e-52	145	470	198	507	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
9.08e-25	146	407	110	363	Tk-subtilisin OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1675 PE=1 SV=1
6.64e-24	134	426	130	416	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1
3.19e-23	146	424	4	252	Subtilisin DY OS=Bacillus licheniformis OX=1402 GN=apr PE=1 SV=1
7.84e-23	119	424	82	357	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.130552	0.869420	CS pos: 16-17. Pr: 0.6405

TMHMM Annotations help

There is no transmembrane helices in SPRG_15000-t26_1-p1.

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