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_15001-t26_1-p1

CAZy Family

GT71

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
728		78012.53	6.1740

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	5.24e-93	157	418	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.
395035	Peptidase_S8	1.24e-44	157	418	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.
173803	Peptidases_S8_Subtilisin_subset	2.19e-43	159	416	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.
173799	Peptidases_S8_Subtilisin_like	8.78e-43	158	418	2	259	Peptidase S8 family domain in Subtilisin-like proteins. 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.
173800	Peptidases_S8_subtilisin_Vpr-like	6.83e-41	157	427	1	279	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
0.0	1	728	1	748
0.0	1	728	1	745
2.10e-272	1	728	1	751
2.17e-271	1	728	1	748
8.31e-75	492	728	441	691

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.91e-23	146	418	126	393	Chain A, Subtilisin-like serine protease [Thermococcus kodakarensis],3AFG_B Chain B, Subtilisin-like serine protease [Thermococcus kodakarensis]
5.50e-23	138	418	16	302	Chain A, Tk-subtilisin [Thermococcus kodakarensis]
8.34e-23	138	418	5	291	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]
8.63e-23	138	418	7	293	Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1]
1.00e-22	138	418	16	302	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.30e-39	48	464	114	507	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
1.80e-22	146	418	149	416	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1
7.40e-22	138	418	109	395	Tk-subtilisin OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1675 PE=1 SV=1
6.59e-20	113	417	87	357	Alkaline elastase YaB OS=Bacillus sp. (strain YaB) OX=72578 GN=ale PE=1 SV=1
2.94e-19	113	417	88	359	M-protease OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=aprE PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002649	0.997324	CS pos: 16-17. Pr: 0.9359

TMHMM Annotations help

There is no transmembrane helices in SPRG_15001-t26_1-p1.

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