CAZyme Information: SPRG_21483-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_21483-t26_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
509		54601.04	7.6714

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: location=KK583374:11905-13510(+)

Full Sequence      

MTGKNGYGVAPGAQWISCRGLSGKTGSTWALLECLQFMICPTLPDGSNPDCSKGAHVVNN
SWGSKEYNPIYEDAFAALHKAGIIPVVSNGNNGPACATTGNPGGYPNVISVGAIGSSNNE
PTKLAYFSSKGPATYRDKRGVQHTVVKPTISAPGYFTLSATNQSDHATANFAGTSMAAPH
VAGVIALMKSTAKWYTNDVNNTVYDGALNCGGVSDTAWPNNRYGYGRINADKIFKDGKFV
STPAPTTKAPVSQLANIKSFCTYKKTVLSEWNNQLFIDTIKNNKNEGFVIDLKYNIIQSA
SSEDGCLSLIKDSSNTNAVALRECKGDATQIWKFDTVAKRIVHPQSGFCLTSNAAKLGAG
PSVAPCSSGAVSQYFDQCDNVKEKSYVKLITKNNKVISEFYSGVYADWVSDSVNELFTYD
AAAKTLQVTSNGECLDAFRDGDKFGLHTYACDATNVNQKWIIDAAGHKIKHATHSNLCLD
VDPTNSTHAAQVWECHNANSNQWIDAVAY

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	3.79e-61	3	202	68	255	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.
173800	Peptidases_S8_subtilisin_Vpr-like	2.55e-30	8	232	84	294	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.
173803	Peptidases_S8_Subtilisin_subset	5.68e-29	8	198	61	220	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	1.08e-27	8	226	75	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.
173787	Peptidases_S8_S53	1.62e-27	6	198	63	232	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56438.1|CBM13	1.53e-284	1	509	207	748
AIG56170.1|CBM13	4.55e-283	1	509	209	745
AIG56171.1|CBM13	1.04e-208	1	509	218	751
AIG56439.1|CBM13	4.96e-206	1	509	215	748
AIG56036.1|CBM13|GH17	5.71e-85	261	509	448	691

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AFG_A	2.84e-14	8	232	201	414	Chain A, Subtilisin-like serine protease [Thermococcus kodakarensis],3AFG_B Chain B, Subtilisin-like serine protease [Thermococcus kodakarensis]
1MPT_A	4.29e-13	8	231	81	265	Chain A, M-PROTEASE [Alkalihalobacillus clausii KSM-K16],1WSD_A Chain A, M-protease [Alkalihalobacillus clausii KSM-K16]
3A3P_A	6.04e-13	8	230	103	320	Chain A, Tk-subtilisin [Thermococcus kodakarensis]
2Z56_A	7.35e-13	8	230	92	309	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]
2Z30_A	7.48e-13	8	230	94	311	Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P16397|SUBF_BACSU	5.00e-21	3	230	289	508	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
sp|Q5JIZ5|TKSP_THEKO	7.66e-14	8	232	224	437	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1
sp|P20724|ELYA_BACYA	2.47e-12	8	231	190	374	Alkaline elastase YaB OS=Bacillus sp. (strain YaB) OX=72578 GN=ale PE=1 SV=1
sp|P58502|TKSU_THEKO	3.09e-12	8	230	196	413	Tk-subtilisin OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1675 PE=1 SV=1
sp|P72186|PLS_PYRFU	4.03e-12	8	235	414	657	Pyrolysin OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=pls PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999141	0.000903

TMHMM  Annotations     

There is no transmembrane helices in SPRG_21483-t26_1-p1.