CAZyme Information: SDRG_13040-t26_1-p1

Basic Information

• Species: Saprolegnia diclina
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
• CAZyme ID: SDRG_13040-t26_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
329		35593.65	5.1804

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SdiclinaVS20	17448	1156394	89	17359

• Gene Location: location=JH767186:108696-110857(-)

Full Sequence      

MKAALILAAIATATHAKVASSVLRALEVDGATDVFVRFADSPLESGEIAEGATRQEVFEI
LSERTEEASKSIDDVTKGLETKTLWIVPGTFIKAADQATVDKLAQHRGIKTIEHLPEISL
DPVLTQTTADATAAANATIQWGVQTVGAPDVWKHFDGKGVVIGSIDTGARYTHELIKDSW
RADRGWYDPYDHSAFPEDFDGHGTHTIGTMTGKNGFGVAPGAQWISCRGLYKGTGTSQAL
LDAKTLQVAGNGECLDAFRDGDKFGLHTYACDATNGNQKWIIDAADHKIKHATHNNLCLD
VDPTNPTHAAQVWECHNWNTNQWIDAVAY

Enzyme Prediction     

No EC number prediction in SDRG_13040-t26_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	2.76e-29	157	243	1	99	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.
395527	Ricin_B_lectin	4.66e-13	229	323	27	126	Ricin-type beta-trefoil lectin domain.
238092	RICIN	1.29e-11	233	324	31	123	Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture.
395035	Peptidase_S8	2.12e-11	157	243	1	101	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.
173810	Peptidases_S8_Thermitase_like	7.67e-11	140	243	10	117	Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan 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 the 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	1.07e-128	1	329	1	748
AIG56170.1|CBM13	1.32e-105	1	329	1	745
AIG56439.1|CBM13	5.35e-66	1	329	1	748
AIG56171.1|CBM13	7.48e-56	1	248	1	256
AIG56036.1|CBM13|GH17	1.95e-30	244	329	606	691

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3A3P_A	2.19e-07	138	262	16	147	Chain A, Tk-subtilisin [Thermococcus kodakarensis]
2Z56_A	2.81e-07	138	262	5	136	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]
2Z2Y_A	2.81e-07	138	262	5	136	Chain A, Tk-subtilisin [Thermococcus kodakarensis KOD1],2Z2Y_C Chain C, Tk-subtilisin [Thermococcus kodakarensis KOD1]
2Z2X_A	2.81e-07	138	262	5	136	Crystal structure of mature form of Tk-subtilisin [Thermococcus kodakarensis KOD1]
2Z30_A	2.84e-07	138	262	7	138	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	1.39e-16	68	243	116	320	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
sp|Q5VJ77|SUB1_TRIVC	1.81e-06	102	228	82	215	Subtilisin-like protease 1 (Fragment) OS=Trichophyton verrucosum OX=63417 GN=SUB1 PE=3 SV=1
sp|Q64K30|SUB1_ARTBE	1.81e-06	102	228	82	215	Subtilisin-like protease 1 (Fragment) OS=Arthroderma benhamiae OX=63400 GN=SUB1 PE=3 SV=1
sp|P58502|TKSU_THEKO	1.89e-06	138	262	109	240	Tk-subtilisin OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1675 PE=1 SV=1
sp|D4DIW9|SUB1_TRIVH	2.13e-06	102	228	82	215	Subtilisin-like protease 1 OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=SUB1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.279492	0.720488	CS pos: 16-17. Pr: 0.6215

TMHMM  Annotations     

There is no transmembrane helices in SDRG_13040-t26_1-p1.