CAZyme Information: SPRG_22269-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_22269-t26_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
342	KK583264|CGC1	36982.44	5.0614

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=KK583264:137498-139858(-)

Full Sequence      

MKAFLILSTMAAAASAKVASSVLRALEVDGNADVFVRFADASSALEAATIESNKPLERQE
VFEILSDATATGQKSIEAATAGFEVTPTWIVSGAFIKAADKALIEKLTLNRVIKSVEQVP
DMELDPVLSKSTTDDITAPAASPNQWGIDTVGAPAIWKYTNGSGIVIGSIDTGARHTHLL
LKDSWRADRGSSDPYNRTAVPEDLRPLGTHTIGTMEKSYVKLITKTNKVISEFYSGVYAD
WVSDSVNELFVYDSAAKTLQAASNGQCLDAYRDGDKFGLHTYACDATNGNQKWIIDAANH
KIKHATHNNLCLDVDPTNPSNAAQVWECHNANTNQWIDAVKY

Enzyme Prediction     

No EC number prediction in SPRG_22269-t26_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395527	Ricin_B_lectin	7.66e-17	247	336	37	126	Ricin-type beta-trefoil lectin domain.
238092	RICIN	3.86e-15	239	337	27	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.
173807	Peptidases_S8_BacillopeptidaseF-like	1.30e-12	162	215	1	62	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	3.38e-12	258	336	4	82	Ricin-type beta-trefoil lectin domain.
214672	RICIN	5.39e-12	239	337	22	116	Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56170.1|CBM13	1.17e-104	1	342	1	745
AIG56438.1|CBM13	1.63e-101	1	342	1	748
AIG56171.1|CBM13	1.12e-68	217	342	626	751
AIG56439.1|CBM13	2.13e-67	217	342	623	748
AIG56036.1|CBM13|GH17	1.39e-44	213	342	562	691

PDB Hits     

SPRG_22269-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

SPRG_22269-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.018905	0.981079	CS pos: 16-17. Pr: 0.8190

TMHMM  Annotations     

There is no transmembrane helices in SPRG_22269-t26_1-p1.