ID W2GAU0_PHYPR Unreviewed; 720 AA.
AC W2GAU0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE Flags: Fragment;
GN ORFNames=L915_14785 {ECO:0000313|EMBL:ETK79370.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK79370.1};
RN [1] {ECO:0000313|EMBL:ETK79370.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK79370.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
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DR EMBL; KI687997; ETK79370.1; -; Genomic_DNA.
DR AlphaFoldDB; W2GAU0; -.
DR EnsemblProtists; ETK79370; ETK79370; L915_14785.
DR VEuPathDB; FungiDB:PPTG_15963; -.
DR Proteomes; UP000053236; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 643..717
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 720
FT /evidence="ECO:0000313|EMBL:ETK79370.1"
SQ SEQUENCE 720 AA; 78606 MW; E696F40E48A68CB5 CRC64;
MGCPGGRYHD KLHQRRPRGS DDSNCLINAT YQLNEDAVLE YAKAHVGSYF ETPMTIRGEI
NGSWGWTTTQ MREFVGGIQR IAMEENGGHP MIYGTDAVHG NALLLDTVFF GQQINGAASF
NTELVYEQGR ITARDTLAAG IPWVFGPVLD IAHNPLWPRT YETFGEDPHL AAVMGDATIR
GMQSNNQTAA CMKHWIGYSW NPTGHDKDGV TISDFDLLNT FGPSFKAGID AGVLTGMQNY
ISVNGVPTVE STRLLKTLLR NDFEFDGMMV TDYGEIDALE DFHRVARTTA EATKFTLERT
SIDMSMVGVG TTFTNGTYAL IGEELTILDR LKDSVRRIIK LKLQLGLYDN PLPGEENLAL
VGNDNDVAAA LNLARESAVL LQNDDNVLPI KKDALVFLTG HSADNVGYQC GGWTIQVQGV
SGNDMFSHGS SVKQGIEEIV GNDSFSYFNG LNVNGSYSDN DLNTAKKLAS EAEYTVVVIG
EEPYEEKTGD IDDLTLPVGQ IQYVKELASI GTKVIVVLFE GRPRLLGDLP EHVYAVINGF
LPCELGGKAI AEIIYGDVNP SGRLPITYPK HSGNVMIPYR HRVSTQCATG DYCVPQWTFG
HGLSYTNFTY SDMSISTTNV TSSSDSVNVS VTVTNSGSVA GKETVMLFLT QPYRSISVPE
VKQLKKFSKI SLDAGASQTV TFELTAADWS VYYPQIGQGL KLVAEDADYV VAIKPETDCD
//