ID W2WH75_PHYPR Unreviewed; 811 AA.
AC W2WH75;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=F441_14294 {ECO:0000313|EMBL:ETP09940.1};
OS Phytophthora parasitica CJ01A1.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP09940.1, ECO:0000313|Proteomes:UP000018958};
RN [1] {ECO:0000313|EMBL:ETP09940.1, ECO:0000313|Proteomes:UP000018958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP09940.1,
RC ECO:0000313|Proteomes:UP000018958};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ01A1.";
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP09940.1}.
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DR EMBL; ANIX01002815; ETP09940.1; -; Genomic_DNA.
DR AlphaFoldDB; W2WH75; -.
DR EnsemblProtists; ETP09940; ETP09940; F441_14294.
DR Proteomes; UP000018958; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..811
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004827303"
FT DOMAIN 668..742
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 792..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 88923 MW; 0DB5E8618CC7B097 CRC64;
MWTSWITAAS LAATATLAVA NDDAYETKAQ AIVDGFSTAQ VIGQMTQVDI STVMNKDNTL
NEDYVRAYAQ QYVGSYLNTI WDEPLGEKYG WNATEWRAVV SRIQEITMEE NGGHPIIYGL
DSVHGANYVT GAVIFGQQIN SGASFNPDLV HKAGQITARD TQAAGIPWVF GPILEISQNP
LWSRTYETFS EDPYLVTVLG EALVRGLQSY NQTGACMKHF IGYSKTPTGH DRDNVIMDDF
DLLNYFLPPF KAAIEAGALS TMENYISING EPVIANPRIL NDLLRSDLGF DGLLVSDWAE
INNLKDWHRV AETYEDAVRL SLTHTSLDMS MVPNDTSFIN YTENMLVGYP QYETRLRESA
KRIVKMKLKL GLYENPVPGE EFEFLVGNDE DKAVALDLAR ESIVLLKNNE SVLPLAKDAS
VFLTGHSADN VGYQCGGWSI AWQGYSGNEM FLNGISVRQG FEDLVGNNSF TYFNGLYENG
TYSEADLAKA VELAGQHEYT IAVIGEKQYT EKPGDIDDLA LPPGQIEYVE ALAATGTKVI
IVLFEGRPRL LGSLPDTASA IIDGLLPCEL GGKAMAEIIY GDVNPSGRLP ISYPKDPANV
AIPYYHRVNT QCAYDHCWMQ WDFGAGLSYT EFNYSAVSLD STTITNADAF TVTATVTVTN
VGTRAGKETV MLFLTQPYRT ISVPEVKMLK KFKKIELQPG ESQDVSFTLT ADDWSVYDPQ
IGNGFKKVTE DSNYVVAIKP DTWCNVYKNI TNPLCAVFKI DTGRDNFGLP PPVANVTGTD
APVLQGTVAI PGTTEPPADE AGAGTVEAGN Y
//