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Database: UniProt
Entry: A0A329S8J6_9STRA
LinkDB: A0A329S8J6_9STRA
Original site: A0A329S8J6_9STRA 
ID   A0A329S8J6_9STRA        Unreviewed;       851 AA.
AC   A0A329S8J6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=PC110_g11802 {ECO:0000313|EMBL:RAW31872.1};
OS   Phytophthora cactorum.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW31872.1, ECO:0000313|Proteomes:UP000251314};
RN   [1] {ECO:0000313|EMBL:RAW31872.1, ECO:0000313|Proteomes:UP000251314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10300 {ECO:0000313|EMBL:RAW31872.1,
RC   ECO:0000313|Proteomes:UP000251314};
RA   Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT   "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (JAN-2018) 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:RAW31872.1}.
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DR   EMBL; MJFZ01000303; RAW31872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A329S8J6; -.
DR   STRING; 29920.A0A329S8J6; -.
DR   Proteomes; UP000251314; 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   InterPro; IPR000601; PKD_dom.
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.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251314};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..851
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016385733"
FT   DOMAIN          671..710
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          795..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  92759 MW;  3166F309FAE46D3F CRC64;
     MNVDLVLGLL CWACSSASWV ALAAATAPAA HDLVYDPNTS IFAGFRRSVE PPTAYNGVDI
     DALLANMTIR QKAAQMTQMD IYSMMNGDER DPKKALKREV VARYARTGVG SILNSPFAGG
     PVGGRTGWSA SDWREVIGQI HQIYKEEGVA VPMLYGVDTI HGATYVRGAT LFGQPISAAA
     SFNPELVYKM GAVAAKDTLS AGIPWIFSPV LGIAVQPKWS RVYETFGEDP LVSSVMGAAL
     IKGLQSSGKV AACMKHFIGY SNVREGLDRA DNVITDWELV NYYAPSFLAA VRAGVRTAME
     SYVSVNGIPV IASKKLLVDL LRDDMNFTGL LVSDYSEVDR MYSEHHLVRS VADAVRVTLQ
     ETSLDMNMSP DLQAFGDTIE SLVTKGLISE SRLDESVRRI LETKRDLGLL EPDYYDEFER
     NGVDIAATVG NASDQEDALK LAQESVILLE NHNSALPIDL TKETNIFVTG PVSDNKGFQC
     GGWSVFWQGS SDSTLFPNGV TLKEAVQAKA SSSGGQIKVT HLEVVDIDGN VSPQDLQRGL
     QLAAKSEYTL VVLGEPNYAE KTGDLLESMA LPAGQLWYLE ELTKLNSTKV VVVLISGRPR
     LLDGAHNHAD AVILSMLPCE QGGQALADVI FGDVNPSARL PITYPARSTQ LLPYFHRVNT
     RCQPYNECPV QWKFGHGLSY TRFEYSTLRL NSTHVHAATG ALKVAVTVTN HGTLPGKEVV
     LLFVAQRFRR VSVPETKLLK AFKKLNELAP GASQDVEFVL TPEDWSYYEP HAVGRGFQRQ
     VEPGEFVVSL LPSSTDTSTM AAPRSLDDSS ERYNQRKNRG GPGFMMPNNS KWPSAASEYA
     SGLSVSFYVI P
//
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