ID A0A0W0FFP1_9AGAR Unreviewed; 623 AA.
AC A0A0W0FFP1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=WG66_12259 {ECO:0000313|EMBL:KTB35161.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB35161.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB35161.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB35161.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KTB35161.1}.
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DR EMBL; LATX01002012; KTB35161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FFP1; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
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; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF26; BETA-GLUCOSIDASE; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KTB35161.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 182..343
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 623 AA; 68199 MW; 0B72E7B8FE456201 CRC64;
MSDWHGTYST DLAINAGMEL EMPGPPRWRT ENLIKHCLTS QKIFMETINE RIYNLLTFIQ
RQARLNPEVV YGDGEERTRP DSPGTRKFCR KLAADGIVLL KNQGEVLPIS PKKYKKIAVI
GPNAKDRVIS GGGSAFLKAS YVITPFDGIK EGAANDLEID YTVGCYAHKY LPTLEHCLVT
GHNEPGWLCT FYNHNADGSL TEPIASYVLQ DTRVKLNDFL PEGLTPTWSI KLTGKLTVEQ
SMSFELGLTV AGRAKLWIDG KMTIDNWTKQ TPGDFFYGQG TIEEKATIDL KGGESVDVLV
EYTNTAPSSG ENGGNSAQPA LMRGVRLGGC EKINPEAAIK AAETLASQSD LVVFVGGLTS
EWESEGFDRP TLDLPGRQNE VITRVAAANP RTVVVTQAGS ATSMPWVDSV AGIIQAWYLG
NETGNAIADI LYGIVNPSGR LPLTLPKRLE DIAAYPNLRS EHGKIHYHED IFMGYKHFQA
KGVQPLFHFG HGLSYTRFSL SGLTIKNASK GDSVATEVSV TVKNEGSVSG SEVVQVYISY
PDNGITHPRL QLRGFAKARN VAPGSSSKVT IPLDKYAVSY WDNNKHCWLV VAGEYGVHVG
FSCDDIVLEE KLKISEAFAW TGL
//
