ID   R1H3B2_BOTPV            Unreviewed;       933 AA.
AC   R1H3B2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN   ORFNames=UCRNP2_282 {ECO:0000313|EMBL:EOD52909.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD52909.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; KB915675; EOD52909.1; -; Genomic_DNA.
DR   RefSeq; XP_007579610.1; XM_007579548.1.
DR   AlphaFoldDB; R1H3B2; -.
DR   STRING; 1287680.R1H3B2; -.
DR   KEGG; npa:UCRNP2_282; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; DMTMAGD; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
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; IPR019800; Glyco_hydro_3_AS.
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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-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; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          854..922
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   933 AA;  100513 MW;  BEAEE37E6A575742 CRC64;
     MERFEIEEPP PPYERPPSYS AARLDHMRQT LRRVLAFALL ALVVIATIVF FVVLEQPESC
     TPHNSNALNG CKNVTIDLNA QALNDSSPDD ALWGATSPPF YPSPWMDGTG GWAEAYAKAQ
     EFVKQMTLLE KVNLTTGTGW EGGPCVGNVG PVPRLGLHSL CMQDSPTGIR FTDYNSAFTS
     GGTVAASFDR RIWYQRGYDM GAEFNGKGID VLLGPVVGPL GRTPTGGRNW EGFSPDPALS
     GIAVAETIKG IQDAGVIACT KHYIVNEQEH FRQAPEAQGF GVNITESISS NLDDITLHEL
     YLWPFADAVR AGTGAIMCSY NQINNSYGCQ NSHLLNYILK GELGFQGFIM SDWQAQHSGV
     GSSLAGMDMA MPGDTLFSTG DAFWGANMTL AVVNGTIPDW RLDDSATRIM AAYFFANRDK
     NVVPTNFNSW TLDTFGYANA IADANFGQVN HHVNVRANHA KNIREAAAKS TVLLKNVNGT
     LPLTGKEKLI GVFGSDAGDA QSGPNGCDNR GCTNGTLAMG WGSGTANFPY LISPLTAIQN
     EVYANNGNID WVTDDYNYDR AFALAAQVSH ALVFVNSDSG EGFINYDGNI GDRNNLTVWH
     DGEALIANVT SVNNNTIVVI HSVGPVELGA FNDNPNVTAI IWAGLPGEQS GNALADVLYG
     RVNPGAKLPF TFGAKREDYG TELLYEPNNG EGAPQDNSNE GVFIDYRSFD KNNVTPTYEF
     GFGLSYTTFS YSDLQVVKHT VADYTPNTGN TTAAPVLGNF STDLADYQFP EGFQPIPGYI
     YPYLNSTDAA TANNDPVAEY GQPNESYIPD GALDGSPQSK IPAGGAPGGN PALYDVLFTV
     TALVTNTGDV VGDEVPQLYV SLGGPNDPVN QLRGFERYTI EPGASARFGV DVTRRDLSNW
     DPVSQNWVIS DYAKTVRVGS SSRNLPLEVE LDI
//