ID   W6ZK70_COCMI            Unreviewed;       788 AA.
AC   W6ZK70;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=COCMIDRAFT_81780 {ECO:0000313|EMBL:EUC50403.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC50403.1};
RN   [1] {ECO:0000313|EMBL:EUC50403.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC50403.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; KI963923; EUC50403.1; -; Genomic_DNA.
DR   RefSeq; XP_007683060.1; XM_007684870.1.
DR   AlphaFoldDB; W6ZK70; -.
DR   STRING; 930090.W6ZK70; -.
DR   GeneID; 19125934; -.
DR   KEGG; bor:COCMIDRAFT_81780; -.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   HOGENOM; CLU_004542_5_1_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000054032; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EUC50403.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..788
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004890091"
FT   DOMAIN          707..776
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   788 AA;  85668 MW;  741917FBB5703969 CRC64;
     MRSPLYSAAS LLIGYILYLP SSANGLARRN DTAQAVYKDA AAPLEDRVSD LLSRMTIEEK
     TAQLIQGDIS NWINTTTNAI NQTGLEWNFR VRAGQFYVGY PMPAEWISNG IKIGQEYLKQ
     NTTLGIPALV QTEAIHGLLV GNATIYNSPI GQACSFDPEL IHDMAVAIAK ESLALGINQL
     FAPLADLARE LRFGRVEETY GEDPFLAGEM AYEYVKGVQS LNVSATVKHF AGFSAPEQGL
     NTGPVHGGER ELRTTWLPPF HRAIIDADAW NIMGAYHSYD GIPSVADGHL QETILRDEWG
     YKYWLTSDAG ATDRLCCAFK LCQCKTKDKP IDSEAVTLMA LPNGNDVEMG GGSYNYANIP
     RLVEEGKLDI EVVNRAVSRQ LRAKFRQGLF EHPYQGLPLD EIDSAIHTDE HVALARKLEA
     DSIVLLENKN NVLPLSKSAN VAVIGPMANI TNLGDYVVYR SQYNPTNVTP LQGIQKASNG
     TITFAQGCER WSNDQSGFSD AVAAAKAADV AVVVVGTWSR DQQELWQGLN ATTGEHVDVA
     SLNLVGAMGP LVQAIIETGK PTIVVYSSGK PVTEPWISDN AAGLLQMFYP GEQGGNGLAD
     VLFGDVTPSG KLSVSFPYDV GTLPIYYDYL NSGRATDSGA ILPNGTLKFG HQYVLNNPQP
     LYEFGYGLSY ANFTYSDVKL SKTEVSPSDT VTVTVSVTNS SPVDGKEVVQ VYVQDVFASV
     VVPNKELKGF KKVLVKAGET VDVSIDLEVS KWGVWDRRMK YVVEKGDFIV HVGSSSLDLR
     GNGTVTVV
//