ID   K1WRD6_MARBU            Unreviewed;       875 AA.
AC   K1WRD6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   03-MAY-2023, entry version 45.
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=MBM_02147 {ECO:0000313|EMBL:EKD20195.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20195.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD20195.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20195.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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; JH921430; EKD20195.1; -; Genomic_DNA.
DR   RefSeq; XP_007290036.1; XM_007289974.1.
DR   AlphaFoldDB; K1WRD6; -.
DR   STRING; 1072389.K1WRD6; -.
DR   GeneID; 18758082; -.
DR   KEGG; mbe:MBM_02147; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   InParanoid; K1WRD6; -.
DR   OMA; YYPSPWA; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006753; 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: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   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..875
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003854909"
FT   DOMAIN          798..866
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   875 AA;  94204 MW;  B4D233B5D446F373 CRC64;
     MFFTSITGVT MLACLATNIN VASSLVSRQT SPDATTSDSR FSEPFYPSPW MNGQGEWADA
     YAKAKDFVSQ LTLLEKVNLT TGVGWQGEQC VGQVGSIPRL GFRSLCMQDS PVGVRFADYV
     SVFPSGQTVA ATFDRSLFYA RGYALGKEHK AKGVTVQLGP VAGPIGRSPA GGRNWEGFSP
     DPYLTGVAMA ETVKGTQDAG VIACAKHFIA NEQESFRQAS EAVGYGFNIT ESISSNIDDV
     TMHEVYAWPF ADAVRAGVGS IMCSYNQINN SYGCQNSKLL NDLLKNELGF QGFVMSDWQA
     QHSGAASAAA GLDMSMPGDT IFNSAETFWG TNLTLAVING TVPEWRIDDM ALRIMAAYFK
     VGLTLNEPPI NFDSWTLDTF GPLHASVGAN IQQVNWHVDV RDDHGALIRD IGARATVLLK
     NVNNALPLSK PKFIAVIGSD AGPNINGPNS CTDRACNDGT LGMAWGSGTA NFPYLVTPDT
     ALQNQALADG TRYESILDNY ATSKIEALVA QADATAIVFV NANSGEGYIS FDGNEGDRRN
     LTLWHSGDDL IKNVSAICNN TIVVIHSTGP TLVTEWYDNP NVTAILWAGV PGQESGNSIT
     DVLYGKVNPA ARTPFTWGAT RESYGTDVLY TPNNGQAAPQ DDFVEGVFID YRAFDRSNST
     PIYEFGFGLS YTTFEYSELT VTKHDASAYT PTTGMTEAAP VLGNFSTDLS DYLFPNASFP
     HIWQYIYPYL NTTDARAASA DPFYGQTAEE FLPPGAIDGS PQPLLAAGGA PGGNPQLYDV
     LYTVTAQIQN TGSCYGEEVP QLYISHGGPN QPKVVLRGFD RLSIDAGASA TFQAEITRRD
     ISNWDPVSQN WVITDAPKTV YVGSSSRRLL LSQAL
//