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Database: UniProt
Entry: A0A428UKV6_9HYPO
LinkDB: A0A428UKV6_9HYPO
Original site: A0A428UKV6_9HYPO 
ID   A0A428UKV6_9HYPO        Unreviewed;       824 AA.
AC   A0A428UKV6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=CEP52_001116 {ECO:0000313|EMBL:RSM14916.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM14916.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM14916.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM14916.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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         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}.
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:RSM14916.1}.
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DR   EMBL; NKCK01000005; RSM14916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428UKV6; -.
DR   STRING; 1325735.A0A428UKV6; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000287144; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; 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   Pfam; PF07691; PA14; 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.
DR   PROSITE; PS51820; PA14; 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:UP000287144}.
FT   DOMAIN          398..540
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   824 AA;  91152 MW;  ADD99107816FEC40 CRC64;
     MSASAPLDVE TLINQLTLDE KVELLAGQGS FRMTGLPDHG IPALITSDGP HGIRGRRSFT
     RLPSPMLPSA TAMGATFNAE LLHKVGRLLG DEAKARGVDV LLAPTICLQR SPLIGRGFEA
     FGEDPFLSGI LGSRYINGVQ ERGVATSVKH YAAHDQSDNS IEDNVCMTQR TLREVHMLPF
     QLALRDSNPW TIMTAYNKIN GIHVSEDPLL LKQILRDEWG FKGLVMSDWF GTYSTSEAIN
     AGLDLEMPGP TDWRGKRLSI AVNCRKVSQA TVDESVRNVL NLINKVRGGE SLNDSPPSNT
     PEQRALIRQL VAEGIVLLKD EKRQLPIKNP DKVKFGLIGD HVKNPALCGG GSAEVEPYYS
     VTPYDAIVEV VGAENVSYAA GCHSFRFSPL LKGLTTSSGA EGWDVEIFGE NPDDHPEAPA
     VVSVVAEKQL IDVPESLHKS IPTKYFVRAR ARYTAETSGI FRFGFSTSGK GKLKVDGQEV
     IDLWTSQPPK TDSTACFNRL SMERFHDIEV IKGQVFELEA LQVNEKSCWW HEDQSIKDAA
     ELASKVDIPI MITGLSSDYE YEGSDRKNLR LPGRVDELIQ AVLSANKNAI IVTQSGCPIE
     MPWESQASTL LHAWFGGQET GHGLADVLFG KVNPSGRLSL TFPKSIKHTP AYLTFSKADY
     DIVYGEGVFI GHRYYEMVDR EPLFYFGHGL SYSKFDYSKL EVPHDFASAV DHKMQISVDV
     TNKGPYPGSE VVQVYIHDPE SSVQRPVREL KAFAKVHLDV DETKTVTLTL DKYSLSFWSQ
     EVSKWKAEAG EYMVIVAASS NPKDEIMRAS FFLSETFLLE WTVN
//
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