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Database: UniProt
Entry: A0A0F8V470_9EURO
LinkDB: A0A0F8V470_9EURO
Original site: A0A0F8V470_9EURO 
ID   A0A0F8V470_9EURO        Unreviewed;       838 AA.
AC   A0A0F8V470;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=ARAM_002962 {ECO:0000313|EMBL:KKK26559.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26559.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK26559.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26559.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-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         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:KKK26559.1}.
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DR   EMBL; JZBS01000353; KKK26559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8V470; -.
DR   STRING; 308745.A0A0F8V470; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF10; 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   SMART; SM00758; PA14; 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   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000034291}.
FT   DOMAIN          395..555
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   838 AA;  91813 MW;  9683C14F82E602B8 CRC64;
     MPKLDVEKTI EELTIGEKIA LTSGIDFWHT ASVPRLNVPS LRMSDGPNGV RGTRFFNGVP
     AACFPCATAL GATWDAELLY SVGQLMGEEA IAKGAHVILG PTINTQRSPL GGRGFESFAE
     DGVLSGILAG NCSKGIQEKG VAACLKHFVC NDQEHERLAV DSIITDRALR EIYLMPFHLA
     MRICKTACVM TAYNKVNGTH VSENKKIITD ILRKEWGWDG LVMSDWFGVY STSEAINAGL
     DIEMPGKTRW RGDALAHAIS SNKVPEFVMD ERARNILNLI NYVEPLGIPE GAEEKVLNRP
     EDKALLRRAA AESIVLMKNE DNILPLSKEK SIVVIGPNTK IAAYCGGGSA SLDAYYTVTP
     FDGVSAKSQG EVKFSQGVYS HKDLPQLGPH MKTEDGKTGF MFRVYDEPAS SPNRELLHEL
     HLVSSLGFLM DYRHPKIKSF TYYIDMEGFF APEQDGIYDF GVTVVGTGKL LVDGELVVDN
     SKNQRPGSAF FGTGTVEERG SKELKAGQTY KVVLQFGSAP TSDLDTRGVV VFGPGGFRFG
     AARRTTQEEL ISKAVEAATN ADQVVVFAGL TSEWETEGHD RDHMDLPPGS DEMISRVLDA
     NPNSVVVIQS GTPVTMPWVS KSKVLLQAWF GGNECGNGIA DVLYGDVNPS GKLPLSFPVR
     LQDNPAYLNF RSEGGRVLYG EDIYVGYRYY EKVDLAPLFP FGYGLSYTSF SRSDLILNTT
     PEQPKIGDGE PITATVTVTN TGKVAGAETV QLWVIPPSTN VNRPVRELKG FAKVTLEPGE
     QKTVDIVVEK KLATSWWDEK REMWASEKGR YEVLITGTGE ETLKSSFTVE KTRFWIGL
//
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