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
//