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Database: UniProt
Entry: W9IG49_FUSOX
LinkDB: W9IG49_FUSOX
Original site: W9IG49_FUSOX 
ID   W9IG49_FUSOX            Unreviewed;       851 AA.
AC   W9IG49;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FOYG_05870 {ECO:0000313|EMBL:EWY92290.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY92290.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY92290.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) 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}.
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DR   EMBL; JH717842; EWY92290.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9IG49; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000030753; 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   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   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:UP000030753}.
FT   DOMAIN          398..560
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   851 AA;  92736 MW;  207BC352A9087F6B CRC64;
     MRYARMDVEA LIQQLTLEEK VQLTAGVGWW HTAAIERLSI PPIRLSDGPN GVRGTHFFDS
     TPSSCLPCGT ALGATWNTDL IHRLGRLLSD EAHAKGAHVL LGPTVNIQRG PLGGRGFESF
     SEDPVLSGIL AGHYVRGVQS NGVSATMKHF ACNDMESARM AVDVQITERA LREVYLLSFM
     IAVEMASPRV FMTAYNKVNG THAPDNHHLL QDILRDEWKW DGLVVSDWFG TYSTTEAINA
     GQDLEMPGPT RWRGETLVHA VTSNKVKRST LDERVRNILK LVKHSIENTS IPPNAPETQL
     QSEENSRLLR EAAAESVVLL KNDKGVLPLD PAKPVAVIGP NADISTYCGG GSASLRAYHT
     VSPLEGIRGT AKDVSFTKGL YGHRSLPQIG KLLKTVGEQR QGFTLRIYND PPPSSGADTR
     KVLETRILDD SNIWFVDYEH PALEQIWYAD IEGVLTPEKT GEWDFGLCVH GTGELFIDGE
     LVVSNVVDQK PGSSFLGCGT VEKTGSRMLE GGKSYNVVVR WGCDKTSDLK VSGVVDFGQG
     GMRLGGCPRL EPRQALQDAA ELAKSVDQVV LCVGTSGEWE SEGQDRANMS LPPGSDDLIS
     AVLQANPNTV VLIQSGTPVS MPWVDQASTI AQAWFGGNEA GNGIADVLFG AMNPSGKLPI
     TMPRRVSDNP SALSFRSEGG RVLYSEDVHV GYRWYDTLDI EPLFPFGHGL SYTTFTLSDL
     RVEEHGESES KKLIVSVNVT NTGSRAGAAV VQVYVKPPHP TPLTASALDT ITRSIKELKG
     FAKINLVPGA NGRAKVELDV LRATSYWSER EDYWCSDAGD YTVLVGMSSR CEFLDKTFTV
     QNATTWRGLR T
//
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