UniProt: A0A395S2W4

Database: UniProt
Entry: A0A395S2W4_FUSSP

LinkDB:  A0A395S2W4_FUSSP 
Original site:  A0A395S2W4_FUSSP

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   A0A395S2W4_FUSSP        Unreviewed;       808 AA.
AC   A0A395S2W4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FSPOR_6441 {ECO:0000313|EMBL:RGP66701.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP66701.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP66701.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP66701.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP66701.1}.
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DR   EMBL; PXOF01000090; RGP66701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395S2W4; -.
DR   STRING; 5514.A0A395S2W4; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000266152; 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:UP000266152}.
FT   DOMAIN          386..537
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   808 AA;  88623 MW;  22C34674DCCB93DC CRC64;
     MDIQAILKSL TLEEKVSLLS GTPDDFTSIA GIPGKNIPPL QTADSINGIR PTEFDSSLTT
     ACFPNTACIA STWNTDLLKE LGLDLTRQAK LKNAQFILGP TINIQRDPRA GRNFECFSED
     PLLSGYMAAA IVNGIQNQGF LACAKHFVCN DSETQRRYYN VDESPHGRTL REIYLAAWSF
     LLQRSNPAGV MTAKDLIHDV LREEWNYKGL VMSDWFGTRS TVESMMAGVD VEMPVPIFRG
     QKLIAAINSG DVSEDVIDAS VSRLLDLRNR TREAQGEGSV KSEIIPATND VALRLAHEGI
     VLLKNENKAL PLQGLDDLKV AVVGEYAKKA VFTGGGSASC NPQYRQVPLD LLRQEFPSTE
     SVSYASGVRM RRIIPVVPSD IITTDQGQKG VEVSYFNAGC NQPFLTETLE EATINLMTRT
     KPGLELAGSH VRMTGNLVPK TTGTHILALR HSGSFIVEVD GVTLFTGDAP DITTEQFLFN
     LRKLESRIEF PMEAGKSYRI SVNMSSREPV VGEPTPYGLT LAFEEEYSEK QAIQEAVDVA
     KASDVTIIYA GRSEQYESEG FDLEEITLPT NQVDMIREVA AASKKTVVLL HCGNPIDINS
     FVSDVDAILN MHFPGQEGPQ AMVDILTGKV NPSGRLTATW FKTLQDWPSF GNFPAEKDGN
     GSFVIKYAEG LAIGYRAPVP ASRIQFPFGH GLSYTSFSYD NLRANLETSS VASTIKVSVC
     VTNSGSVFGK EVVQLYISPP EHTADWRPSR ELKEFTKVGL SPGETKTISI DLDVTTFNSH
     WSESSRAWVV DGGEYSIEVG NRRTTFVI
//

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