UniProt: M7SSZ3

Database: UniProt
Entry: M7SSZ3_EUTLA

LinkDB:  M7SSZ3_EUTLA 
Original site:  M7SSZ3_EUTLA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   M7SSZ3_EUTLA            Unreviewed;       822 AA.
AC   M7SSZ3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=UCREL1_5621 {ECO:0000313|EMBL:EMR67387.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR67387.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
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; KB706451; EMR67387.1; -; Genomic_DNA.
DR   RefSeq; XP_007793528.1; XM_007795337.1.
DR   AlphaFoldDB; M7SSZ3; -.
DR   STRING; 1287681.M7SSZ3; -.
DR   KEGG; ela:UCREL1_5621; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; TMMTPYY; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000012174; 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:UP000012174}.
FT   DOMAIN          400..561
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   822 AA;  90003 MW;  EFF70A69AA29925C CRC64;
     MAQKRLTPDF DVDDVLGKLT LTEKVALLSG RDTWHTNSVP WLGIPSLRVS DGPNGVRGIK
     FFNGTPAAYL PCGTALGATW DPDLIERGGA LQAEEAILKG VSVILGPTVN IQRSPLGGRG
     FEAFSEDPFL LESLAAASIK GMQSKGVATC LKHFVCNDQE DQRMSTNSIV TERALREIYL
     KPFQTVQQIC PPWTYMSSYN RVNGIHVSED RRLLQDVLRD EWGYDGLIMS DWFATYSSSE
     AILSGLDLKL PGPSYSRGDT IRHAMAAGKL KEYHLDGRAK EMLKLVKKVL PLGLEEDAEE
     KGNDNPETSK LLRTLARESI VLLKNESSVL PLDPRKSTAV IGPNAAHAAF CGSGSTMMTP
     YYAVSPLERL KAQFKGVNYA LGCAGWKKLP PLSRLTKTRD GRPGIDMTVY LEPSTVDGRR
     VVDEMYVADS AMDFCDYIPD DVKDGGAFYA DFTGTLRPEV SADYEFSCNV LGTVRIYVDS
     KLLIDNATSQ TRGDSFFGQG TRDEVAKVFL EKGRKYEIRA DFGSLATSPL DVPLASAFGG
     GGLRLGCSRV FDSQDEIKGA VDLAKQCEQV VLCVGLNGEW ELEGVDRQSM NLPGLTEQLI
     RDVVAANPRT AIVVQSGTPV TMPWIDAVPA VLQAWYGGNE TGNAIADVVA GVTSWSAKLP
     LTFPIRLEDN PTFLNFGSQG DRKTKREVIF PFGHGLNYTT FELTNLKLTE RAESILISVE
     VANTGKIDGS QVVQVYVAPE SPPVPRPVKE LRGFKKVQVP AGQRETATME LAIKTATSYW
     DEIRNMWISA KGEYTILVGD SSANTPLSGK FRVQKDTWWK GL
//

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