ID F8PPC9_SERL3 Unreviewed; 836 AA.
AC F8PPC9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SERLA73DRAFT_159096 {ECO:0000313|EMBL:EGO02006.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL945477; EGO02006.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PPC9; -.
DR STRING; 936435.F8PPC9; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; F8PPC9; -.
DR OMA; TYYVDME; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000008063; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGO02006.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 387..556
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 836 AA; 90595 MW; 0DC00FBB1A0042F6 CRC64;
MAHILDVEET LAKLSLNGKI KLLAGNGWWH THAVPEADVP PMRMSDGPNG VRGLRFFNGV
PASCFPSSTG LGSSFDVDLA LQVGKALGDE ARAKSCHILL APTVNTQRSP LGGRGFESFS
EDPVVNGNIA AAYINGVQSK GVAATIKHYV ANDQEFQRFS ISSDMSERAL REIYLKPFQI
ALRDSDPWAL MTAANETRLQ EWGYKGMTMS DWIGVYSTSE SISAGLDLEM PGPTVMRGKA
VERALAGEKL FLSDVDNRVR KILELIQRAQ ASGVPFNGPE EGVDTPELRQ LLRTAASDAI
VLLKNEKKIL PLSSQSGLKR IAVIGPNAKQ AFTSGGGSAR LLSTYTVSPL EGITAAAKEL
GAEISYTIGA TSHKYLPEAS PFIKSSHGGK PALLEFWNES PNSTFLNTTP SFSEQLTPCA
WSTPTANTNI FLADGVDTSK VKEVCWIRYS TIFVPDEDGD WEFGLNIAGN GNLFLDGKLV
IDLSTSPEQG ENFFAMGTVD LKAVVKGLKA GEEHNLEIRL SNEEFVARGC PLPCHGGLRL
GAFCKTESEE ALKKAVQVAK DSDVAIVVVG LNHEWESEGY DRPDLELPGL MNRLVSEVLR
VNPKTVVVNQ SGTPVSMPWV NEAPTLVQAF YGGNELGNGL ADVLFGKVNP SGKLALTFPK
RLADTPSYPS YGPHGQEYGK ILYNEGIFVG YRSYEIRDLA PLFAFGYGLS YTTFEYSGVE
TSAVSEDGHF SVSFTVKNTG SVTGREAAQV YISDPQCSLP RPVKELKGFT KVTLKAGEAK
KVQVNLNRDA LSFYDERQMS WVAEAGKFDV FVAASSDDVR LSAQVELTKS FTWKGL
//