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Database: UniProt
Entry: F8PMR0_SERL3
LinkDB: F8PMR0_SERL3
Original site: F8PMR0_SERL3 
ID   F8PMR0_SERL3            Unreviewed;       865 AA.
AC   F8PMR0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=SERLA73DRAFT_158615 {ECO:0000313|EMBL:EGO02892.1};
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; GL945476; EGO02892.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8PMR0; -.
DR   STRING; 936435.F8PMR0; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   InParanoid; F8PMR0; -.
DR   OMA; VNDTYAC; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000008063; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGO02892.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT   DOMAIN          785..854
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   865 AA;  93557 MW;  F9E64B70A63B0B3D CRC64;
     MFYDRIKAVM AGKDGLGKAA VVTLHSAFCT RGTQCSRTVE LCNAHHGHRS SELAFVKAKG
     VEHGDEHIFD RDLVVCLVVD AILCIDLNLN APFITFVASY IAPAIAPSAS FTHLVLSKHN
     SFSSDPTLIP DFAPAWAAAY SKAKQHLADY TLEEKVNITT GVGWGNGLCV GNIPANKNFP
     GLCLEDSPLA VRFADFVTAF PAGITTASTW NRALIRARGL ALGSEHKGKG VNVALGPMMN
     MGRIAQGGRN WEGFGADPFL TGEAAYETIL GMQNGGVQAC AKHFINNEQE HMRTQDSANV
     DDRTQHEIYA HPFLRSVMAG VSSVMCSYNL INDTYACNND KMINDILKRE YGFQGYVMSD
     WQATMATLSA VAGLDMTMPG DITFDSGDSY FGGNLTAFVQ NGTISQARVD DMATRIIAGW
     YYLHQESDYP EVSFNAFNTL DEATNKHVNV QSDHYKIVRE IGAAGSVLLK NERGALPLNK
     PRNLILVGSD AGPGISGPNE FSDQGGSDRF LAMGWGSGTG LFPYLITPYE AIQERARQDG
     SSIFWDFDDW NTANAQTLVT GQSAAIVFIN SDSGEDYITV DGNEGDRKNL TAWHNGDNLI
     QAVASNNNNT IVVVNSVGPL IIEPWIEHPN VTAVVWASIG GQEGGNAIAD VLYGAYNPSG
     RLPYTIAKSP ADYPAQLITG GSGSDILAIN YTEGLFIDYR HFDAANIEPR FEFGFGLSYT
     TFEYSQVDIS AISSSDHPQQ SLIQAWENGD ATPIAEGSST ALWLHEPAFK VTFHVKNTGS
     LSGTEIPQLY IHHPASAAEP PSVLKGFTNV KVSPGQTEHV SITLSRYDLS IWDVVAQGWR
     KPSGEITFSV GASSRDFKLN GTIPT
//
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