ID R7SVM7_DICSQ Unreviewed; 803 AA.
AC R7SVM7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=DICSQDRAFT_155963 {ECO:0000313|EMBL:EJF59983.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF59983.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF59983.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF59983.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
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DR EMBL; JH719419; EJF59983.1; -; Genomic_DNA.
DR RefSeq; XP_007367196.1; XM_007367134.1.
DR AlphaFoldDB; R7SVM7; -.
DR GeneID; 18837557; -.
DR KEGG; dsq:DICSQDRAFT_155963; -.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OMA; MSAYHSY; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000053319; 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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC 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 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EJF59983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..803
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004455826"
FT DOMAIN 723..792
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 803 AA; 87154 MW; E893DB783BD9C5F7 CRC64;
MRVLALALLP LFSVVAADTA RSRFDVRDDL HFPLHARATN KDGSTPVYKN SKASIEDRVN
DLLPRMTIQE KVAQIIQGDM NGWMDFNDPL DDTLTFNQTG LRAMMATKAG SIWGGYLTPW
DKFVFGVTVG QKYLMENTTL GIPAIIQSEG LHGFTNNGTI WPSPIGLAAS FNPALLQEAA
KTIADEAEGL GFSQIFAPVL DLSRELRWGR VEENFGEDPF LTGEMGHAYV TGLQSGRRRN
VSSTAIGRMA ATCKHFAAFG SPQGGLNTAQ VTGGERELRT NYLKPFNRAC VEAFSIMTAY
SSYDGIPAIA NTHLLTDILR TEWGYPYWVT ADAGSVDLLI NQHGLCDTRE CAAKIALENG
LQGEMGGGTY TYLTLPDQVQ AGTVDISYVD ETVKAMLRTK FALGLFENPY PYEDYLSTLR
TPETRELLHS MEQETIILLE NRNNTLPLSK SINSVALIGP QVDRVSFGDY VFFNASLNGI
SPLAGFTQLL SNTSVQIKYA QGCELWSNDP SGIPTAVEAA KSADAAIVMV GTWTLDQTLL
WTPGTNATTG EHVDLSDLGL VGAQMQLVQA IKDAGKPTIV VLVSGKPVAE PWIQAHADAV
VQQFYPGELG GLALAEVIFG DVNPSGKLPV SFPRSVGTTP VFYNYLKGGR FIDPGEVLDD
GTLIFGHQYV LDTPTPIWSF GHGLSYTTFN YTDLTLSKST IGTNEDFSVS VTVHNTGDRD
GKEVVQVYAT DVVSSVVTPN QELVGFQKVD LASGESKTVT INVNSSQLAL WSLRNSWVVE
SGTFAIKVGT SDQTFLNTTL TVQ
//
