ID D8Q418_SCHCM Unreviewed; 806 AA.
AC D8Q418;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SCHCODRAFT_55674 {ECO:0000313|EMBL:EFI97154.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI97154.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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; GL377306; EFI97154.1; -; Genomic_DNA.
DR RefSeq; XP_003032057.1; XM_003032011.1.
DR AlphaFoldDB; D8Q418; -.
DR STRING; 578458.D8Q418; -.
DR GeneID; 9596143; -.
DR KEGG; scm:SCHCO_02627157; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02627157; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR InParanoid; D8Q418; -.
DR OMA; MSAYHSY; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000007431; 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:EFI97154.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..806
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120512"
FT DOMAIN 725..794
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 806 AA; 86832 MW; 0BCCB25094AC38C9 CRC64;
MRSAHILGFL CLGPSVALAS YSFDDEFADL GISLHSRAEN VDGSLPVYKD PTADIEARVE
DLLPRMTIKE KVSQLIQGDM NGWMNFSDPL DNTLVHNETG VAEMLDAKGG MIWVGYQTPY
DKFVYGVEIG QRYLMENTTL GIPALVQSEG LHGFTNNGTI FPSPIGLAAT FNTSLISAIA
KVIADESEPL GINHIFAPVL DLARELRWGR VEEGFGEDPF LTGELGAAFV EGLQSGRRQN
ASDTAVARVA ATCKHFAAFG SPQGGLNIAP VTGGERELRT MYLRPFKRAC LDALSFMTAY
SSYDGVPTAA DPHILIEILR EEWGYPYFVV SDAGSVDLQI TTHGTCEDRA CAARNVLVDG
RSGEMGGGTY TFFTLEDQVK NGTVAESDLD EVVRTLLRTK FALGLFENPY PYKDYTSQIR
TEETLEVLHQ ADLESIVLLE NRNDVLPLDA GSLGSIALIG PQAGRVSMGD YVFLNASDNG
ITPVDGFKQY LEGVGSQTIV NYAEGCKLWS NDESGFDEAV AAAEASDVAI VMVGTWTLDQ
TNLWTPGTNA TTGEHVDISS LALVGAQLRL AQAIHATGVP TIVVLVSGKP VAEPWIQAEP
AAVLQQFYPG ELGGLALAEI IFGEYSPSGK LPVSYPRSVG TAPAFYNYLK GARPIDAGSV
LEDGTLMFGH QYVLDSPVPL WSFGHGLSYT TFNYTDLVVP STIGTADDFE VEVTMHNTGT
RDAAETVQVY MTDVFSSVMT PNQELVGFAK VFLPAGSSRT ITIPVHNDQL AVWSARGTWV
VEPGAFTIKI GTSEEAYLST TLTVVA
//
