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Database: UniProt
Entry: A0A0D0CCB6_9AGAR
LinkDB: A0A0D0CCB6_9AGAR
Original site: A0A0D0CCB6_9AGAR 
ID   A0A0D0CCB6_9AGAR        Unreviewed;       741 AA.
AC   A0A0D0CCB6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=GYMLUDRAFT_251201 {ECO:0000313|EMBL:KIK52498.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK52498.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK52498.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK52498.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KN834842; KIK52498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CCB6; -.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000053593; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF14; BETA-GLUCOSIDASE D-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:KIK52498.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..741
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002207836"
FT   TRANSMEM        709..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          647..717
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          19..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  79853 MW;  0FFCCFB3421C96C5 CRC64;
     MLQTAFLILL VLGATAAPSD STDQTLDSPS FFPPSAPSLR STPSYNETAI LSSGYLDLGE
     WQDAYNQASA FVSTLTNEEK VLLITRQDIP DKFTALNILD STVAPNTYYF VSTFPGSEAL
     AMTWDKDLIY NVGHAIGSEH YNLGLNALNG PVTTPMGRSP WGGRNDKSLG PDAYLNGAGF
     GRMVAGISSS GSITIGQHII LYEQETNRTG GVTTFVPNTP LTGSYKVVVD DKAFHETYLR
     PWYDGVKNGL GGAMCAMNAF NGTRSCENAE LMNNYLKTEI GFLASYSEMS SYNAAISGMD
     YSATTYWSND TILAGINNGS ISQARLDDMA VRGIMAWYKH GQNSGTPTYV SFTAYSNVRA
     NHSAIIRDAA AKSIVLLKNN GVLPLGDDTS TMVLFGAHAG SALGGPNFQF SVLGSNDTYQ
     GHLAAAGGSG TGSMSYIITP HHVLTNVAEK NGIMLFWIMN NTWTSEEING GVGSFAFYTS
     STVAPITYAS YAGQAEVSIV FINAWSGEGA DRSELRNDEQ DELVATVAAN CNNTIVVVNT
     VGPRILDAWI DHENVTAVLY AGMLGQQSGN SIVDVLYGRN ISPRYEFGYG LSYTTFAYGE
     FSVQKQSDLA PGFFTGAHAV GGRADLWDEA ATVTFTITNT GTVAGTEIAQ LYMTYPSVAE
     QPIRQLRGFE KVAIEPGESE TVTLRLLKRD FAFWNVTVTV ARSFLRYKLL IIVFKSCVFS
     IQGISVTLAW SKIAMTFMIV G
//
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