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Entry: A0A3D8RB64_9HELO
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Original site: A0A3D8RB64_9HELO 
ID   A0A3D8RB64_9HELO        Unreviewed;       893 AA.
AC   A0A3D8RB64;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=BP6252_07818 {ECO:0000313|EMBL:RDW71255.1};
OS   Coleophoma cylindrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Coleophoma.
OX   NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW71255.1, ECO:0000313|Proteomes:UP000256645};
RN   [1] {ECO:0000313|EMBL:RDW71255.1, ECO:0000313|Proteomes:UP000256645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP6252 {ECO:0000313|EMBL:RDW71255.1,
RC   ECO:0000313|Proteomes:UP000256645};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose.
CC       {ECO:0000256|ARBA:ARBA00024983}.
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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDW71255.1}.
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DR   EMBL; PDLM01000008; RDW71255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8RB64; -.
DR   STRING; 1849047.A0A3D8RB64; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000256645; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
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; IPR019800; Glyco_hydro_3_AS.
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:SF25; 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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..893
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017600189"
FT   DOMAIN          795..870
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   893 AA;  94201 MW;  8405B98E0815EE8B CRC64;
     MLALLLLLLP LPLTLALVSP PNFAPDIKSF YKLEAEAKNS AGTVGKRDSV PAEYVAAPYY
     PTPPGGWITS WADSFAKAQV VVANMTLAEK VNLTSGSGEL MGPCVGNTGS ALRFGIPNLC
     LQDGALGLAA TDNITAFPAG VTTGATWNKD LFYQRGYALG QEARGKGVNI LLGPMVGPLG
     RKPRGGRGWE GFGTDPVLQA VAGSETIKGI QANGVIATIK HLVGNEQEKY RMDIIPHGLM
     KAISSNIDDR TLHELYLWPF AEGIKTGVGA VMTSYNDVNG SAASQNSMLI NGILKDELGF
     QGITMTDWLA QISGVGSALA GLDMAMPGDG DIPFLGLSYW ASDLSTAVLN GTVPVSRLND
     MVTRIVATWY QLGQDQDYPL PNFSANTAAA TGPCYPAALI SPTCVTNQYV NVQGDHAVVA
     RNVSREAITM LKNENSTLPL STAATVFVFG TDAENNPSGP NSCSQRDCDT GVLGMGWGSG
     TANYPYLDAP IDAINRKLVT NATYYNSDTF PSITTVGADD IAIVFINSDS GENQHTVEGN
     NGDRDASGLY AWHNGDALVE AAAAVFSNVV VVVHTVGPIL VENWIDLPSV QAVVFAYLPG
     QEAGDSLTDI LFGDYSPSGH LPWSIPVAES DYPASVSLQG FALGQVQDTF SEGLYIDYRY
     LNKNNISPRY PFGHGLSYTT FTRSATISSV GTLTSTPPAR AAKGSTPVYS NAIPPASEVD
     WPTGFSAVSR YLYPYLNDPE AISATGTFAY PTGYSNTSHA DPVAGGDLGG NPALWDTMFS
     ISVTVTNTGL VAGKSVAMVF VQYPSDSAYD VPIIQLRAFD KTSTLAPGGK ETLTLTITRK
     DLSVWDVVTQ NWVVPVSGSK PFLFWVGDSS GGLTLACESL SLACSGGRTA PVV
//
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