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Database: UniProt
Entry: A0A074S7V1_9AGAM
LinkDB: A0A074S7V1_9AGAM
Original site: A0A074S7V1_9AGAM 
ID   A0A074S7V1_9AGAM        Unreviewed;       845 AA.
AC   A0A074S7V1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN   ORFNames=V565_037230 {ECO:0000313|EMBL:KEP52998.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP52998.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP52998.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP52998.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA   Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA   Zafar N., Nierman W.;
RL   Submitted (DEC-2013) 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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|RuleBase:RU361161}.
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:KEP52998.1}.
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DR   EMBL; AZST01000078; KEP52998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074S7V1; -.
DR   STRING; 1423351.A0A074S7V1; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000027456; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF26; BETA-GLUCOSIDASE; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 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.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
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|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027456}.
FT   DOMAIN          406..564
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   845 AA;  92620 MW;  8930AD17DD6E4525 CRC64;
     MTATNPFLHV NVEELVSKLS QEEKVLLLGA PNWWNTSKIE RLGVPSVRMS DGPNGVRGSS
     HFLSSPAQCI PCATALGSTF DPELIHEVGS FLAVEAKTKS ATVLLAPTCN IQRSPLGGRS
     FESFSEDPHL SGHLAAAYVA GLQDNGVAAT IKHFVANDQE HERMAVDTIL SERALREIYL
     MPFMIAQRDS GPWAYMTAYN QVHGVHVSEC KRILGDILRK EWGFNGLVMS DWYGTYSVDI
     ALNAGLDLEM PGPPRWRQPA LVNHAMTCRK LLPSTLNLRA KTVLDFVQKL AQTSPDVVFG
     DGEERTRDDP KDREFNRKLA GRAIVLLKNE QEVLPLKKKK LLVVGPNVQA RVISGGGSAF
     LKPSYVITPW DGIIAAKPEG VDVKFEVGCY AHKFLPTLEN LLTTSDGQPG WEACFYTHDE
     NQQPKDEVAK FNLNDTRVKL NDFLPEGLTP SWTIKLKGTL KVDKTAPFEF GLTVAGRAKL
     WVNGKMTIDN WTHQRPGEFF YGQGSAEEKA VVDLKAGEAV DIYVEYDNLA PAPKGVQMQP
     ALMRGVRLGG AEKIDPDEAL KAATKAAAEA DAVIAVVGLN HEWESEGFDR PNLSLPGRQD
     ELIEAVAKAN KNTVVVIQAG SAVSMPWVDD VAGVLQSWYL GNEAGNAIGD ILFGKLNPSG
     RLPITLPKRE EDIPAHLSFG SEMGKVYYRE DVFVGYKYYQ ARKVAPLFPF GFGLSYTTFE
     LSDLKVEGPS SHDSSLEVKA SVNVKNTGSV KGSETIQLYV TQPAGPITHP KLQLRAFGKA
     ADLEPGASTT VKLSFGKYGV SFWHEEDETW RADAGKYEVL VGTSSVDLPL SSSFELKQTF
     SWRGL
//
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