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
//