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Database: UniProt
Entry: A0A420Y5K3_9PEZI
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ID   A0A420Y5K3_9PEZI        Unreviewed;       815 AA.
AC   A0A420Y5K3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   22-FEB-2023, entry version 10.
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=DL546_004149 {ECO:0000313|EMBL:RKU43020.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU43020.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU43020.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU43020.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) 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|ARBA:ARBA00004987, 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:RKU43020.1}.
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DR   EMBL; QVQW01000048; RKU43020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420Y5K3; -.
DR   STRING; 177199.A0A420Y5K3; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000275385; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF5; BETA-GLUCOSIDASE M-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   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          733..802
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   815 AA;  88693 MW;  0D3DE914D1D5F3B3 CRC64;
     MVGNMMLTPT LQTASYLRLF SLVLILLTFS FLVSIVQYDQ YCTTTSQPGV VQSLLCYTRC
     STTIDATSAA PSPSEPDYNG LSPSVYPSPA ANGTSTKAWA AAYVKAKHLL AQMTTAEKVN
     ITHGWPGSCV GNTGAVSRLG VPPLCFADGP AGIRGQEFVS AFPAGIHLGA TWDKELMHKY
     GRALGAEYHG RGVNVALGPV AGPLGRIARG GRNWEGFSND PYLSGVGMGA VTRGIQDAGV
     IATPKHWILN EQELRRRETD LGEAISSNVD ERALHELYVF PFMNALREGA GSIMCSYQRA
     NHSYGCQNSK LLNGILKTEL GFEGFVVSDW DGQKSGVASA NAGLDVTMPS AGFWGDKLLE
     AVNNGTVDED RLDDMATRLL AAWFLLHQEK GYPPPAIYSH TQQHPPVDVQ ADHAQLIREI
     GAAGTVLVKN VNRTLPLKTP RFLCIYGYDA VVKASPWENP DRFNGGYEVN FGWNTLNGTL
     ISGGGSGSTT PPYVVSPFQA IQERVARDKG ILRWDFLSDK PSPAYANTEA CLVFINAYAS
     ESFDRTTLAD EFSDRLVSNV ADQCSNTVVI IHSAGIRTVS SWIDHPNVTA VVFAGLPGQE
     SGNSLVDVLY GDVNPSGRLP YTVAKKESDY GRLLNSTVSF DKYPEDNFDE GLYVDYRAFD
     RDGIEPQFEF GFGLSYTTFD YSNLSISLKG ETTTSEWPDP EIEVVQGGHP SLWDTVATVT
     CTIANAGEVD GAEVAQLYVG IPGDDTPARQ LRGFERLGPL APGESRQAVF ELTRRDLSIW
     DVVSQQWRLR RGEYGIWVGT SSRDLRLKDT VKIEE
//
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