ID A0A072NVY2_9EURO Unreviewed; 854 AA.
AC A0A072NVY2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=A1O9_12479 {ECO:0000313|EMBL:KEF51562.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF51562.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF51562.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF51562.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-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|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:KEF51562.1}.
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DR EMBL; AMGV01000023; KEF51562.1; -; Genomic_DNA.
DR RefSeq; XP_013254152.1; XM_013398698.1.
DR AlphaFoldDB; A0A072NVY2; -.
DR STRING; 1182545.A0A072NVY2; -.
DR GeneID; 25287373; -.
DR VEuPathDB; FungiDB:A1O9_12479; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000027920; 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:SF28; BETA-GLUCOSIDASE-RELATED; 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|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:UP000027920}.
FT DOMAIN 406..567
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 854 AA; 92725 MW; 22009F09B82CCB55 CRC64;
MGSIAPDFTT YDDFHVDQVL AKLTPDEKIS LISGSDPWHT APIPRFHVPK IRLTDGPNGV
RGTKFFNGVP AACLPCGTAL ASTWDIELVR QGGALQGREA IAKGASVILG PTTNMQRSPL
GGRGFESFSE DPVLAGHISA ATVCGIQSTG VAATIKHFVC NDQEHERQSV DCVVSERALR
EIYLMPFQIA ERLARPKCYM TAYNKVNGLH ASSSKELIQN VLREEWGFDG LVMSDWFGVY
SVVDSIKAGL DLEMPGPTYM RGQLVKHALG SGRLLAREVD ARAKEVLKLV RSLLPLGIPE
DCPEEAVDTP ETAALLRKIA SNSLVLLKNV GKILPFSDSK TIGVIGPNAA FAAYCGGGSA
ALAPYYAVTP LDGVRARYKE DKVKYELGAP GWKKLPLLSQ IARRSDFQPG FDAKVFLEAP
SSNVQRKPVD SFTVTTSDIF LADYKNDHIE GNLFYMEFDA SFTPDETAEY EFSLSVSGTA
KLYVAGQCVV DNATNQTAGD SFFGSGTVEE TGTIALQKGE KYPIHISFGT LPTRTYTVEG
ANPFGAGGLR AGGFRKIEIE TELERAATLA KSVDQVLLCV GLNGDWESEG YDRSTMDLPA
GSDDLIRAVL QANSNTAVVV QSGTPVTLLP WAKDAPAIIQ AWYGGNETGN AIADVVFGVT
NPSGKLPLSF PVRNEDNPAF LNYRSERGRT VYGEGVYIGY RFYERTKREV AFPFGHGLSY
TSFELSSLQL QIHESAEKAR NDLDAVISVS VDVANTGLLP GAQVVQVYAA AQAASVGRPV
KELKGFTKVF LQSSERRRVS IEMSLKYVTS FWDEQAHAWV QEQGRYTLHV GDSSAHTPLT
VDFEVAETVW WNGL
//
