ID A0A165DIS6_9BASI Unreviewed; 880 AA.
AC A0A165DIS6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 22.
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=CALCODRAFT_458655 {ECO:0000313|EMBL:KZT52896.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT52896.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT52896.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT52896.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV424052; KZT52896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DIS6; -.
DR STRING; 1353952.A0A165DIS6; -.
DR InParanoid; A0A165DIS6; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000076842; 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:SF10; 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 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:UP000076842}.
FT DOMAIN 427..600
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 880 AA; 95218 MW; 8652EC00B5EE9D41 CRC64;
MTNSVNGTTA NVAFIRDGPK EVDVEATIAS LSIQDKVKLL AGKDFWHFAD VPAAGIGSVR
TSDGANGVRG TQFFNNVPSS CFPCATGIGS SFDLPLAYEI GRALSAECKA KNVHVLLGPT
VNTLRNPLAG RGFESFSEDP FVNGMMAAEY IRGIQSEGVA ACLKHFVCND QEHERMSSDS
VVTMRALREI YLEPFRLALK QSPPLALMTS YNRLNGTHTS ENSFLLSDIL RKEWGWDGLV
VSDWTGVVST VESMKAGLDV EMPGPGVFRG ETVLRCLSGG KLEVEDVDDR VRNVLKLHNH
AVRSGIPFNG AEGYRDTPEL RALLRKAASS SIVLLKNAPV GSSSTPLLPL RAERGRKIAV
IGPNAAFAQV SGGGSAAVFA SWSVSPLVAI REVAQEAGAT VGYAVGAQTF RYVPSAELDS
CICVPGTSTP GIRMQFWKDG RGGEWSHEEG GFFDQCGEIE EAEEYETTTK SANFLMIDGL
PFDKISQTPF IRMTMTFTPT SSGPWLFGLA SVGEVNLYLD GRLLIENNRA YTPGEILFGL
GSSELRVIAP KLEEGRQYAL ELRMHVSQEK MVPGPFTCAG GLQMGATRWA EEGVVIAEAV
SLAKESDLAI VVVGLNGDWE SEGFDRKDMD LPGSMNALCH AVLGANENTV IVNQTGTPVT
MPWLDRTPAV LQAFYGGNEL GNGLADVLFG KVNPSGKLAM TFPKRLQDCN TYESFGATTP
TPGKVMYTEG IYVGYRHFDH ADVQPLYPFG HGLSYTTFSY FSLTFSRISA SSELTVQLQV
KNTGVVSGQE VVQVYVADVA PALPKAPKEL KGFATVELLP GETKTVTVQL GRDAFRHWEE
RQNCWVADKG RYRVLAGASS SDIRLEVSVD VQEPLRWTGL
//