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Database: UniProt
Entry: A0A074XM17_9PEZI
LinkDB: A0A074XM17_9PEZI
Original site: A0A074XM17_9PEZI 
ID   A0A074XM17_9PEZI        Unreviewed;       951 AA.
AC   A0A074XM17;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-FEB-2023, entry version 33.
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=M436DRAFT_71080 {ECO:0000313|EMBL:KEQ75601.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ75601.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ75601.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ75601.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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}.
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DR   EMBL; KL584705; KEQ75601.1; -; Genomic_DNA.
DR   RefSeq; XP_013429796.1; XM_013574342.1.
DR   AlphaFoldDB; A0A074XM17; -.
DR   STRING; 1043004.A0A074XM17; -.
DR   GeneID; 25414881; -.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000027730; 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; 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:SF12; BETA-GLUCOSIDASE A-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   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..951
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001704000"
FT   DOMAIN          808..876
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   951 AA;  102446 MW;  47995419B140143E CRC64;
     MSGFKSLALL LAAQLANAQG GYPNPPVAGL PFPGTNYPGS EVPYAVAGAQ FNQTSPPYYP
     SPWGTGAGEW ASAYEKAIAF VSQLTLAEKV NLTTVSSWES EKCVGNTGSI PRLGFKSLCL
     QDSPLGVRFG DFVSAFSAGV TVAATWDRSL AYTRGNDMGS EHRDKGVDVM LGPVVGPLGR
     SPEGGRNWEG FSPDPVLSGI LNAETVKGIQ DAGVIACTKH YILNEQEHFR QGGPNISDAV
     SANVDDITLH ELYVWPFADA VRAGTGSVMC SYNQANNSYV CQNSHLLNKV LKSELGFQGF
     VVSDWSGQHS GVSSALAGLD MTMPGDVGFD SGTSFWGANL TIAVLNGTVP QYRIDDMAVR
     IVAAWYLVDR EDHQVENAPN FSSWTTRTFG YRHYIAQEGY EQLNYHVDVQ EDHRDNIREV
     AAKGTVLLKN NGALPLKGTE QLVGVFGEDA ADNQYGPNGC SDRGCDNGTL AMGWGSGTAN
     FPYLVAPHSA IENEVRSHGK SVESILDRAA FSQIDVLAQR ADEVNGACIV FANADAGEGY
     IIVDGNQGDR NNLTLWQGGE EVISHVAGLC KNTIVVLHTV GPVLINDWYD HENITAILWA
     GVPGQESGNA IVDVLYGKVN PSGKLPFTLG KTRESYGTDL LYEYNNGGAA PQTQFEEGVF
     IDYRAFDRAG ETPVYEFGYG LSYTNFSYSD ISVSVNTSAP AYVPASGFTE AAPVYGSISN
     NSADYVFPAD VRPIEYYIYP YLNSTNLRAS SQDPYYGSNY SFPAGSASSA PQPLLPASGA
     PGGNPGLYDI LYTVTATVTN TGSVEGEEVP QLYISLGGPD DPAVVLRQFD KFSIAPGASK
     TFTAQITRRD ISNWSPALDD WYVSEYPKTV YVGSSSRKLP LKAALPANGA TSPGTGNVFE
     PFVESLFISL YHSRWLQQLD YLHPALWLPL DLVERAGVVK SRRTHDDDIR F
//
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