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Database: UniProt
Entry: G3YAY1_ASPNA
LinkDB: G3YAY1_ASPNA
Original site: G3YAY1_ASPNA 
ID   G3YAY1_ASPNA            Unreviewed;       441 AA.
AC   G3YAY1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE            EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE   AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
DE   Flags: Fragment;
GN   ORFNames=ASPNIDRAFT_123981 {ECO:0000313|EMBL:EHA19845.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA19845.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA19845.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
CC   -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC       biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:EHA19845.1}.
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DR   EMBL; ACJE01000019; EHA19845.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3YAY1; -.
DR   STRING; 380704.G3YAY1; -.
DR   HOGENOM; CLU_004624_4_2_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          82..321
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   NON_TER         441
FT                   /evidence="ECO:0000313|EMBL:EHA19845.1"
SQ   SEQUENCE   441 AA;  50104 MW;  188E2A6757642932 CRC64;
     MGLNSTWNDS AQANENVPPL NEKFPYGSQP IRGVNLGGWL SIEPFIVPSL FDTYTSSEGI
     IDEWTLSEKL GDSAASVIEK HYATFITEQD FADIRDAGLD HVRIQFSYWA IKTYDGDPYV
     PKIAWRYLLR AIEYCRKYGL RVNLDPHGIP GSQNGWNHSG RQGTIGWLNG TDGELNRQRS
     LEMHDQLSQF FAQDRYKNVV TIYGLVNEPL MLSLPVEKVL NWTTEATNLV QKNGIKAWVT
     VHDGFLNLDK WDKMLKTRPS NMMLDTHQYT VFNTGEIVLN HTRRVELICE SWYSMIQQIN
     ITSTGWGPTI CGEWSQADTD CAQYVNNVGR GTRWEGTFSL TDSTQYCPTA SEGTCSCTQA
     NAVPGVYSEG YKTFLQTYAE AQMSAFESAM GWFYWTWATE SAAQWSYRTA WKNGYMPKKA
     YSPSFKCGDT IPSFGNLPEY Y
//
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