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Database: UniProt
Entry: H0EP31_GLAL7
LinkDB: H0EP31_GLAL7
Original site: H0EP31_GLAL7 
ID   H0EP31_GLAL7            Unreviewed;       450 AA.
AC   H0EP31;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE            EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN   ORFNames=M7I_4399 {ECO:0000313|EMBL:EHK99720.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK99720.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK99720.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
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:EHK99720.1}.
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DR   EMBL; AGUE01000108; EHK99720.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EP31; -.
DR   HOGENOM; CLU_004624_2_0_1; -.
DR   InParanoid; H0EP31; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
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:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..450
FT                   /note="glucan 1,3-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003532045"
FT   DOMAIN          149..404
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   450 AA;  49768 MW;  FBAD1F48A89965D5 CRC64;
     MRFSPVLPVL LATSALAAPV PEPGLISSIL SSITNTVNTI LSDLGVTLQT NGASHGPVWN
     CYKLTFPQIV VSIERFKHSL IWPKNVNFVD WKTYKANGVN LGAWLEQEQN YDIDFWNTGA
     PEAMDEWTWC KTLGPKCGPL LEQRYATWVT TADIDKLAAT GINTLRIPTT YAAWIDWPES
     EFYHGNQQKY LRTITNYAIE KYGMHVIVGL HSLPGGVNSL DIGEAFGHGD WFFNATKLEW
     SMKAVDGVLS FFKNSGHLGS FTFAPLNEVS DTHLAGFGSA AGLTTNGTNW VNTYIKACLK
     KIAKIDKRIP LMLQDSFQGE PFWSPFYDAG TNIVIDTHIY YFAAAGTYSQ YVAPAICGQG
     SAAKGDGKFP VFVGEWSLQT QYNNTLGNRK TLFDTQRYSW AQYVSGGAFW NIRNKNTVAV
     DGEGTTGDYW DYMSLIDAGV ATPVTNASYC
//
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