ID A0A316Z7J2_9BASI Unreviewed; 486 AA.
AC A0A316Z7J2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=FA09DRAFT_330226 {ECO:0000313|EMBL:PWN97541.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN97541.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN97541.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN97541.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819294; PWN97541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316Z7J2; -.
DR STRING; 58919.A0A316Z7J2; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000245946; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:PWN97541.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245946};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..486
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016441722"
FT DOMAIN 134..382
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 452..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 53795 MW; 1DA7B92CED9C30EB CRC64;
MRSLRTAPAA VSLLVSLALL AAAVLAAPLE PRLAHKHRSL ASAAVSASNV SDAAMPAGNV
SDAALRAVSA KRINARFGRD KLVRGVNLGG WFLLEAWETP HVFLTSDIER QQLSDEWAWM
GAKGARAKPD LVAHYNSYYT EQDFAEMAQA GLNTVRIPLP FWTFVPTVSP EPYLVNRQRA
ALRRALGWSL KHGLDVVLDL HALPGNINGQ DNGGRLGQQD WAKDPKNLDR SIAALQNMVE
LYVNNASYGG VVKAIQVANE PRINAQLSLP FLGAYHKRAL AAVRNAVSPT ALVRPTTMFS
DAFQDVTKYN YMFPQGDFPP QQLVVDKHFY FVKQWDRSLP DNDEELLRHV CAIGPRLRKA
HAVRPVVVGE FSLGRTTRCV DYHDCKGRTI AHDLPSLNSK SNNLFMRRFA EAQLATYEQA
GGWIMWTWKT DAAAAWSYQA ARNQGWLPSD VSDPTQRLYT PAPGSATDQR CVSEQPSRAP
RFAMQS
//
