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Database: UniProt
Entry: A0A428TW69_9HYPO
LinkDB: A0A428TW69_9HYPO
Original site: A0A428TW69_9HYPO 
ID   A0A428TW69_9HYPO        Unreviewed;       414 AA.
AC   A0A428TW69;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=glucan endo-1,6-beta-glucosidase {ECO:0000256|ARBA:ARBA00038935};
DE            EC=3.2.1.75 {ECO:0000256|ARBA:ARBA00038935};
DE   AltName: Full=Beta-1,6-glucanase B {ECO:0000256|ARBA:ARBA00042025};
DE   AltName: Full=Endo-1,6-beta-D-glucanase B {ECO:0000256|ARBA:ARBA00041472};
DE   AltName: Full=Endo-1,6-beta-glucanase B {ECO:0000256|ARBA:ARBA00043257};
GN   ORFNames=CEP52_005723 {ECO:0000313|EMBL:RSM06318.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM06318.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM06318.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM06318.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. Acts on lutean,
CC       pustulan and 1,6-oligo-beta-D-glucosides.
CC       {ECO:0000256|ARBA:ARBA00037628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC         glucans.; EC=3.2.1.75; Evidence={ECO:0000256|ARBA:ARBA00036633};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:RSM06318.1}.
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DR   EMBL; NKCK01000046; RSM06318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428TW69; -.
DR   STRING; 1325735.A0A428TW69; -.
DR   Proteomes; UP000287144; 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; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   PANTHER; PTHR31297:SF39; 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:UP000287144};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..414
FT                   /note="glucan endo-1,6-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019180931"
FT   DOMAIN          96..385
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   414 AA;  47348 MW;  B1B81E290F6E6DDA CRC64;
     MLTSSLFTAL AALASSAHAW LPTDNSHPGL NKRDVTLFTY PLQPGSNKRW LPSSNKIRGV
     NLGSLFVYEP WIDSQEWANT GCEGEKSEFD CVMNKGQESA DKAFQEHWKR FITQEDLDEM
     ASYGLNTIRV PLGYWLKEDL VDASEHFPKG GLDYLTQLCG WASDRGFYII LDLHGAPGAQ
     EPNQPFTGQY APSVGFYNDY NYGRAVEWLE WITDIIHTKN EYRNVGMLEL VNEPLNWDKA
     VDSLRSTYYP NAYKAIRKVE DNLKVTTNDR LHIQMMGSLW GSGNPTEFLS DTSFTAFDDH
     RYLKWDTSVE VSQSAYIQKS CQDDRNTDGP TIVGEWSIAV PDNVEQTDAW KPQSQKDFYS
     KWFAAQVHAY EEHTLGWVFW TWKTNLGDDY RWSYRDAARA GVIPKDLNSL PNVC
//
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