ID   M7URS7_BOTF1            Unreviewed;       424 AA.
AC   M7URS7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=BcDW1_1665 {ECO:0000313|EMBL:EMR89683.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR89683.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000966};
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; KB707735; EMR89683.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7URS7; -.
DR   SMR; M7URS7; -.
DR   STRING; 1290391.M7URS7; -.
DR   HOGENOM; CLU_029718_0_1_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..424
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004086706"
FT   DOMAIN          126..393
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   424 AA;  44251 MW;  4133F99E1F896C5D CRC64;
     MRFTNFVLAA GLTATAFAAP VAVRDEDDSC VADYDETTSA AVVAQTTLPS SSAAVVAATS
     VAPSSSAVKT SAAVVQASSA ASPVVASSSP AATSSTKAAS STKAAVAAAS SGSTAAGKLR
     WIGASESGAE FGQGNLPGVV GTDYTFPNTT AIQTLIDGGM NIFRVPFLFE RMAQSSITAS
     LDATYLASYK EVIDYITAAG ATAVMEAHNY GRYDNNIITS TSDFGTFWGN FATEFKDNSN
     VIFDCNNEFH DEPTATIYAE LNQACVTAIR GVGATSQYIF VEGTSYTGAW TWVSSGNSVS
     MLNITDPEDK LVYEFHQYLD SDGSGTSATC VSSTIGAERI ADATAWLKAN NLKGVIGEFA
     GGVNADCESA ISGMLDALAA DNEYWLGALW WGAGPWWGDY IYAFEPPTGV AYKQYFDTLV
     SYVA
//