ID A0A384JDH0_BOTFB Unreviewed; 229 AA. AC A0A384JDH0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-AUG-2022, entry version 11. DE RecName: Full=Endo-beta-1,4-glucanase D {ECO:0000256|RuleBase:RU368122}; DE Short=Endoglucanase D {ECO:0000256|RuleBase:RU368122}; DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU368122}; DE AltName: Full=Carboxymethylcellulase D {ECO:0000256|RuleBase:RU368122}; DE AltName: Full=Cellulase D {ECO:0000256|RuleBase:RU368122}; GN ORFNames=BCIN_03g05890 {ECO:0000313|EMBL:ATZ48364.1}; OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis OS cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=332648 {ECO:0000313|EMBL:ATZ48364.1, ECO:0000313|Proteomes:UP000001798}; RN [1] {ECO:0000313|EMBL:ATZ48364.1, ECO:0000313|Proteomes:UP000001798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10 {ECO:0000313|EMBL:ATZ48364.1, RC ECO:0000313|Proteomes:UP000001798}; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). RN [2] {ECO:0000313|EMBL:ATZ48364.1, ECO:0000313|Proteomes:UP000001798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10 {ECO:0000313|EMBL:ATZ48364.1, RC ECO:0000313|Proteomes:UP000001798}; RX PubMed=23104368; DOI=10.1128/EC.00164-12; RA Staats M., van Kan J.A.; RT "Genome update of Botrytis cinerea strains B05.10 and T4."; RL Eukaryot. Cell 11:1413-1414(2012). RN [3] {ECO:0000313|EMBL:ATZ48364.1, ECO:0000313|Proteomes:UP000001798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10 {ECO:0000313|EMBL:ATZ48364.1, RC ECO:0000313|Proteomes:UP000001798}; RX PubMed=26913498; DOI=10.1111/mpp.12384; RA Van Kan JA, Stassen JH, Mosbach A, Van Der Lee TA, Faino L, Farmer AD, RA Papasotiriou DG, Zhou S, Seidl MF, Cottam E, Edel D, Hahn M, Schwartz DC, RA Dietrich RA, Widdison S Scalliet.G.; RT "A gapless genome sequence of the fungus Botrytis cinerea."; RL Mol. Plant Pathol. 18:75-89(2017). CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4 CC glycosidic bonds. Involved in the degradation of complex natural CC cellulosic substrates. {ECO:0000256|RuleBase:RU368122}. 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|RuleBase:RU368122}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU368122}. CC -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase catalytic CC module at the N-terminus, a linker rich in serines and threonines, and CC a C-terminal carbohydrate-binding module (CBM). The genes for catalytic CC modules and CBMs seem to have evolved separately and have been linked CC by gene fusion. {ECO:0000256|RuleBase:RU368122}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. CC {ECO:0000256|ARBA:ARBA00009585}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP009807; ATZ48364.1; -; Genomic_DNA. DR VEuPathDB; FungiDB:Bcin03g05890; -. DR Proteomes; UP000001798; Chromosome bcin03. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030248; F:cellulose binding; IEA:UniProtKB-UniRule. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniRule. DR InterPro; IPR005103; AA9. DR Pfam; PF03443; AA9; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU368122}; KW Cellulose degradation {ECO:0000256|RuleBase:RU368122}; KW Disulfide bond {ECO:0000256|RuleBase:RU368122}; KW Glycosidase {ECO:0000256|RuleBase:RU368122}; KW Hydrolase {ECO:0000256|RuleBase:RU368122}; KW Polysaccharide degradation {ECO:0000256|RuleBase:RU368122}; KW Reference proteome {ECO:0000313|Proteomes:UP000001798}; KW Secreted {ECO:0000256|RuleBase:RU368122}; KW Signal {ECO:0000256|RuleBase:RU368122, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..229 FT /note="Endo-beta-1,4-glucanase D" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5017037546" SQ SEQUENCE 229 AA; 23945 MW; DD28E9D3DC16503A CRC64; MRSSDITFVL LSVVATVRSH ATFQELWINS VDQVGSCVRL PPTNSPITDL TSTDLRCNVG GTVGVSGVCS VAAGGNVTVE MHQQPGDRSC ANEAIGGAHY GPVILYMSKV SNAATDTGSG SWFKVDQEGY DQTLNANCGK RSFTIPSTLA PGDYLLRAEV IALHVAGSVG GAQLYMSCFQ LRVTGSGSKN PTGVLFPGAY SATDPGILIN IYQTINNYTI PGPTTVFTG //