ID A0A194UM39_9PEZI Unreviewed; 173 AA.
AC A0A194UM39;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE RecName: Full=Cellulase {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
GN ORFNames=VP1G_00207 {ECO:0000313|EMBL:KUI52721.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI52721.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PROSITE-
CC ProRule:PRU10069};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000256|ARBA:ARBA00007793}.
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DR EMBL; KN714666; KUI52721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UM39; -.
DR STRING; 694573.A0A194UM39; -.
DR OrthoDB; 2941630at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd22278; DPBB_GH45_endoglucanase; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR Pfam; PF03330; DPBB_1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS50842; EXPANSIN_EG45; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..173
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008265645"
FT DOMAIN 32..137
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000259|PROSITE:PS50842"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
SQ SEQUENCE 173 AA; 17638 MW; B95E1985C318BD69 CRC64;
MKLTITTLLT MAAAAAALSG KATTTRYYDG TEGACGCGTS SGLYSWQTGI STNIYTAAGS
QALFGSDGST WCGSGCGVCY NLTSTGSSAC SSCGTGGVEG ESIIVMVTNL CPNDGNSQWC
PDVGGTNEYG YSYHFDIMAQ SEVFGDNVVA DFEEVDCPSA ATSDYSQCTC ASS
//
