ID A0A423WHM6_9PEZI Unreviewed; 171 AA.
AC A0A423WHM6;
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=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=VSDG_01924 {ECO:0000313|EMBL:ROW02886.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW02886.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW02886.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW02886.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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}.
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:ROW02886.1}.
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DR EMBL; LJZO01000004; ROW02886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WHM6; -.
DR STRING; 252740.A0A423WHM6; -.
DR Proteomes; UP000284375; 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; IPR002963; Expansin.
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 PANTHER; PTHR31867; EXPANSIN-A15; 1.
DR PANTHER; PTHR31867:SF2; EXPANSIN-A7; 1.
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:UP000284375};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..171
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018988623"
FT DOMAIN 32..171
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 171 AA; 17710 MW; 632CF9139708A030 CRC64;
MKLTIIMPLI MAAAVKALSG KATTTRYYDG AKGACGCGTD SSLFSWQEGI SDGVYTAAGS
QALFGADGST WCGSGCGTCY KLTSTGDAAC SSCGTGGAAD ESITVMVTNL CPYNGNQQWC
PNAGSTNDYG YNYHFDIMAK SEIFGDNVVV DFEEVDCPGA ATSDFQQCEC A
//
