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Database: UniProt
Entry: A0A0N0RU70_9HYPO
LinkDB: A0A0N0RU70_9HYPO
Original site: A0A0N0RU70_9HYPO 
ID   A0A0N0RU70_9HYPO        Unreviewed;       327 AA.
AC   A0A0N0RU70;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=ESCO_003539 {ECO:0000313|EMBL:KOS22753.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS22753.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS22753.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-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};
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:KOS22753.1}.
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DR   EMBL; LGSR01000002; KOS22753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0RU70; -.
DR   STRING; 150374.A0A0N0RU70; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000053831; 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; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF5; CBM1 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.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          22..274
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   327 AA;  35348 MW;  0C2138DD315920B1 CRC64;
     MPGIDFGCDI DGYAIPLKGY GGGDGLAQMQ HFTKDDGMNI FRLPFTWQFI GRNALGKLDK
     VNTEAYDALV QACLSTGAYC MLDAHNFGRY NGSIIGQGGP SNEVFANLWS QLATKYAKED
     RVVFGLMNEP HDLDIDMWAQ TCQVAVNAIR KAGATKQIIL LPGTNFASAE TFVSTGSAAA
     LANVTNPDGS IDNLILDLHK YLDINNSGSH VECTTDNVEG FGSIVSWLRE NKRQAIISET
     GASMDPSCMT DFCAQNKYLA ANTDVIIGFV AWGAGSFDQT YILTLTPTGK PGAYVDNKLM
     KECILDQFNV DLTPTPPPAP FEPDPGR
//
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