ID   GUN_ROBSP               Reviewed;         385 AA.
AC   P23044; Q9P981;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   22-FEB-2023, entry version 89.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethyl-cellulase I;
DE            Short=CMCase I;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Endoglucanase I;
DE   Flags: Precursor;
GN   Name=eg 1;
OS   Robillarda sp. (strain Y-20).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Robillarda.
OX   NCBI_TaxID=72589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kashiwagi Y.;
RT   "Endoglucanase gene from cellulolytic fungi, Robillarda sp. Y-20.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-385, AND PROTEIN SEQUENCE OF 18-35.
RX   PubMed=2277031; DOI=10.1093/oxfordjournals.jbchem.a123211;
RA   Yoshigi N., Taniguchi H., Sasaki T.;
RT   "Cloning and sequencing of the endo-cellulase cDNA from Robillarda sp. Y-
RT   20.";
RL   J. Biochem. 108:388-392(1990).
CC   -!- FUNCTION: Active towards carboxymethyl cellulose.
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB030819; BAA90480.1; -; Genomic_DNA.
DR   AlphaFoldDB; P23044; -.
DR   SMR; P23044; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EGL5A_ROBSP; -.
DR   GlyCosmos; P23044; 6 sites, No reported glycans.
DR   UniPathway; UPA00696; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
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: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.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:2277031"
FT   CHAIN           18..385
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000184049"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        27..28
FT                   /note="SS -> GN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   385 AA;  41428 MW;  149604D42369AD33 CRC64;
     MKLVFSALAS LLSGASATIY YAGVAESSGE FGVWSATQTP GTGLPGRFGV DYAFISEAAV
     DVHVDQNHLN LFRVAFLLER MCPPATGLGA AFNETHFDYF KEAVDYITVT KGAYAILDPH
     NYMRYNDPSY QPFSGSVIGN TSDSTAATTE QFGEFWGELA SRFNDNERVI FGLMNEPHDM
     ATSLVLANNQ AAIDAIRAAN ASNLIIMPGN SWTGGHSWTE GSDPSSALLN QFKDPLNNTA
     IDIHEYLDYD FSGGHLECVS DPETNLAALT AWLKENNLKA FITEFGGSNS TSCQEMLPDL
     INYMADNAEY IGWTAWAAGP FWGPNSPCCT NSTQLGSLEP GSTAVDGSPG LYDTVWLPVI
     QPLVPTELQW SGPASISGGE LTSRA
//