ID   GUN_ASPAC               Reviewed;         237 AA.
AC   P22669;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   22-FEB-2023, entry version 104.
DE   RecName: Full=Endoglucanase-1;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Endoglucanase I;
DE   AltName: Full=FI-CMCase;
DE   Flags: Precursor;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F-50;
RX   PubMed=2216782; DOI=10.1093/nar/18.19.5884;
RA   Ooi T., Shinmyo A., Okada H., Murao S., Kawaguchi T., Arai M.;
RT   "Complete nucleotide sequence of a gene coding for Aspergillus aculeatus
RT   cellulase (FI-CMCase).";
RL   Nucleic Acids Res. 18:5884-5884(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PYROGLUTAMATE
RP   FORMATION AT GLN-17.
RC   STRAIN=F-50;
RX   PubMed=2249253; DOI=10.1007/bf00318384;
RA   Ooi T., Shinmyo A., Okada H., Hara S., Ikenaka T., Murao S., Arai M.;
RT   "Cloning and sequence analysis of a cDNA for cellulase (FI-CMCase) from
RT   Aspergillus aculeatus.";
RL   Curr. Genet. 18:217-222(1990).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By cellulosic materials and hemicelluloses.
CC   -!- MISCELLANEOUS: Will also hydrolyze 1,4-linkages in beta-D-glucans also
CC       containing 1,3-linkages.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC       {ECO:0000305}.
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DR   EMBL; D00546; BAA00435.1; -; Genomic_DNA.
DR   EMBL; X52525; CAA36757.1; -; mRNA.
DR   PIR; S12610; S12610.
DR   PDB; 5GM3; X-ray; 1.59 A; A/B=19-237.
DR   PDB; 5GM4; X-ray; 1.92 A; A/B/C/D/E/F/G=19-237.
DR   PDB; 5GM5; X-ray; 1.73 A; A/B/C/D/E/F/G=18-237.
DR   PDBsum; 5GM3; -.
DR   PDBsum; 5GM4; -.
DR   PDBsum; 5GM5; -.
DR   AlphaFoldDB; P22669; -.
DR   SMR; P22669; -.
DR   CAZy; GH12; Glycoside Hydrolase Family 12.
DR   VEuPathDB; FungiDB:ASPACDRAFT_126244; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR002594; GH12.
DR   PANTHER; PTHR34002; BLR1656 PROTEIN; 1.
DR   PANTHER; PTHR34002:SF10; PUTATIVE-RELATED; 1.
DR   Pfam; PF01670; Glyco_hydro_12; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..237
FT                   /note="Endoglucanase-1"
FT                   /id="PRO_0000008018"
FT   MOD_RES         17
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2249253"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          45..56
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          61..71
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          110..123
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          132..142
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          148..157
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          160..169
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   HELIX           191..201
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:5GM3"
FT   STRAND          209..234
FT                   /evidence="ECO:0007829|PDB:5GM3"
SQ   SEQUENCE   237 AA;  25560 MW;  8F173571A8AE6931 CRC64;
     MKAFHLLAAL AGAAVAQQAQ LCDQYATYTG GVYTINNNLW GKDAGSGSQC TTVNSASSAG
     TSWSTKWNWS GGENSVKSYA NSGLTFNKKL VSQISQIPTT ARWSYDNTGI RADVAYDLFT
     AADINHVTWS GDYELMIWLA RYGGVQPIGS QIATATVDGQ TWELWYGANG SQKTYSFVAP
     TPITSFQGDV NDFFKYLTQN HGFPASSQYL ITLQFGTEPF TGGPATLSVS NWSASVQ
//