ID   GUN1_HUMGT              Reviewed;         435 AA.
AC   Q12622;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Endoglucanase EG-1;
DE            EC=3.2.1.4;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Cellulase;
DE   Flags: Precursor;
GN   Name=EG-1;
OS   Humicola grisea var. thermoidea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; mitosporic Ascomycota;
OC   Humicola.
OX   NCBI_TaxID=5528;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IFO 9854;
RA   Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The biological conversion of cellulose to glucose
CC       generally requires three types of hydrolytic enzymes: (1)
CC       Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC       Exocellobiohydrolases that cut the dissaccharide cellobiose from
CC       the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-
CC       glucosidases which hydrolyze the cellobiose and other short cello-
CC       oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C)
CC       family.
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DR   EMBL; D63516; BAA09786.1; -; Genomic_DNA.
DR   HSSP; P56680; 1A39.
DR   SMR; Q12622; 21-418.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   BRENDA; 3.2.1.4; 278774.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   Gene3D; G3DSA:2.70.100.10; Glyco_hydro_7; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   ProDom; PD186135; Glyco_hydro_7; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL        1     20       By similarity.
FT   CHAIN        21    435       Endoglucanase EG-1.
FT                                /FTId=PRO_0000007916.
FT   ACT_SITE    217    217       Nucleophile (By similarity).
FT   ACT_SITE    222    222       Proton donor (By similarity).
FT   MOD_RES      21     21       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   CARBOHYD    109    109       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (By similarity).
FT   DISULFID     38     44       By similarity.
FT   DISULFID     71     93       By similarity.
FT   DISULFID     83     89       By similarity.
FT   DISULFID    160    385       By similarity.
FT   DISULFID    192    215       By similarity.
FT   DISULFID    196    214       By similarity.
FT   DISULFID    235    254       By similarity.
FT   DISULFID    243    248       By similarity.
FT   DISULFID    259    335       By similarity.
SQ   SEQUENCE   435 AA;  47890 MW;  25EB3D62D96B65FA CRC64;
     MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY IVLDSLSHPI
     HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP
     DGRVPSPRVY LLDKTERRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKH
     NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL
     YLCEGEECAF EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL
     EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ GMGEALTRGM
     VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP FPEVTYTNLR WGEIGSTYQE
     VQKPKPKPGP GPRSD
//