ID   GUN1_TRILO     STANDARD;      PRT;   463 AA.
AC   Q12714;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   21-MAR-2006, entry version 46.
DE   Endoglucanase EG-1 precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase)
DE   (Cellulase).
GN   Name=egl1;
OS   Trichoderma longibrachiatum.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; mitosporic Hypocreales; Trichoderma.
OX   NCBI_TaxID=5548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CECT 2606;
RX   PubMed=1369161; DOI=10.1007/BF00170088;
RA   Gonzalez R., Ramon D., Perez-Gonzalez J.A.;
RT   "Cloning, sequence analysis and yeast expression of the egl1 gene from
RT   Trichoderma longibrachiatum.";
RL   Appl. Microbiol. Biotechnol. 38:370-375(1992).
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 nonreducing end of the cellulose polymer chain; (3)
CC       Beta-1,4-glucosidases which hydrolyze the cellobiose and other
CC       short cello-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 protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding)
CC       domain.
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DR   EMBL; X60652; CAA43059.1; -; Genomic_DNA.
DR   PIR; A48375; A48375.
DR   HSSP; P07981; 1EG1.
DR   SMR; Q12714; 23-393.
DR   InterPro; IPR000254; CBD_fun.
DR   InterPro; IPR008985; ConA_like_lec_gl.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   ProDom; PD186135; Glyco_hydro_7; 1.
DR   SMART; SM00236; fCBD; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    463       Endoglucanase EG-1.
FT                                /FTId=PRO_0000007914.
FT   DOMAIN      427    463       CBM1.
FT   REGION       23    397       Catalytic.
FT   REGION      402    427       Linker.
FT   ACT_SITE    218    218       Nucleophile (By similarity).
FT   ACT_SITE    223    223       Proton donor (By similarity).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    164    164       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    204    204       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    208    208       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    394    394       N-linked (GlcNAc...) (Potential).
FT   DISULFID    435    452       By similarity.
FT   DISULFID    446    462       By similarity.
SQ   SEQUENCE   463 AA;  48337 MW;  B3AC3DFD3ADD2B1C CRC64;
     MAPSATLPLT TAILAIGRLV AAQQPGTSTP EVHPKLTTYK CTTSGGCVAQ DTSVVLDWNY
     RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCYIEGVDYA ASGVTASGST LTLNQYMPSS
     SGGYSSVSPR LYLLGPDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ
     YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS GQGFCCNEMD ILEGNSRANA LTPHSCTATA
     CDSAGCGFNP YGSGYPNYFG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYRQNGV
     DIPSAKPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGRAGPC
     SSTEGNPSNI LANNPGTHVV YSNIRWGDIG STTNSTGGNP PPPPPPASST TFSTTRRSST
     TSSSPSCTQT HWGQCGGIGY TGCKTCTSGT TCQYGNDYYS QCL
//