ID   GUN1_TRILO              Reviewed;         463 AA.
AC   Q12714;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   22-FEB-2023, entry version 102.
DE   RecName: Full=Endoglucanase EG-1;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=egl1;
OS   Trichoderma longibrachiatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; 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 generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; X60652; CAA43059.1; -; Genomic_DNA.
DR   PIR; A48375; A48375.
DR   AlphaFoldDB; Q12714; -.
DR   SMR; Q12714; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; EGL7A_TRILO; -.
DR   GlyCosmos; Q12714; 5 sites, No reported glycans.
DR   BRENDA; 3.2.1.4; 6448.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF1; ENDO-BETA-1,4-GLUCANASE CELB; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..463
FT                   /note="Endoglucanase EG-1"
FT                   /id="PRO_0000007914"
FT   DOMAIN          427..463
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          23..397
FT                   /note="Catalytic"
FT   REGION          390..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..427
FT                   /note="Linker"
FT   COMPBIAS        410..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        435..452
FT                   /evidence="ECO:0000250"
FT   DISULFID        446..462
FT                   /evidence="ECO:0000250"
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
//