GUN1_HYPJR
ID GUN1_HYPJR Reviewed; 459 AA.
AC A0A024SNB7;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Endoglucanase EG-1;
DE EC=3.2.1.4 {ECO:0000250|UniProtKB:P07981};
DE AltName: Full=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=egl1; ORFNames=M419DRAFT_5304;
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
RN [2]
RP GLYCOSYLATION AT ASN-78; ASN-204 AND ASN-394.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=12499406; DOI=10.1093/glycob/cwf089;
RA Hui J.P., White T.C., Thibault P.;
RT "Identification of glycan structure and glycosylation sites in
RT cellobiohydrolase II and endoglucanases I and II from Trichoderma reesei.";
RL Glycobiology 12:837-849(2002).
CC -!- FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-
CC glucosidic bonds in cellulose. The degradation of cellulose involves an
CC interplay between different cellulolytic enzymes. Hydrolysis starts
CC with EGs, which cut internal glycosidic linkages to reduce the
CC polymerization degree of the substrate and creates new chain ends for
CC exocellobiohydrolases (CBHs). The CBH release the disaccharide
CC cellobiose from the non-reducing end of the cellulose polymer chain.
CC Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short
CC cello-oligosaccharides into glucose units.
CC {ECO:0000250|UniProtKB:P07981}.
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 Evidence={ECO:0000250|UniProtKB:P07981};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07981}.
CC -!- DOMAIN: The enzyme consists of two functional domains, a catalytic core
CC joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-,
CC and proline-rich, highly glycosylated linker sequence.
CC {ECO:0000250|UniProtKB:P62694}.
CC -!- PTM: Asn-204 contains mainly a high-mannose-type glycan (Hex(7-
CC 9)GlcNAc(2)), with a small fraction (8%) bearing a single GlcNAc at
CC this site. {ECO:0000269|PubMed:12499406}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; KI911139; ETS07075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024SNB7; -.
DR SMR; A0A024SNB7; -.
DR iPTMnet; A0A024SNB7; -.
DR EnsemblFungi; ETS07075; ETS07075; M419DRAFT_5304.
DR KEGG; trr:M419DRAFT_5304; -.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000024376; Unassembled WGS sequence.
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; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..459
FT /note="Endoglucanase EG-1"
FT /id="PRO_5001534088"
FT DOMAIN 423..459
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 23..397
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT REGION 390..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..423
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT COMPBIAS 406..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT ACT_SITE 223
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT SITE 164
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12499406"
FT SITE 208
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12499406"
FT SITE 281
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12499406"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:12499406"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:12499406"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12499406"
FT DISULFID 41..47
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 71..92
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 82..88
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 161..360
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 193..216
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 197..215
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 236..241
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 246..315
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 423..439
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 431..448
FT /evidence="ECO:0000250|UniProtKB:P07981"
FT DISULFID 442..458
FT /evidence="ECO:0000250|UniProtKB:P07981"
SQ SEQUENCE 459 AA; 48208 MW; D235A256F808CBB9 CRC64;
MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ DTSVVLDWNY
RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA ASGVTTSGSS LTMNQYMPSS
SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ
YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA
CDSAGCGFNP YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV
DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGNAGPC
SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP PPASSTTFST TRRSSTTSSS
PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY SNDYYSQCL
