GUN2_HYPJR
ID GUN2_HYPJR Reviewed; 418 AA.
AC A0A024SH20;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Endoglucanase EG-II;
DE Short=EGII;
DE EC=3.2.1.4 {ECO:0000250|UniProtKB:P07982};
DE AltName: Full=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=egl2; ORFNames=M419DRAFT_72489;
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-124.
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:P07982}.
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:P07982};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07982}.
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:P07982}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; KI911141; ETS04885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024SH20; -.
DR SMR; A0A024SH20; -.
DR iPTMnet; A0A024SH20; -.
DR EnsemblFungi; ETS04885; ETS04885; M419DRAFT_72489.
DR KEGG; trr:M419DRAFT_72489; -.
DR HOGENOM; CLU_029718_1_1_1; -.
DR OrthoDB; 722981at2759; -.
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 InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..418
FT /note="Endoglucanase EG-II"
FT /id="PRO_5001537231"
FT DOMAIN 22..57
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 58..91
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT REGION 63..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..418
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT ACT_SITE 239
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:12499406"
FT DISULFID 107..113
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT DISULFID 183..190
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT DISULFID 323..359
FT /evidence="ECO:0000250|UniProtKB:P07982"
FT DISULFID 364..414
FT /evidence="ECO:0000250|UniProtKB:P07982"
SQ SEQUENCE 418 AA; 44155 MW; D0F9B9284E062FED CRC64;
MNKSVAPLLL AASILYGGAA AQQTVWGQCG GIGWSGPTNC APGSACSTLN PYYAQCIPGA
TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI AGFDFGCTTD GTCVTSKVYP
PLKNFTGSNN YPDGIGQMQH FVNDDGMTIF RLPVGWQYLV NNNLGGNLDS TSISKYDQLV
QGCLSLGAYC IVDIHNYARW NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP
HDVNINTWAA TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS
TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE TGGGNVQSCI
QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTG SGNSWTDTSL VSSCLARK
