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UniProtKB/Swiss-Prot entry P07982


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GUN2_TRIRE
Primary accession number P07982
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on August 1, 1988 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Endoglucanase EG-II [Precursor]
Synonyms EGLII
EC 3.2.1.4
Endo-1,4-beta-glucanase
Cellulase
Gene name
Name: egl2
From
Trichoderma reesei (Hypocrea jecorina) [TaxID: 51453] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-58, AND PYROGLUTAMATE FORMATION AT GLN-22.
STRAIN=VTT-D-80133;
DOI=10.1016/0378-1119(88)90541-0; PubMed=3384334 [NCBI, ExPASy, EBI, Israel, Japan]
Saloheimo M., Lehtovaara P., Penttilae M., Teeri T.T., Staahlberg J., Johansson G., Pettersson G., Clayssens M., Tomme P., Knowles J.K.C.;
"EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme.";
Gene 63:11-21(1988).
[2]
PROTEIN SEQUENCE OF 87-99.
PubMed=3356188 [NCBI, ExPASy, EBI, Israel, Japan]
Stahlberg J., Johansson G., Pettersson G.;
"A binding-site-deficient, catalytically active, core protein of endoglucanase III from the culture filtrate of Trichoderma reesei.";
Eur. J. Biochem. 173:179-183(1988).
[3]
ACTIVE SITE GLU-350.
DOI=10.1016/0014-5793(93)81202-B; PubMed=8093602 [NCBI, ExPASy, EBI, Israel, Japan]
Macarron R., van Beeumen J., Henrissat B., de la Mata I., Claeyssens M.;
"Identification of an essential glutamate residue in the active site of endoglucanase III from Trichoderma reesei.";
FEBS Lett. 316:137-140(1993).
Comments
  • FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
  • CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
  • SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
  • SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.
  • CAUTION: Was originally called endoglucanase EG-III.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M19373; AAA34213.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S28372; S28372.
3D structure databases
HSSP P00725; 2CBH. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P07982.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0043169; Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0008810; Molecular function: cellulase activity (inferred from electronic annotation from EC).
GO:0030248; Molecular function: cellulose binding (inferred from electronic annotation from InterPro).
GO:0030245; Biological process: cellulose catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000254; CBD_fun.
IPR001547; Glyco_hydro_5.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
Pfam PF00734; CBM_1; 1.
PF00150; Cellulase; 1.
Pfam graphical view of domain structure.
ProDom PD001821; CBD_fungal; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00236; fCBD; 1.
SMART graphical view of domain structure.
PROSITE PS00562; CBM1_1; 1.
PS51164; CBM1_2; 1.
PS00659; GLYCOSYL_HYDROL_F5; 1.
PROSITE graphical view of domain structure (profiles).
Other
ProtoNet P07982.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21      
CHAIN   22   418  397     Endoglucanase EG-II. PRO_0000007874
DOMAIN   22    57  36     CBM1. 
REGION   58    91  34     Linker. 
REGION   92   418  327     Catalytic. 
ACT_SITE   239   239        Proton donor (By similarity). 
ACT_SITE   350   350        Nucleophile. 
MOD_RES   22    22        Pyrrolidone carboxylic acid. 
CARBOHYD   124   124        N-linked (GlcNAc...) (Potential). 
DISULFID   29    46        By similarity. 
DISULFID   40    56        By similarity. 
Sequence information
Length: 418 AA [This is the length of the unprocessed precursor] Molecular weight: 44227 Da [This is the MW of the unprocessed precursor] CRC64: 26A492D55237A49B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNKSVAPLLL AASILYGGAV AQQTVWGQCG GIGWSGPTNC APGSACSTLN PYYAQCIPGA 

        70         80         90        100        110        120 
TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI AGFDFGCTTD GTCVTSKVYP 

       130        140        150        160        170        180 
PLKNFTGSNN YPDGIGQMQH FVNEDGMTIF RLPVGWQYLV NNNLGGNLDS TSISKYDQLV 

       190        200        210        220        230        240 
QGCLSLGAYC IVDIHNYARW NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP 

       250        260        270        280        290        300 
HDVNINTWAA TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS 

       310        320        330        340        350        360 
TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE TGGGNVQSCI 

       370        380        390        400        410 
QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTS SGNSWTDTSL VSSCLARK 

P07982 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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