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Protein
Submitted name:

Beta-1,4-glucanase

Gene

egl

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16503.
BRENDAi3.2.1.4. 6451.

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.
mycoCLAPiEGL12A_TRIRE.

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-1,4-glucanaseImported (EC:3.2.1.4Imported)
Submitted name:
Endo-beta-1,4-glucanaseImported
Gene namesi
Name:eglImported
OrganismiHypocrea jecorina (Trichoderma reesei)Imported
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 234218Sequence analysisPRO_5007696645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Pyrrolidone carboxylic acidCombined sources
Disulfide bondi20 ↔ 48Combined sources
Glycosylationi180 – 1801N-linked (GlcNAc...)Combined sourcesCAR_5007364437

Keywords - PTMi

Pyrrolidone carboxylic acidCombined sources

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI123232.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8VX-ray1.90A/B/C/D/E/F18-234[»]
1OA2X-ray1.50A/B/C/D/E/F17-234[»]
1OLQX-ray1.70A/B18-234[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 12 (cellulase H) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG410IKN9. Eukaryota.
ENOG410XRKF. LUCA.
OMAiQPIGSQI.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
[Graphical view]
PfamiPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

O00095-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLQVLPAL IPAALAQTSC DQWATFTGNG YTVSNNLWGA SAGSGFGCVT
60 70 80 90 100
AVSLSGGASW HADWQWSGGQ NNVKSYQNSQ IAIPQKRTVN SISSMPTTAS
110 120 130 140 150
WSYSGSNIRA NVAYDLFTAA NPNHVTYSGD YELMIWLGKY GDIGPIGSSQ
160 170 180 190 200
GTVNVGGQSW TLYYGYNGAM QVYSFVAQTN TTNYSGDVKN FFNYLRDNKG
210 220 230
YNAAGQYVLS YQFGTEPFTG SGTLNVASWT ASIN
Length:234
Mass (Da):25,159
Last modified:July 1, 1997 - v1
Checksum:iDF476EEDE384ADD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU149644 Genomic DNA. Translation: ABV71388.1.
AB003694 Genomic DNA. Translation: BAA20140.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU149644 Genomic DNA. Translation: ABV71388.1.
AB003694 Genomic DNA. Translation: BAA20140.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8VX-ray1.90A/B/C/D/E/F18-234[»]
1OA2X-ray1.50A/B/C/D/E/F17-234[»]
1OLQX-ray1.70A/B18-234[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI123232.

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.
mycoCLAPiEGL12A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IKN9. Eukaryota.
ENOG410XRKF. LUCA.
OMAiQPIGSQI.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16503.
BRENDAi3.2.1.4. 6451.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
[Graphical view]
PfamiPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization and heterologous expression of the gene encoding a low-molec ular-mass endoglucanase from Trichoderma reesei QM9414."
    Okada H., Tada K., Sekiya T., Yokoyama K., Takahashi A., Tohda H., Kumagai H., Morikawa Y.
    Appl. Environ. Microbiol. 64:55-563(1998)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: QM9414Imported.
  2. "The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution."
    Sandgren M., Shaw A., Ropp T.H., Wu S., Bott R., Cameron A.D., Stahlberg J., Mitchinson C., Jones T.A.
    J. Mol. Biol. 308:295-310(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 18-234, GLYCOSYLATION AT ASN-180, DISULFIDE BONDS.
  3. "Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability."
    Sandgren M., Gualfetti P.J., Shaw A., Gross L.S., Saldajeno M., Day A.G., Jones T.A., Mitchinson C.
    Protein Sci. 12:848-860(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 17-234, PYRROLIDONE CARBOXYLIC ACID AT GLN-17, GLYCOSYLATION AT ASN-180, DISULFIDE BONDS.
  4. "The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability."
    Sandgren M., Gualfetti P.J., Paech C., Paech S., Shaw A., Gross L.S., Saldajeno M., Berglund G.I., Jones T.A., Mitchinson C.
    Protein Sci. 12:2782-2793(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 18-234, GLYCOSYLATION AT ASN-180, DISULFIDE BONDS.
  5. "Cloning and characterization of endoglucanase genes from Trichoderma spp."
    Shaikh Z.J., Bhat S., Kuruvunashetti M.S.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: IABT1003Imported.

Entry informationi

Entry nameiO00095_HYPJE
AccessioniPrimary (citable) accession number: O00095
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 1997
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.