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Q12714 (GUN1_TRILO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase EG-1

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:egl1
OrganismTrichoderma longibrachiatum
Taxonomic identifier5548 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 463441Endoglucanase EG-1
PRO_0000007914

Regions

Domain427 – 46337CBM1
Region23 – 397375Catalytic
Region402 – 42726Linker

Sites

Active site2181Nucleophile By similarity
Active site2231Proton donor By similarity

Amino acid modifications

Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Disulfide bond435 ↔ 452 By similarity
Disulfide bond446 ↔ 462 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12714 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B3AC3DFD3ADD2B1C

FASTA46348,337
        10         20         30         40         50         60 
MAPSATLPLT TAILAIGRLV AAQQPGTSTP EVHPKLTTYK CTTSGGCVAQ DTSVVLDWNY 

        70         80         90        100        110        120 
RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCYIEGVDYA ASGVTASGST LTLNQYMPSS 

       130        140        150        160        170        180 
SGGYSSVSPR LYLLGPDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ 

       190        200        210        220        230        240 
YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS GQGFCCNEMD ILEGNSRANA LTPHSCTATA 

       250        260        270        280        290        300 
CDSAGCGFNP YGSGYPNYFG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYRQNGV 

       310        320        330        340        350        360 
DIPSAKPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGRAGPC 

       370        380        390        400        410        420 
SSTEGNPSNI LANNPGTHVV YSNIRWGDIG STTNSTGGNP PPPPPPASST TFSTTRRSST 

       430        440        450        460 
TSSSPSCTQT HWGQCGGIGY TGCKTCTSGT TCQYGNDYYS QCL 

« Hide

References

[1]"Cloning, sequence analysis and yeast expression of the egl1 gene from Trichoderma longibrachiatum."
Gonzalez R., Ramon D., Perez-Gonzalez J.A.
Appl. Microbiol. Biotechnol. 38:370-375(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CECT 2606.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60652 Genomic DNA. Translation: CAA43059.1.
PIRA48375.

3D structure databases

ProteinModelPortalQ12714.
SMRQ12714. Positions 23-393, 428-463.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7A_TRILO.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN1_TRILO
AccessionPrimary (citable) accession number: Q12714
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries