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P22669 (GUN_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 78. 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-1

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Endoglucanase I
FI-CMCase
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Secreted.

Induction

By cellulosic materials and hemicelluloses.

Miscellaneous

Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMPyrrolidone carboxylic acid
   Technical termDirect protein sequencing
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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 237221Endoglucanase-1
PRO_0000008018

Amino acid modifications

Modified residue171Pyrrolidone carboxylic acid Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22669 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 8F173571A8AE6931

FASTA23725,560
        10         20         30         40         50         60 
MKAFHLLAAL AGAAVAQQAQ LCDQYATYTG GVYTINNNLW GKDAGSGSQC TTVNSASSAG 

        70         80         90        100        110        120 
TSWSTKWNWS GGENSVKSYA NSGLTFNKKL VSQISQIPTT ARWSYDNTGI RADVAYDLFT 

       130        140        150        160        170        180 
AADINHVTWS GDYELMIWLA RYGGVQPIGS QIATATVDGQ TWELWYGANG SQKTYSFVAP 

       190        200        210        220        230 
TPITSFQGDV NDFFKYLTQN HGFPASSQYL ITLQFGTEPF TGGPATLSVS NWSASVQ 

« Hide

References

[1]"Complete nucleotide sequence of a gene coding for Aspergillus aculeatus cellulase (FI-CMCase)."
Ooi T., Shinmyo A., Okada H., Murao S., Kawaguchi T., Arai M.
Nucleic Acids Res. 18:5884-5884(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: F-50.
[2]"Cloning and sequence analysis of a cDNA for cellulase (FI-CMCase) from Aspergillus aculeatus."
Ooi T., Shinmyo A., Okada H., Hara S., Ikenaka T., Murao S., Arai M.
Curr. Genet. 18:217-222(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: F-50.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00546 Genomic DNA. Translation: BAA00435.1.
X52525 mRNA. Translation: CAA36757.1.
PIRS12610.

3D structure databases

ProteinModelPortalP22669.
SMRP22669. Positions 21-236.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH12. Glycoside Hydrolase Family 12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013319. Glyco_hydro_11/12.
IPR002594. Glyco_hydro_12.
[Graphical view]
PfamPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGUN_ASPAC
AccessionPrimary (citable) accession number: P22669
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 13, 2013
This is version 78 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