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P23044 (GUN_ROBSP) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Carboxymethyl-cellulase I
Short name=CMCase I
Endo-1,4-beta-glucanase
Endoglucanase I
Gene names
Name:eg 1
OrganismRobillarda sp. (strain Y-20)
Taxonomic identifier72589 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotamitosporic AscomycotaRobillarda

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active towards carboxymethyl cellulose.

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Sequence caution

The sequence described in Ref.2 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 1717 Ref.2
Chain18 – 385368Endoglucanase 1
PRO_0000184049

Sites

Active site1761Proton donor By similarity
Active site2841Nucleophile By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2371N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict27 – 282SS → GN AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P23044 [UniParc].

Last modified February 20, 2007. Version 2.
Checksum: 149604D42369AD33

FASTA38541,428
        10         20         30         40         50         60 
MKLVFSALAS LLSGASATIY YAGVAESSGE FGVWSATQTP GTGLPGRFGV DYAFISEAAV 

        70         80         90        100        110        120 
DVHVDQNHLN LFRVAFLLER MCPPATGLGA AFNETHFDYF KEAVDYITVT KGAYAILDPH 

       130        140        150        160        170        180 
NYMRYNDPSY QPFSGSVIGN TSDSTAATTE QFGEFWGELA SRFNDNERVI FGLMNEPHDM 

       190        200        210        220        230        240 
ATSLVLANNQ AAIDAIRAAN ASNLIIMPGN SWTGGHSWTE GSDPSSALLN QFKDPLNNTA 

       250        260        270        280        290        300 
IDIHEYLDYD FSGGHLECVS DPETNLAALT AWLKENNLKA FITEFGGSNS TSCQEMLPDL 

       310        320        330        340        350        360 
INYMADNAEY IGWTAWAAGP FWGPNSPCCT NSTQLGSLEP GSTAVDGSPG LYDTVWLPVI 

       370        380 
QPLVPTELQW SGPASISGGE LTSRA 

« Hide

References

[1]"Endoglucanase gene from cellulolytic fungi, Robillarda sp. Y-20."
Kashiwagi Y.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and sequencing of the endo-cellulase cDNA from Robillarda sp. Y-20."
Yoshigi N., Taniguchi H., Sasaki T.
J. Biochem. 108:388-392(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-385, PROTEIN SEQUENCE OF 18-35.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB030819 Genomic DNA. Translation: BAA90480.1.

3D structure databases

ProteinModelPortalP23044.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.
mycoCLAPEGL5A_ROBSP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN_ROBSP
AccessionPrimary (citable) accession number: P23044
Secondary accession number(s): Q9P981
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 20, 2007
Last modified: October 16, 2013
This is version 72 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries