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P38534 (GUNX_PRUPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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 CX

EC=3.2.1.4
Alternative name(s):
CX-cellulase
Endo-1,4-beta-glucanase
OrganismPrunus persica (Peach) (Amygdalus persica)
Taxonomic identifier3760 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Protein attributes

Sequence length251 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Degrades carboxymethylcellulose (CMC).

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›251›251Endoglucanase CX
PRO_0000184060

Experimental info

Non-terminal residue11
Non-terminal residue2511

Sequences

Sequence LengthMass (Da)Tools
P38534 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 653185E0F4763EAC

FASTA25127,476
        10         20         30         40         50         60 
PEDMDTPRNV YKVSTQNPGS DVAAETAAAL AAASIVFKDS DPSYSGKLLH TAMKVFDFAD 

        70         80         90        100        110        120 
RYRGSYSDSI GSVVCPFYCS YSGHHDELLW GASWIHRASQ NRSYLVYIKS NGHILGEDDD 

       130        140        150        160        170        180 
GFSASWDDKE TGTKVLLVSK SFLERHVEEF QLYKAHSGNY ICSLLPGTSN FQGQYTPGGL 

       190        200        210        220        230        240 
LYKASESNLQ YVTSTTLLLL TYAKYLRTNG GVATCGSSKV TAETLISEAK KQVDYILGNN 

       250 
PAKISYMVGF G 

« Hide

References

[1]Bonghi C., Tonutti P., Ramina A.
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Redhaven.
Tissue: Abscission zone.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z23119 mRNA. Translation: CAA80665.1.
PIRS39202.

3D structure databases

ProteinModelPortalP38534.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
[Graphical view]
PfamPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGUNX_PRUPE
AccessionPrimary (citable) accession number: P38534
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries