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P49713 (FUCO_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. 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:
Putative alpha-L-fucosidase

EC=3.2.1.51
Alternative name(s):
Alpha-L-fucoside fucohydrolase
Gene names
ORF Names:W03G11.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins By similarity.

Catalytic activity

An alpha-L-fucoside + H2O = L-fucose + an alcohol.

Sequence similarities

Belongs to the glycosyl hydrolase 29 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfucose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-L-fucosidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

fucose binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 482466Putative alpha-L-fucosidase
PRO_0000010316

Sites

Site2761May be important for catalysis By similarity

Amino acid modifications

Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P49713 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 8818D452AD261A5D

FASTA48256,460
        10         20         30         40         50         60 
MIFLIFSILF LHLANCDYTP DWESLDNRPL PSWYDDSKFG IFCHWGLYSV PAFRSEWMWW 

        70         80         90        100        110        120 
YWKGTQPDKD VVNFVDKNYK PGTTYADFAK DFTAEYFNAN QFAETVKTSG ARYFVFTSKH 

       130        140        150        160        170        180 
HEGFTMWPSR TSWNWNSMDI GPKRDIVGEL RDAFKKTDVH FGLYFSQFEW FHPMFLDDGK 

       190        200        210        220        230        240 
FNTTFYPEQV SYPQMIDIVT KYNPEVVWSD GEWDKSDDYW KAKEFLAWLY NSSPVKDQVV 

       250        260        270        280        290        300 
VNDRWGTGTM GKHGGFMTYS DHYDPGKLLE KKWENCMTLD KHSWGNRRDM KASEVNTAYE 

       310        320        330        340        350        360 
IIEQLARTIA CNGNLLLNVG PNMHGQIPAI FEDRLEEIGR FVNITSEAIF GTRPWIHQND 

       370        380        390        400        410        420 
TSASNVWYTS KYSSGKKPLK NLYQNVYNFQ LEEHTIVYAW ILDTSHEQFE LKSVKTTKNT 

       430        440        450        460        470        480 
TATILGTDVV LTGFEESDSM IILSSKIDWK KLPRRDIIVL KIEKAASYLR NPLMSTNEHH 


VQ 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67738 Genomic DNA. Translation: CAA91546.2.
PIRT26127.
RefSeqNP_510020.2. NM_077619.3.
UniGeneCel.24951.

3D structure databases

ProteinModelPortalP49713.
SMRP49713. Positions 17-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.W03G11.3.

Protein family/group databases

CAZyGH29. Glycoside Hydrolase Family 29.

Proteomic databases

PaxDbP49713.
PRIDEP49713.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaW03G11.3; W03G11.3; W03G11.3.
GeneID189173.
KEGGcel:CELE_W03G11.3.
UCSCW03G11.3. c. elegans.

Organism-specific databases

CTD189173.
WormBaseW03G11.3; CE37417; WBGene00012225.

Phylogenomic databases

eggNOGCOG3669.
HOGENOMHOG000029598.
InParanoidP49713.
KOK01206.
OMAQFTAEFF.
OrthoDBEOG7DC249.
PhylomeDBP49713.

Enzyme and pathway databases

BRENDA3.2.1.51. 1045.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR016286. FUC_metazoa-typ.
IPR000933. Glyco_hydro_29.
IPR018526. Glyco_hydro_29_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10030. PTHR10030. 1 hit.
PfamPF01120. Alpha_L_fucos. 1 hit.
[Graphical view]
PIRSFPIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSPR00741. GLHYDRLASE29.
SMARTSM00812. Alpha_L_fucos. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00385. ALPHA_L_FUCOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio941460.
PROP49713.

Entry information

Entry nameFUCO_CAEEL
AccessionPrimary (citable) accession number: P49713
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase