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Reviewed, UniProtKB/Swiss-Prot Q8J0Q0 (MNS1_CANAL)

Last modified January 19, 2010. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase
    EC=3.2.1.113
Alternative name(s):
    Man(9)-alpha-mannosidase
Gene names
Name: MNS1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Involved in the maturation of Asn-linked oligosaccharides. Trim a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 By similarity.

Catalytic activity

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Cofactor

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

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Ontologies

Keywords
   LigandCalcium
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Mannosyl-oligosaccharide 1,2-alpha-mannosidase
PRO_0000210318

Amino acid modifications

Disulfide bond320 ↔ 363 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8J0Q0-1 [UniParc].

Last modified October 1, 2003. Version 2.
Checksum: C3581A0D889CCAF2

FASTA56564,659
        10         20         30         40         50         60 
MLLKGFMLSL VLYAVYHLAS NGGQFMFDFS GQSKWERAQS EVRQAILDSW HTYEKYGWGY 

        70         80         90        100        110        120 
DVYHPIKQEG ENMGPKPLGW MIVDSLDTLM IMDCPEEVSR ARDWIKNDLD YTFDYNVNTF 

       130        140        150        160        170        180 
ETTIRMLGGL LSAYHFSNDD VYLDKAVQLA NALHGAYDSP SGIPYSSVNL KSGKGIKNHV 

       190        200        210        220        230        240 
DNGASSTAEA ATVQLEMKYL SKLTGEILWW NLAEKVMQVL ESNKPQDGLV PIYVNPDTGK 

       250        260        270        280        290        300 
YQGHLIRLGS RGDSYYEYLL KQYLQTNKQE LVYWDMYRES VEGVKKHLVS DSYPSGLTFI 

       310        320        330        340        350        360 
GELDNGIGGK LSTKMDHLVC FYGGLLALGA TGGLTLNEAQ SLKSWNEERE ADFKLGEELT 

       370        380        390        400        410        420 
YTCYKMYHDV SPTGLSPEIV VFNEDTSKSK DFIIKPLDRH NLQRPETVES LFYLYRLTGD 

       430        440        450        460        470        480 
VKYREMGYEI FQNFIKYTKV VNSEGEVSFS SLSDVTSFDS NGLPKFKDNT ESFWWAETLK 

       490        500        510        520        530        540 
YLYLLFDDTN KIPLTDYVFN TEAHPFPRFD TNDYFKTGWR RKIDENEKAQ MRESKVIDKS 

       550        560 
NLPEAQPVDK SADQEAKEII EEIAG

« Hide

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References

[1]"Identification of the alpha1,2-mannosidase gene (Mns1) in Candida albicans."
Mora-Montes H.M., Flores-Carreon A., Ponce-Noyola P., Lopez-Romero E., Zinker-Ruzal S.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26555.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY167027 Genomic DNA. Translation: AAN86059.2.

3D structure databases

SMRQ8J0Q0. Positions 38-520.
ModBaseSearch...

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Enzyme and pathway databases

BRENDA3.2.1.113. 1124.

Family and domain databases

InterProIPR001382. Glyco_hydro_47.
[Graphical view]
Gene3DG3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
PANTHERPTHR11742. Glyco_hydro_47. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
ProtoNetSearch...

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Entry information

Entry nameMNS1_CANAL
AccessionPrimary (citable) accession number: Q8J0Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2003
Last modified: January 19, 2010
This is version 34 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents