Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q59Q79 (ALG1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:
Chitobiosyldiphosphodolichol beta-mannosyltransferase

EC=2.4.1.142
Alternative name(s):
Asparagine-linked glycosylation protein 1
Beta-1,4-mannosyltransferase
GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
Gene names
Name:ALG1
ORF Names:CaO19.4410, CaO19.11888
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man5 intermediate on the cytoplasmic surface of the ER By similarity.

Catalytic activity

GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase group 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Chitobiosyldiphosphodolichol beta-mannosyltransferase
PRO_0000080253

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain44 – 456413Lumenal Potential

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q59Q79 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 91C937DB823D4A11

FASTA45652,325
        10         20         30         40         50         60 
MGEIIKYKGF DHVWQYSGPW LYCLIGIYIS LPVLAYHILP WIFHKNRSNK RKTISIFVLG 

        70         80         90        100        110        120 
DLGHSPRMCY HASSFSKLDY YVNLCGYVET EPSHQIVDDV NIDIIPIEAI KNTNNLPYIM 

       130        140        150        160        170        180 
FAILKVVRQC GKIWSILWDT RGSDYIMIQN PPSIPILLIV ILFKTVFSRE TKLIIDWHNL 

       190        200        210        220        230        240 
NYTILNLRYN NLNHPFVKLV KLYEKILGQF ANLNITVTKS MKKYLVKEFG FQKSKIVTLY 

       250        260        270        280        290        300 
DRPGVQFQPL SNKREFMSEH KLFEDIDIEK YKVLISSTSF TPDEDFNILL DALKNYENTP 

       310        320        330        340        350        360 
NTPPILLIVT GKGPLKGKFL ETVDKLEFTN KVCVKSAWLS SEDYPKVLAC ADLGISLHTS 

       370        380        390        400        410        420 
SSGIDLPMKI VDFFGCGVPV VSLDFPAIDE LVKNKVNGLI TNSKSDQTKE VARLVTEVFT 

       430        440        450 
DDALLRSIKE GALEESNSRW DENWMQTFSS IFENKS 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000179 Genomic DNA. Translation: EAK92630.1.
AACQ01000178 Genomic DNA. Translation: EAK92650.1.
RefSeqXP_711858.1. XM_706765.1.
XP_723598.1. XM_718505.1.

3D structure databases

ProteinModelPortalQ59Q79.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ59Q79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3646517.
3646537.
KEGGcal:CaO19.11888.
cal:CaO19.4410.

Organism-specific databases

CGDCAL0001745. ALG1.

Phylogenomic databases

PhylomeDBQ59Q79.

Family and domain databases

InterProIPR001296. Glyco_trans_1.
[Graphical view]
KOK03842.
PfamPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALG1_CANAL
AccessionPrimary (citable) accession number: Q59Q79
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families