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Q9UTI3 (ARD1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N-terminal acetyltransferase A complex catalytic subunit ard1
Short name=NatA complex subunit ARD1
EC=2.3.1.88
Gene names
Name:ard1
ORF Names:SPAC15E1.08
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover By similarity.

Catalytic activity

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.

Subunit structure

Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of at least ard1 and nat1 By similarity.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the acetyltransferase family. ARD1 subfamily.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processN-terminal peptidyl-methionine acetylation

Inferred by curator. Source: GeneDB_Spombe

   Cellular componentNatA complex

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

cytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionpeptide alpha-N-acetyltransferase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177N-terminal acetyltransferase A complex catalytic subunit ard1
PRO_0000310300

Regions

Domain1 – 153153N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
Q9UTI3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: ABE46773A259B82B

FASTA17720,305
        10         20         30         40         50         60 
MDIRPARISD LTGMQNCNLH NLPENYQLKY YLYHAISWPM LSYVATDPKG RVVGYVLAKM 

        70         80         90        100        110        120 
EEEPKDGIPH GHITSVSVMR SYRHLGLAKR LMVQSQRAMV EVYGAKYMSL HVRKSNRAAI 

       130        140        150        160        170 
HLYRDTLQFD VQGIESKYYA DGEDAYAMHK DFSTLKFDTP ETNDELAKTV QSLALNN

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB52427.1.
PIRT37723.
RefSeqNP_594309.1. NM_001019732.1.

3D structure databases

ProteinModelPortalQ9UTI3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9UTI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC15E1.08.1; SPAC15E1.08.1:pep; SPAC15E1.08.
GeneID2542765.
GenomeReviewsGene locus ard1 in contig CU329670_GR.
KEGGspo:SPAC15E1.08.
NMPDRfig|4896.1.peg.4279.

Organism-specific databases

GeneDB_SpombeSPAC15E1.08.

Phylogenomic databases

eggNOGfuNOG08135.
GeneTreeEFGT00050000003150.
HOGENOMHBG742014.
OMAMVENFGA.
OrthoDBEOG4SXRNS.

Gene expression databases

ArrayExpressQ9UTI3.

Family and domain databases

InterProIPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KOK00670.
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARD1_SCHPO
AccessionPrimary (citable) accession number: Q9UTI3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

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