Reviewed, UniProtKB/Swiss-Prot Q9UTI3 (ARD1_SCHPO)

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	peptide alpha-N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 177	177	N-terminal acetyltransferase A complex catalytic subunit ard1		PRO_0000310300
Regions
	Domain	1 – 153	153	N-acetyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q9UTI3-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: ABE46773A259B82B	FASTA	177	20,305
	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

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. , 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: ATCC 38366 / 972.

[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.
PIR	T37723.
RefSeq	NP_594309.1.
3D structure databases
SMR	Q9UTI3. Positions 1-151.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UTI3.
Genome annotation databases
GeneID	2542765.
GenomeReviews	Gene locus ard1 in contig CU329670_GR.
KEGG	spo:SPAC15E1.08.
NMPDR	fig|4896.1.peg.4279.
Organism-specific databases
GeneDB_Spombe	SPAC15E1.08.
Phylogenomic databases
eggNOG	fuNOG08135.
HOGENOM	HBG742014.
OMA	SWPEASF.
OrthoDB	EOG951G72.
PhylomeDB	Q9UTI3.
Enzyme and pathway databases
BRENDA	2.3.1.88. 653.
Gene expression databases
ArrayExpress	Q9UTI3.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GCN5-rel_AcTrfase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARD1_SCHPO

Accession

Primary (citable) accession number: Q9UTI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 2000
Last modified:	January 19, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)