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Protein

N-terminal acetyltransferase A complex catalytic subunit ard1

Gene

ard1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

  • peptide alpha-N-acetyltransferase activity Source: PomBase
  • peptide-glutamate-N-acetyltransferase activity Source: PomBase
  • peptide-serine-N-acetyltransferase activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
N-terminal acetyltransferase A complex catalytic subunit ard1 (EC:2.3.1.88)
Short name:
NatA complex subunit ARD1
Gene namesi
Name:ard1
ORF Names:SPAC15E1.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC15E1.08.
PomBaseiSPAC15E1.08.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • cytosolic ribosome Source: GO_Central
  • NatA complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177N-terminal acetyltransferase A complex catalytic subunit ard1PRO_0000310300Add
BLAST

Proteomic databases

MaxQBiQ9UTI3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi279215. 2 interactions.
DIPiDIP-60549N.
MINTiMINT-4710538.

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi8 – 103Combined sources
Helixi11 – 166Combined sources
Turni17 – 204Combined sources
Helixi22 – 254Combined sources
Helixi28 – 369Combined sources
Beta strandi43 – 464Combined sources
Beta strandi52 – 609Combined sources
Helixi65 – 673Combined sources
Beta strandi71 – 788Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 863Combined sources
Helixi87 – 10317Combined sources
Beta strandi106 – 1138Combined sources
Helixi117 – 1248Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi145 – 1517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KVMX-ray2.60E/F/G/H1-156[»]
4KVOX-ray3.15E/F/G/H1-156[»]
4KVXX-ray2.00A/B1-156[»]
ProteinModelPortaliQ9UTI3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 153153N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000078523.
InParanoidiQ9UTI3.
KOiK00670.
OMAiAHMADEV.
OrthoDBiEOG71K6FX.
PhylomeDBiQ9UTI3.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UTI3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIRPARISD LTGMQNCNLH NLPENYQLKY YLYHAISWPM LSYVATDPKG
60 70 80 90 100
RVVGYVLAKM EEEPKDGIPH GHITSVSVMR SYRHLGLAKR LMVQSQRAMV
110 120 130 140 150
EVYGAKYMSL HVRKSNRAAI HLYRDTLQFD VQGIESKYYA DGEDAYAMHK
160 170
DFSTLKFDTP ETNDELAKTV QSLALNN
Length:177
Mass (Da):20,305
Last modified:May 1, 2000 - v1
Checksum:iABE46773A259B82B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52427.1.
PIRiT37723.
RefSeqiNP_594309.1. NM_001019732.2.

Genome annotation databases

EnsemblFungiiSPAC15E1.08.1; SPAC15E1.08.1:pep; SPAC15E1.08.
GeneIDi2542765.
KEGGispo:SPAC15E1.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52427.1.
PIRiT37723.
RefSeqiNP_594309.1. NM_001019732.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KVMX-ray2.60E/F/G/H1-156[»]
4KVOX-ray3.15E/F/G/H1-156[»]
4KVXX-ray2.00A/B1-156[»]
ProteinModelPortaliQ9UTI3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279215. 2 interactions.
DIPiDIP-60549N.
MINTiMINT-4710538.

Proteomic databases

MaxQBiQ9UTI3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC15E1.08.1; SPAC15E1.08.1:pep; SPAC15E1.08.
GeneIDi2542765.
KEGGispo:SPAC15E1.08.

Organism-specific databases

EuPathDBiFungiDB:SPAC15E1.08.
PomBaseiSPAC15E1.08.

Phylogenomic databases

HOGENOMiHOG000078523.
InParanoidiQ9UTI3.
KOiK00670.
OMAiAHMADEV.
OrthoDBiEOG71K6FX.
PhylomeDBiQ9UTI3.

Miscellaneous databases

PROiQ9UTI3.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARD1_SCHPO
AccessioniPrimary (citable) accession number: Q9UTI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.