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Protein

N-terminal acetyltransferase A complex subunit NAT5

Gene

NAT5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Non-essential 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.

GO - Molecular functioni

  • peptide alpha-N-acetyltransferase activity Source: SGD

GO - Biological processi

  • N-terminal protein amino acid acetylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-33744-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-terminal acetyltransferase A complex subunit NAT5 (EC:2.3.1.-)
Short name:
NatA complex subunit NAT5
Gene namesi
Name:NAT5
Ordered Locus Names:YOR253W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR253W.
SGDiS000005779. NAT5.

Subcellular locationi

GO - Cellular componenti

  • NatA complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 176176N-terminal acetyltransferase A complex subunit NAT5PRO_0000240642Add
BLAST

Proteomic databases

MaxQBiQ08689.
PeptideAtlasiQ08689.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5.1 Publication

Protein-protein interaction databases

BioGridi34643. 24 interactions.
IntActiQ08689. 4 interactions.
MINTiMINT-2782295.

Structurei

3D structure databases

ProteinModelPortaliQ08689.
SMRiQ08689. Positions 8-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 176163N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000238056.
InParanoidiQ08689.
OMAiIAYYSEI.
OrthoDBiEOG7H79DC.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF13673. Acetyltransf_10. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRDICTLDN VYANNLGMLT KLAHVTVPNL YQDAFFSALF AEDSLVAKNK
60 70 80 90 100
KPSSKKDVHF TQMAYYSEIP VGGLVAKLVP KKQNELSLKG IQIEFLGVLP
110 120 130 140 150
NYRHKSIGSK LLKFAEDKCS ECHQHNVFVY LPAVDDLTKQ WFIAHGFEQV
160 170
GETVNNFIKG VNGDEQDAIL LKKHIS
Length:176
Mass (Da):19,727
Last modified:November 1, 1996 - v1
Checksum:i4F09DC597A690BA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75161 Genomic DNA. Translation: CAA99475.1.
AY557750 Genomic DNA. Translation: AAS56076.1.
BK006948 Genomic DNA. Translation: DAA11020.1.
PIRiS67150.
RefSeqiNP_014896.3. NM_001183672.3.

Genome annotation databases

EnsemblFungiiYOR253W; YOR253W; YOR253W.
GeneIDi854427.
KEGGisce:YOR253W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75161 Genomic DNA. Translation: CAA99475.1.
AY557750 Genomic DNA. Translation: AAS56076.1.
BK006948 Genomic DNA. Translation: DAA11020.1.
PIRiS67150.
RefSeqiNP_014896.3. NM_001183672.3.

3D structure databases

ProteinModelPortaliQ08689.
SMRiQ08689. Positions 8-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34643. 24 interactions.
IntActiQ08689. 4 interactions.
MINTiMINT-2782295.

Proteomic databases

MaxQBiQ08689.
PeptideAtlasiQ08689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR253W; YOR253W; YOR253W.
GeneIDi854427.
KEGGisce:YOR253W.

Organism-specific databases

EuPathDBiFungiDB:YOR253W.
SGDiS000005779. NAT5.

Phylogenomic databases

HOGENOMiHOG000238056.
InParanoidiQ08689.
OMAiIAYYSEI.
OrthoDBiEOG7H79DC.

Enzyme and pathway databases

BioCyciYEAST:G3O-33744-MONOMER.

Miscellaneous databases

PROiQ08689.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF13673. Acetyltransf_10. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides."
    Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y., Ehrenhofer-Murray A., Rospert S.
    Mol. Cell. Biol. 23:7403-7414(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NATA COMPLEX.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNAT5_YEAST
AccessioniPrimary (citable) accession number: Q08689
Secondary accession number(s): D6W2V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2370 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.