Q03503 (NAA30_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-alpha-acetyltransferase 30
EC=2.3.1.88

Alternative name(s):
L-A virus GAG protein N-acetyltransferase subunit MAK3
Maintenance of killer protein 3
N-terminal acetyltransferase C complex catalytic subunit MAK3
Short name=NatC complex subunit MAK3
NatC catalytic subunit

Gene names

Name:	MAK3
Synonyms:	NAA30
Ordered Locus Names:	YPR051W
ORF Names:	YP9499.08

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus Gag protein. Ref.5
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of MAK3, MAK10 and MAK31. Ref.5
Subcellular location	Cytoplasm. Nucleus Ref.6.
Miscellaneous	Present with 1940 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the acetyltransferase family. MAK3 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal protein amino acid acetylation Inferred from mutant phenotype Ref.5. Source: SGD
Cellular_component	NatC complex Inferred from direct assay PubMed 10504710. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptide alpha-N-acetyltransferase activity Inferred from mutant phenotype Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAK10	Q02197	5	EBI-10388,EBI-10924

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 176	176	N-alpha-acetyltransferase 30		PRO_0000074560
Regions
	Domain	3 – 159	157	N-acetyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q03503 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: DFBF10376FE89913	FASTA	176	20,457
	10 20 30 40 50 60 MEIVYKPLDI RNEEQFASIK KLIDADLSEP YSIYVYRYFL NQWPELTYIA VDNKSGTPNI 70 80 90 100 110 120 PIGCIVCKMD PHRNVRLRGY IGMLAVESTY RGHGIAKKLV EIAIDKMQRE HCDEIMLETE 130 140 150 160 170 VENSAALNLY EGMGFIRMKR MFRYYLNEGD AFKLILPLTE KSCTRSTFLM HGRLAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2 terminus is necessary for virus particle assembly." Tercero J.C., Wickner R.B. J. Biol. Chem. 267:20277-20281(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae." Tercero J.C., Riles L.E., Wickner R.B. J. Biol. Chem. 267:20270-20276(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[5]	"NatC Nalpha-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p." Polevoda B., Sherman F. J. Biol. Chem. 276:20154-20159(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE NATC COMPLEX, FUNCTION OF THE NATC COMPLEX.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M95912 Genomic RNA. Translation: AAA34753.1. Z49219 Genomic DNA. Translation: CAA89170.1. Z71255 Genomic DNA. Translation: CAA94997.1. BK006949 Genomic DNA. Translation: DAA11474.1.
PIR	B44031.
RefSeq	NP_015376.1. NM_001184148.1.
3D structure databases
ProteinModelPortal	Q03503.
SMR	Q03503. Positions 4-144.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1427N.
IntAct	Q03503. 4 interactions.
MINT	MINT-383720.
STRING	4932.YPR051W.
Proteomic databases
PaxDb	Q03503.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPR051W; YPR051W; YPR051W.
GeneID	856163.
KEGG	sce:YPR051W.
Organism-specific databases
CYGD	YPR051w.
SGD	S000006255. MAK3.
Phylogenomic databases
eggNOG	COG0456.
GeneTree	ENSGT00390000005665.
HOGENOM	HOG000196601.
KO	K00670.
OMA	LAVESTY.
OrthoDB	EOG4X3M9V.
Gene expression databases
Genevestigator	Q03503.
GermOnline	YPR051W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	981310.

Entry information

Entry name

NAA30_YEAST

Accession

Primary (citable) accession number: Q03503
Secondary accession number(s): D6W458

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program