NAA30_YEAST
ID NAA30_YEAST Reviewed; 176 AA.
AC Q03503; D6W458;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=N-alpha-acetyltransferase 30;
DE EC=2.3.1.256 {ECO:0000250|UniProtKB:Q147X3};
DE AltName: Full=L-A virus GAG protein N-acetyltransferase subunit MAK3;
DE AltName: Full=Maintenance of killer protein 3;
DE AltName: Full=N-terminal acetyltransferase C complex catalytic subunit MAK3;
DE Short=NatC complex subunit MAK3;
DE AltName: Full=NatC catalytic subunit;
GN Name=MAK3; Synonyms=NAA30; OrderedLocusNames=YPR051W; ORFNames=YP9499.08;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400344; DOI=10.1016/s0021-9258(19)88697-0;
RA Tercero J.C., Wickner R.B.;
RT "MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2
RT terminus is necessary for virus particle assembly.";
RL J. Biol. Chem. 267:20277-20281(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP MUTAGENESIS.
RX PubMed=1339437; DOI=10.1016/s0021-9258(19)88696-9;
RA Tercero J.C., Riles L.E., Wickner R.B.;
RT "Localized mutagenesis and evidence for post-transcriptional regulation of
RT MAK3. A putative N-acetyltransferase required for double-stranded RNA virus
RT propagation in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:20270-20276(1992).
RN [5]
RP IDENTIFICATION IN THE NATC COMPLEX, AND FUNCTION OF THE NATC COMPLEX.
RX PubMed=11274203; DOI=10.1074/jbc.m011440200;
RA Polevoda B., Sherman F.;
RT "NatC Nalpha-terminal acetyltransferase of yeast contains three subunits,
RT Mak3p, Mak10p, and Mak31p.";
RL J. Biol. Chem. 276:20154-20159(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=17261844; DOI=10.1083/jcb.200607151;
RA Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.;
RT "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein
RT that contributes to ER to Golgi traffic.";
RL J. Cell Biol. 176:255-261(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalytic component of the NatC N-terminal acetyltransferase,
CC which catalyzes acetylation of the N-terminus Met of L-A virus GAG
CC protein and possibly GRH1. {ECO:0000269|PubMed:11274203,
CC ECO:0000269|PubMed:17261844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-
CC [protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-
CC COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-
CC [protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-
CC COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC complex, which is composed of MAK3, MAK10 and MAK31.
CC {ECO:0000269|PubMed:11274203}.
CC -!- INTERACTION:
CC Q03503; Q02197: MAK10; NbExp=3; IntAct=EBI-10388, EBI-10924;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily.
CC {ECO:0000305}.
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DR EMBL; M95912; AAA34753.1; -; Genomic_RNA.
DR EMBL; Z49219; CAA89170.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94997.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11474.1; -; Genomic_DNA.
DR PIR; B44031; B44031.
DR RefSeq; NP_015376.1; NM_001184148.1.
DR PDB; 6YGA; X-ray; 2.40 A; A=1-159.
DR PDB; 6YGB; X-ray; 2.45 A; A=1-159.
DR PDB; 6YGC; X-ray; 2.99 A; A=1-159.
DR PDB; 6YGD; X-ray; 2.75 A; A=1-159.
DR PDBsum; 6YGA; -.
DR PDBsum; 6YGB; -.
DR PDBsum; 6YGC; -.
DR PDBsum; 6YGD; -.
DR AlphaFoldDB; Q03503; -.
DR SMR; Q03503; -.
DR BioGRID; 36226; 270.
DR ComplexPortal; CPX-781; NatC N-alpha-acetyltransferase complex.
DR DIP; DIP-1427N; -.
DR IntAct; Q03503; 5.
DR MINT; Q03503; -.
DR STRING; 4932.YPR051W; -.
DR iPTMnet; Q03503; -.
DR MaxQB; Q03503; -.
DR PaxDb; Q03503; -.
DR PRIDE; Q03503; -.
DR EnsemblFungi; YPR051W_mRNA; YPR051W; YPR051W.
DR GeneID; 856163; -.
DR KEGG; sce:YPR051W; -.
DR SGD; S000006255; MAK3.
DR VEuPathDB; FungiDB:YPR051W; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00390000005665; -.
DR HOGENOM; CLU_013985_0_3_1; -.
DR InParanoid; Q03503; -.
DR OMA; HELSEPY; -.
DR BioCyc; YEAST:YPR051W-MON; -.
DR BRENDA; 2.3.1.256; 984.
DR PRO; PR:Q03503; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03503; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031417; C:NatC complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IMP:SGD.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR044542; NAA30-like.
DR PANTHER; PTHR45896; PTHR45896; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..176
FT /note="N-alpha-acetyltransferase 30"
FT /id="PRO_0000074560"
FT DOMAIN 3..159
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 55..72
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6YGA"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:6YGA"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6YGA"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:6YGA"
SQ SEQUENCE 176 AA; 20457 MW; DFBF10376FE89913 CRC64;
MEIVYKPLDI RNEEQFASIK KLIDADLSEP YSIYVYRYFL NQWPELTYIA VDNKSGTPNI
PIGCIVCKMD PHRNVRLRGY IGMLAVESTY RGHGIAKKLV EIAIDKMQRE HCDEIMLETE
VENSAALNLY EGMGFIRMKR MFRYYLNEGD AFKLILPLTE KSCTRSTFLM HGRLAT
