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 27-MAR-2024, entry version 179. 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; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 273. 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; 4932-YPR051W; -. DR PeptideAtlas; Q03503; -. DR EnsemblFungi; YPR051W_mRNA; YPR051W; YPR051W. DR GeneID; 856163; -. DR KEGG; sce:YPR051W; -. DR AGR; SGD:S000006255; -. 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; LCIFARH; -. DR OrthoDB; 20718at2759; -. DR BioCyc; YEAST:YPR051W-MONOMER; -. DR BRENDA; 2.3.1.256; 984. DR BioGRID-ORCS; 856163; 0 hits in 10 CRISPR screens. 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:0006474; P:N-terminal protein amino acid acetylation; IMP:SGD. DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR044542; NAA30-like. DR PANTHER; PTHR45896; N-ALPHA-ACETYLTRANSFERASE 30; 1. DR PANTHER; PTHR45896:SF1; N-ALPHA-ACETYLTRANSFERASE 30; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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 //