ID   ARD1_YEAST              Reviewed;         238 AA.
AC   P07347; D3DKV8;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=N-terminal acetyltransferase A complex catalytic subunit ARD1;
DE            Short=NatA complex subunit ARD1;
DE            EC=2.3.1.255 {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
DE   AltName: Full=Arrest-defective protein 1;
GN   Name=ARD1; OrderedLocusNames=YHR013C;
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=3907857; DOI=10.1016/0092-8674(85)90178-3;
RA   Whiteway M., Szostak J.W.;
RT   "The ARD1 gene of yeast functions in the switch between the mitotic cell
RT   cycle and alternative developmental pathways.";
RL   Cell 43:483-492(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=2551674; DOI=10.1002/j.1460-2075.1989.tb03615.x;
RA   Mullen J.R., Kayne P.S., Moerschell R.P., Tsunasawa S., Gribskov M.,
RA   Colavito-Shepanski M., Grunstein M., Sherman F., Sternglanz R.;
RT   "Identification and characterization of genes and mutants for an N-terminal
RT   acetyltransferase from yeast.";
RL   EMBO J. 8:2067-2075(1989).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NAT1, AND SELF-ASSOCIATION.
RX   PubMed=1600941; DOI=10.1002/j.1460-2075.1992.tb05267.x;
RA   Park E.C., Szostak J.W.;
RT   "ARD1 and NAT1 proteins form a complex that has N-terminal
RT   acetyltransferase activity.";
RL   EMBO J. 11:2087-2093(1992).
RN   [7]
RP   IDENTIFICATION IN THE NATA COMPLEX.
RX   PubMed=14517307; DOI=10.1128/mcb.23.20.7403-7414.2003;
RA   Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y.,
RA   Ehrenhofer-Murray A., Rospert S.;
RT   "The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to
RT   the ribosome and interacts with nascent polypeptides.";
RL   Mol. Cell. Biol. 23:7403-7414(2003).
RN   [8]
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   [9]
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).
CC   -!- FUNCTION: Catalytic component of the NatA N-terminal acetyltransferase,
CC       which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly
CC       and Met-Ala. N-acetylation plays a role in normal eukaryotic
CC       translation and processing, protect against proteolytic degradation and
CC       protein turnover. {ECO:0000269|PubMed:1600941,
CC       ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC         Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC         ChEBI:CHEBI:133369; EC=2.3.1.255;
CC         Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC         Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC         ChEBI:CHEBI:83683; EC=2.3.1.255;
CC         Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC         Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC         ChEBI:CHEBI:83690; EC=2.3.1.255;
CC         Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC         Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC         ChEBI:CHEBI:133371; EC=2.3.1.255;
CC         Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC         N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC         Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC         Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC         ChEBI:CHEBI:133375; EC=2.3.1.255;
CC         Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC       complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate.
CC       {ECO:0000269|PubMed:14517307}.
CC   -!- INTERACTION:
CC       P07347; P07347: ARD1; NbExp=2; IntAct=EBI-2796, EBI-2796;
CC       P07347; P12945: NAT1; NbExp=10; IntAct=EBI-2796, EBI-11868;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 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; M11621; AAA66323.1; -; Genomic_DNA.
DR   EMBL; U10400; AAB68937.1; -; Genomic_DNA.
DR   EMBL; AY557822; AAS56148.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06702.1; -; Genomic_DNA.
DR   PIR; S46783; TWBYA1.
DR   RefSeq; NP_011877.1; NM_001179143.1.
DR   PDB; 4HNW; X-ray; 2.80 A; B=1-238.
DR   PDB; 4HNX; X-ray; 2.34 A; B=1-238.
DR   PDB; 4HNY; X-ray; 2.25 A; B/D=1-238.
DR   PDB; 4XNH; X-ray; 2.10 A; B=1-238.
DR   PDB; 4XPD; X-ray; 2.81 A; B=1-238.
DR   PDB; 4Y49; X-ray; 3.95 A; B/H/N=1-238.
DR   PDB; 6HD5; EM; 4.80 A; u=1-238.
DR   PDB; 6HD7; EM; 3.40 A; u=1-238.
DR   PDB; 6O07; X-ray; 2.70 A; B=1-238.
DR   PDBsum; 4HNW; -.
DR   PDBsum; 4HNX; -.
DR   PDBsum; 4HNY; -.
DR   PDBsum; 4XNH; -.
DR   PDBsum; 4XPD; -.
DR   PDBsum; 4Y49; -.
DR   PDBsum; 6HD5; -.
DR   PDBsum; 6HD7; -.
DR   PDBsum; 6O07; -.
DR   AlphaFoldDB; P07347; -.
DR   EMDB; EMD-0201; -.
DR   EMDB; EMD-0202; -.
DR   SMR; P07347; -.
DR   BioGRID; 36440; 376.
DR   ComplexPortal; CPX-783; NatA N-alpha-acetyltransferase complex.
DR   DIP; DIP-6788N; -.
DR   IntAct; P07347; 32.
DR   MINT; P07347; -.
DR   STRING; 4932.YHR013C; -.
DR   MaxQB; P07347; -.
DR   PaxDb; 4932-YHR013C; -.
DR   PeptideAtlas; P07347; -.
DR   EnsemblFungi; YHR013C_mRNA; YHR013C; YHR013C.
DR   GeneID; 856404; -.
DR   KEGG; sce:YHR013C; -.
DR   AGR; SGD:S000001055; -.
DR   SGD; S000001055; ARD1.
DR   VEuPathDB; FungiDB:YHR013C; -.
DR   eggNOG; KOG3235; Eukaryota.
DR   GeneTree; ENSGT00940000174781; -.
DR   HOGENOM; CLU_013985_7_2_1; -.
DR   InParanoid; P07347; -.
DR   OMA; MSMQNAN; -.
DR   OrthoDB; 275667at2759; -.
DR   BioCyc; YEAST:YHR013C-MONOMER; -.
DR   BRENDA; 2.3.1.255; 984.
DR   BRENDA; 2.3.1.258; 984.
DR   BioGRID-ORCS; 856404; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P07347; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P07347; Protein.
DR   GO; GO:0031415; C:NatA complex; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:1990190; F:peptide-glutamate-alpha-N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:1990189; F:peptide-serine-alpha-N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:SGD.
DR   GO; GO:0061606; P:N-terminal protein amino acid propionylation; IMP:SGD.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR045047; Ard1-like.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR23091; N-TERMINAL ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR23091:SF4; N-TERMINAL AMINO-ACID N(ALPHA)-ACETYLTRANSFERASE NATA; 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; Reference proteome; Transferase.
FT   CHAIN           1..238
FT                   /note="N-terminal acetyltransferase A complex catalytic
FT                   subunit ARD1"
FT                   /id="PRO_0000074529"
FT   DOMAIN          35..195
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   CONFLICT        37
FT                   /note="I -> T (in Ref. 1; AAA66323)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           13..23
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:4HNY"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   STRAND          45..49
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:4HNY"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:4HNY"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   STRAND          90..100
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:4HNX"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:4HNW"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           129..145
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           159..166
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   STRAND          187..193
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:4XNH"
FT   TURN            205..208
FT                   /evidence="ECO:0007829|PDB:4HNY"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:4HNY"
FT   HELIX           224..233
FT                   /evidence="ECO:0007829|PDB:4HNY"
SQ   SEQUENCE   238 AA;  27603 MW;  AEB02BA5012D1137 CRC64;
     MPINIRRATI NDIICMQNAN LHNLPENYMM KYYMYHILSW PEASFVATTT TLDCEDSDEQ
     DENDKLELTL DGTNDGRTIK LDPTYLAPGE KLVGYVLVKM NDDPDQQNEP PNGHITSLSV
     MRTYRRMGIA ENLMRQALFA LREVHQAEYV SLHVRQSNRA ALHLYRDTLA FEVLSIEKSY
     YQDGEDAYAM KKVLKLEELQ ISNFTHRRLK ENEEKLEDDL ESDLLEDIIK QGVNDIIV
//