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   30-AUG-2017, entry version 167.
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;
OC   Saccharomycetes; 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
RT   cell 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.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=2551674;
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-
RT   terminal acetyltransferase from yeast.";
RL   EMBO J. 8:2067-2075(1989).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NAT1, AND
RP   SELF-ASSOCIATION.
RX   PubMed=1600941;
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
RT   to 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.,
RA   Dephoure N., 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
CC       acetyltransferase, which catalyzes acetylation of proteins
CC       beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a
CC       role in normal eukaryotic translation and processing, protect
CC       against proteolytic degradation and protein turnover.
CC       {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-glycyl-[protein] =
CC       an N-terminal-N(alpha)-acetyl-glycyl-[protein] + CoA.
CC       {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-alanyl-[protein]
CC       = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA.
CC       {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-seryl-[protein] =
CC       an N-terminal-N(alpha)-acetyl-L-seryl-[protein] + CoA.
CC       {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-valyl-[protein] =
CC       an N-terminal-N(alpha)-acetyl-L-valyl-[protein] + CoA.
CC       {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-cysteinyl-
CC       [protein] = an N-terminal-N(alpha)-acetyl-L-cysteinyl-[protein] +
CC       CoA. {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-threonyl-
CC       [protein] = an N-terminal-N(alpha)-acetyl-L-threonyl-[protein] +
CC       CoA. {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-
CC       associate. {ECO:0000269|PubMed:14517307}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-2796, EBI-2796;
CC       P12945:NAT1; NbExp=11; IntAct=EBI-2796, EBI-11868;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3310 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1
CC       subfamily. {ECO:0000305}.
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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   PDBsum; 4HNW; -.
DR   PDBsum; 4HNX; -.
DR   PDBsum; 4HNY; -.
DR   PDBsum; 4XNH; -.
DR   PDBsum; 4XPD; -.
DR   PDBsum; 4Y49; -.
DR   ProteinModelPortal; P07347; -.
DR   SMR; P07347; -.
DR   BioGrid; 36440; 328.
DR   DIP; DIP-6788N; -.
DR   IntAct; P07347; 32.
DR   MINT; MINT-617928; -.
DR   STRING; 4932.YHR013C; -.
DR   MaxQB; P07347; -.
DR   PRIDE; P07347; -.
DR   EnsemblFungi; YHR013C; YHR013C; YHR013C.
DR   GeneID; 856404; -.
DR   KEGG; sce:YHR013C; -.
DR   EuPathDB; FungiDB:YHR013C; -.
DR   SGD; S000001055; ARD1.
DR   GeneTree; ENSGT00550000074803; -.
DR   HOGENOM; HOG000078523; -.
DR   InParanoid; P07347; -.
DR   KO; K20791; -.
DR   OMA; HNLPENY; -.
DR   OrthoDB; EOG092C4MWD; -.
DR   BioCyc; YEAST:YHR013C-MONOMER; -.
DR   PRO; PR:P07347; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
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-N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016573; P:histone acetylation; IMP:SGD.
DR   GO; GO:0018002; P:N-terminal peptidyl-glutamic acid acetylation; IBA:GO_Central.
DR   GO; GO:0017198; P:N-terminal peptidyl-serine acetylation; 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   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 2.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Complete proteome; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN         1    238       N-terminal acetyltransferase A complex
FT                                catalytic subunit ARD1.
FT                                /FTId=PRO_0000074529.
FT   DOMAIN       35    195       N-acetyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00532}.
FT   CONFLICT     37     37       I -> T (in Ref. 1; AAA66323).
FT                                {ECO:0000305}.
FT   STRAND        3      7       {ECO:0000244|PDB:4XNH}.
FT   HELIX        10     12       {ECO:0000244|PDB:4XNH}.
FT   HELIX        13     23       {ECO:0000244|PDB:4XNH}.
FT   HELIX        27     29       {ECO:0000244|PDB:4HNY}.
FT   HELIX        30     39       {ECO:0000244|PDB:4XNH}.
FT   TURN         41     43       {ECO:0000244|PDB:4XNH}.
FT   STRAND       45     49       {ECO:0000244|PDB:4XNH}.
FT   HELIX        66     69       {ECO:0000244|PDB:4HNY}.
FT   TURN         70     72       {ECO:0000244|PDB:4HNY}.
FT   STRAND       85     87       {ECO:0000244|PDB:4XNH}.
FT   STRAND       90    100       {ECO:0000244|PDB:4XNH}.
FT   HELIX       104    106       {ECO:0000244|PDB:4HNX}.
FT   STRAND      107    109       {ECO:0000244|PDB:4HNW}.
FT   STRAND      112    120       {ECO:0000244|PDB:4XNH}.
FT   HELIX       122    124       {ECO:0000244|PDB:4XNH}.
FT   STRAND      126    128       {ECO:0000244|PDB:4XNH}.
FT   HELIX       129    145       {ECO:0000244|PDB:4XNH}.
FT   STRAND      148    155       {ECO:0000244|PDB:4XNH}.
FT   HELIX       159    166       {ECO:0000244|PDB:4XNH}.
FT   TURN        167    169       {ECO:0000244|PDB:4XNH}.
FT   STRAND      172    177       {ECO:0000244|PDB:4XNH}.
FT   STRAND      187    193       {ECO:0000244|PDB:4XNH}.
FT   HELIX       196    199       {ECO:0000244|PDB:4XNH}.
FT   HELIX       201    204       {ECO:0000244|PDB:4XNH}.
FT   TURN        205    208       {ECO:0000244|PDB:4HNY}.
FT   STRAND      220    222       {ECO:0000244|PDB:4HNY}.
FT   HELIX       224    233       {ECO:0000244|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
//