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}. 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 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 //