ARD1_YEAST
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 03-AUG-2022, entry version 198.
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}.
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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 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 SMR; P07347; -.
DR BioGRID; 36440; 349.
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; P07347; -.
DR PRIDE; P07347; -.
DR EnsemblFungi; YHR013C_mRNA; YHR013C; YHR013C.
DR GeneID; 856404; -.
DR KEGG; sce:YHR013C; -.
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 BioCyc; YEAST:YHR013C-MON; -.
DR BRENDA; 2.3.1.255; 984.
DR BRENDA; 2.3.1.258; 984.
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-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:0006474; P:N-terminal protein amino acid acetylation; IDA:SGD.
DR GO; GO:0061606; P:N-terminal protein amino acid propionylation; IMP:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 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; 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
