NAA40_YEAST
ID NAA40_YEAST Reviewed; 285 AA.
AC Q04751; D6VZP3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000250|UniProtKB:Q86UY6};
DE EC=2.3.1.257 {ECO:0000305|PubMed:12915400};
DE AltName: Full=Histone-specific N-acetyltransferase NAT4 {ECO:0000305};
GN Name=NAT4 {ECO:0000312|SGD:S000004673}; OrderedLocusNames=YMR069W;
GN ORFNames=YM9916.08;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=12915400; DOI=10.1074/jbc.c300355200;
RA Song O.-K., Wang X., Waterborg J.H., Sternglanz R.;
RT "An Nalpha-acetyltransferase responsible for acetylation of the N-terminal
RT residues of histones H4 and H2A.";
RL J. Biol. Chem. 278:38109-38112(2003).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC acetylation of the N-terminal residues of histones H4 and H2A.
CC {ECO:0000269|PubMed:12915400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[histone H4]; Xref=Rhea:RHEA:50596,
CC Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.257;
CC Evidence={ECO:0000305|PubMed:12915400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-seryl-[histone H2A];
CC Xref=Rhea:RHEA:50600, Rhea:RHEA-COMP:12742, Rhea:RHEA-COMP:12744,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257;
CC Evidence={ECO:0000305|PubMed:12915400};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48952; CAA88794.1; -; Genomic_DNA.
DR EMBL; AY557984; AAS56310.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09967.1; -; Genomic_DNA.
DR PIR; S52829; S52829.
DR RefSeq; NP_013785.1; NM_001182567.1.
DR AlphaFoldDB; Q04751; -.
DR SMR; Q04751; -.
DR BioGRID; 35244; 93.
DR DIP; DIP-2745N; -.
DR IntAct; Q04751; 2.
DR MINT; Q04751; -.
DR STRING; 4932.YMR069W; -.
DR iPTMnet; Q04751; -.
DR PaxDb; Q04751; -.
DR PRIDE; Q04751; -.
DR EnsemblFungi; YMR069W_mRNA; YMR069W; YMR069W.
DR GeneID; 855091; -.
DR KEGG; sce:YMR069W; -.
DR SGD; S000004673; NAT4.
DR VEuPathDB; FungiDB:YMR069W; -.
DR eggNOG; KOG2488; Eukaryota.
DR HOGENOM; CLU_087674_0_0_1; -.
DR InParanoid; Q04751; -.
DR OMA; IYLYEIQ; -.
DR BioCyc; YEAST:G3O-32771-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR PRO; PR:Q04751; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04751; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:SGD.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039949; NAA40.
DR PANTHER; PTHR20531; PTHR20531; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..285
FT /note="N-alpha-acetyltransferase 40"
FT /id="PRO_0000074636"
FT DOMAIN 88..274
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 163..165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 187..189
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 195..200
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 233
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT SITE 186
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
SQ SEQUENCE 285 AA; 32334 MW; 20127B782E1F5F1A CRC64;
MRSSVYSENT YNCIRTSKEH LTERRRVAMA PMFQHFLNLC VEKFPESIEH KDTDGNGNFT
TAILEREIIY IPEDDTDSID SVDSLKCINY KLHKSRGDQV LDACVQLIDK HLGAKYRRAS
RIMYGNRKPW KANKLAEMKS AGLVYVCYWD NGVLGAFTSF MLTEETGLVE GDALHEVSVP
VIYLYEVHVA SAHRGHGIGR RLLEHALCDG VARHTRRMCD NFFGVALTVF SDNTRARRLY
EALGFYRAPG SPAPASPTIR HTRHGGGRVV VPCDPLYYVY CLHMP
