ID   NAA20_MACFA             Reviewed;         178 AA.
AC   Q2PFM2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=N-alpha-acetyltransferase 20;
DE            EC=2.3.1.254 {ECO:0000250|UniProtKB:P61599};
DE   AltName: Full=Methionine N-acetyltransferase;
DE   AltName: Full=N-acetyltransferase 5;
DE   AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
DE   AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
DE            Short=NatB complex subunit NAT5;
DE   AltName: Full=NatB catalytic subunit;
GN   Name=NAA20; Synonyms=NAT5; ORFNames=QtrA-15925;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the NatB complex which catalyzes
CC       acetylation of the N-terminal methionine residues of peptides beginning
CC       with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle
CC       functions are overrepresented in the pool of NatB substrates. Required
CC       for maintaining the structure and function of actomyosin fibers and for
CC       proper cellular migration. {ECO:0000250|UniProtKB:P61599}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] =
CC         CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-
CC         [protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-
CC         COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254;
CC         Evidence={ECO:0000250|UniProtKB:P61599};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] =
CC         CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-
CC         [protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-
CC         COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254;
CC         Evidence={ECO:0000250|UniProtKB:P61599};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA
CC         + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein];
CC         Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254;
CC         Evidence={ECO:0000250|UniProtKB:P61599};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC         + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC         Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254;
CC         Evidence={ECO:0000250|UniProtKB:P61599};
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC       which is composed of NAA20 and NAA25. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61599}. Nucleus
CC       {ECO:0000250|UniProtKB:P61599}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB220565; BAE73098.1; -; mRNA.
DR   RefSeq; NP_001270877.1; NM_001283948.1.
DR   AlphaFoldDB; Q2PFM2; -.
DR   SMR; Q2PFM2; -.
DR   STRING; 9541.XP_005568286.1; -.
DR   GeneID; 102145138; -.
DR   CTD; 51126; -.
DR   VEuPathDB; HostDB:ENSMFAG00000042031; -.
DR   eggNOG; KOG3234; Eukaryota.
DR   OMA; SGEIMGY; -.
DR   OrthoDB; 1355894at2759; -.
DR   Proteomes; UP000233100; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..178
FT                   /note="N-alpha-acetyltransferase 20"
FT                   /id="PRO_0000249840"
FT   DOMAIN          2..157
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   178 AA;  20368 MW;  C5CCEA50CD60E097 CRC64;
     MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
     AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
     NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE