ID   NAA20_XENLA             Reviewed;         178 AA.
AC   Q7ZXR3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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; BC044290; AAH44290.1; -; mRNA.
DR   RefSeq; NP_001080646.1; NM_001087177.1.
DR   AlphaFoldDB; Q7ZXR3; -.
DR   SMR; Q7ZXR3; -.
DR   MaxQB; Q7ZXR3; -.
DR   DNASU; 380338; -.
DR   GeneID; 380338; -.
DR   KEGG; xla:380338; -.
DR   CTD; 380338; -.
DR   Xenbase; XB-GENE-6078268; naa20.S.
DR   OMA; SGEIMGY; -.
DR   OrthoDB; 1355894at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 380338; Expressed in brain and 19 other tissues.
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_0000249842"
FT   DOMAIN          2..157
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          159..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  20354 MW;  C5CCEA50D5C3E097 CRC64;
     MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
     AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
     NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIVPLPH PVRPEDIE