NAA20_DANRE
ID NAA20_DANRE Reviewed; 178 AA.
AC Q58ED9; A2VD34;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=zgc:110819;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-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}.
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; BC091957; AAH91957.1; -; mRNA.
DR EMBL; BC129286; AAI29287.1; -; mRNA.
DR RefSeq; NP_001014351.1; NM_001014329.2.
DR AlphaFoldDB; Q58ED9; -.
DR SMR; Q58ED9; -.
DR STRING; 7955.ENSDARP00000057699; -.
DR PaxDb; Q58ED9; -.
DR Ensembl; ENSDART00000057700; ENSDARP00000057699; ENSDARG00000039493.
DR GeneID; 541516; -.
DR KEGG; dre:541516; -.
DR CTD; 51126; -.
DR ZFIN; ZDB-GENE-050327-47; naa20.
DR eggNOG; KOG3234; Eukaryota.
DR GeneTree; ENSGT00550000075046; -.
DR HOGENOM; CLU_013985_7_1_1; -.
DR InParanoid; Q58ED9; -.
DR OMA; SGEIMGY; -.
DR OrthoDB; 1355894at2759; -.
DR PhylomeDB; Q58ED9; -.
DR TreeFam; TF105829; -.
DR PRO; PR:Q58ED9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000039493; Expressed in muscle tissue and 27 other tissues.
DR ExpressionAtlas; Q58ED9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031416; C:NatB complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
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_0000249841"
FT DOMAIN 2..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT CONFLICT 96
FT /note="L -> S (in Ref. 1; AAI29287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20358 MW; 7830F49E23ABDFD2 CRC64;
MTTLRAFTCD DLFKFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMEMLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE
