NAA40_DANRE
ID NAA40_DANRE Reviewed; 237 AA.
AC Q568K5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000250|UniProtKB:Q86UY6};
DE EC=2.3.1.257 {ECO:0000250|UniProtKB:Q86UY6};
DE AltName: Full=N-acetyltransferase 11;
DE AltName: Full=N-alpha-acetyltransferase D {ECO:0000250|UniProtKB:Q86UY6};
DE Short=NatD {ECO:0000250|UniProtKB:Q86UY6};
GN Name=naa40; Synonyms=nat11; ORFNames=zgc:110241;
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=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC acetylation of the N-terminal residues of histones H4 and H2A. In
CC contrast to other N-alpha-acetyltransferase, has a very specific
CC selectivity for histones H4 and H2A N-terminus and specifically
CC recognizes the 'Ser-Gly-Arg-Gly sequence'.
CC {ECO:0000250|UniProtKB:Q86UY6, ECO:0000250|UniProtKB:Q8VE10}.
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:0000250|UniProtKB:Q86UY6};
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:0000250|UniProtKB:Q86UY6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UY6}. Nucleus
CC {ECO:0000250|UniProtKB:Q86UY6}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC092819; AAH92819.1; -; mRNA.
DR RefSeq; NP_001017632.1; NM_001017632.1.
DR AlphaFoldDB; Q568K5; -.
DR SMR; Q568K5; -.
DR STRING; 7955.ENSDARP00000029934; -.
DR PaxDb; Q568K5; -.
DR DNASU; 550325; -.
DR Ensembl; ENSDART00000039265; ENSDARP00000029934; ENSDARG00000024109.
DR GeneID; 550325; -.
DR KEGG; dre:550325; -.
DR CTD; 79829; -.
DR ZFIN; ZDB-GENE-050417-105; naa40.
DR eggNOG; KOG2488; Eukaryota.
DR GeneTree; ENSGT00390000014903; -.
DR HOGENOM; CLU_051699_4_0_1; -.
DR InParanoid; Q568K5; -.
DR OMA; AYLHYRF; -.
DR OrthoDB; 1489686at2759; -.
DR PhylomeDB; Q568K5; -.
DR TreeFam; TF315129; -.
DR PRO; PR:Q568K5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000024109; Expressed in blastula and 23 other tissues.
DR ExpressionAtlas; Q568K5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Lipoprotein; Myristate; Nucleus;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..237
FT /note="N-alpha-acetyltransferase 40"
FT /id="PRO_0000284899"
FT DOMAIN 63..216
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 127..129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 140..142
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 148..153
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 179
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT SITE 139
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 237 AA; 27356 MW; 38DF4AF0439E2A37 CRC64;
MGRKSNRAKE KKQRRLEERA AMDAVCAKVD AANKLEDPLS AMPVFKKYDR NGLNLQIECK
RVTALSPDTV EWAYELTRAN MQTLYEQSEW GWKEREKREE MKDERAWYLL ARDADSTPLA
FSHFRFDVEC GDEVLYCYEV QLESKVRRKG LGKFLIQILQ LIANSTQMKK VMLTVFKHNH
GAYQFFREAL QFEIDETSPS MSGCCGEDCS YEILSRRTKY GEVSGHAHGG HCGGCCH
