NAA40_XENLA
ID NAA40_XENLA Reviewed; 236 AA.
AC Q6NUH2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
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;
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 (APR-2004) 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; BC068615; AAH68615.1; -; mRNA.
DR RefSeq; NP_001087260.1; NM_001093791.1.
DR AlphaFoldDB; Q6NUH2; -.
DR SMR; Q6NUH2; -.
DR BioGRID; 101095; 1.
DR MaxQB; Q6NUH2; -.
DR DNASU; 414673; -.
DR GeneID; 414673; -.
DR KEGG; xla:414673; -.
DR CTD; 414673; -.
DR Xenbase; XB-GENE-5846126; naa40.L.
DR OMA; AYLHYRF; -.
DR OrthoDB; 1489686at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 414673; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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..236
FT /note="N-alpha-acetyltransferase 40"
FT /id="PRO_0000284900"
FT DOMAIN 63..217
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 236 AA; 27120 MW; BC0F4DE30A927DAC CRC64;
MGRKSVRAKE KKQKRLEERA AMAAVCAKVQ AANQLGDPLG AFPVFKKFDR NGLNLSIECC
KVSDLDQKTI DWAFELTKTN MQLLYEQSEW GWKEREKREE LTDERAWYLI ARDELAALVA
FVHFRFDVEC GDEVLYCYEV QLETRVRRKG VGKFLVQILQ LMANSTQMKK VVLTVFKHNH
GAYQFFRDAL QFEIDETSPS VSGCCSDDCT YEILSKRTKF GDTPHSHTGH CAGCCH
