NAA50_XENLA
ID NAA50_XENLA Reviewed; 170 AA.
AC Q6GP53;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=N-alpha-acetyltransferase 50;
DE EC=2.3.1.258 {ECO:0000250|UniProtKB:Q9GZZ1};
DE AltName: Full=N-acetyltransferase NAT13;
DE AltName: Full=N-epsilon-acetyltransferase 50 {ECO:0000250|UniProtKB:Q9GZZ1};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9GZZ1};
DE AltName: Full=NatE catalytic subunit;
GN Name=naa50; Synonyms=nat13;
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=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of
CC proteins that retain their initiating methionine. Has a broad substrate
CC specificity: able to acetylate the initiator methionine of most
CC peptides, except for those with a proline in second position. Also
CC displays N-epsilon-acetyltransferase activity by mediating acetylation
CC of the side chain of specific lysines on proteins. The relevance of N-
CC epsilon-acetyltransferase activity is however unclear. Required for
CC sister chromatid cohesion during mitosis by promoting binding of
CC CDCA5/sororin to cohesin. {ECO:0000250|UniProtKB:Q9GZZ1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein];
CC Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein];
CC Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein];
CC Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein];
CC Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein];
CC Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ1}. Nucleus
CC {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in
CC interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
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DR EMBL; BC073291; AAH73291.1; -; mRNA.
DR RefSeq; NP_001085750.1; NM_001092281.1.
DR AlphaFoldDB; Q6GP53; -.
DR SMR; Q6GP53; -.
DR DNASU; 444177; -.
DR GeneID; 444177; -.
DR KEGG; xla:444177; -.
DR CTD; 444177; -.
DR Xenbase; XB-GENE-996007; naa50.S.
DR OrthoDB; 1536763at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 444177; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; 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 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..170
FT /note="N-alpha-acetyltransferase 50"
FT /id="PRO_0000284906"
FT DOMAIN 6..155
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 138..141
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT ACT_SITE 112
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 77..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 79..90
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 117..126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
SQ SEQUENCE 170 AA; 19499 MW; 9691C55E2F509991 CRC64;
MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLAY FNDIAVGAVC
CRVDHSQNQK RLYIMTLGCL APYRRLGIGT KMLNHVLNIC EKDGTFDNIY LHVQISNESA
IDFYRKFGFE IIETKKNYYK RIEPADAHVL QKNLKISSPG QNADVQKSEN
