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Database: UniProt
Entry: F7HM45_MACMU
LinkDB: F7HM45_MACMU
Original site: F7HM45_MACMU 
ID   F7HM45_MACMU            Unreviewed;       172 AA.
AC   F7HM45;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=N-alpha-acetyltransferase 50 {ECO:0000256|ARBA:ARBA00039544};
DE            EC=2.3.1.258 {ECO:0000256|ARBA:ARBA00039121};
DE   AltName: Full=N-epsilon-acetyltransferase 50 {ECO:0000256|ARBA:ARBA00042533};
DE   AltName: Full=NatE catalytic subunit {ECO:0000256|ARBA:ARBA00042626};
GN   Name=NAA50 {ECO:0000313|Ensembl:ENSMMUP00000039993.3,
GN   ECO:0000313|VGNC:VGNC:110351};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000039993.3, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000039993.3}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000039993.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036404};
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:0000256|ARBA:ARBA00035859};
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:0000256|ARBA:ARBA00036162};
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:0000256|ARBA:ARBA00036197};
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:0000256|ARBA:ARBA00036718};
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:0000256|ARBA:ARBA00036884};
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:0000256|ARBA:ARBA00036534};
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:0000256|ARBA:ARBA00036417};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC       {ECO:0000256|ARBA:ARBA00009342}.
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DR   AlphaFoldDB; F7HM45; -.
DR   SMR; F7HM45; -.
DR   Ensembl; ENSMMUT00000029797.4; ENSMMUP00000039993.3; ENSMMUG00000055908.1.
DR   VEuPathDB; HostDB:ENSMMUG00000055908; -.
DR   VGNC; VGNC:110351; NAA50.
DR   GeneTree; ENSGT00390000009110; -.
DR   HOGENOM; CLU_013985_5_3_1; -.
DR   TreeFam; TF314841; -.
DR   Proteomes; UP000006718; Chromosome 2.
DR   Bgee; ENSMMUG00000055908; Expressed in hindlimb stylopod muscle and 22 other cell types or tissues.
DR   ExpressionAtlas; F7HM45; baseline and differential.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR42919; N-ALPHA-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42919:SF8; N-ALPHA-ACETYLTRANSFERASE 50; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..158
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   172 AA;  19696 MW;  564940FB8C51462D CRC64;
     DKGTVISRIE LGDVTPHNIK QLKRLNQVIF PVSYNDKFYK DVLEVGELAK LAYFNDIAVG
     AVCCRVDHSQ NQKRLYIMTL GCLAPYRRLG IGTKMLNHVL NICEKDGTFD NIYLHVQISN
     ESAIDFYRKF GFEIIETKKN YYKRIEPADA HVLQKNLKVP SGQNADVQKT DN
//
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