ID A0AAA9SJL0_BOVIN Unreviewed; 129 AA. AC A0AAA9SJL0; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 27-NOV-2024, entry version 4. 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:ENSBTAP00000086476.1, GN ECO:0000313|VGNC:VGNC:53590}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000086476.1, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000086476.1, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000086476.1, RC ECO:0000313|Proteomes:UP000009136}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000086476.1} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000086476.1}; RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-methionyl-L-alanyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA + H(+); 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=N-terminal L-methionyl-L-leucyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA + H(+); 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=N-terminal L-methionyl-L-lysyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein] + CoA + H(+); 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=N-terminal L-methionyl-L-phenylalanyl-[protein] + acetyl-CoA = CC N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA CC + H(+); 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=N-terminal L-methionyl-L-seryl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein] + CoA + H(+); 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=N-terminal L-methionyl-L-threonyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein] + CoA + CC H(+); Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA- CC COMP:12733, 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=N-terminal L-methionyl-L-tyrosyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA + CC H(+); Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA- CC COMP:12718, 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=N-terminal L-methionyl-L-valyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein] + CoA + H(+); 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}. 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 SMR; A0AAA9SJL0; -. DR Ensembl; ENSBTAT00000127125.1; ENSBTAP00000086476.1; ENSBTAG00000007784.7. DR VGNC; VGNC:53590; NAA50. DR GeneTree; ENSGT00390000009110; -. DR Proteomes; UP000009136; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro. DR FunFam; 3.40.630.30:FF:000074; N(alpha)-acetyltransferase 50, NatE catalytic subunit; 1. DR Gene3D; 3.40.630.30; -; 2. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR051556; N-term/lysine_N-AcTrnsfr. 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:UP000009136}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 48..115 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|PROSITE:PS51186" SQ SEQUENCE 129 AA; 14886 MW; D36C0EE340819268 CRC64; MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLGT KMLNHVLNIC EKDGTFDNIY LHVQISNESA IDFYRKFGFE IIETKKNYYK RIEPADAHVL QKNLKVPSGQ NADVQKTDN //