ID B9ELZ1_SALSA Unreviewed; 178 AA.
AC B9ELZ1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=N-alpha-acetyltransferase 20 {ECO:0000256|ARBA:ARBA00039529};
DE EC=2.3.1.254 {ECO:0000256|ARBA:ARBA00039120};
DE AltName: Full=Methionine N-acetyltransferase {ECO:0000256|ARBA:ARBA00042723};
DE AltName: Full=N-acetyltransferase 5 {ECO:0000256|ARBA:ARBA00041220};
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20 {ECO:0000256|ARBA:ARBA00042743};
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5 {ECO:0000256|ARBA:ARBA00042702};
DE AltName: Full=NatB catalytic subunit {ECO:0000256|ARBA:ARBA00042295};
GN Name=NAT5 {ECO:0000313|EMBL:ACM08538.1};
GN Synonyms=LOC106607684 {ECO:0000313|RefSeq:XP_014060363.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACM08538.1};
RN [1] {ECO:0000313|EMBL:ACM08538.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACM08538.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACM08538.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACM08538.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACM08538.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACM08538.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:XP_014060363.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014060363.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-
CC COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254;
CC Evidence={ECO:0000256|ARBA:ARBA00036044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein];
CC Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254;
CC Evidence={ECO:0000256|ARBA:ARBA00035918};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-
CC [protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-
CC COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254;
CC Evidence={ECO:0000256|ARBA:ARBA00036121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254;
CC Evidence={ECO:0000256|ARBA:ARBA00036101};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC which is composed of NAA20 and NAA25. {ECO:0000256|ARBA:ARBA00038748}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000256|ARBA:ARBA00025786}.
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 EMBL; BT056666; ACM08538.1; -; mRNA.
DR RefSeq; XP_014060363.1; XM_014204888.1.
DR STRING; 8030.ENSSSAP00000105764; -.
DR PaxDb; 8030-ENSSSAP00000105764; -.
DR GeneID; 106607684; -.
DR KEGG; sasa:106607684; -.
DR OMA; DAHDMRK; -.
DR OrthoDB; 5471170at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
DR Bgee; ENSSSAG00000076414; Expressed in camera-type eye and 15 other cell types or tissues.
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; PTHR45910; N-ALPHA-ACETYLTRANSFERASE 20; 1.
DR PANTHER; PTHR45910:SF1; N-ALPHA-ACETYLTRANSFERASE 20; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|EMBL:ACM08538.1}.
FT DOMAIN 2..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 157..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 178 AA; 20275 MW; 7830F0CF3AD3AFD2 CRC64;
MTTLRAFTCD DLFKFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMEMLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSSDT EKKSIVPIPH PVRPEDIE
//
