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Database: UniProt
Entry: A8X9I7_CAEBR
LinkDB: A8X9I7_CAEBR
Original site: A8X9I7_CAEBR 
ID   A8X9I7_CAEBR            Unreviewed;       197 AA.
AC   A8X9I7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000256|ARBA:ARBA00015043};
DE            EC=2.3.1.257 {ECO:0000256|ARBA:ARBA00012950};
GN   ORFNames=CBG09255 {ECO:0000313|EMBL:CAP29299.1,
GN   ECO:0000313|WormBase:CBG09255}, CBG_09255
GN   {ECO:0000313|EMBL:CAP29299.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29299.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP29299.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP29299.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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:0000256|ARBA:ARBA00000345};
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:0000256|ARBA:ARBA00001388};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008870}.
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DR   EMBL; HE600954; CAP29299.1; -; Genomic_DNA.
DR   RefSeq; XP_002636811.1; XM_002636765.1.
DR   AlphaFoldDB; A8X9I7; -.
DR   STRING; 6238.A8X9I7; -.
DR   EnsemblMetazoa; CBG09255.1; CBG09255.1; WBGene00030871.
DR   GeneID; 8578806; -.
DR   KEGG; cbr:CBG_09255; -.
DR   CTD; 8578806; -.
DR   WormBase; CBG09255; CBP16558; WBGene00030871; -.
DR   eggNOG; KOG2488; Eukaryota.
DR   HOGENOM; CLU_051699_1_1_1; -.
DR   InParanoid; A8X9I7; -.
DR   OMA; NVGPYYK; -.
DR   OrthoDB; 5481499at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043998; F:histone H2A acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:1990189; F:peptide-serine-alpha-N-acetyltransferase activity; IBA:GO_Central.
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   InterPro; IPR039949; NAA40.
DR   PANTHER; PTHR20531; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   PANTHER; PTHR20531:SF1; N-ALPHA-ACETYLTRANSFERASE 40; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          37..196
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   197 AA;  22534 MW;  A4CC25BFA42F387B CRC64;
     MPVDSKKLVK KASQLMKPVE KLDCETPRST TTDGETITFE YMWATHLSDE DFEWVYALFK
     ANMLDMYQKS QWGYDENSKR NELRATTSRF IIAINSKGEK IGYTTYRFVV DHNIPVAYCW
     ELQILPAYQN KGIGSMMLDT LERLSARTNM AKVMATVFLY NAPSLGFFHK HGYVSDVTCP
     SDDSGLDYAI LSKETPS
//
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