ID A0A0D9QS56_PLAFR Unreviewed; 347 AA.
AC A0A0D9QS56;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000256|ARBA:ARBA00015043};
DE EC=2.3.1.257 {ECO:0000256|ARBA:ARBA00012950};
GN ORFNames=AK88_00396 {ECO:0000313|EMBL:KJP89940.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP89940.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP89940.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; KQ001647; KJP89940.1; -; Genomic_DNA.
DR RefSeq; XP_012333470.1; XM_012478047.1.
DR AlphaFoldDB; A0A0D9QS56; -.
DR EnsemblProtists; KJP89940; KJP89940; AK88_00396.
DR GeneID; 24265710; -.
DR VEuPathDB; PlasmoDB:AK88_00396; -.
DR OMA; NMERLYN; -.
DR OrthoDB; 196510at2759; -.
DR Proteomes; UP000054561; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043998; F:histone H2A acetyltransferase activity; IEA:InterPro.
DR GO; GO:0010485; F:histone H4 acetyltransferase activity; 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 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 252..317
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00583"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 39390 MW; 288A9C193E6BC23A CRC64;
MNNEREGDAA EGDVVRTAAG KSSSPSTIRK TRKSIQKKGC AERNKNKPHV KYNNGELIKV
IKNCKQNDSI FDYIGGSYRM YFLLNRGNGV HGQTQVGCDS PGGKSAHTPF ILFESINAFE
LKKHPASEPV FSTMFHMTKA NMERLYNESN FLSRGWSDEK KWKELRSDRC KLILGFVHKP
EGSEDGVTSD EPNVTESVLA GGEPHLSFLQ RVHNANGTNE RTNEDRTQDV HDYLTKHALV
CFVHYRLTAD YPPNEHTTIC YLYEIQIVPE FTKMGIGQHL ISMLEALCRR INVPKILCTV
LKNNVKAVSF YKTKCSFQLD ESSPDNFTSD DSEEECEYEI LKRVVFS
//
