GenomeNet

Database: UniProt
Entry: A0A0L1IB99_PLAFA
LinkDB: A0A0L1IB99_PLAFA
Original site: A0A0L1IB99_PLAFA 
ID   A0A0L1IB99_PLAFA        Unreviewed;       335 AA.
AC   A0A0L1IB99;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000256|ARBA:ARBA00015043};
DE            EC=2.3.1.257 {ECO:0000256|ARBA:ARBA00012950};
GN   ORFNames=PFMG_03108 {ECO:0000313|EMBL:KNG76914.1};
OS   Plasmodium falciparum IGH-CR14.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=580059 {ECO:0000313|EMBL:KNG76914.1, ECO:0000313|Proteomes:UP000054562};
RN   [1] {ECO:0000313|Proteomes:UP000054562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG   The Broad Institute Genome Sequencing Platform;
RA   Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA   Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "Annotation of Plasmodium falciparum IGH-CR14.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG   The Broad Institute Genome Sequencing Platform;
RA   Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Godfrey P., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Wirth D.F., Nusbaum C., Birren B.;
RT   "The genome sequence of Plasmodium falciparum IGH-CR14.";
RL   Submitted (JUL-2015) 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}.
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; GG665222; KNG76914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L1IB99; -.
DR   EnsemblProtists; KNG76914; KNG76914; PFMG_03108.
DR   Proteomes; UP000054562; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054562};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNG76914.1}.
FT   DOMAIN          210..314
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00583"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  40415 MW;  8CFB42DE051EF3B6 CRC64;
     MRILKKEIGK KKEEKKRKGN NNHTHNLKSR NEKEELIQRL KRCHDNDNIF NYIDEKYKKY
     IIKKNRNDSS QNNSINKEKN ENYIHNEIEG SKHLGSSSFI FFESINSYEL KKYKSAFSIY
     NILLNITKIN MQKLYDENNF LNKGWSDQEK LKELKSDRSK LILGFLKKKK EQNRYDHEQN
     QYDHEQNQYD HKQHPSEHET YDSKFFITKN TNNHFIDIIK TNDKNQIDDF LKTNPIVCFV
     HFRFTPDYYP YQKNIICYLY EIQIIKEYIK IGIGTHLINI LEQLCKNIHI HKILCTVLKS
     NYKAVMFYKN KCSFQMDESS PDNFYSDSHL SKDVI
//
DBGET integrated database retrieval system