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Database: UniProt
Entry: Q8III2_PLAF7
LinkDB: Q8III2_PLAF7
Original site: Q8III2_PLAF7 
ID   Q8III2_PLAF7            Unreviewed;       608 AA.
AC   Q8III2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
GN   ORFNames=PF3D7_1118600 {ECO:0000313|EMBL:CZT98848.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT98848.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:CZT98848.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000256|RuleBase:RU361211};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
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DR   EMBL; LN999945; CZT98848.1; -; Genomic_DNA.
DR   RefSeq; XP_001347863.1; XM_001347827.1.
DR   AlphaFoldDB; Q8III2; -.
DR   SMR; Q8III2; -.
DR   STRING; 36329.Q8III2; -.
DR   PaxDb; 5833-PF11_0192; -.
DR   EnsemblProtists; CZT98848; CZT98848; PF3D7_1118600.
DR   GeneID; 810739; -.
DR   KEGG; pfa:PF3D7_1118600; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1118600; -.
DR   HOGENOM; CLU_011815_1_0_1; -.
DR   InParanoid; Q8III2; -.
DR   OMA; MWGLDPL; -.
DR   OrthoDB; 118560at2759; -.
DR   PhylomeDB; Q8III2; -.
DR   BRENDA; 2.3.1.48; 4889.
DR   Proteomes; UP000001450; Chromosome 11.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:GeneDB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043983; P:histone H4-K12 acetylation; IDA:GeneDB.
DR   GO; GO:0043984; P:histone H4-K16 acetylation; IDA:GeneDB.
DR   GO; GO:0043981; P:histone H4-K5 acetylation; IDA:GeneDB.
DR   GO; GO:0043982; P:histone H4-K8 acetylation; IDA:GeneDB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR025995; Tudor-knot.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Acyltransferase {ECO:0000313|EMBL:CZT98848.1};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|RuleBase:RU361211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CZT98848.1}.
FT   DOMAIN          328..599
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          35..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        502
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   608 AA;  71134 MW;  27618CA7B05D4E38 CRC64;
     MVLGGKNENK VNVIKGAGSI GKYIMKENGS KIKEVGEWNN SSENENSDNN NNDREDNIKE
     KVDNNNKNDD NNNNDREDNI KEKVDNNNNN DDNNNDNNNN NKSDNNNNKS DNNNNKSDNY
     NNKIGDVSNI PSTNTSTVSN KIQGKGSVSY KSKEKTGDHS SNNKNTKGNN NKVRTSGKVI
     NSLSKYSDSY ALIFPNALPV KQVLWGLDPL NKVWRYCSIV YARPKNKVLN DTNFMFPLNM
     NKNEIINKVN NELNNNNSVS MSEGDYDYYV HWEKFDRRLD CWLAYENLRL LDKEPDDGLP
     LIKDNDNVSD HEHAGIDKEY LREHEENTKL KTINQIRFGK YLIDTWYFSP YPKEYQNIDI
     LYICEFCLSF FKEYSELKRH IEKCEIRHPP GNEIYREEKI SIFEIDGSYF RIYCENLCFL
     SKLFLDHKTL KHRVNLFLFY VITEYDEYGY HITGYFSKEK YSKNNVSCIL TLPQHQKKGY
     GKFLINFSYF LSQTEKRTGT PERPLSDLGV ASYMAYWYET ILKVLINYEQ LSIQELSEIT
     SIETNDIISC LEEKDIFKNS LNGLDSFYYI NPKQLEFILN KLKQTNNTQL SKNKLHWVSY
     DYYLALYE
//
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