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
//