H2A_PLAFA
ID H2A_PLAFA Reviewed; 132 AA.
AC P40282;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Histone H2A;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1518525; DOI=10.1016/0166-6851(92)90102-p;
RA Creedon K.A., Kaslow D.C., Rathod P.K., Wellems T.E.;
RT "Identification of a Plasmodium falciparum histone 2A gene.";
RL Mol. Biochem. Parasitol. 54:113-115(1992).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; M86865; AAA29612.1; -; mRNA.
DR PIR; A45564; A45564.
DR AlphaFoldDB; P40282; -.
DR SMR; P40282; -.
DR EnsemblProtists; CAG24993; CAG24993; PF3D7_0617800.
DR VEuPathDB; PlasmoDB:PF3D7_0617800; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000170100; -.
DR VEuPathDB; PlasmoDB:Pf7G8_060022700; -.
DR VEuPathDB; PlasmoDB:PfCD01_060023200; -.
DR VEuPathDB; PlasmoDB:PfDd2_060022500; -.
DR VEuPathDB; PlasmoDB:PfGA01_060022800; -.
DR VEuPathDB; PlasmoDB:PfGB4_060022200; -.
DR VEuPathDB; PlasmoDB:PfGN01_060023500; -.
DR VEuPathDB; PlasmoDB:PfHB3_060022000; -.
DR VEuPathDB; PlasmoDB:PfIT_060021600; -.
DR VEuPathDB; PlasmoDB:PfKE01_060023900; -.
DR VEuPathDB; PlasmoDB:PfKH01_060024800; -.
DR VEuPathDB; PlasmoDB:PfKH02_060024300; -.
DR VEuPathDB; PlasmoDB:PfML01_000104000; -.
DR VEuPathDB; PlasmoDB:PfML01_060021600; -.
DR VEuPathDB; PlasmoDB:PfNF135_060022000; -.
DR VEuPathDB; PlasmoDB:PfNF166_060022200; -.
DR VEuPathDB; PlasmoDB:PfNF54_060022800; -.
DR VEuPathDB; PlasmoDB:PfSD01_060021700; -.
DR VEuPathDB; PlasmoDB:PfSN01_060022700; -.
DR VEuPathDB; PlasmoDB:PfTG01_060023100; -.
DR OMA; FQMAGRG; -.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT CHAIN 1..132
FT /note="Histone H2A"
FT /id="PRO_0000055269"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 14122 MW; 09543242F02020CE CRC64;
MSAKGKTGRK KASKGTSNSA KAGLQFPVGR IGRYLKKGKY AKRVGAGAPV YLAAVLEYLC
AEILELAGNA ARDNKKSRIT PRHIQLAVRN DEELNKFLAG VTFASGGVLP NIHNVLLPKK
SQLKAGTANQ DY
