H2A_TRYCR
ID H2A_TRYCR Reviewed; 135 AA.
AC P35066;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Histone H2A;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8078513; DOI=10.1016/0166-6851(94)90129-5;
RA Puerta C., Martin J., Alonso C., Lopez M.C.;
RT "Isolation and characterization of the gene encoding histone H2A from
RT Trypanosoma cruzi.";
RL Mol. Biochem. Parasitol. 64:1-10(1994).
RN [2]
RP SEQUENCE REVISION TO 5; 92 AND 106.
RA Lopez Lopez M.C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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; X67287; CAA47703.2; -; Genomic_DNA.
DR PIR; S25119; S25119.
DR AlphaFoldDB; P35066; -.
DR SMR; P35066; -.
DR VEuPathDB; TriTrypDB:BCY84_17372; -.
DR VEuPathDB; TriTrypDB:C3747_22g1865c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1866c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1867c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1868c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1869c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1870c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1871c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1872c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1873c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1874c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1875c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1876c; -.
DR VEuPathDB; TriTrypDB:C3747_22g1878c; -.
DR VEuPathDB; TriTrypDB:C3747_259g205c; -.
DR VEuPathDB; TriTrypDB:C4B63_242g10; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_125; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0093800; -.
DR VEuPathDB; TriTrypDB:TcCL_NonESM00496; -.
DR VEuPathDB; TriTrypDB:TcCLB.508321.21; -.
DR VEuPathDB; TriTrypDB:TcCLB.511817.151; -.
DR VEuPathDB; TriTrypDB:TcG_03831; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092810; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092820; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092830; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092840; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092850; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092860; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092870; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092880; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092890; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092900; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092910; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092920; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092930; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092940; -.
DR VEuPathDB; TriTrypDB:TcYC6_0092950; -.
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 3: Inferred from homology;
KW Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT CHAIN 1..135
FT /note="Histone H2A"
FT /id="PRO_0000055287"
SQ SEQUENCE 135 AA; 14366 MW; DC41BCE5983EA93B CRC64;
MATPKQAAKK ASKKRSGGRS AKAGLIFPVG RVGSLLRRGQ YARRIGASGA VYMAAVLEYL
TAELLELSVK AASQQAKKPK RLTPRTVTLA VRHDDDLGML LKDVTLSRGG VMPSLNKALA
KKHKSSKKAR ATPSA