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H2A2_LEIIN
ID   H2A2_LEIIN              Reviewed;         132 AA.
AC   P27892;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Histone H2A.2;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MHOM/FR/78/LEM 75;
RX   PubMed=1555581; DOI=10.1111/j.1432-1033.1992.tb16770.x;
RA   Soto M., Requena J.M., Gomez L.C., Navarrete I., Alonso C.;
RT   "Molecular characterization of a Leishmania donovani infantum antigen
RT   identified as histone H2A.";
RL   Eur. J. Biochem. 205:211-216(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; X61936; CAA43940.1; -; mRNA.
DR   PIR; S22391; S22391.
DR   AlphaFoldDB; P27892; -.
DR   SMR; P27892; -.
DR   VEuPathDB; TriTrypDB:LINF_210016800; -.
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   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.2"
FT                   /id="PRO_0000055247"
SQ   SEQUENCE   132 AA;  13819 MW;  44272EDB598A0F49 CRC64;
     MATPRSAKKA ARKSGSKSAK CGLIFPVGRV GGMMRRGQYA RRIGASGAVY LAAVLEYLTA
     ELLELSVKAA AQSGKKRCRL NPRTVMLAAR HDDDIGTLLK NVTLSHSGVV PSVSKAVAKK
     KGGKKGRATP SA
 
 
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