ID   H2B_LEIEN               Reviewed;         111 AA.
AC   P27893;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Histone H2B;
OS   Leishmania enriettii.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1986223; DOI=10.1128/mcb.11.1.240-249.1991;
RA   Genske J.E., Cairns B.R., Stack S.P., Landfear S.M.;
RT   "Structure and regulation of histone H2B mRNAs from Leishmania enriettii.";
RL   Mol. Cell. Biol. 11:240-249(1991).
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   -!- DEVELOPMENTAL STAGE: The expression of this protein depends on the
CC       parasite life cycle. It accumulates to a higher level in the
CC       extracellular promastigotes than in the intracellular amastigotes.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   EMBL; M38215; AAA29248.1; -; Genomic_DNA.
DR   EMBL; M38215; AAA29246.1; -; Genomic_DNA.
DR   EMBL; M38215; AAA29247.1; -; Genomic_DNA.
DR   PIR; A39671; A39671.
DR   AlphaFoldDB; P27893; -.
DR   SMR; P27893; -.
DR   VEuPathDB; TriTrypDB:CUR178_06364; -.
DR   VEuPathDB; TriTrypDB:CUR178_06365; -.
DR   VEuPathDB; TriTrypDB:CUR178_06366; -.
DR   VEuPathDB; TriTrypDB:LENLEM3045_090020300; -.
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; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000558; Histone_H2B.
DR   PANTHER; PTHR23428; PTHR23428; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT   CHAIN           1..111
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071903"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   111 AA;  12310 MW;  E2324094BDF97EF8 CRC64;
     MASQRLAPRK SSAAHKSHRK PKRSWNVYVS RSLKAINSHM SMSGRTMKIV NSYVNDVMER
     IAMEAASIVR AHKKLTLGAR EVQTAVRLVL PPELAKHAMA EGTKAVSNSC R