ID   H3_LEIIN                Reviewed;         129 AA.
AC   P40285;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Histone H3;
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=7918653; DOI=10.1016/0167-4781(94)90082-5;
RA   Soto M., Requena J.M., Morales G., Alonso C.;
RT   "The Leishmania infantum histone H3 possesses an extremely divergent N-
RT   terminal domain.";
RL   Biochim. Biophys. Acta 1219:533-535(1994).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; X77591; CAA54693.1; -; mRNA.
DR   AlphaFoldDB; P40285; -.
DR   SMR; P40285; -.
DR   STRING; 5671.XP_001463740.1; -.
DR   VEuPathDB; TriTrypDB:LINF_160011400; -.
DR   eggNOG; KOG1745; Eukaryota.
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; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT   CHAIN           1..129
FT                   /note="Histone H3"
FT                   /id="PRO_0000221354"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14629 MW;  C8AB2EA73C906100 CRC64;
     MSRTKETARA KRTITSKKSK KAPSGASGVK RSHRRWRPGT CAIREIRKFQ KSTSLLIQCA
     PFQRLVRGVE RQKEGLRFQS SAIMALQEAT EAYIVSLMAD TNLACIHAKR VTIQPKDIQL
     ALRLRGERH