ID   H3_ENTHI                Reviewed;         135 AA.
AC   Q06196;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Histone H3;
GN   Name=H3;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SFL-3;
RX   PubMed=8341328; DOI=10.1016/0166-6851(93)90229-q;
RA   Foedinger M., Ortner S., Plaimauer B., Wiedermann G., Scheiner O.,
RA   Duchene M.;
RT   "Pathogenic Entamoeba histolytica: cDNA cloning of a histone H3 with a
RT   divergent primary structure.";
RL   Mol. Biochem. Parasitol. 59:315-322(1993).
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 H3 family. {ECO:0000305}.
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DR   EMBL; L02418; AAA29101.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q06196; -.
DR   SMR; Q06196; -.
DR   STRING; 5759.rna_EHI_135080-1; -.
DR   VEuPathDB; AmoebaDB:EHI5A_009610; -.
DR   VEuPathDB; AmoebaDB:EHI7A_018000; -.
DR   VEuPathDB; AmoebaDB:EHI8A_002440; -.
DR   VEuPathDB; AmoebaDB:EHI_135080; -.
DR   VEuPathDB; AmoebaDB:KM1_008280; -.
DR   eggNOG; KOG1745; Eukaryota.
DR   OMA; SDCERRK; -.
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   3: Inferred from homology;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..135
FT                   /note="Histone H3"
FT                   /id="PRO_0000221353"
SQ   SEQUENCE   135 AA;  15010 MW;  8D64D7AE8C2BB6E5 CRC64;
     MARTKGHIER PSNKSAKAVK NVAFKAAKKM LSKDSTKKKR AHPGAVALTE IKVLQRSTEL
     LLRKAPFQAL VREIAQVSKS DLRFQSAAIS ALQEAAEAYL VGLFEDTNLC AIHAKRITIM
     PKDMQLARRI RGERT