ID   H3_EUPCR                Reviewed;         136 AA.
AC   P90543;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Histone H3;
OS   Euplotes crassus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Moneuplotes.
OX   NCBI_TaxID=5936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9037053; DOI=10.1073/pnas.94.4.1332;
RA   Jahn C.L., Ling Z., Tebeau C.M., Klobutcher L.A.;
RT   "An unusual histone H3 specific for early macronuclear development in
RT   Euplotes crassus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1332-1337(1997).
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; U75429; AAB39721.1; -; Genomic_DNA.
DR   AlphaFoldDB; P90543; -.
DR   SMR; P90543; -.
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; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW   Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..136
FT                   /note="Histone H3"
FT                   /id="PRO_0000221304"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15531 MW;  3D52AC07C741CE48 CRC64;
     MARTKQTARK NVGGKAPRKH IGQKSARKTA STTAGMKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQEFK GDLRFQSSAV LALQEAAEAY LVSLFEDTNL CAIHAKRVTI
     MPKDMQLARR IRGERS