ID   H4_EUPCR                Reviewed;         107 AA.
AC   P80739; P90544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Histone H4;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16.
RX   PubMed=9103980; DOI=10.1111/j.1574-6968.1997.tb10314.x;
RA   Salvini M., Bini E., Santucci A., Batistoni R.;
RT   "H4 histone in the macronucleus of Blepharisma japonicum (Protozoa,
RT   Ciliophora, Heterotrichida).";
RL   FEMS Microbiol. Lett. 149:93-98(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-107.
RX   PubMed=2470096; DOI=10.1073/pnas.86.9.3252;
RA   Harper D.S., Jahn C.L.;
RT   "Differential use of termination codons in ciliated protozoa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3252-3256(1989).
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 H4 family. {ECO:0000305}.
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DR   EMBL; U75430; AAB39722.1; -; Genomic_DNA.
DR   PIR; C30309; C30309.
DR   AlphaFoldDB; P80739; -.
DR   SMR; P80739; -.
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   CDD; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR035425; CENP-T/H4_C.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Direct protein sequencing; DNA-binding; Nucleosome core;
KW   Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9103980"
FT   CHAIN           2..107
FT                   /note="Histone H4"
FT                   /id="PRO_0000158317"
FT   DNA_BIND        17..21
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        5
FT                   /note="G -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   107 AA;  11630 MW;  34121F476551ED24 CRC64;
     MPGRGKGGKG GKGYGKVGAK RHAKKALRET ILGVTKPAIR RLARRGGVKR ISSLVYEETR
     AVLKGFLESV IRDSVTYTEH AKRKTVTALD VVYALKRQGK TLYGFGG