ID   H4_BLAAD                Reviewed;         103 AA.
AC   Q8J1L3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Histone H4;
GN   Name=ahsb4;
OS   Blastobotrys adeninivorans (Yeast) (Arxula adeninivorans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Blastobotrys.
OX   NCBI_TaxID=409370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LS3;
RA   Wartmann T., Bellebna C., Boeer E., Gellissen G., Kunze G.;
RT   "The constitutive AHSB4-promoter - a novel component of the Arxula
RT   adeninivorans-based expression platform.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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   -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by
CC       promoting dissociation of the H2A-H2B dimers from nucleosomes.
CC       {ECO:0000250|UniProtKB:P02309}.
CC   -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR   EMBL; AJ535732; CAD59972.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J1L3; -.
DR   SMR; Q8J1L3; -.
DR   PRIDE; Q8J1L3; -.
DR   PhylomeDB; Q8J1L3; -.
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   GO; GO:0006352; P:DNA-templated transcription, initiation; 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   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00047; HISTONE_H4; 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..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158279"
FT   DNA_BIND        17..21
FT   MOD_RES         92
FT                   /note="N6-glutaryllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02309"
SQ   SEQUENCE   103 AA;  11398 MW;  6A3A6008C509CD61 CRC64;
     MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISAL IYEETRSVLK
     TFLESVIRDA VTYTEHAKRK TVTSLDVVYA LKRQGRTLYG FGG