ID   H4_ENCCU                Reviewed;         103 AA.
AC   Q8SQP4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Histone H4;
GN   Name=HHF1; OrderedLocusNames=ECU09_0440;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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-94 (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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590451; CAD27016.1; -; Genomic_DNA.
DR   RefSeq; XP_955597.1; XM_950504.1.
DR   AlphaFoldDB; Q8SQP4; -.
DR   SMR; Q8SQP4; -.
DR   STRING; 284813.Q8SQP4; -.
DR   GeneID; 860382; -.
DR   KEGG; ecu:ECU09_0440; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_0440; -.
DR   HOGENOM; CLU_109117_2_3_1; -.
DR   InParanoid; Q8SQP4; -.
DR   OMA; QKEHING; -.
DR   OrthoDB; 1594208at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
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; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   CHAIN           1..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158314"
FT   DNA_BIND        20..24
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         94
FT                   /note="N6-glutaryllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02309"
SQ   SEQUENCE   103 AA;  11377 MW;  99157B2D0327AF67 CRC64;
     MNTQSIGAKG KSKAAKGIAK RHRKQSSLSD SISKPAIRRI ARRAGVRRVG GGCFKEINNA
     AREYIRDTLS IACIYATHAK RKTITCSDIL HSLKRMGIKY IGY