ID A0A183W1V6_TRIRE Unreviewed; 132 AA.
AC A0A183W1V6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Histone H4 {ECO:0000256|ARBA:ARBA00020836, ECO:0000256|RuleBase:RU000528};
GN ORFNames=TRE_LOCUS6715 {ECO:0000313|EMBL:VDQ02595.1};
OS Trichobilharzia regenti (Nasal bird schistosome).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000671701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TRE_0000671701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDQ02595.1, ECO:0000313|Proteomes:UP000280995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 {ECO:0000256|ARBA:ARBA00002001, ECO:0000256|RuleBase:RU000528}.
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. {ECO:0000256|RuleBase:RU000528}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H4 family.
CC {ECO:0000256|ARBA:ARBA00006564, ECO:0000256|RuleBase:RU000528}.
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DR EMBL; UZAO01057215; VDQ02595.1; -; Genomic_DNA.
DR STRING; 157069.A0A183W1V6; -.
DR WBParaSite; TRE_0000671701-mRNA-1; TRE_0000671701-mRNA-1; TRE_0000671701.
DR Proteomes; UP000280995; Unassembled WGS sequence.
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; Histone, subunit A; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR PANTHER; PTHR10484; HISTONE H4; 1.
DR PANTHER; PTHR10484:SF0; HISTONE H4; 1.
DR Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU000528};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000528};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW ECO:0000256|RuleBase:RU000528};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000528};
KW Reference proteome {ECO:0000313|Proteomes:UP000280995}.
FT DOMAIN 45..107
FT /note="CENP-T/Histone H4 histone fold"
FT /evidence="ECO:0000259|Pfam:PF15511"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 15013 MW; E86DAD8FB97F0DFC CRC64;
MSGRGKGGKG LGKGRAKRHR KVLRDNVQGI TKQAIHRLVR RGGVKHISGL IYEETRGVLK
VFLENLIRDA VTYTEHEERK TVTAIDVVYA LKRQGRTESR GMSRQLCRAK GQMWLKRCRQ
SSIYGDHNLT SL
//
