ID J4C940_THEOR Unreviewed; 421 AA.
AC J4C940;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Histone H4 {ECO:0000256|RuleBase:RU000528};
GN ORFNames=TOT_040000253 {ECO:0000313|EMBL:BAM41873.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41873.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41873.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41873.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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|RuleBase:RU000528}.
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
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; AP011949; BAM41873.1; -; Genomic_DNA.
DR RefSeq; XP_009692174.1; XM_009693879.1.
DR AlphaFoldDB; J4C940; -.
DR STRING; 869250.J4C940; -.
DR EnsemblProtists; BAM41873; BAM41873; TOT_040000253.
DR GeneID; 20716336; -.
DR KEGG; tot:TOT_040000253; -.
DR VEuPathDB; PiroplasmaDB:TOT_040000253; -.
DR eggNOG; KOG1643; Eukaryota.
DR eggNOG; KOG3467; Eukaryota.
DR OrthoDB; 230291at2759; -.
DR Proteomes; UP000003786; Chromosome 4.
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:0004807; F:triose-phosphate isomerase activity; IEA:InterPro.
DR CDD; cd00076; H4; 1.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR PANTHER; PTHR10484; HISTONE H4; 1.
DR PANTHER; PTHR10484:SF0; HISTONE H4; 1.
DR Pfam; PF15511; CENP-T_C; 1.
DR Pfam; PF00121; TIM; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
DR PROSITE; PS51440; TIM_2; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000003786}.
FT DOMAIN 34..96
FT /note="CENP-T/Histone H4 histone fold"
FT /evidence="ECO:0000259|Pfam:PF15511"
SQ SEQUENCE 421 AA; 47194 MW; 4840EE534DC32216 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGV TKPAIRRLAR RGGVKRISGL IYEEVRGVLK
VFLENVVKDS VTYTEHARRK TVTAMDVVYS LKRQGRTLYG FGDSNYFVRN FKSLKNFFSN
RNSHDSNYNL YNSIANNGTL QTSTELKYED SHELRGKHLI IVCNWKCYLN NELANKFIRL
YGKLKFPRNI EIITCPASIH LNSMVAHYRE INSSCVPCSQ NVSDRSKSFG PYTGEITAGM
LKDLGVNWTI VGHRESEISE NTTSKNTKIV NKKVINAFNA GLNVILCIGS NFKIPQIHTG
EPENFNSNIP KHLSQELQEC LNGLDLNGGQ RLVVAYEPQC SVGTEKPADP ELVSKVIEEL
RASMGERGRM IKFIYGGSID GKNAVSYLKR KGIDGIMVGR AAQEESFMNL LENIIKMSRD
Y
//
