ID R9A992_WALI9 Unreviewed; 103 AA.
AC R9A992;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Histone H4 {ECO:0000256|RuleBase:RU000528};
GN ORFNames=J056_000678 {ECO:0000313|EMBL:EOR00480.1}, J056_001039
GN {ECO:0000313|EMBL:EOR00153.1}, J056_001870
GN {ECO:0000313|EMBL:EOQ99314.1}, J056_002783
GN {ECO:0000313|EMBL:EOQ98830.1}, J056_002851
GN {ECO:0000313|EMBL:EOQ98741.1}, J056_004653
GN {ECO:0000313|EMBL:EOR00841.1}, J056_004720
GN {ECO:0000313|EMBL:EOR00908.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ98741.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
RN [2] {ECO:0000313|EMBL:EOQ98741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 {ECO:0000313|EMBL:EOQ98741.1};
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Haloadaptations revealed by genome and transcriptome sequencing of the
RT halophilic fungus Wallemia ichthyophaga.";
RL Submitted (MAR-2013) 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|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; KE007252; EOQ98741.1; -; Genomic_DNA.
DR EMBL; KE007249; EOQ98830.1; -; Genomic_DNA.
DR EMBL; KE007242; EOQ99314.1; -; Genomic_DNA.
DR EMBL; KE007236; EOR00153.1; -; Genomic_DNA.
DR EMBL; KE007234; EOR00480.1; -; Genomic_DNA.
DR EMBL; KE007232; EOR00841.1; -; Genomic_DNA.
DR EMBL; KE007232; EOR00908.1; -; Genomic_DNA.
DR RefSeq; XP_009268118.1; XM_009269843.1.
DR RefSeq; XP_009268185.1; XM_009269910.1.
DR RefSeq; XP_009268581.1; XM_009270306.1.
DR RefSeq; XP_009268942.1; XM_009270667.1.
DR RefSeq; XP_009269773.1; XM_009271498.1.
DR RefSeq; XP_009270323.1; XM_009272048.1.
DR RefSeq; XP_009270391.1; XM_009272116.1.
DR STRING; 1299270.R9A992; -.
DR GeneID; 20373630; -.
DR GeneID; 20373991; -.
DR GeneID; 20374822; -.
DR GeneID; 20375735; -.
DR GeneID; 20375803; -.
DR GeneID; 20377605; -.
DR GeneID; 20377672; -.
DR KEGG; wic:J056_000678; -.
DR KEGG; wic:J056_001039; -.
DR KEGG; wic:J056_001870; -.
DR KEGG; wic:J056_002783; -.
DR KEGG; wic:J056_002851; -.
DR KEGG; wic:J056_004653; -.
DR KEGG; wic:J056_004720; -.
DR eggNOG; KOG3467; Eukaryota.
DR HOGENOM; CLU_109117_2_3_1; -.
DR OrthoDB; 2782612at2759; -.
DR Proteomes; UP000014064; 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 InterPro; IPR019809; Histone_H4_CS.
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.
DR PROSITE; PS00047; HISTONE_H4; 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:UP000014064}.
FT DOMAIN 38..97
FT /note="CENP-T/Histone H4 histone fold"
FT /evidence="ECO:0000259|Pfam:PF15511"
SQ SEQUENCE 103 AA; 11448 MW; B74A432A2EC3CA28 CRC64;
MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDS VTYTEHAKRK TVTALDVVYA LKRQGRVLYG FGQ
//
