ID K8EFG9_9CHLO Unreviewed; 163 AA.
AC K8EFG9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Histone H2B {ECO:0000256|RuleBase:RU000451};
GN ORFNames=Bathy05g02660 {ECO:0000313|EMBL:CCO16771.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO16771.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO16771.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO16771.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) 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}.
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:RU000451}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|RuleBase:RU000451}.
CC -!- SIMILARITY: Belongs to the histone H2B family.
CC {ECO:0000256|ARBA:ARBA00006846, ECO:0000256|RuleBase:RU000451}.
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DR EMBL; FO082274; CCO16771.1; -; Genomic_DNA.
DR RefSeq; XP_007513213.1; XM_007513151.1.
DR AlphaFoldDB; K8EFG9; -.
DR STRING; 41875.K8EFG9; -.
DR GeneID; 19015769; -.
DR KEGG; bpg:Bathy05g02660; -.
DR eggNOG; KOG1744; Eukaryota.
DR Proteomes; UP000198341; Chromosome_5.
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; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; HISTONE H2B; 1.
DR PANTHER; PTHR23428:SF70; HISTONE H2B; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|RuleBase:RU000451};
KW DNA-binding {ECO:0000256|RuleBase:RU000451};
KW Nucleosome core {ECO:0000256|RuleBase:RU000451};
KW Nucleus {ECO:0000256|RuleBase:RU000451};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT DOMAIN 6..89
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
SQ SEQUENCE 163 AA; 18457 MW; D98612F4ECBACB2C CRC64;
MAGKKPAKKT VKGGAKKSSK KKVETYKIYI YKVLKQVHPD TGISSKAMSI MNSFINDIFE
KIATEAAKLA RYNKKPTVTS REIQTSVRLI LPGELAKHAV SEGTKAVTSA FFFKFLQRVE
IYSPFQFSLY DYFSHHQNNR VYLRVSVHGL FSLLVTTTRA KTN
//
