ID A0A1I7U4Q9_9PELO Unreviewed; 122 AA.
AC A0A1I7U4Q9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Histone H2B {ECO:0000256|RuleBase:RU000451};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g14828.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g14828.t1, ECO:0000313|WBParaSite:Csp11.Scaffold629.g14833.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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|ARBA:ARBA00011538, ECO:0000256|RuleBase:RU000451}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, 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 AlphaFoldDB; A0A1I7U4Q9; -.
DR STRING; 1561998.A0A1I7U4Q9; -.
DR WBParaSite; Csp11.Scaffold629.g14828.t1; Csp11.Scaffold629.g14828.t1; Csp11.Scaffold629.g14828.
DR WBParaSite; Csp11.Scaffold629.g14833.t1; Csp11.Scaffold629.g14833.t1; Csp11.Scaffold629.g14833.
DR eggNOG; KOG1744; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
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:SF367; H2B.W HISTONE 2; 1.
DR PANTHER; PTHR23428; 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}.
FT DOMAIN 11..97
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13489 MW; 24695A47AD75960A CRC64;
MPPKPSAKGA KKAAKTVTKP KDGKKRKHSR KESYSVYIYR VLKQVHPDTG VSSKAMSIMN
SFVNDVFERI AAEASRLAHY NKRSTISSRE IQTAVRLILP GELAKHAVSE GTKAVTKYTS
SK
//