ID   A0A0N5BKM0_STREA        Unreviewed;       123 AA.
AC   A0A0N5BKM0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Histone H2B {ECO:0000256|RuleBase:RU000451};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000647600.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000647600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0N5BKM0; -.
DR   STRING; 174720.A0A0N5BKM0; -.
DR   WBParaSite; SPAL_0000647600.1; SPAL_0000647600.1; SPAL_0000647600.
DR   Proteomes; UP000046392; 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          8..98
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   123 AA;  13547 MW;  0ABA85BDFF26FFCD CRC64;
     MAPPTASKGK KAVKSQKAVR PSDKKGRRKA RKETYSIYIY RVLKQVHPDT GISSKAMSIM
     NSFVNDVFER IAGEASKLAT YNKKSTISSR EIQTSVRLIL PGELAKHAVS EGTKAVTKYT
     SSK
//