ID A8DWE8_NEMVE Unreviewed; 104 AA.
AC A8DWE8;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Histone H2A/H2B/H3 domain-containing protein {ECO:0000259|Pfam:PF00125};
DE Flags: Fragment;
GN ORFNames=NEMVEDRAFT_v1g157309 {ECO:0000313|EMBL:EDO25461.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO25461.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO25461.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H2B family.
CC {ECO:0000256|ARBA:ARBA00006846}.
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DR EMBL; DS479531; EDO25461.1; -; Genomic_DNA.
DR RefSeq; XP_001617561.1; XM_001617511.1.
DR AlphaFoldDB; A8DWE8; -.
DR STRING; 45351.A8DWE8; -.
DR EnsemblMetazoa; EDO25461; EDO25461; NEMVEDRAFT_v1g157309.
DR GeneID; 5495712; -.
DR KEGG; nve:5495712; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; A8DWE8; -.
DR OrthoDB; 2910606at2759; -.
DR PhylomeDB; A8DWE8; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 6..97
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 104
FT /evidence="ECO:0000313|EMBL:EDO25461.1"
SQ SEQUENCE 104 AA; 11589 MW; 5F190806970F2727 CRC64;
MPPKSGKKPE ASKGKKNVVA GDKKKRKGRR KESYAIYIYK VLKQVHPDTG ISSKAMGIMN
SFVNDIFERI AAESSRLAHY NKKSTISSRE IQTAIRLLLP GELA
//
