ID A0A0V0VHM6_9BILA Unreviewed; 119 AA.
AC A0A0V0VHM6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Histone H2B {ECO:0000256|RuleBase:RU000451};
GN Name=H2B-VII {ECO:0000313|EMBL:KRX62869.1};
GN ORFNames=T06_13540 {ECO:0000313|EMBL:KRX70034.1}, T06_7711
GN {ECO:0000313|EMBL:KRX62869.1}, T06_8523 {ECO:0000313|EMBL:KRX51431.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX62869.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX62869.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX62869.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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: Nucleus {ECO:0000256|RuleBase:RU000451}.
CC -!- SIMILARITY: Belongs to the histone H2B family.
CC {ECO:0000256|ARBA:ARBA00006846, ECO:0000256|RuleBase:RU000451}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX62869.1}.
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DR EMBL; JYDK01000968; KRX51431.1; -; Genomic_DNA.
DR EMBL; JYDK01000507; KRX62869.1; -; Genomic_DNA.
DR EMBL; JYDK01000310; KRX70034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VHM6; -.
DR STRING; 92179.A0A0V0VHM6; -.
DR Proteomes; UP000054673; 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 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:UP000054673}.
FT DOMAIN 14..94
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 119 AA; 13439 MW; A72E65501FAE9A9C CRC64;
MTPKGIKKAG ELQKVAKSGD RRRRRLRKES FASYIYKVLK QVHADTGISS RAMSIMNSFV
NDIFDRLAAE ASRLAQYNQR HTITSREIQT AVRLLLPGEL CKHAVSEGTK AVNKYNCGR
//