ID   H2B2A_MELV              Reviewed;         269 AA.
AC   A0A097I2B5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Histone doublet H2B-H2A {ECO:0000303|PubMed:34297924};
DE   AltName: Full=Histone H2B-H2A fusion protein {ECO:0000303|PubMed:34297924};
DE   AltName: Full=MV-H2B-H2A {ECO:0000303|PubMed:34297924};
GN   ORFNames=MEL_369 {ECO:0000312|EMBL:AIT54982.1};
OS   Melbournevirus (MelV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Marseilleviridae; Marseillevirus;
OC   unclassified Marseillevirus.
OX   NCBI_TaxID=1560514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25275139; DOI=10.1128/jvi.02414-14;
RA   Doutre G., Philippe N., Abergel C., Claverie J.M.;
RT   "Genome analysis of the first Marseilleviridae representative from
RT   Australia indicates that most of its genes contribute to virus fitness.";
RL   J. Virol. 88:14340-14349(2014).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DOMAIN.
RX   PubMed=34297924; DOI=10.1016/j.cell.2021.06.032;
RA   Liu Y., Bisio H., Toner C.M., Jeudy S., Philippe N., Zhou K., Bowerman S.,
RA   White A., Edwards G., Abergel C., Luger K.;
RT   "Virus-encoded histone doublets are essential and form nucleosome-like
RT   structures.";
RL   Cell 184:4237-4250.e19(2021).
CC   -!- FUNCTION: Histone-like protein that is recruited to viral factories
CC       during viral replication and participates in viral DNA packaging and
CC       virion production probably by forming unstable nucleosome-like
CC       particles (PubMed:34297924). May compact the viral DNA
CC       (PubMed:34297924). {ECO:0000269|PubMed:34297924}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:34297924}. Host
CC       cytoplasm {ECO:0000269|PubMed:34297924}. Virion
CC       {ECO:0000269|PubMed:34297924}. Note=Localize to cytoplasmic viral
CC       factories after virus infection (PubMed:34297924). Also present in the
CC       nucleus but at much lower concentration (PubMed:34297924). The viral
CC       histones that localize in the nucleus apparently do not interact with
CC       host genomic DNA and can leave the nucleus to associate with the viral
CC       factory (PubMed:34297924). {ECO:0000269|PubMed:34297924}.
CC   -!- INDUCTION: Expression of viral histones begins 2-4 hpi and continues
CC       along the infectious cycle. {ECO:0000269|PubMed:34297924}.
CC   -!- DOMAIN: The N-terminus is similar to eukaryotic H2B, whereas the
CC       central region is similar to eukaryotic H2A.
CC       {ECO:0000269|PubMed:34297924}.
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DR   EMBL; KM275475; AIT54982.1; -; Genomic_DNA.
DR   RefSeq; YP_009094870.1; NC_025412.1.
DR   PDB; 7LV8; EM; 3.40 A; D/H=1-104.
DR   PDB; 7N8N; EM; 3.89 A; B/D=2-269.
DR   PDBsum; 7LV8; -.
DR   PDBsum; 7N8N; -.
DR   SMR; A0A097I2B5; -.
DR   GeneID; 21012390; -.
DR   KEGG; vg:21012390; -.
DR   Proteomes; UP000207668; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.20.10; -; 2.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   PANTHER; PTHR23430; PTHR23430; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA condensation; Host cytoplasm; Host nucleus; Virion.
FT   CHAIN           1..269
FT                   /note="Histone doublet H2B-H2A"
FT                   /id="PRO_0000454837"
FT   REGION          1..168
FT                   /note="Histone fold"
FT                   /evidence="ECO:0000305|PubMed:34297924"
FT   REGION          210..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  28829 MW;  FDBA6FF502376754 CRC64;
     MATQKETTRK RDKSVNFRLG LRNMLAQIHP DISVQTEALS ELSNIAVFLG KKISHGAVTL
     LPEGTKTIKS SAVLLAAGDL YGKDLGRHAV GEMTKAVTRY GSAKESKEGS RSSKAKLQIS
     VARSERLLRE HGGCSRVSEG AAVALAAAIE YFMGEVLELA GNAARDSKKV RISVKHITLA
     IQNDAALFAV VGKGVFSGAG VSLISVPIPR KKARKTTEKE ASSPKKKAAP KKKKAASKQK
     KSLSDKELAK LTKKELAKYE KEQGMSPGY