ID   DVNP5_HEMSX             Reviewed;         132 AA.
AC   K9NVA6;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Dinoflagellate viral nucleoprotein 5 {ECO:0000303|PubMed:29670105};
DE            Short=DNVP5 {ECO:0000303|PubMed:29670105};
OS   Hematodinium sp.
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Syndiniales; Syndiniaceae;
OC   Hematodinium; unclassified Hematodinium.
OX   NCBI_TaxID=173654;
RN   [1] {ECO:0000312|EMBL:AFY23231.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION.
RX   PubMed=23159597; DOI=10.1016/j.cub.2012.10.036;
RA   Gornik S.G., Ford K.L., Mulhern T.D., Bacic A., McFadden G.I., Waller R.F.;
RT   "Loss of nucleosomal DNA condensation coincides with appearance of a novel
RT   nuclear protein in dinoflagellates.";
RL   Curr. Biol. 22:2303-2312(2012).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=29670105; DOI=10.1038/s41467-018-03993-4;
RA   Irwin N.A.T., Martin B.J.E., Young B.P., Browne M.J.G., Flaus A.,
RA   Loewen C.J.R., Keeling P.J., Howe L.J.;
RT   "Viral proteins as a potential driver of histone depletion in
RT   dinoflagellates.";
RL   Nat. Commun. 9:1535-1535(2018).
CC   -!- FUNCTION: DNA-binding protein, which similarly to histones, may compact
CC       DNA into chromatin. {ECO:0000269|PubMed:29670105,
CC       ECO:0000305|PubMed:23159597}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23159597,
CC       ECO:0000269|PubMed:29670105}. Chromosome {ECO:0000269|PubMed:23159597}.
CC       Note=Localizes to condensed chromosomes (PubMed:23159597). Localizes
CC       upstream and downstream of transcription start sites of chromatin
CC       (PubMed:29670105). {ECO:0000269|PubMed:23159597,
CC       ECO:0000269|PubMed:29670105}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:23159597}.
CC   -!- MISCELLANEOUS: In yeast, DVNP5 binds to histone binding sites in
CC       chromatin and displaces nucleosomes, and impairs transcription and
CC       inhibits cell growth. {ECO:0000269|PubMed:29670105}.
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DR   EMBL; JX839700; AFY23231.1; -; mRNA.
DR   AlphaFoldDB; K9NVA6; -.
DR   SMR; K9NVA6; -.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   InterPro; IPR043928; DNVP.
DR   Pfam; PF19060; DVNP; 1.
PE   1: Evidence at protein level;
KW   Chromosome; DNA condensation; DNA-binding; Nucleus; Phosphoprotein.
FT   CHAIN           1..132
FT                   /note="Dinoflagellate viral nucleoprotein 5"
FT                   /id="PRO_0000450801"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..45
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   132 AA;  14359 MW;  10018DB1571EA7A3 CRC64;
     MAAMKKAMKV KKSAKKSAKK SGKKGGMKKK AKRVSKVARG KRAKSSVFRG TKERTSGGLT
     KNSLVKNKQG RVVSKKQSEH GKKIFKKHGL QKWIDAVTKA RKALGIKGFQ AVGGSSAKGK
     ILLAKSRSFY KK