ID   VHLP_ASFP4              Reviewed;         104 AA.
AC   P0C9E3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Viral histone-like protein;
DE   AltName: Full=DNA-binding protein pA104R {ECO:0000250|UniProtKB:P68742};
DE   AltName: Full=pA104R;
GN   OrderedLocusNames=Pret-047;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-binding protein that plays a critical role in nucleoid
CC       compaction, genome replication and DNA replication and transcription
CC       (By similarity). Binds to both ssDNA and dsDNA with a binding site
CC       covering about 15 nucleotides (By similarity). Displays DNA-
CC       supercoiling activity only when associated with the viral DNA
CC       topoisomerase 2 (By similarity). {ECO:0000250|UniProtKB:P68742}.
CC   -!- ACTIVITY REGULATION: Stilbene derivatives SD1 and SD4 disrupt the
CC       binding between pA104R and DNA and inhibit the viral replication in
CC       primary alveolar macrophages. {ECO:0000250|UniProtKB:P68742}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P68742}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P68742}. Note=Found
CC       in association with viral nucleoid. {ECO:0000250|UniProtKB:P68742}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000250|UniProtKB:P68742}.
CC   -!- MISCELLANEOUS: Host antibody response against A104R protein is higher
CC       in asymptomatic than in chronically infected hosts.
CC       {ECO:0000250|UniProtKB:P68742}.
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9E3; -.
DR   Proteomes; UP000000859; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.520.10; -; 1.
DR   InterPro; IPR000119; Hist_DNA-bd.
DR   InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR   InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR   PANTHER; PTHR33175; PTHR33175; 1.
DR   Pfam; PF00216; Bac_DNA_binding; 1.
DR   SMART; SM00411; BHL; 1.
DR   SUPFAM; SSF47729; SSF47729; 1.
DR   PROSITE; PS00045; HISTONE_LIKE; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Late protein; Virion.
FT   CHAIN           1..104
FT                   /note="Viral histone-like protein"
FT                   /id="PRO_0000373161"
FT   SITE            57
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            69
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            72
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            74
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            83
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            85
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            92
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            94
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            96
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
FT   SITE            97
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P68742"
SQ   SEQUENCE   104 AA;  11609 MW;  939515B48C793AF8 CRC64;
     MSTKKKPTIT KQELYSLVAA DTQLNKALIE RIFTSQQKII QNALKHNQEV IIPPGIKFTV
     VTVKAKPARQ GHNPATGEPI QIKAKPEHKA VKIRALKPVH DMLN