ID   DNBI_SHV21              Reviewed;        1128 AA.
AC   P24910;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=6, KFRF1;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2154888; DOI=10.1016/0042-6822(90)90107-3;
RA   Albrecht J.-C., Fleckenstein B.;
RT   "Structural organization of the conserved gene block of Herpesvirus saimiri
RT   coding for DNA polymerase, glycoprotein B, and major DNA binding protein.";
RL   Virology 174:533-542(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RX   PubMed=1850023; DOI=10.1128/jvi.65.5.2457-2466.1991;
RA   Nicholas J., Coles L.S., Newman C., Honess R.W.;
RT   "Regulation of the herpesvirus saimiri (HVS) delayed-early 110-kilodalton
RT   promoter by HVS immediate-early gene products and a homolog of the Epstein-
RT   Barr virus R trans activator.";
RL   J. Virol. 65:2457-2466(1991).
CC   -!- FUNCTION: Single-stranded DNA-binding protein required for DNA
CC       replication.
CC   -!- FUNCTION: Plays several crucial roles in viral infection. Participates
CC       in the opening of the viral DNA origin to initiate replication by
CC       interacting with the origin-binding protein. May disrupt loops,
CC       hairpins and other secondary structures present on ssDNA to reduce and
CC       eliminate pausing of viral DNA polymerase at specific sites during
CC       elongation. Promotes viral DNA recombination by performing strand-
CC       transfer, characterized by the ability to transfer a DNA strand from a
CC       linear duplex to a complementary single-stranded DNA circle. Can also
CC       catalyze the renaturation of complementary single strands.
CC       Additionally, reorganizes the host cell nucleus, leading to the
CC       formation of prereplicative sites and replication compartments. This
CC       process is driven by the protein which can form double-helical
CC       filaments in the absence of DNA. {ECO:0000255|HAMAP-Rule:MF_04007}.
CC   -!- SUBUNIT: Homooligomers. Forms double-helical filaments necessary for
CC       the formation of replication compartments within the host nucleus.
CC       Interacts with the origin-binding protein. Interacts with the helicase
CC       primase complex; this interaction stimulates primer synthesis activity
CC       of the helicase-primase complex. Interacts with the DNA polymerase.
CC       Interacts with the alkaline exonuclease; this interaction increases its
CC       nuclease processivity. {ECO:0000255|HAMAP-Rule:MF_04007}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007}.
CC       Note=In the absence of DNA replication, found in the nuclear framework-
CC       associated structures (prereplicative sites). As viral DNA replication
CC       proceeds, it migrates to globular intranuclear structures (replication
CC       compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
CC   -!- SIMILARITY: Belongs to the herpesviridae major DNA-binding protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_04007}.
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; X64346; CAA45629.1; -; Genomic_DNA.
DR   EMBL; M31122; AAA46162.1; -; Genomic_DNA.
DR   EMBL; M60849; AAA46157.1; -; Genomic_DNA.
DR   RefSeq; NP_040208.1; NC_001350.1.
DR   SMR; P24910; -.
DR   PRIDE; P24910; -.
DR   GeneID; 1682456; -.
DR   KEGG; vg:1682456; -.
DR   Proteomes; UP000000587; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.190.40; -; 2.
DR   HAMAP; MF_04007; HSV_DNBI; 1.
DR   InterPro; IPR035989; DBP_sf.
DR   InterPro; IPR043031; Viral_ssDBP_head.
DR   InterPro; IPR000635; Viral_ssDNA-bd.
DR   Pfam; PF00747; Viral_DNA_bp; 1.
DR   SUPFAM; SSF118208; SSF118208; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Host nucleus; Metal-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..1128
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000115755"
FT   ZN_FING         453..466
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   REGION          1098..1128
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1128 AA;  127458 MW;  BA3ADE861381328D CRC64;
     MATKTAQPSA DNLGSRAPVE PCGYIYVYPK EGFPFKEASL LGNKNVGASA MSLPLLSDLT
     VESNFSFNVK AVHKKIDMTT LLVRVSAYHR EAIVFFNTDL FEPIFVGPGL DILCSDARSL
     FGYTNFVPRT DLRDTVDIKD LYAPFYSEDS CFMAVVVTEG FKERLYFGNL VPIIAQGLKV
     QINGREAVKI PLYDEDLFSK SHEHLPRFYI PSVSKYLHDS VFTSIAQALR IRDVESVIRA
     SEKQSIQDQY KLAKIVNSKD FSLQSVKCQD ASAFMVIDCI AAELAMSYGL SFLEAPQDPC
     AVLDYTSWPI FETAETEEDR IKAIQDWNAM MSVHVYTHLF STNSVLYLTK INKQTQSNKS
     EQNVYNTYFM QHGLAYAADA TQRENGEPAF SGAPKFSGGT YTLYHLALAS SFSPHLLARN
     CYYMQFCQHQ KSTTNANYSV PQYVGTAAAS DLCELCQGTC PASCIHTLFY RLKDRFPPVL
     GSQRRDPYVV TGVSGQYNDL DMLGNFATFR EKEDEAVQNA ESEKYTYWQL IQNVVEKLST
     MGVTEGTVGS ELITDIQSFL KTFRDIDNVV DSEVVKFMNC LVKNNINFRE TIKTVHHVLH
     YCCNVFWQAP CAMFLNLFYK SVLAIIQDIC LPIAMTYEQD NPSIGMMPSE WLKVHYQTIW
     TNFKSSCLDR GVLTGSEHKI VHTDMFCDFL NIDSALSGQI VPMKMQVRLA KALLTVPKTI
     KIKNRIVFSN SSMTETIQSG FIKSATKKDS YIVTGPYMKF LNSLHKVMFP NAKISALYLW
     HTFSQKKQLP VLPGISRENM VELANYVETS SKMHDDMNVL DIIPTTLLTY AKVRLNNTIL
     RTCGQTQFYA TTLQCLLPTL QTISATEYPH VLLDQSIMSV DHYLSSIKDK HALTVQTTLK
     EDIATVGKQR PIVTVPLVVN KYTGINGNTQ IFQCGNLGYF MGRGVDRNLI PDSTGFRRQN
     NSSYMRRRHV FMTPMVAHLV KKNSNLNNLT FEVETIRKNV QNIFEDKDNL NIFDNVVLEL
     VKGLGDSCEN ITEDDLQFYL GEYYIMSDEI WSRFQIITDS GAPWSVENVT KVLGCNKQEE
     CKFEFVGVEE QLSCVPPQIE EFAPQATLST LAASRKRKIT SILSDIDL