ID   DNBI_EBVB9              Reviewed;        1128 AA.
AC   P03227; Q777A7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 91.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; ORFNames=BALF2;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
RN   [2]
RP   FUNCTION.
RX   PubMed=8806519; DOI=10.1006/viro.1996.0432;
RA   Tsurumi T., Kobayashi A., Tamai K., Yamada H., Daikoku T., Yamashita Y.,
RA   Nishiyama Y.;
RT   "Epstein-Barr virus single-stranded DNA-binding protein: purification,
RT   characterization, and action on DNA synthesis by the viral DNA
RT   polymerase.";
RL   Virology 222:352-364(1996).
RN   [3]
RP   INTERACTION WITH BALF5; BMRF1 AND BGLF5.
RX   PubMed=9434720; DOI=10.1006/viro.1997.8891;
RA   Zeng Y., Middeldorp J., Madjar J.J., Ooka T.;
RT   "A major DNA binding protein encoded by BALF2 open reading frame of
RT   Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding
RT   proteins: DNAase, EA-D, and DNA polymerase.";
RL   Virology 239:285-295(1997).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA   Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA   Illanes D., Sarracino D., Kieff E.;
RT   "Proteins of purified Epstein-Barr virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15731235; DOI=10.1128/jvi.79.6.3409-3418.2005;
RA   Daikoku T., Kudoh A., Fujita M., Sugaya Y., Isomura H., Shirata N.,
RA   Tsurumi T.;
RT   "Architecture of replication compartments formed during Epstein-Barr virus
RT   lytic replication.";
RL   J. Virol. 79:3409-3418(2005).
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       ECO:0000269|PubMed:9434720}.
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       ECO:0000269|PubMed:8806519}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:15534216}.
CC       Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007,
CC       ECO:0000269|PubMed:15731235}. Note=In the absence of DNA replication,
CC       found in the nuclear framework-associated structures (prereplicative
CC       sites). As viral DNA replication proceeds, it migrates to globular
CC       intranuclear structures (replication compartments). {ECO:0000255|HAMAP-
CC       Rule:MF_04007}.
CC   -!- SIMILARITY: Belongs to the herpesviridae major DNA-binding protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_04007}.
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DR   EMBL; V01555; CAA24808.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53467.1; -; Genomic_DNA.
DR   PIR; A43045; QQBE47.
DR   RefSeq; YP_401717.1; NC_007605.1.
DR   SMR; P03227; -.
DR   IntAct; P03227; 8.
DR   MINT; P03227; -.
DR   PRIDE; P03227; -.
DR   DNASU; 3783678; -.
DR   GeneID; 3783678; -.
DR   KEGG; vg:3783678; -.
DR   Proteomes; UP000153037; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   DNA replication; DNA-binding; Host nucleus; Reference proteome; Virion;
KW   Virion tegument.
FT   CHAIN           1..1128
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000115758"
FT   REGION          1104..1128
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1128 AA;  123122 MW;  283D5258031A16D6 CRC64;
     MQGAQTSEDN LGSQSQPGPC GYIYFYPLAT YPLREVATLG TGYAGHRCLT VPLLCGITVE
     PGFSINVKAL HRRPDPNCGL LRATSYHRDI YVFHNAHMVP PIFEGPGLEA LCGETREVFG
     YDAYSALPRE SSKPGDFFPE GLDPSAYLGA VAITEAFKER LYSGNLVAIP SLKQEVAVGQ
     SASVRVPLYD KEVFPEGVPQ LRQFYNSDLS RCMHEALYTG LAQALRVRRV GKLVELLEKQ
     SLQDQAKVAK VAPLKEFPAS TISHPDSGAL MIVDSAACEL AVSYAPAMLE ASHETPASLN
     YDSWPLFADC EGPEARVAAL HRYNASLAPH VSTQIFATNS VLYVSGVSKS TGQGKESLFN
     SFYMTHGLGT LQEGTWDPCR RPCFSGWGGP DVTGTNGPGN YAVEHLVYAA SFSPNLLARY
     AYYLQFCQGQ KSSLTPVPET GSYVAGAAAS PMCSLCEGRA PAVCLNTLFF RLRDRFPPVM
     STQRRDPYVI SGASGSYNET DFLGNFLNFI DKEDDGQRPD DEPRYTYWQL NQNLLERLSR
     LGIDAEGKLE KEPHGPRDFV KMFKDVDAAV DAEVVQFMNS MAKNNITYKD LVKSCYHVMQ
     YSCNPFAQPA CPIFTQLFYR SLLTILQDIS LPICMCYEND NPGLGQSPPE WLKGHYQTLC
     TNFRSLAIDK GVLTAKEAKV VHGEPTCDLP DLDAALQGRV YGRRLPVRMS KVLMLCPRNI
     KIKNRVVFTG ENAALQNSFI KSTTRRENYI INGPYMKFLN TYHKTLFPDT KLSSLYLWHN
     FSRRRSVPVP SGASAEEYSD LALFVDGGSR AHEESNVIDV VPGNLVTYAK QRLNNAILKA
     CGQTQFYISL IQGLVPRTQS VPARDYPHVL GTRAVESAAA YAEATSSLTA TTVVCAATDC
     LSQVCKARPV VTLPVTINKY TGVNGNNQIF QAGNLGYFMG RGVDRNLLQA PGAGLRKQAG
     GSSMRKKFVF ATPTLGLTVK RRTQAATTYE IENIRAGLEA IISQKQEEDC VFDVVCNLVD
     AMGEACASLT RDDAEYLLGR FSVLADSVLE TLATIASSGI EWTAEAARDF LEGVWGGPGA
     AQDNFISVAE PVSTASQASA GLLLGGGGQG SGGRRKRRLA TVLPGLEV