ID   DNBI_EHV2               Reviewed;        1145 AA.
AC   Q66611;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=6;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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}.
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DR   EMBL; U20824; AAC13793.1; -; Genomic_DNA.
DR   PIR; S55600; S55600.
DR   RefSeq; NP_042602.1; NC_001650.2.
DR   SMR; Q66611; -.
DR   GeneID; 1461061; -.
DR   KEGG; vg:1461061; -.
DR   Proteomes; UP000007083; Genome.
DR   GO; GO:0042025; C:host cell nucleus; 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; 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; Reference proteome.
FT   CHAIN           1..1145
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000406168"
FT   REGION          1115..1145
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1145 AA;  126491 MW;  AB45BCDD3C5C472C CRC64;
     MNSNRAAAGP VEENVGTQAS VGPCGFVYLY PGDTFPVEEA SLLGNLHAGG EVFSLPLLSG
     LTVEADFHVN VKAVHKKLDP ATVSVKASAY HREVIVFANA ACFKPIFAGP GLEGLCAASR
     QLFGYAEFEE RAGGAARPFE LADLGHLLPG AESHIAGVVV TESFKERLYR GQLVVVESQI
     QSVRVGECDA FKVPLYDGEL FAKSPCRENL RYFYHAGVSR YLFEAHYTSL AQALRVRDVP
     GLIGALERQS FHDQYKLPKV YECREFPATG HRGAGDCSLT IVDSVATELA VSYGLSFLEV
     PQEGTALLSY DKWPIFEGCE TPEQRVEALT QFNAKQAVHV HSQLFSGNSV LYLARVQKQA
     SNRGGGGENV YNSFFMGHGL ACLAEPTQKE NGLPSFPGVP ASALSGSNYS LHHLAYAASF
     SPQMLARHCY YLQFAQHQKS SNNSGYNVPT YVGTAANTPM CELCRGSCPA SCVNTLFYRL
     RDRFPPVVAS VRRDPYVVTG VAGAYNDLDI AGNFANYRDK DEESNQSEER EKFTYWQVTQ
     TVLERLSEAG ICEGGEDVGD AIHNIGSFLK VFKEIDGIVD GEVARFINSM VKNNVNYRES
     IKSIHHIVQY VCNVYWQPPC PVFLNLYYRC VLAVVQDICL PTCMMYEQEN PAVGVSPGEW
     LKMHYQTLWT NFKNSCIDKG VLTGTEYKVV HKDQFCDFFD VDSAARGEFV SCKTQVRISR
     ALMMAPRVMK IKNRIIFSNS PGTESIQNAF VRGTPKGDSC VVSGPYMRFL STYHSQLFPG
     AKISPLFLWH TFSKKRQLPV FPNVPRESVT ELANYVEQNS RLHGETSIID VVPENFYTYA
     KVRLNNALFR ACGQTQFYAT TIHCLTPKIQ TVPAEEYPHA LGARGVADVG EYLGAARELT
     VPTVQCTSRD NICEVGKCRP IVTLPLVVNK YTGVTGNSQI FQCANLGYFI GRGVDKNLIP
     DAGSFKKQGV STSMRKRHVF MTPLSDHLLR RSVQGAAVAF EIEGVRRRVQ QILSDGDNPH
     VIRDVVLQLV KSLGSECRSV SEYDLEYYMG QYYIFAGDVS ERLQRLSDLG GDWSEEWALS
     VLGEEEDPLG GELEFEKVED AECLGHPQQD EFALAPQAAA PQYSGSSSVA GKKRKANVIL
     GDLDL