ID   DNBI_EHV1V              Reviewed;        1209 AA.
AC   Q6S6P0;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-JUN-2021, entry version 44.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; OrderedLocusNames=31;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAS45915.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45915.1; -; Genomic_DNA.
DR   SMR; Q6S6P0; -.
DR   PRIDE; Q6S6P0; -.
DR   Proteomes; UP000008296; 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; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1209
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000115751"
FT   ZN_FING         503..516
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   REGION          290..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1209
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   MOTIF           849..850
FT                   /note="Required for filament formation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1209 AA;  129956 MW;  4011AA5B39DD739F CRC64;
     MESAPKTVSL PVSPLGYVYA RQKASLQTGT VSLTAARSVD SDLAVLPVIR GLTVEQTFTT
     NVAVVAGSKT TGLGGTGITL KLTPSHFNPS AFVFYGGSVI GASSNAPNLT RACEAARRRF
     GFSAFSSPPV ENAVETSGEE ICASLNLSPE TTALYLVVTE SFKEMVYVCN TFLHYGGTST
     VTIDGQDAMK IPIYPVQLYM PDVNRLASEP FNAKHRSIGD EFVYSRPFFN SDLCRLLHGY
     VLGPAAVALR VRNLDGVARG AAHLALDENH EGSVLPQDVT FTLFDSTQGN AGKGSGRAQR
     QGDGSGSKNS ASSGIERRLA SVMAADTALS VDSIMGAGIY DTELPSVEDW PVLSSGDDTE
     SLEALGAYAA RLSGLVGAMV FSANSVLYMT EVDDGGPADG KDGSNPSYHR FYLIAAPYVA
     GNPQTDKDGR VLPHTADQQA APINGSNQEF SLDYLALACG FCPQILARLL FYLERCDAGT
     FGGRNETDAL RYLANTLESD VPCGLCNQAT RPACAHTTLH RLRQRLPRFG APVRAPIGIF
     GTMNSAYSDC DVLGNYASYG ALKRPNDNEA PKSIMQDTYR ATMERLVNEL EQAKLIDKET
     LAQASPCSAP TSVVHDQASF IGLLSNIKDT IEGAAEQFMR TLVEARDFKI REGLADANHT
     MSISLDPYSS SFCPVTSFLA RRTVFAVLQD LVLSQCHCLF YGQSVEGRNF RNQFQPVLRR
     RFLDMLNGGF ITAKTVTVTV SDSGVLAPDL TRPASEPPTK DYDGDMARVS MEVLRDLRVK
     NRVLFSNGGA NMSEAARARV AGMASAYRRP DKGSNILNGA VGFLVKQYHG VLFPRGHPPG
     IDTPNPQWFW TLLQRNQMPA RLLSKEDIET ITAIKRFSDE YSAINFINLT PNNIGELAQF
     YFANLVLKYC DHSQYFINGL TAIVVGSRRP RDPAAVLAWI DRTINGAADV EPAAQEVLQR
     LGSNPAAWTG TFTSTNMVRY VMDQRPMVVI GLSISKYNGS AGNNRVFQAG NWNGLNGGKN
     VCPLMAFDRT RRFVLACPRV GFTCEAGGFG TGVRENTLSE QVRGIVSEGG PMVQTAVFAA
     VLHALGARTQ HLAVDDWIGL VDDEFLAASL DALNATVVDQ FGEWSVEAAQ ELVKNMEAQT
     TAGAVAAGEG AFDFGACVGD TPQQSTSAFN GGLAMAAAPA GQKRSLPDDI LFDMGAPPEK
     KSGLTFDML