ID   DNBI_VZVO               Reviewed;        1199 AA.
AC   Q4JQU6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   02-JUN-2021, entry version 53.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; ORFNames=ORF29;
OS   Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC   Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA   Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT   its parental virus.";
RL   J. Virol. 76:11447-11459(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merk);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
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; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57643.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57714.1; -; Genomic_DNA.
DR   SMR; Q4JQU6; -.
DR   IntAct; Q4JQU6; 8.
DR   PRIDE; Q4JQU6; -.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; Genome.
DR   GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
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..1199
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000385136"
FT   ZN_FING         497..510
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   REGION          289..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1199
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   MOTIF           841..842
FT                   /note="Required for filament formation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   MOTIF           1146..1148
FT                   /note="Required for filament formation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   COMPBIAS        289..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1199 AA;  131712 MW;  1ABB1E2D11655EC8 CRC64;
     MENTQKTVTV PTGPLGYVYA CRVEDLDLEE ISFLAARSTD SDLALLPLMR NLTVEKTFTS
     SLAVVSGART TGLAGAGITL KLTTSHFYPS VFVFHGGKHV LPSSAAPNLT RACNAARERF
     GFSRCQGPPV DGAVETTGAE ICTRLGLEPE NTILYLVVTA LFKEAVFMCN VFLHYGGLDI
     VHINHGDVIR IPLFPVQLFM PDVNRLVPDP FNTHHRSIGE GFVYPTPFYN TGLCHLIHDC
     VIAPMAVALR VRNVTAVARG AAHLAFDENH EGAVLPPDIT YTYFQSSSSG TTTARGARRN
     DVNSTSKPSP SGGFERRLAS IMAADTALHA EVIFNTGIYE ETPTDIKEWP MFIGMEGTLP
     RLNALGSYTA RVAGVIGAMV FSPNSALYLT EVEDSGMTEA KDGGPGPSFN RFYQFAGPHL
     AANPQTDRDG HVLSSQSTGS SNTEFSVDYL ALICGFGAPL LARLLFYLER CDAGAFTGGH
     GDALKYVTGT FDSEIPCSLC EKHTRPVCAH TTVHRLRQRM PRFGQATRQP IGVFGTMNSQ
     YSDCDPLGNY APYLILRKPG DQTEAAKATM QDTYRATLER LFIDLEQERL LDRGAPCSSE
     GLSSVIVDHP TFRRILDTLR ARIEQTTTQF MKVLVETRDY KIREGLSEAT HSMALTFDPY
     SGAFCPITNF LVKRTHLAVV QDLALSQCHC VFYGQQVEGR NFRNQFQPVL RRRFVDLFNG
     GFISTRSITV TLSEGPVSAP NPTLGQDAPA GRTFDGDLAR VSVEVIRDIR VKNRVVFSGN
     CTNLSEAARA RLVGLASAYQ RQEKRVDMLH GALGFLLKQF HGLLFPRGMP PNSKSPNPQW
     FWTLLQRNQM PADKLTHEEI TTIAAVKRFT EEYAALNFIN LPPTCIGELA QFYMANLILK
     YCDHSQYLIN TLTSIITGAR RPRDPSSVLH WIRKDVTSAA DIETQAKALL EKTENLPELW
     TTAFTSTHLV RAAMNQRPMV VLGISISKYH GAAGNNRVFQ AGNWSGLNGG KNVCPLFTFD
     RTRRFIITCP RGGFICPVTG PSSGNRETTL SDQVRGIIVS GGAMVQLAIY ATVVRAVGAR
     AQHMAFDDWL SLTDDEFLAR DLEELHDQII QTLETPWTVE GALEAVKILD EKTTAGDGET
     PTNLAFNFDS CEPSHDTTSN VLNISGSTVP GLKRPPEDDE LFDLSGIPIK HGNITMEMI