ID   DNBI_SUHVF              Reviewed;        1175 AA.
AC   P11870; Q5PPC5;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   02-DEC-2020, entry version 56.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=ICP8; ORFNames=UL29;
OS   Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1)
OS   (Pseudorabies virus (strain Indiana-Funkhauser / Becker)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31523;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14671123; DOI=10.1128/jvi.78.1.424-440.2004;
RA   Klupp B.G., Hengartner C.J., Mettenleiter T.C., Enquist L.W.;
RT   "Complete, annotated sequence of the pseudorabies virus genome.";
RL   J. Virol. 78:424-440(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RX   PubMed=2542904; DOI=10.1093/nar/17.9.3597;
RA   Pederson N.E., Enquist L.W.;
RT   "The nucleotide sequence of a pseudorabies virus gene similar to ICP18.5 of
RT   herpes simplex virus type 1.";
RL   Nucleic Acids Res. 17:3597-3597(1989).
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; BK001744; DAA02152.1; -; Genomic_DNA.
DR   EMBL; X14573; CAA32711.1; -; Genomic_DNA.
DR   PIR; S04145; S04145.
DR   RefSeq; YP_068332.1; NC_006151.1.
DR   SMR; P11870; -.
DR   PRIDE; P11870; -.
DR   GeneID; 2952495; -.
DR   KEGG; vg:2952495; -.
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..1175
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000116281"
FT   ZN_FING         496..509
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   REGION          1151..1175
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   MOTIF           825..826
FT                   /note="Required for filament formation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1175 AA;  125351 MW;  FA7C5137F15732FF CRC64;
     MEAAAKTVTV RAAPLGYVYV TPIEALRRDL LALLVARSAD DAAAVAPLVR GLTVEAGFAG
     HVAVVAGART TGLGGGLTLK LTPNHFHPNV FFFHNGDCVP PSSAAPALSR ACEAARARFG
     FSAYRTPVDN AEETTGAEVC ARLGLAADAH AAYLVVADGF KEAVYLCNAF LHYGGAGTVS
     INGHEAWRVP LYPVHLFMPD VNRLVADPFN AKNRSISEEF VYPRPFFNGP LCRLLHGYVL
     GPAAVATRVR NLDAVARGAA HLAFDENHES AVLPADVTFT LFEQRRRGGD AAAGGLERRM
     ASVMSADAAL SLEALVAAGV YDEEPPALDD WPVLSEAGAK DGGAAAASAG APVSQAAALG
     AYVSRAAGLV GALVFSSNSV LYLTEVDDAG AADARKEGAG PSFNRFYQVA APYLAGNPQT
     DKDGRVLLHT ASQPATAPGN HDFAMDHLVM ACGFCPQLLA RVLFYLERCD AGTFVGRGDV
     DAVRYVAGSL DAEVPCSLCD RASRPACAHT TLHRLRHRSR ASARRRSPMG VFGTMNSAYS
     DCDVLGNYAS YGALKRPNDS EPPKAIMQDT YRAAVDRLLA DVAGARIGET VTDHAGFRHA
     LRALRDTVEQ AADRFVRTLV ETRDFKLRDA LYDANHTMSL SLDPYSGALC PATSFLARRT
     LLAVLQDLAL SQCHGVLHGQ PVEGRNFRNQ FQPVLRRRVV DMLNGGFVTA KTVTVTLADG
     IVAPDPTKGS AEPPARDHDG DLARVSFEVL RELRVKSRVM FSTGSGSLSD AARARVAGLA
     GAYQRPDTAV DVLNGPLGFL LKQHHATLFP RGKPPGGQSP NPQWFWTLLQ RNQLPARLLT
     KDDIETIAAV KRFSVDYGAI NYVNLTPGTV AELAQFYLAN LILRYCDHKQ FFINSLTGIT
     MQSKRPRDPA AVMAWVRRPL ADAADAERAA REVLDAPRDD TWVATYTSSH LLRSVMASRP
     LVVLGLGVSK YHGMAGNNRV FQAGNWSGLN GGKHVCPLMV FDRTRHFVLA CPRVGFTCSQ
     TGGGAGLHDH SLGEHVKTIL ADGGPLVQTA VYAAVLHALG ARTQHLEPDD WRAIVDDEFL
     AAALAEINGR VADRDGRWSV EAAAELVRDL EGQTGADGGE ETAFDFGACG AGGDVAGLAP
     ASLVPAELGG KRPPPEDDLF DMGAPPEKRL TFDML