ID   DNBI_MUHVS              Reviewed;        1191 AA.
AC   P30672;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   23-FEB-2022, entry version 74.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=UL57;
OS   Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX   NCBI_TaxID=10367;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1329325; DOI=10.1016/0042-6822(92)90198-x;
RA   Messerle M., Keil G.M., Schneider K., Koszinowski U.H.;
RT   "Characterization of the murine cytomegalovirus genes encoding the major
RT   DNA binding protein and the ICP18.5 homolog.";
RL   Virology 191:355-367(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA   Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT   "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL   J. Virol. 70:8833-8849(1996).
CC   -!- FUNCTION: Single-stranded DNA-binding protein required for DNA
CC       replication.
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; X67021; CAA47414.1; -; Genomic_DNA.
DR   EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A44051; A44051.
DR   SMR; P30672; -.
DR   PRIDE; P30672; -.
DR   Proteomes; UP000008774; 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; -; 1.
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..1191
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000115761"
FT   REGION          1122..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1168..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1191
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   MOTIF           820..821
FT                   /note="Required for filament formation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   COMPBIAS        1174..1191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1191 AA;  131641 MW;  5BA4A7F07D7E1B9A CRC64;
     MADDDLSSLA PVAPAVWMFF LKKTRELADI VAAMSLCDKA TPVVIAPLLI DLTVDRDFCG
     AVRTPMSTYE GGVLTKVTSF CPFAFFFHNT DEILDVVEDH GDVVHLCDDA RRRFGVQAFS
     PLANRDRTDV DVLCDELGIA PAEYTGHVVC GNGLKELLYA GQLIPCPEEA VKVQVGAVDG
     VKVPLYPYTL FSGGADAAHA DGPSAAVACD DPWVLEHGFY DPALSEALFY FMFTSWGQSL
     RVCETSRLIE AGLQQFVEDT QQTVKLTPFK KYHGYTSQKL TAVERDQLMT VDAVCSELAF
     SYASIYLDSV YEFSTASNFL EWPLVKNAKT HADLLDNLRD FQLHLAKHIA ALIFSSNSIL
     YQTRIVFVPS AGKGANSNPS AQDSLLKSIR FFNGLTGMYD DILNDAKKTI RFEGAVGRDE
     KYSPHHLAYF CGTSPQLFST LMWFFNRMSI YSTGVTSGDT VFSHIVNAGS KLCGACGGRC
     CHTCYATSFI RVNTRLPGIP KQIKKEPVVV TLLSRAFADA DLLGNYGKRY GLESREAGDG
     GGGGAGGRTD EVAAGPPAGG ASGLNFVSVD RMKYLGQVLD YCKKNSLIDA ITGEDIINVR
     TKRDFVATVT ALNQTIDDAV CRFAMDVRRS GHGRDEISGS TQSFNLDLSP YATAFSPVLS
     FQYYRTMFSI IQNLALINAA SYVVDNPLTT AQISKWVTLH FQSICGAFGT TPLKKGFLNV
     KDTKNLKSVE FERIMDFRSF QETGRYRKIS TEIKSCKMSV QSLKSCRIKN RPISKTPQSS
     VFFKKGALQR KNPIKGCLSF LLFRCHEKLF PRCGLSCLEF WQRVLQNSLP RSVNVGKVED
     FDNLVRFLLT VTDDYDESDV VDIQPDCLLS YVENRFHNKF LYMFGFRDYM STIQGMSTRL
     TPQNHSQFPC LLKDAPKFAS IAEYVLHFKK MKLDGVKAPQ VATITREPVL KKLFDGRSLV
     SVSFAVEKYS SSMGTRDVFQ FGQIGYYVGS GVDRSLNTGS MGTQDYRFMR YRYIIATKLV
     DVLIRRSRRE NVMYDRDVVR SRVLAALDST GLDVDPELAA IAELMEGRDE GDIPEIDDIL
     FYVDQQEYIA RSMYRKMRSL AERGVTDFSL ASLREATATN ATAAGSAAGG GGSATEGGGG
     GAAADESGPM YDFSALFSRR DEAEDVNAGL INGDDVRGDD EFELPSKRSR L