ID   DNBI_HHV7J              Reviewed;        1131 AA.
AC   P52339;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=U41;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(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}.
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DR   EMBL; U43400; AAC54703.1; -; Genomic_DNA.
DR   PIR; T41943; T41943.
DR   SMR; P52339; -.
DR   PRIDE; P52339; -.
DR   Proteomes; UP000009246; 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..1131
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000115754"
FT   REGION          1112..1131
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT   MOTIF           790..791
FT                   /note="Required for filament formation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1131 AA;  129009 MW;  52C97388D1B6D04F CRC64;
     MADDNETVVS APICTAAWLY ILPKEQKLIE ILTTLSLMEK RKSVVISPLL LNLTVENDFF
     PTVKTPIINY GGTVITKITS FMPVCFFFHG TDVFLKEAED HGNLDKLCKQ TREKFNLQEF
     VVNGNRKSVD IGKICESVGR NADDVLCHIV VGNGFKELLF AGLLIPCVEE QIQVQVGECL
     AIKIPLYSAT LFESEETLCI DTCTEFIQEN GFYAPQISEV LFYLIFTSWG MTLRFNNTLE
     LIKAGLKQFI QDTEQTVKLA PNKTYHGIPG QKLSPIEKDH LMLVDAVITE LTFSYTAEYL
     DSIYENNQIM NFSEWPIIKS AETHEEKIVE LKKLRLHLSS HVAALVFAAN SILYSNKLAY
     ISNTKQAFNS AITQETLLRS IQFCNSLSSL NEDFYNDARK LIKCNSSPCK EDKFSAFHLA
     YACATCPQIL SHIIWNLNRM SIYNTNCGNS EIYNHIVNCS SNLCEFCEGK CCHSCIGTAL
     IRINSRLPQI SKTTKKEPIV MTMFSRFYAD VDVLGSFGKK GVNESKDPMK EAQTTPSLDR
     FKFLGMIHDY CKKNNLIDAI TGEDNLNFKS QNDFVNMIND LIQCIEEAVS KCISEMRKTQ
     TSREQIENCL QSFNIDTTPL SLAFSPFFVF TYYKVILIVL QNLALIIGTG YVVDRPCTGN
     LISKWLMQQY QSLYGAFYNS HFKKGFLNMK TVKIASNVDM EQYIDFNLFK SGKYAKTSIQ
     AKLCRLSMQC LKDFRVKNRP FNKPNKNTQN NPFFKKVKQK KNPLSGCLSF LLFKYHERLF
     PNLKISCLEF WQRILLNNMP KTIDIGNVED MRSFIKFTFR VTNSYDEIDL LDIQPECLLS
     FIEYYFHNKL LSVLGYRDYL TSLHALTSKL VPQNPMLFPV FLKEHPTFSS VQEYVMHVKK
     LVGNGLKEPM TASLTKEPNF GSIFTGRSII TFGLMIEKFV SVASRDYFHF GQLGWIAGSG
     VDRNLNPPSS GLQDFRFMRQ KFVIATKLCD IIVKKVKREA IVYDVEVIRG KVLNIIESLS
     NSVNPELLIL AEVMKDRDSK PTMDDMLFYV DGREPLAKSV MNKIQHLTDL NVHDFSLSTL
     LSVFEEQVED SAAIYDFSEL LVEGNEQGFG ILKCEETEHE NEEPSLKKAR L