DNBI_TUHV2
ID DNBI_TUHV2 Reviewed; 1193 AA.
AC Q9WRL7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 23-FEB-2022, entry version 62.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007};
OS Tupaiid herpesvirus (strain 2) (TuHV-2) (Herpesvirus tupaia (strain 2)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae.
OX NCBI_TaxID=132678;
OH NCBI_TaxID=37347; Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10392721; DOI=10.1016/s0168-1702(99)00012-x;
RA Bahr U., Springfeld C., Tidona C.A., Darai G.;
RT "Structural organization of a conserved gene cluster of Tupaia herpesvirus
RT encoding the DNA polymerase, glycoprotein B, a probable processing and
RT transport protein, and the major DNA binding protein.";
RL Virus Res. 60:123-136(1999).
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; AF084543; AAD42933.1; -; Genomic_DNA.
DR SMR; Q9WRL7; -.
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.
FT CHAIN 1..1193
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115756"
FT REGION 1125..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1193
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 827..828
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1193 AA; 129835 MW; 7BCA52E1B6FAC67D CRC64;
MEDDLNTLAP LGPAAWLFVC PRQDEWCDVL AALSLCDRSS SVAIAPLLVD LTVDRDFQVA
VRTPISRYEG GVLTKVTSMW PAAFVFHNAE AIVSRTEDHG DVGGLCAEAR ARFGVASYRA
EAERADTDFT ELWAALGVDG ARVVMYAVVG YGLKELLYAG QLVPCVEEAR TVLLGAVEAF
KLPLYPATLF ADGDATADGA AAVGLRSRTP FVDRRGLYVS ALSEALFYYV FTALGQALRF
GHTEHLIDEG MKQFLQDTQN SVKLAPQKRY YGYLSQKLTP GERDQLLLCD AIACELAFSF
ASVYFDSAYE PAPLMNYSEW PLVRAAEGHA DLLRRLSELK LHLSAHVGAL VFSGNSVLYQ
TRIAFFSAAN KVPAGGTAQD GLLKAVQFCN GLTCLTEDAL NDACRTVKFE GPGGGGGGRD
EQFTPQHLAW ACATSPHLMS DLVWYLNRLA IYNTGQNGGS ALYEHLVHCA VNLCPACRGR
CCQSCYQTAF VRIQTRLPPL PKQLKREPFV LTLFSRFLCD VDVLGTFGKR YAGDAKEPSA
ASLAAAPGEA RKVGDEAGLG AGGGGPGGRL GVNVDRLKYF NQILDYCKRN SLIDPSTGED
TLAVRGRADF MSALSGLNRC VDEAAMALVS EVRMKSNRDE VAGATQAFNL DLNPYAVAFS
PLLAHQYYRA FFLIVQNLAL VSASSYVVDN PLTVSSLSRW LLQHFQSICG AFASNSARKG
LLFTKDAKCS KSVEFERFMD FALYAASGRH VLLSTETKLC KLSVCMLRTC RVKNRPIPRG
GKGLPVSVFF KRDVVQRRNP VRGCLAFLLY AFHERLFPGC GLSCLDFWQK VYHNALPKSV
AIGKMEEFNA FVKYVLNVTT EYNEHDLIDV PPSNLLSYVE YRFHNKFLCF YGFGDYLSTL
HGLSTKLVPQ NHLNFPHLLA ASPKFASVAE YVLYFKKLKL DGVPPPHVAT FSRESLVRSV
FENRSLVTVA FGIEKYSTSG GSREVFHFGQ IGYFAGNGVE RSLNVNSMGG GDYRYMRQRF
VLATRLVDLL LRRSRRETVL FDADLLRTRV LAALESHDTQ LDPELAAIAE IMDGRGGEPP
EYEDVLFFVD GQECLAASIV GKIKELIKKG VEDFSLTALG ADAGAGGGPA GSAGGPESGG
GAGAAGGEGT YDLSALFLDV ENECVVLEGP TAAALDGGGD GDECAFPAKR LRL
