DNBI_HHV11
ID DNBI_HHV11 Reviewed; 1196 AA.
AC P04296; B9VQF7; Q09IA4;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 25-MAY-2022, entry version 116.
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 Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999714; DOI=10.1093/nar/13.22.8143;
RA Quinn J.P., McGeoch D.J.;
RT "DNA sequence of the region in the genome of herpes simplex virus type 1
RT containing the genes for DNA polymerase and the major DNA binding
RT protein.";
RL Nucleic Acids Res. 13:8143-8163(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1062-1196.
RX PubMed=2457278; DOI=10.1016/0042-6822(88)90584-3;
RA Hammerschmidt W., Conraths F., Mankertz J., Buhk H.-J., Pauli G.,
RA Ludwig H.;
RT "Common epitopes of glycoprotein B map within the major DNA-binding
RT proteins of bovine herpesvirus type 2 (BHV-2) and herpes simplex virus type
RT 1 (HSV-1).";
RL Virology 165:406-418(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH DNA POLYMERASE, AND FUNCTION.
RX PubMed=3031068; DOI=10.1016/s0021-9258(18)61341-9;
RA O'Donnell M.E., Elias P., Funnell B.E., Lehman I.R.;
RT "Interaction between the DNA polymerase and single-stranded DNA-binding
RT protein (infected cell protein 8) of herpes simplex virus 1.";
RL J. Biol. Chem. 262:4260-4266(1987).
RN [7]
RP INTERACTION WITH UL9, AND FUNCTION.
RX PubMed=7961904; DOI=10.1016/s0021-9258(19)62048-x;
RA Boehmer P.E., Craigie M.C., Stow N.D., Lehman I.R.;
RT "Association of origin binding protein and single strand DNA-binding
RT protein, ICP8, during herpes simplex virus type 1 DNA replication in
RT vivo.";
RL J. Biol. Chem. 269:29329-29334(1994).
RN [8]
RP INTERACTION WITH PROTEIN UL8, AND FUNCTION.
RX PubMed=9129659; DOI=10.1099/0022-1317-78-4-857;
RA Hamatake R.K., Bifano M., Hurlburt W.W., Tenney D.J.;
RT "A functional interaction of ICP8, the herpes simplex virus single-stranded
RT DNA-binding protein, and the helicase-primase complex that is dependent on
RT the presence of the UL8 subunit.";
RL J. Gen. Virol. 78:857-865(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9151871; DOI=10.1128/jvi.71.6.4771-4781.1997;
RA Lukonis C.J., Burkham J., Weller S.K.;
RT "Herpes simplex virus type 1 prereplicative sites are a heterogeneous
RT population: only a subset are likely to be precursors to replication
RT compartments.";
RL J. Virol. 71:4771-4781(1997).
RN [10]
RP INTERACTION WITH UL12, AND FUNCTION.
RX PubMed=15078942; DOI=10.1128/jvi.78.9.4599-4608.2004;
RA Reuven N.B., Antoku S., Weller S.K.;
RT "The UL12.5 gene product of herpes simplex virus type 1 exhibits nuclease
RT and strand exchange activities but does not localize to the nucleus.";
RL J. Virol. 78:4599-4608(2004).
RN [11]
RP INTERACTION WITH ICP27.
RX PubMed=15582656; DOI=10.1016/j.virol.2004.10.003;
RA Olesky M., McNamee E.E., Zhou C., Taylor T.J., Knipe D.M.;
RT "Evidence for a direct interaction between HSV-1 ICP27 and ICP8 proteins.";
RL Virology 331:94-105(2005).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26676794; DOI=10.1128/jvi.02854-15;
RA Darwish A.S., Grady L.M., Bai P., Weller S.K.;
RT "ICP8 filament Formation Is Essential for Replication Compartment Formation
RT during Herpes Simplex Virus Infection.";
RL J. Virol. 90:2561-2570(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-1136.
RX PubMed=15507432; DOI=10.1074/jbc.m406780200;
RA Mapelli M., Panjikar S., Tucker P.A.;
RT "The crystal structure of the herpes simplex virus 1 ssDNA-binding protein
RT suggests the structural basis for flexible, cooperative single-stranded DNA
RT binding.";
RL J. Biol. Chem. 280:2990-2997(2005).
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 ECO:0000269|PubMed:15078942, ECO:0000269|PubMed:26676794,
CC ECO:0000269|PubMed:3031068, ECO:0000269|PubMed:7961904,
CC ECO:0000269|PubMed:9129659}.
CC -!- SUBUNIT: Homooligomers. Forms double-helical filaments necessary for
CC the formation of replication compartments within the host nucleus
CC (PubMed:26676794). Interacts with the origin-binding protein
CC (PubMed:7961904). Interacts with the helicase primase complex; this
CC interaction stimulates primer synthesis activity of the helicase-
CC primase complex (PubMed:9129659). Interacts with the DNA polymerase
CC (PubMed:3031068). Interacts with the alkaline exonuclease; this
CC interaction increases its nuclease processivity (PubMed:15078942).
CC Interacts with ICP27; this interaction plays a role in the stimulation
CC of late gene transcription (PubMed:15582656). {ECO:0000255|HAMAP-
CC Rule:MF_04007, ECO:0000269|PubMed:15078942,
CC ECO:0000269|PubMed:15582656, ECO:0000269|PubMed:26676794,
CC ECO:0000269|PubMed:3031068, ECO:0000269|PubMed:7961904,
CC ECO:0000269|PubMed:9129659}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007,
CC ECO:0000269|PubMed:26676794, ECO:0000269|PubMed:9151871}. Note=In the
CC absence of DNA replication, found in the nuclear framework-associated
CC structures (prereplicative sites). As viral DNA replication proceeds,
CC 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; X14112; CAA32322.1; -; Genomic_DNA.
DR EMBL; X03181; CAA26940.1; -; Genomic_DNA.
DR EMBL; M21631; AAA45787.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63491.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62252.1; -; Genomic_DNA.
DR PIR; A03790; DNBEV1.
DR RefSeq; YP_009137104.1; NC_001806.2.
DR PDB; 1URJ; X-ray; 3.00 A; A/B=1-1136.
DR PDBsum; 1URJ; -.
DR SMR; P04296; -.
DR BioGRID; 971471; 20.
DR ELM; P04296; -.
DR IntAct; P04296; 53.
DR MINT; P04296; -.
DR PRIDE; P04296; -.
DR GeneID; 2703458; -.
DR KEGG; vg:2703458; -.
DR EvolutionaryTrace; P04296; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; 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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Host nucleus; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1196
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115743"
FT ZN_FING 499..512
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT REGION 1158..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1196
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 843..844
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 1142..1144
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT COMPBIAS 1171..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 44
FT /note="S -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 224
FT /note="K -> N (in strain: Nonneuroinvasive mutant HF10 and
FT 17 syn+)"
FT VARIANT 306
FT /note="A -> P (in strain: Nonneuroinvasive mutant HF10 and
FT 17 syn+)"
FT VARIANT 428
FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 475
FT /note="A -> G (in strain: Nonneuroinvasive mutant HF10 and
FT 17 syn+)"
FT VARIANT 964
FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 310..331
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 358..377
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 413..417
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 459..469
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 504..509
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 511..517
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 575..588
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 603..606
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 610..636
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 643..647
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 651..657
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 667..693
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 703..716
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 717..720
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 721..731
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 744..746
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 764..777
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 816..821
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 823..826
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 840..849
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 861..878
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 888..903
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 913..923
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 925..927
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 928..933
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 941..950
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 951..954
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 960..967
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 969..974
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 978..987
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 999..1004
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1009..1011
FT /evidence="ECO:0007829|PDB:1URJ"
FT STRAND 1022..1028
FT /evidence="ECO:0007829|PDB:1URJ"
FT TURN 1031..1033
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1049..1056
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1064..1073
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1078..1082
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1085..1091
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1095..1111
FT /evidence="ECO:0007829|PDB:1URJ"
FT HELIX 1120..1125
FT /evidence="ECO:0007829|PDB:1URJ"
SQ SEQUENCE 1196 AA; 128350 MW; 453799162E5B99E9 CRC64;
METKPKTATT IKVPPGPLGY VYARACPSEG IELLALLSAR SGDSDVAVAP LVVGLTVESG
FEANVAVVVG SRTTGLGGTA VSLKLTPSHY SSSVYVFHGG RHLDPSTQAP NLTRLCERAR
RHFGFSDYTP RPGDLKHETT GEALCERLGL DPDRALLYLV VTEGFKEAVC INNTFLHLGG
SDKVTIGGAE VHRIPVYPLQ LFMPDFSRVI AEPFNANHRS IGEKFTYPLP FFNRPLNRLL
FEAVVGPAAV ALRCRNVDAV ARAAAHLAFD ENHEGAALPA DITFTAFEAS QGKTPRGGRD
GGGKGAAGGF EQRLASVMAG DAALALESIV SMAVFDEPPT DISAWPLFEG QDTAAARANA
VGAYLARAAG LVGAMVFSTN SALHLTEVDD AGPADPKDHS KPSFYRFFLV PGTHVAANPQ
VDREGHVVPG FEGRPTAPLV GGTQEFAGEH LAMLCGFSPA LLAKMLFYLE RCDGAVIVGR
QEMDVFRYVA DSNQTDVPCN LCTFDTRHAC VHTTLMRLRA RHPKFASAAR GAIGVFGTMN
SMYSDCDVLG NYAAFSALKR ADGSETARTI MQETYRAATE RVMAELETLQ YVDQAVPTAM
GRLETIITNR EALHTVVNNV RQVVDREVEQ LMRNLVEGRN FKFRDGLGEA NHAMSLTLDP
YACGPCPLLQ LLGRRSNLAV YQDLALSQCH GVFAGQSVEG RNFRNQFQPV LRRRVMDMFN
NGFLSAKTLT VALSEGAAIC APSLTAGQTA PAESSFEGDV ARVTLGFPKE LRVKSRVLFA
GASANASEAA KARVASLQSA YQKPDKRVDI LLGPLGFLLK QFHAAIFPNG KPPGSNQPNP
QWFWTALQRN QLPARLLSRE DIETIAFIKK FSLDYGAINF INLAPNNVSE LAMYYMANQI
LRYCDHSTYF INTLTAIIAG SRRPPSVQAA AAWSAQGGAG LEAGARALMD AVDAHPGAWT
SMFASCNLLR PVMAARPMVV LGLSISKYYG MAGNDRVFQA GNWASLMGGK NACPLLIFDR
TRKFVLACPR AGFVCAASSL GGGAHESSLC EQLRGIISEG GAAVASSVFV ATVKSLGPRT
QQLQIEDWLA LLEDEYLSEE MMELTARALE RGNGEWSTDA ALEVAHEAEA LVSQLGNAGE
VFNFGDFGCE DDNATPFGGP GAPGPAFAGR KRAFHGDDPF GEGPPDKKGD LTLDML
