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Major DNA-binding protein

 DNBI_HHV11              Reviewed;        1196 AA.
P04296; B9VQF7; Q09IA4;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
30-AUG-2017, entry version 102.
RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=ICP8;
ORFNames=UL29;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2999714; DOI=10.1093/nar/13.22.8143;
Quinn J.P., McGeoch D.J.;
"DNA sequence of the region in the genome of herpes simplex virus type
1 containing the genes for DNA polymerase and the major DNA binding
protein.";
Nucleic Acids Res. 13:8143-8163(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
McNab D., Perry L.J., Scott J.E., Taylor P.;
"The complete DNA sequence of the long unique region in the genome of
herpes simplex virus type 1.";
J. Gen. Virol. 69:1531-1574(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1062-1196.
PubMed=2457278; DOI=10.1016/0042-6822(88)90584-3;
Hammerschmidt W., Conraths F., Mankertz J., Buhk H.-J., Pauli G.,
Ludwig H.;
"Common epitopes of glycoprotein B map within the major DNA-binding
proteins of bovine herpesvirus type 2 (BHV-2) and herpes simplex virus
type 1 (HSV-1).";
Virology 165:406-418(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nonneuroinvasive mutant HF10;
PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
"Determination and analysis of the DNA sequence of highly attenuated
herpes simplex virus type 1 mutant HF10, a potential oncolytic
virus.";
Microbes Infect. 9:142-149(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 syn+;
Cunningham C., Davison A.J.;
"Herpes simplex virus type 1 bacterial artificial chromosome.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH DNA POLYMERASE, AND FUNCTION.
PubMed=3031068;
O'Donnell M.E., Elias P., Funnell B.E., Lehman I.R.;
"Interaction between the DNA polymerase and single-stranded DNA-
binding protein (infected cell protein 8) of herpes simplex virus 1.";
J. Biol. Chem. 262:4260-4266(1987).
[7]
INTERACTION WITH UL9, AND FUNCTION.
PubMed=7961904;
Boehmer P.E., Craigie M.C., Stow N.D., Lehman I.R.;
"Association of origin binding protein and single strand DNA-binding
protein, ICP8, during herpes simplex virus type 1 DNA replication in
vivo.";
J. Biol. Chem. 269:29329-29334(1994).
[8]
INTERACTION WITH PROTEIN UL8, AND FUNCTION.
PubMed=9129659; DOI=10.1099/0022-1317-78-4-857;
Hamatake R.K., Bifano M., Hurlburt W.W., Tenney D.J.;
"A functional interaction of ICP8, the herpes simplex virus single-
stranded DNA-binding protein, and the helicase-primase complex that is
dependent on the presence of the UL8 subunit.";
J. Gen. Virol. 78:857-865(1997).
[9]
SUBCELLULAR LOCATION.
PubMed=9151871;
Lukonis C.J., Burkham J., Weller S.K.;
"Herpes simplex virus type 1 prereplicative sites are a heterogeneous
population: only a subset are likely to be precursors to replication
compartments.";
J. Virol. 71:4771-4781(1997).
[10]
INTERACTION WITH UL12, AND FUNCTION.
PubMed=15078942; DOI=10.1128/JVI.78.9.4599-4608.2004;
Reuven N.B., Antoku S., Weller S.K.;
"The UL12.5 gene product of herpes simplex virus type 1 exhibits
nuclease and strand exchange activities but does not localize to the
nucleus.";
J. Virol. 78:4599-4608(2004).
[11]
INTERACTION WITH ICP27.
PubMed=15582656; DOI=10.1016/j.virol.2004.10.003;
Olesky M., McNamee E.E., Zhou C., Taylor T.J., Knipe D.M.;
"Evidence for a direct interaction between HSV-1 ICP27 and ICP8
proteins.";
Virology 331:94-105(2005).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26676794; DOI=10.1128/JVI.02854-15;
Darwish A.S., Grady L.M., Bai P., Weller S.K.;
"ICP8 filament Formation Is Essential for Replication Compartment
Formation during Herpes Simplex Virus Infection.";
J. Virol. 90:2561-2570(2015).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-1136.
PubMed=15507432; DOI=10.1074/jbc.M406780200;
Mapelli M., Panjikar S., Tucker P.A.;
"The crystal structure of the herpes simplex virus 1 ssDNA-binding
protein suggests the structural basis for flexible, cooperative
single-stranded DNA binding.";
J. Biol. Chem. 280:2990-2997(2005).
-!- FUNCTION: Plays several crucial roles in viral infection.
Participates in the opening of the viral DNA origin to initiate
replication by interacting with the origin-binding protein. May
disrupt loops, hairpins and other secondary structures present on
ssDNA to reduce and eliminate pausing of viral DNA polymerase at
specific sites during elongation. Promotes viral DNA recombination
by performing strand-transfer, characterized by the ability to
transfer a DNA strand from a linear duplex to a complementary
single-stranded DNA circle. Can also catalyze the renaturation of
complementary single strands. Additionally, reorganizes the host
cell nucleus, leading to the formation of prereplicative sites and
replication compartments. This process is driven by the protein
which can form double-helical filaments in the absence of DNA.
{ECO:0000255|HAMAP-Rule:MF_04007, ECO:0000269|PubMed:15078942,
ECO:0000269|PubMed:26676794, ECO:0000269|PubMed:3031068,
ECO:0000269|PubMed:7961904, ECO:0000269|PubMed:9129659}.
-!- SUBUNIT: Homooligomers. Forms double-helical filaments necessary
for the formation of replication compartments within the host
nucleus (PubMed:26676794). Interacts with the origin-binding
protein (PubMed:7961904). Interacts with the helicase primase
complex; this interaction stimulates primer synthesis activity of
the helicase-primase complex (PubMed:9129659). Interacts with the
DNA polymerase (PubMed:3031068). Interacts with the alkaline
exonuclease; this interaction increases its nuclease processivity
(PubMed:15078942). Interacts with ICP27; this interaction plays a
role in the stimulation of late gene transcription
(PubMed:15582656). {ECO:0000255|HAMAP-Rule:MF_04007,
ECO:0000269|PubMed:15078942, ECO:0000269|PubMed:15582656,
ECO:0000269|PubMed:26676794, ECO:0000269|PubMed:3031068,
ECO:0000269|PubMed:7961904, ECO:0000269|PubMed:9129659}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04007, ECO:0000269|PubMed:26676794,
ECO:0000269|PubMed:9151871}. Note=In the absence of DNA
replication, found in the nuclear framework-associated structures
(prereplicative sites). As viral DNA replication proceeds, it
migrates to globular intranuclear structures (replication
compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
-!- SIMILARITY: Belongs to the herpesviridae major DNA-binding protein
family. {ECO:0000255|HAMAP-Rule:MF_04007}.
-----------------------------------------------------------------------
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EMBL; X14112; CAA32322.1; -; Genomic_DNA.
EMBL; X03181; CAA26940.1; -; Genomic_DNA.
EMBL; M21631; AAA45787.1; -; Genomic_DNA.
EMBL; DQ889502; ABI63491.1; -; Genomic_DNA.
EMBL; FJ593289; ACM62252.1; -; Genomic_DNA.
PIR; A03790; DNBEV1.
RefSeq; YP_009137104.1; NC_001806.2.
PDB; 1URJ; X-ray; 3.00 A; A/B=1-1136.
PDBsum; 1URJ; -.
SMR; P04296; -.
BioGrid; 971471; 18.
ELM; P04296; -.
IntAct; P04296; 53.
MINT; MINT-191337; -.
PRIDE; P04296; -.
GeneID; 2703458; -.
KEGG; vg:2703458; -.
KO; K19442; -.
OrthoDB; VOG0900000X; -.
EvolutionaryTrace; P04296; -.
Proteomes; UP000009294; Genome.
Proteomes; UP000180652; Genome.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
HAMAP; MF_04007; HSV_DNBI; 1.
InterPro; IPR000635; Viral_ssDNA-bd.
Pfam; PF00747; Viral_DNA_bp; 1.
SUPFAM; SSF118208; SSF118208; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA replication; DNA-binding;
Host nucleus; Metal-binding; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 1196 Major DNA-binding protein.
/FTId=PRO_0000115743.
ZN_FING 499 512 {ECO:0000255|HAMAP-Rule:MF_04007}.
REGION 1170 1196 Required for nuclear localization.
{ECO:0000255|HAMAP-Rule:MF_04007}.
MOTIF 843 844 Required for filament formation.
{ECO:0000255|HAMAP-Rule:MF_04007}.
MOTIF 1142 1144 Required for filament formation.
{ECO:0000255|HAMAP-Rule:MF_04007}.
VARIANT 44 44 S -> A (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 224 224 K -> N (in strain: Nonneuroinvasive
mutant HF10 and 17 syn+).
VARIANT 306 306 A -> P (in strain: Nonneuroinvasive
mutant HF10 and 17 syn+).
VARIANT 428 428 V -> A (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 475 475 A -> G (in strain: Nonneuroinvasive
mutant HF10 and 17 syn+).
VARIANT 964 964 A -> T (in strain: Nonneuroinvasive
mutant HF10).
STRAND 18 25 {ECO:0000244|PDB:1URJ}.
HELIX 31 37 {ECO:0000244|PDB:1URJ}.
STRAND 47 50 {ECO:0000244|PDB:1URJ}.
STRAND 64 73 {ECO:0000244|PDB:1URJ}.
STRAND 81 90 {ECO:0000244|PDB:1URJ}.
STRAND 92 98 {ECO:0000244|PDB:1URJ}.
HELIX 100 102 {ECO:0000244|PDB:1URJ}.
HELIX 112 123 {ECO:0000244|PDB:1URJ}.
HELIX 132 137 {ECO:0000244|PDB:1URJ}.
HELIX 141 148 {ECO:0000244|PDB:1URJ}.
STRAND 154 162 {ECO:0000244|PDB:1URJ}.
TURN 163 165 {ECO:0000244|PDB:1URJ}.
HELIX 166 170 {ECO:0000244|PDB:1URJ}.
STRAND 174 176 {ECO:0000244|PDB:1URJ}.
HELIX 178 180 {ECO:0000244|PDB:1URJ}.
STRAND 182 186 {ECO:0000244|PDB:1URJ}.
STRAND 189 198 {ECO:0000244|PDB:1URJ}.
HELIX 199 202 {ECO:0000244|PDB:1URJ}.
HELIX 234 243 {ECO:0000244|PDB:1URJ}.
HELIX 245 251 {ECO:0000244|PDB:1URJ}.
HELIX 257 269 {ECO:0000244|PDB:1URJ}.
HELIX 310 331 {ECO:0000244|PDB:1URJ}.
HELIX 342 344 {ECO:0000244|PDB:1URJ}.
HELIX 346 348 {ECO:0000244|PDB:1URJ}.
STRAND 353 355 {ECO:0000244|PDB:1URJ}.
HELIX 358 377 {ECO:0000244|PDB:1URJ}.
TURN 382 384 {ECO:0000244|PDB:1URJ}.
STRAND 385 390 {ECO:0000244|PDB:1URJ}.
STRAND 406 411 {ECO:0000244|PDB:1URJ}.
TURN 413 417 {ECO:0000244|PDB:1URJ}.
TURN 430 433 {ECO:0000244|PDB:1URJ}.
HELIX 448 454 {ECO:0000244|PDB:1URJ}.
TURN 455 457 {ECO:0000244|PDB:1URJ}.
HELIX 459 469 {ECO:0000244|PDB:1URJ}.
HELIX 485 490 {ECO:0000244|PDB:1URJ}.
TURN 491 494 {ECO:0000244|PDB:1URJ}.
TURN 504 509 {ECO:0000244|PDB:1URJ}.
HELIX 511 517 {ECO:0000244|PDB:1URJ}.
HELIX 519 521 {ECO:0000244|PDB:1URJ}.
STRAND 533 538 {ECO:0000244|PDB:1URJ}.
HELIX 575 588 {ECO:0000244|PDB:1URJ}.
HELIX 603 606 {ECO:0000244|PDB:1URJ}.
HELIX 610 636 {ECO:0000244|PDB:1URJ}.
HELIX 643 647 {ECO:0000244|PDB:1URJ}.
STRAND 651 657 {ECO:0000244|PDB:1URJ}.
HELIX 667 693 {ECO:0000244|PDB:1URJ}.
HELIX 703 716 {ECO:0000244|PDB:1URJ}.
TURN 717 720 {ECO:0000244|PDB:1URJ}.
STRAND 721 731 {ECO:0000244|PDB:1URJ}.
TURN 744 746 {ECO:0000244|PDB:1URJ}.
STRAND 748 750 {ECO:0000244|PDB:1URJ}.
STRAND 759 761 {ECO:0000244|PDB:1URJ}.
STRAND 764 777 {ECO:0000244|PDB:1URJ}.
HELIX 810 812 {ECO:0000244|PDB:1URJ}.
HELIX 816 821 {ECO:0000244|PDB:1URJ}.
HELIX 823 826 {ECO:0000244|PDB:1URJ}.
HELIX 840 849 {ECO:0000244|PDB:1URJ}.
HELIX 861 878 {ECO:0000244|PDB:1URJ}.
HELIX 888 903 {ECO:0000244|PDB:1URJ}.
STRAND 913 923 {ECO:0000244|PDB:1URJ}.
STRAND 925 927 {ECO:0000244|PDB:1URJ}.
HELIX 928 933 {ECO:0000244|PDB:1URJ}.
HELIX 941 950 {ECO:0000244|PDB:1URJ}.
HELIX 951 954 {ECO:0000244|PDB:1URJ}.
STRAND 960 967 {ECO:0000244|PDB:1URJ}.
HELIX 969 974 {ECO:0000244|PDB:1URJ}.
STRAND 978 987 {ECO:0000244|PDB:1URJ}.
STRAND 999 1004 {ECO:0000244|PDB:1URJ}.
HELIX 1009 1011 {ECO:0000244|PDB:1URJ}.
STRAND 1022 1028 {ECO:0000244|PDB:1URJ}.
TURN 1031 1033 {ECO:0000244|PDB:1URJ}.
HELIX 1049 1056 {ECO:0000244|PDB:1URJ}.
HELIX 1064 1073 {ECO:0000244|PDB:1URJ}.
HELIX 1078 1082 {ECO:0000244|PDB:1URJ}.
HELIX 1085 1091 {ECO:0000244|PDB:1URJ}.
HELIX 1095 1111 {ECO:0000244|PDB:1URJ}.
HELIX 1120 1125 {ECO:0000244|PDB:1URJ}.
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


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