DNBI_EHV1B
ID DNBI_EHV1B Reviewed; 1209 AA.
AC P28932; Q6DLI0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 02-JUN-2021, entry version 85.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; OrderedLocusNames=31;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
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; AY665713; AAT67288.1; -; Genomic_DNA.
DR PIR; E36798; DNBEC4.
DR RefSeq; YP_053076.1; NC_001491.2.
DR SMR; P28932; -.
DR GeneID; 1487543; -.
DR KEGG; vg:1487543; -.
DR Proteomes; UP000001189; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW DNA replication; DNA-binding; Host nucleus; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1209
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115750"
FT ZN_FING 503..516
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1209
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 849..850
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1209 AA; 129983 MW; 1A728FB04484FE95 CRC64;
MESAPKTVSL PVSPLGYVYA RQKASLQTGT VSLTAARSVD SDLAVLPVIR GLTVEQTFTT
NVAVVAGSKT TGLGGTGITL KLTPSHFNPN AFVFYGGSVI GASSNAPNLT RACEAARRRF
GFSAFSSPPV ENAVETSGEE ICASLNLSPE TTALYLVVTE SFKEMVYVCN TFLHYGGTST
VTIDGQDAMK IPIYPVQLYM PDVNRLASEP FNAKHRSIGD EFVYSRPFFN SDLCRLLHGY
VLGPAAVALR VRNLDGVARG AAHLALDENH EGSVLPQDVT FTLFDSTQGN AGKGSGRAQR
QGDGSGSKNS ASSGIERRLA SVMAADTALS VDSIMGAGIY DTELPSVEDW PVLSSGDDTE
SLEALGAYAA RLSGLVGAMV FSANSVLYMT EVDDGGPADG KDGSNPSYHR FYLIAAPYVA
GNPQTDKDGR VLPHTADQQA APINGSNQEF SLDYLALACG FCPQILARLL FYLERCDAGT
FGGRNETDAL RYLANTLESD VPCGLCNQAT RPACAHTTLH RLRQRLPRFG APVRAPIGIF
GTMNSAYSDC DVLGNYASYG ALKRPNDNEA PKSIMQDTYR ATMERLVNEL EQAKLIDKET
LAQASPCSAP TSVVHDQASF IGLLSNIKDT IEGAAEQFMR TLVEARDFKI REGLADANHT
MSISLDPYSS SFCPVTSFLA RRTVFAVLQD LVLSQCHCLF YGQSVEGRNF RNQFQPVLRR
RFLDMLNGGF ITAKTVTVTV SDSGVLAPDL TRPASEPPTK DYDGDMARVS MEVLRDLRVK
NRVLFSNGGA NMSEAARARV AGMASAYRRP DKGSNILNGA VGFLVKQYHG VLFPRGHPPG
IDTPNPQWFW TLLQRNQMPA RLLSKEDIET ITAIKRFSDE YSAINFINLT PNNIGELAQF
YFANLVLKYC DHSQYFINGL TAIVVGSRRP RDPAAVLAWI DRTINGAADV EPAAQEVLQR
LGSNPAAWTG TFTSTNMVRY VMDQRPMVVI GLSISKYNGS AGNNRVFQAG NWNGLNGGKN
VCPLMAFDRT RRFVLACPRV GFTCEAGGFG TGVRENTLSE QVRGIVSEGG PMVQTAVFAA
VLHALGARTQ HLAVDDWIGL VDDEFLAASL DALNATVVDQ FGEWSVEAAQ ELVKNMEAQT
TAGAVAAGEG AFDFGACVGD TPQQSTSAFN GGLAMAAAPA GQKRSLPDDI LFDMGAPPEK
KSGLTFDML
