DNBI_BHV2B
ID DNBI_BHV2B Reviewed; 1186 AA.
AC P12639;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 02-JUN-2021, entry version 68.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=UL29;
OS Bovine herpesvirus 2 (strain BMV) (BoHV-2) (Bovine mammillitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841793; DOI=10.1016/0042-6822(88)90583-1;
RA Hammerschmidt W., Conraths F., Mankertz J., Pauli G., Ludwig H.,
RA Buhk H.-J.;
RT "Conservation of a gene cluster including glycoprotein B in bovine
RT herpesvirus type 2 (BHV-2) and herpes simplex virus type 1 (HSV-1).";
RL Virology 165:388-405(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1058-1186.
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M21630; AAA46051.1; -; Genomic_DNA.
DR PIR; A29242; DNBEBG.
DR SMR; P12639; -.
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; Zinc;
KW Zinc-finger.
FT CHAIN 1..1186
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115748"
FT ZN_FING 495..508
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT REGION 1160..1186
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 839..840
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1186 AA; 127287 MW; A586ECC1479FBD2C CRC64;
MENKQKTATT VKVSPGPLGY VYARRLPPEG LTELALLSAR SADSDTAVLP LIAGLTVESG
FDVNVAVVVG SRTTGVGGTG VSLKLMPSHY APSAYVFHGG RHLAPSSAAP NLSLLCDRAR
VQFGFSSFKP KPCEAEGETT GEALCEHLGL NPNESLLYMV IAEGFKEAVY ISNTILHMGG
VGTVTIAGEE VRRIPIYPLQ MFMPDYCRAV ADPFNDRHRA IGEYFAYPLP FFNAKLASLL
FGAAVGPAAV ALRARNVDAV ARAAAHLAFD ENHEGAALPA DITFTAFDPT GSKAGHRNPR
ECGGGFEQRL ASVMAGDAAL ALESIMSMAV FEEPPTDIGT WPMLTCQEST AARAASIGAY
LGRAAGLVGA MVFSSNSALH LTEVDDAGPA DPKDPTKPSF YRFFLVPGTY VAANPQLDRD
GRVVAGHEGR PIVPIVGGNH EFTCEHLATL CGFSPELLAK MLYYLERCDG GVILGRPEMD
TFKYVSDSAH TDVPCCLCSL DNRHSCAHTT LLRLRARHPK FTSTTRGAIG IFGVMNSAYS
DCDVLGNYAS FSAIKRMDVQ ETARAIMQET YRSAVERVMA ELENLNYIDA AVPTSPAKLE
SIITGREALQ TVVSNVKQVV DGEVAQLMRA LVEGRGFRFR EALGEANHAM SLTLDPHASV
PCPLLQMLGR RSNLAVYQDL ALSQCHGVFE GQAVEGRNFR SQFQPVLRRR VLDMFNNGFL
SARTLTVALT DGACISAPGL VSGQHAAAES GFEGDVARVN LGFPKEIRVK SRVLFAGAGP
AASEAARARI AGLQSAYQKS DKRVDILLGP LGFMLKQFHA TLFPNGKPPG SDNPNPQWFW
TALQRNQLPA RLLSREDISL IAFVKRFSVE YGAGNFVNLP PNNISELAMY YMANQILKYC
DHSTYFINTL TALIAGSRRP PNAQAAAAWA PRGGTELEAQ ARSVVANPGD HPGAWTTMFA
SCNLLRPVMA TRPMVVLGLS ISKYYGMAGN DRVFQAGNLA NLLGGKNACP LLIFDRTRKF
VIACPRAGFV CAAVSAGSGA HESSLCEQLR AIIAEGGATV ASDVFAAAAK SLGARVQQLQ
IEDWLALLED EYLSEEMMEL AGRALERGGG EWSLDAALDV AREAEAMVTR HVDAEETFDF
GAFAEDGPAD AGLAVHLQSR RRPLACSDLF GDAPAEKRND LTLDML
