DNBI_HHV1F
ID DNBI_HHV1F Reviewed; 1196 AA.
AC P17469;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 71.
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 F) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10304;
OH NCBI_TaxID=9606; Homo sapiens (Human).
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).
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 PIR; D29242; DNBEHF.
DR SMR; P17469; -.
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..1196
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115744"
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"
SQ SEQUENCE 1196 AA; 128374 MW; BC872584DDB1C8E2 CRC64;
METKPKTATT IKVPPGPLGY VYARACPSEG IELLALLSAR SGDSDVAVAP LVVGLTVESG
FEANVAVVVG SRTTGLGGTA VSLKLTPSHY SSSVYVFHGG RHLDPSTQAP NLTRLCERAR
RHFGFSDYTP RPGDLKHETT GEALCERLGL DPDRALLYLV VTEGFKEAVS INNTFLHLGG
SDKVTIGGAE VHRIPVYPLQ LFMPDFSRVI AEPFNANHRS IGEKFTYPLP FFNRPLNRLL
FEAVVGPAAV ALRCRNVDAV ARAAAHLAFD ENHEGAALPA DITFTAFEAS QGKTPRGERD
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 LEAGARALVD 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
