DNBI_HHV2
ID DNBI_HHV2 Reviewed; 1197 AA.
AC P36384;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 66.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=ICP8, UL29;
OS Human herpesvirus 2 (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10310;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8385914; DOI=10.1007/bf01316894;
RA Toh Y., Liu Y., Tanaka S., Mori R.;
RT "Nucleotide sequence of the major DNA-binding protein gene of herpes
RT simplex virus type 2 and a comparison with the type 1.";
RL Arch. Virol. 129:183-196(1993).
CC -!- FUNCTION: Single-stranded DNA-binding protein required for DNA
CC replication.
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 PIR; A48350; A48350.
DR SMR; P36384; -.
DR ELM; P36384; -.
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..1197
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115746"
FT ZN_FING 499..512
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT REGION 1172..1197
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT REGION 1177..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1197 AA; 128413 MW; C1576BB5B8865BFB CRC64;
MDTKPKTTTT VKVPPGPMGY VYGRACPAEG LELLSLLSAR SGDADVAVAP LIVGLTVESG
FEANVAAVVG SGTTGLGGTA VSLKLMPSHY SPSVYVFHGG RHLAPSTQAP NLTRLCERAR
RHFGFSDYAP RPCDLKHETT GDALCERLGL DPDRALLYLV ITEGFREAVC ISNTFLHLGG
MDKVTIGDAE VHRIPVYPLQ MFMPDFSRVI ADPFNCNHRS IGENFNYPLP FFNRPLARLL
FEAVVGPAAV ALRARNVDAV ARAAAHLAFD ENHEGAALPA DITFTAFEAS QGKPQRGARD
AGNKGPAGGF EQRLASVMAG DAALALESIV SMAVFDEPPP DITTWPLLEG QETPAARAGA
VGAYLARAAG LVGAMVFSTN SALHLTEVDD AGPADPKDHS KPSFYRFFLV PGTHVAANPQ
LDREGHVVPG YEGRPTAPLV GGTQEFAGEH LAMLCGFSPA LLAKMLFYLE RCDGGVIVGR
QEMDVFRYVA DSGQTDVPCN LCTFETRHAC AHTTLMRLRA RHPKFASAAR GAIGVFGTMN
SAYSDCDVLG NYAAFSALKR ADGSENTRTI MQETYRAATE RVMAELEALQ YVDQAVPTAL
GRLETIIGNR EALHTVVNNI KQLVDREVEQ LMRNLIEGRN FKFRDGLAEA NHAMSLSLDP
YTCGPCPLLQ LLARRSNLAV YQDLALSQCH GVFAGQSVEG RNFRNQFQPV LRRRVMDLFN
NGFLSAKTLT VALSEGAAIC APSLTAGQTA PAESSFEGDV ARVTLGFPKE LRVKSRVLFA
GASANASEAA KARVASLQSA YQKPDKRVDI LLGPLGFLLK QFHAVIFPNG KPPGSNQPNP
QWFWTALQRN QLPARLLSRE DIETIAFIKR FSLDYGAINF INLAPNNVSE LAMYYMANQI
LRYCDHSTYF INTLTAVIAG SRRPPSVQAA AAWAPQGGAG LEAGARALMD SLDAHPGAWT
SMFASCNLLR PVMAARPMVV LGLSISKYYG MAGNDRVFQA GNWASLLGGK NACPLLIFDR
TRKFVLACPR AGFVCAASSL GGGAHEHSLC EQLRGIIAEG GAAVASSVFV ATVKSLGPRT
QQLQIEDWLA LLEDEYLSEE MMEFTTRALE RGHGEWSTDA ALEVAHEAEA LVSQLGAAGE
VFNFGDFGDA DDHAASFGGL AAAAAGAAGV ARKRAFHGDD PFGEGPPEKK DLTLDML
