DNBI_GAHVM
ID DNBI_GAHVM Reviewed; 1191 AA.
AC Q9E6P0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 02-JUN-2021, entry version 67.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=MDV042;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14222.1; -; Genomic_DNA.
DR RefSeq; YP_001033958.1; NC_002229.3.
DR SMR; Q9E6P0; -.
DR PRIDE; Q9E6P0; -.
DR GeneID; 4811503; -.
DR KEGG; vg:4811503; -.
DR Proteomes; UP000008072; 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..1191
FT /note="Major DNA-binding protein"
FT /id="PRO_0000406582"
FT ZN_FING 498..511
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1191
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 841..842
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1191 AA; 130715 MW; 9AD425780FB07711 CRC64;
MDGVGKSVKL CGGPIGYIYA TPKCSVPVDE LAILAAKSND CDDAVLPLVA GLTVESDFVW
NVAAVAGTKT TGLGSGGTTL KLVPTHYHPC VFVFYGGDCI KPCTKAPNLT KACDLARERF
GYSAYSSPAP TAFETTGQQI CEALEMDAQN VMLYLVVTEL FKEVIYLCNS FLHFGGSDVV
TINNADVRRI PIYPLHLVLP DFNRITNEPF SEKPRALGEG AIMPKAFYND SLCRLLHGYV
LSTTAVGLRV RNIDAIARGA AHLCFDENHE GTLLPADTTF TAFTPAAETT KGQSKMGKRE
GSDVSGGGYE RRTASLMASD ATLAIENVIS ASVYEDPIPD VNKWPIYCNP VGYADRIEAL
SAYMARVAGL VGAMVFSSNS VIYMTEVGEA GSTEGKETST TAPSFYRFFQ IAAPHLSANP
LVDRDGKPVS GENLSKSTSA SQSEYSLDYL ILACGFCPQL LARFLFYLER CDGGAKACHH
DLDTVKFVSS AIDADMPCEL CDKTSRIYCA HTTIKRLVYR LPKFGYQMRG AMGLFGAMTN
NYCDVNALGS YAQFSTLKRS EGEASRSVMQ DTYRLTVERM MKALEKEGLL TCDDPTNMAS
ADANIRDGNS FIRAISTMKN IIESEASQLM RNLTEIREYN IREGLGDANH TLSLAVEPYA
SGICPVLAFL SRRTIIAVVQ DMALSQCSIV MQGQQVEARN FRTQFQAVLK RRVLELQNAG
FITSKTITVT LEDQQICVPD PSKSQYDSVI SNMEGDLVKV TVEIFRELKV KNKVLFGGGI
AGAASEATKS RLAGMVEAYQ RPTKTMHVLN GPLGFAVKRY HTLLFPDVKM PNGATPNALW
FWILLLRNQL PAGILSKEEE DKSLFIKKFT KSYADMNYIN ISPTCFGDLA QFYLANTILK
YCSHKHFFIN TISALVAVSR RPRDPAIVLP WIERPITKGQ DVAPAAQQLI ASMSDHKDIW
CATFSSTNLV GSIMTTKPFV VIGISISKYH GMAGSTKVFQ SGNWGNIMGG RNVCSLMSFD
RTHRYVMTCP RVGFVAEQPI FSSGIKETTL IDRVRMVLSE ESAAPHAAVY MLALKMVGDR
VRQMELEDWM EITNDEYISS LIDELNKQVE EAEGGWNADA AMTLAKEMVN MAMSIPTDGP
TFDFDACDEN LEGHADGQTI SETNLKRPNM NVFDLEPIPE KRVPVLSVDM L
