DNBI_HCMVM
ID DNBI_HCMVM Reviewed; 1235 AA.
AC F5HDQ6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 32.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=UL57;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Merlin;
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
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; AY446894; AAR31622.1; -; Genomic_DNA.
DR RefSeq; YP_081516.1; NC_006273.2.
DR SMR; F5HDQ6; -.
DR PRIDE; F5HDQ6; -.
DR GeneID; 3077528; -.
DR KEGG; vg:3077528; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
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; -; 1.
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; Reference proteome.
FT CHAIN 1..1235
FT /note="Major DNA-binding protein"
FT /id="PRO_0000416448"
FT REGION 536..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1235
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 846..847
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1235 AA; 133849 MW; 19C62999E24AEE8A CRC64;
MSHEELTALA PVGPAAFLYF SRLNAETQEI LATLSLCDRS SSVVIAPLLA GLTVEADFGV
SVRTPVLCYD GGVLTKVTSF CPFALYFHHT QGIVAFTEDH GDVHRLCEDA RQKYALEAYT
PEADRVPTDL AALCAAVGCQ ASETTVHVVV GNGLKEFLFA GQLIPCVEEA TTVRLHGGEA
VRVPLYPPTL FNSLQLDAEA DEVSLDARSA FVEARGLYVP AVSETLFYYV YTSWCQSLRF
SEPRVLIEAA LRQFVHDSQQ SVKLAPHKRY LGYMSQRLSS LEKDHLMLSD AVVCELAFSF
ASVFFDSAYQ PAESMLFSEW PLVTNATDHR DLIRALTELK LHLSTHVAAL VFSANSVLYQ
HRLVYLQSSA RHPSAGGTAS QETLLKAIQF TNGLSAACED VYNDARKVLK FQGAPLKDER
YGPQHLALVC GTCPQLVSGF VWYLNRVSVY NTGLSGSSTL TNHLVGCAAG LCEACGGTCC
HTCYQTAFVR VRTRLPVVPK QPKKEPCVIT VQSRFLNDVD ILGSFGRRYN VDAKDGGLDG
KGDDGVPGGG AGGGGGRDVS GGPSDGLGGG RGGGGGGDSG GMMGRGGRML GASVDRTYRL
NRILDYCRKM RLIDPVTGED TFSAHGKSDF VAVFSALNKF VDDEALGFVS EVRLKSSRDE
VAGATQAFNL DLNPYAVAFQ PLLAYAYFRS VFYVIQNVAL ITATSYIVDN PLTTNLVSKW
MTQHFQSIHG AFSTTSSRKG FLFTKQIKSS KNSDHDRLLD FRLYAQGTYA VVPMEIKLSR
LSVPTLIMVR VKNRPIYRAG KGNAGSVFFR RDHVPRRNPA KGCLGFLLYR HHERLFPECG
LPCLQFWQKV CSNALPKNVP IGDMGEFNAF VKFLVAVTAD YQEHDLLDVA PDCVLSYVES
RFHNKFLCYY GFKDYIGSLH GLTTRLTTQN HAQFPHVLGA SPRFSSPAEF ALHVKGLKTA
GVPAPMAATV ARESLVRSVF EHRSLVTVPV SVEKYAGINN SKEIYQFGQI GYFSGNGVER
SLNVSSMSGQ DYRFMRQRYL LATRLADVLI KRSRRENVLF DADLIKNRVM LALDAENLDC
DPEVMAVYEI LSVREEIPAS DDVLFFVDGC EALAASLMDK FAALQEQGVE DFSLENLRRV
LDADAQRLTD AAGGEVHDLS ALFAPSGVGA ASGVGGGGLL LGESVAGNSI CFGVPGETGG
GCFLVNAGED EAGGVGGSSG GGGGSGLLPA KRSRL
