DNBI_HCMVA
ID DNBI_HCMVA Reviewed; 1235 AA.
AC P17147; Q7M6M6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [3]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [4]
RP FUNCTION IN DNA REPLICATION.
RX PubMed=8230421; DOI=10.1128/jvi.67.12.6979-6988.1993;
RA Pari G.S., Anders D.G.;
RT "Eleven loci encoding trans-acting factors are required for transient
RT complementation of human cytomegalovirus oriLyt-dependent DNA
RT replication.";
RL J. Virol. 67:6979-6988(1993).
RN [5]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [6]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(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 (PubMed:8230421). May
CC disrupt loops, hairpins and other secondary structures present on ssDNA
CC to reduce and eliminate pausing of viral DNA polymerase at specific
CC sites during elongation. Promotes viral DNA recombination by performing
CC strand-transfer, characterized by the ability to transfer a DNA strand
CC from a linear duplex to a complementary single-stranded DNA circle. Can
CC also 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 ECO:0000269|PubMed:8230421}.
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; X17403; CAA35372.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00162.1; -; Genomic_DNA.
DR PIR; S09820; QQBEW4.
DR SMR; P17147; -.
DR PRIDE; P17147; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
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 1: Evidence at protein level;
KW DNA replication; DNA-binding; Host nucleus; Reference proteome.
FT CHAIN 1..1235
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115759"
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; 133879 MW; 94E8D4F8D3BB2CB6 CRC64;
MSHEELTALA PVGPAAFLYF SRLNAETQEI LATLSLCDRS SSVVIAPLLA GLTVEADFGV
SVRTPVLCYD GGVLTKVTSF CPFALYFHHT QGIVAFTEDH GDVHRLCEDA RQKYALEAYM
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
