DNBI_SCMVC
ID DNBI_SCMVC Reviewed; 1160 AA.
AC P13215;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 23-FEB-2022, 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=UL57;
OS Simian cytomegalovirus (strain Colburn).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=50292;
OH NCBI_TaxID=9539; Macaca (macaques).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2172458; DOI=10.1099/0022-1317-71-10-2451;
RA Anders D.G.;
RT "Nucleotide sequence of a cytomegalovirus single-stranded DNA-binding
RT protein gene: comparison with alpha- and gammaherpesvirus counterparts
RT reveals conserved segments.";
RL J. Gen. Virol. 71:2451-2456(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-308.
RX PubMed=2831398; DOI=10.1128/jvi.62.4.1364-1372.1988;
RA Anders D.G., Gibson W.;
RT "Location, transcript analysis, and partial nucleotide sequence of the
RT cytomegalovirus gene encoding an early DNA-binding protein with
RT similarities to ICP8 of herpes simplex virus type 1.";
RL J. Virol. 62:1364-1372(1988).
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}.
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DR EMBL; D00750; BAA00647.1; -; Genomic_DNA.
DR EMBL; M19868; AAA46066.1; ALT_SEQ; mRNA.
DR SMR; P13215; -.
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; 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 2: Evidence at transcript level;
KW DNA replication; DNA-binding; Host nucleus.
FT CHAIN 1..1160
FT /note="Major DNA-binding protein"
FT /id="PRO_0000115760"
FT REGION 1139..1160
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 808..809
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1160 AA; 129006 MW; 7037716816974B1A CRC64;
MSNEELSALA PVGPAAYVYF TKTNHEMNEV LATLSLCDSS SPVVIAPLLM GLTVDQDFCT
SVRTPVVCYD GGVLTKVTSF CPFALYFYNT QGIVDFSEPH GDVQRLCDET RQRYAIESYM
PEEGRAPTDL AALCTAAGCD PQEVLVHVVV GNGMKEFMYA GQLIPCFEEA APTRLNDCDA
VRVPLYPPTL FGSLQADVDS DELSLDKRSS FVESRGLYVP AVSETLFYYV YTSWCQALRF
SETKVLIEAA LKQFVNDSQQ SVKLAPHKKY FGYTSQKLSS LEKDHLMLSD AVICELGFSF
ASVFLDSAYG ASDSMVYSEW PVVVNATDHR DLIRALTELK LHLSTHISAL LFSCNSILYH
NRLVYLTSNK NASGTGASQE VLLKSIHFAN GLTGLCEDTY NDARKLIKCS GVVAKDERYA
PYHLSLICGT CPQLFSAFIW YLNRVSVYNT GLTGSSTLSN HLIGCSSSLC GACGGTCCHT
CYNTAFVRVQ TRLPQMPRLP KKEPSVVVMQ SRFLNDVDVL GTFGRRYSAE SKEASLDAKA
DEGSASTSNR TASSSVDRTH RLNRILDYCK KMRLIDSVTG EDTMTINGRS DFINLVSSLN
KFVDDEAMSF VSEVRMKSNR DEVLGATQAF NLDLNPFAVS FSPILAYEYY RVIFAIIQNV
ALITATSYIV DNPLTTSLVS RWVTQHFQSI HGAFSTTSSR KGFLFIRNVK SSKNADHDRL
PDFKLYARGT YSVISMEIKL SRLSVPSLLM FRVKNRPISK ASKGTTAHVF FRREHVPKKN
PVKGCLGFLL YKYHDKLFPD CGFSCLQFWQ KVCANALPKN VNIGDMGEFN NFVKFVISVT
ADYNEHDLID VPPDCMLNYL ENRFHNKFLC FYGFKDYIGT LHGLTTRLTY QNHAQFPYLL
GESPNFASAA DFALRLKDLK ATGVTAPLAS TVTRESLMRT IFEQRSLVTV SFSIEKYAGV
NNNKEIYQFG QIGYFSGNGV ERSLNTNSIG GQDYKFMRQR CILATKLSDV LIKRSRRDNV
LFDEDIIKNR VMAALDSENL DVDPELMAMY EILSTREEIP ERDDVLFFVD GCQAVADSLM
EKFSRLQEMG VDDFSLVNLQ QVLDSRPECG GGGGEVHDLS ALFTAASGEA VGNSVGLNAR
GGEHAFDEDC GLLPAKRGRL
