DNBI_HHV8P
ID DNBI_HHV8P Reviewed; 1132 AA.
AC Q2HRD3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 23-FEB-2022, entry version 72.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=ORF6;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP SUBUNIT.
RX PubMed=21047556; DOI=10.1016/j.jsb.2010.10.015;
RA Ozgur S., Damania B., Griffith J.;
RT "The Kaposi's sarcoma-associated herpesvirus ORF6 DNA binding protein forms
RT long DNA-free helical protein filaments.";
RL J. Struct. Biol. 174:37-43(2011).
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 ECO:0000269|PubMed:21047556}.
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; AF148805; ABD28849.1; -; Genomic_DNA.
DR RefSeq; YP_001129352.1; NC_009333.1.
DR SMR; Q2HRD3; -.
DR BioGRID; 1777024; 1.
DR PRIDE; Q2HRD3; -.
DR DNASU; 4961521; -.
DR GeneID; 4961521; -.
DR KEGG; vg:4961521; -.
DR Proteomes; UP000000942; 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; -; 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 1: Evidence at protein level;
KW DNA replication; DNA-binding; Host nucleus; Reference proteome.
FT CHAIN 1..1132
FT /note="Major DNA-binding protein"
FT /id="PRO_0000423834"
FT REGION 1103..1132
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1132 AA; 125409 MW; F71911132BCD0FF1 CRC64;
MALKGPQTLE ENIGSAAPTG PCGYLYAYVT HNFPIGEASL LGNGYPEAKV FSLPLLHGLT
VESDFPLNVK AVHKKIDATT ASVKLTSYHR EAIVFHNTHL FQPIFQGKGL EKLCRESREL
FGFSTFVEQQ HKGTLWSPEA CPQLPCANEI FMAVIVTEGF KERLYGGKLV PVPSQTTPVH
IGEHQAFKIP LYDEDLFGPS RAQELCRFYN PDISRYLHDS IFTGIAQALR VKDVSTVIQA
SERQFVHDQY KIPKLVQAKD FPQCASRGTD GSTLMVIDSL VAELGMSYGL SFIEGPQDSC
EVLNYDTWPI FENCETPDAR LRALEVWHAE QALHIGAQLF AANSVLYLTR VAKLPQKNQR
GDANMYNSFY LQHGLGYLSE ATVKENGASA FKGVPVSALD GSSYTLQHLA YASSFSPHLL
ARMCYYLQFL PHHKNTNSQS YNVVDYVGTA APSQMCDLCQ GQCPAVCINT LFYRMKDRFP
PVLSNVKRDP YVITGTAGTY NDLEILGNFA TFREREEEGN PVEDAPKYTY WQLCQNITEK
LASMGISEGG DALRTLIVDI PSFVKVFKGI DSTVEAELLK FINCMIKNNY NFRENIKSVH
HILQFACNVY WQAPCPVFLT LYYKSLLTVI QDICLTSCMM YEQDNPAVGI VPSEWLKMHF
QTMWTNFKGA CFDKGAITGG ELKIVHQSMF CDLFDTDAAI GGMFAPARMQ VRIARAMLMV
PKTIKIKNRI IFSNSTGAES IQAGFMKPAS QRDSYIVGGP YMKFLNALHK TLFPSTKTSA
LYLWHKIGQT TKNPILPGVS GEHLTELCNY VKASSQAFEE INVLDLVPDT LTSYAKIKLN
SSILRACGQT QFYATTLSCL SPVTQLVPAE EYPHVLGPVG LSSPDEYRVK VAGRSVTIVQ
STLKQAVSTN GRLRPIITVP LVVNKYTGSN GNTNVFHCAN LGYFSGRGVD RNLRPESVPF
KKNNVSSMLR KRHVIMTPLV DRLVKRIVGI NSGEFEAEAV KRSVQNVLED RDNPNLPKTV
VLELVKHLGS SCASLTEEDV IYYLGPYAVL GDEVLSLLST VGQAGVPWTA EGVASVIQDI
IDDCELQFVG PEEPCLIQGQ SVVEELFPSP GVPSLTVGKK RKIASLLSDL DL