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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
 
 
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