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Database: UniProt
Entry: Q9J3N7
LinkDB: Q9J3N7
Original site: Q9J3N7 
ID   OBP_VZVO                Reviewed;         835 AA.
AC   Q9J3N7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Replication origin-binding protein;
DE            Short=OBP;
DE   AltName: Full=OriBP;
GN   ORFNames=ORF51;
OS   Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC   Varicellovirus humanalpha3; Human herpesvirus 3.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=V-Oka(Biken);
RX   PubMed=10720545; DOI=10.1086/315335;
RA   Argaw T., Cohen J.I., Klutch M., Lekstrom K., Yoshikawa T., Asano Y.,
RA   Krause P.R.;
RT   "Nucleotide sequences that distinguish Oka vaccine from parental Oka and
RT   other varicella-zoster virus isolates.";
RL   J. Infect. Dis. 181:1153-1157(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC   Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA   Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT   its parental virus.";
RL   J. Virol. 76:11447-11459(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merck);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
CC   -!- FUNCTION: Functions as a docking protein to recruit essential
CC       components of the viral replication machinery to viral DNA origins. In
CC       the presence of the major DNA-binding protein, opens dsDNA leading to a
CC       conformational change in the origin that facilitates DNA unwinding and
CC       subsequent replication (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with the major DNA-binding protein.
CC       Interacts with the helicase/primase component 52 and the polymerase
CC       accessory protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the herpesviridae OriBP family. {ECO:0000305}.
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DR   EMBL; AF206304; AAF61652.1; -; Genomic_DNA.
DR   EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57660.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57731.1; -; Genomic_DNA.
DR   IntAct; Q9J3N7; 2.
DR   MINT; Q9J3N7; -.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003450; Replication_origin-bd.
DR   Pfam; PF02399; Herpes_ori_bp; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; DNA-binding; Host nucleus;
KW   Nucleotide-binding.
FT   CHAIN           1..835
FT                   /note="Replication origin-binding protein"
FT                   /id="PRO_0000385141"
FT   DOMAIN          54..215
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   835 AA;  94384 MW;  B0386877ACEA9FFB CRC64;
     MSPNTGESNA AVYASSTQLA RALYGGDLVS WIKHTHPGIS LELQLDVPVK LIKPGMSQTR
     PVTVVRAPMG SGKTTALLEW LQHALKADIS VLVVSCRRSF TQTLIQRFND AGLSGFVTYL
     TSETYIMGFK RLIVQLESLH RVSSEAIDSY DVLILDEVMS VIGQLYSPTM RRLSAVDSLL
     YRLLNRCSQI IAMDATVNSQ FIDLISGLRG DENIHTIVCT YAGVGFSGRT CTILRDMGID
     TLVRVIKRSP EHEDVRTIHQ LRGTFFDELA LRLQCGHNIC IFSSTLSFSE LVAQFCAIFT
     DSILILNSTR PLCNVNEWKH FRVLVYTTVV TVGLSFDMAH FHSMFAYIKP MSYGPDMVSV
     YQSLGRVRLL LLNEVLMYVD GSRTRCGPLF SPMLLNFTIA NKFQWFPTHT QITNKLCCAF
     RQRCANAFTR SNTHLFSRFK YKHLFERCSL WSLADSINIL QTLLASNQIL VVLDGMGPIT
     DVSPVQFCAF IHDLRHSANA VASCMRSLRQ DNDSCLTDFG PSGFMADNIT AFMEKYLMES
     INTEEQIKVF KALACPIEQP RLVNTAILGA CIRIPEALEA FDVFQKIYTH YASGWFPVLD
     KTGEFSIATI TTAPNLTTHW ELFRRCAYIA KTLKWNPSTE GCVTQVLDTD INTLFNQHGD
     SLAQLIFEVM RCNVTDAKII LNRPVWRTTG FLDGCHNQCF RPIPTKHEYN IALFRLIWEQ
     LFGARVTKST QTFPGSTRVK NLKKKDLETL LDSINVDRSA CRTYRQLYNL LMSHRHSFSQ
     QRYKITAPAW ARHVYFQAHQ MHLAPHAEAM LQLALSELSP GSWPRINGAV NFESL
//
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