OBP_VZVD
ID OBP_VZVD Reviewed; 835 AA.
AC P09299;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Replication origin-binding protein;
DE Short=OBP;
DE AltName: Full=OriBP;
GN ORFNames=ORF51;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27933.1; -; Genomic_DNA.
DR PIR; G27344; WZBE51.
DR PRIDE; P09299; -.
DR Proteomes; UP000002602; 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:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 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; SSF52540; 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; Reference proteome.
FT CHAIN 1..835
FT /note="Replication origin-binding protein"
FT /id="PRO_0000115873"
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; 94375 MW; A71F5877ACF386FB 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 LMSQRHSFSQ
QRYKITAPAW ARHVYFQAHQ MHLAPHAEAM LQLALSELSP GSWPRINGAV NFESL