OBP_HHV2H
ID OBP_HHV2H Reviewed; 867 AA.
AC P89432;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Replication origin-binding protein;
DE Short=OBP;
DE AltName: Full=OriBP;
GN ORFNames=UL9;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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.
CC -!- SUBUNIT: Homodimer. Interacts with the major DNA-binding protein ICP8.
CC Interacts with the helicase/primase component UL8 and the polymerase
CC accessory protein UL42 (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; Z86099; CAB06769.2; -; Genomic_DNA.
DR IntAct; P89432; 1.
DR MINT; P89432; -.
DR PRIDE; P89432; -.
DR Proteomes; UP000001874; 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:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
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; 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..867
FT /note="Replication origin-binding protein"
FT /id="PRO_0000385140"
FT DOMAIN 86..251
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 867 AA; 95799 MW; 099CE34F7AC4A24E CRC64;
MNVATCTHQT HHAARAPGAT SAPGAASGDP LGARRPIGDD ECEQYTSSVS LARMLYGGDL
AEWVPRVHPK TTIERQQHGP VTFPDASAPT ARCVTVVRAP MGSGKTTALI RWLGEAIHSP
DTSVLVVSCR RSFTQTLATR FAESGLPDFV TYFSSTNYIM NDRPFHRLIV QVESLHRVGP
NLLNNYDVLV LDEVMSTLGQ LYSPTMQQLG RVDALMLRLL RTCPRIIAMD ATANAQLVDF
LCSLRGEKNV HVVIGEYAMP GFSARRCLFL PRLGPEVLQA ALRRRGPAGG APPPDAPPDA
TFFGELEARL AGGDNVCIFS STVSFAEVVA RFCRQFTDRV LLLHSLTPPG DVTTWGRYRV
VIYTTVVTVG LSFDPPHFDS MFAYVKPMNY GPDMVSVYQS LGRVRTLRKG ELLIYMDGSG
ARSEPVFTPM LLNHVVSASG QWPAQFSQVT NLLCRRFKGR CDASHADAAQ ARGSRIYSKF
RYKHYFERCT LACLADSLNI LHMLLTLNCM HVRFWGHDAA LTPRNFCLFL RGIHFDALRA
QRDLRELRCQ DPDTSLSAQA AETEEVGLFV EKYLRPDVAP AEVVALMRGL NSLVGRTRFI
YLVLLEACLR VPMAAHSSAI FRRLYDHYAT GVIPTINAAG ELELVALHPT LNVAPVWELF
RLCSTMAACL QWDSMAGGSG RTFSPEDVLE LLNPHYDRYM QLVFELGHCN VTDGPLLSED
AVKRVADALS GCPPRGSVSE TEHALSLFKI IWGELFGVQL AKSTQTFPGA GRVKNLTKRA
IVELLDAHRI DHSACRTHRQ LYALLMAHKR EFAGARFKLR APAWGRCLRT HASGAQPNTD
IILEAALSEL PTEAWPMMQG AVNFSTL