OBP_HHV11
ID OBP_HHV11 Reviewed; 851 AA.
AC P10193; B9VQD6; Q09IC4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Replication origin-binding protein;
DE Short=OBP;
DE AltName: Full=OriBP;
GN ORFNames=UL9;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988;
RA McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P.,
RA Challberg M.D.;
RT "Structures of herpes simplex virus type 1 genes required for replication
RT of virus DNA.";
RL J. Virol. 62:444-453(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH UL8.
RX PubMed=7931156; DOI=10.1099/0022-1317-75-10-2699;
RA McLean G.W., Abbotts A.P., Parry M.E., Marsden H.S., Stow N.D.;
RT "The herpes simplex virus type 1 origin-binding protein interacts
RT specifically with the viral UL8 protein.";
RL J. Gen. Virol. 75:2699-2706(1994).
RN [6]
RP INTERACTION WITH ICP8, AND FUNCTION.
RX PubMed=7961904; DOI=10.1016/s0021-9258(19)62048-x;
RA Boehmer P.E., Craigie M.C., Stow N.D., Lehman I.R.;
RT "Association of origin binding protein and single strand DNA-binding
RT protein, ICP8, during herpes simplex virus type 1 DNA replication in
RT vivo.";
RL J. Biol. Chem. 269:29329-29334(1994).
RN [7]
RP INTERACTION WITH UL42.
RX PubMed=9454723; DOI=10.1006/viro.1997.8953;
RA Monahan S.J., Grinstead L.A., Olivieri W., Parris D.S.;
RT "Interaction between the herpes simplex virus type 1 origin-binding and DNA
RT polymerase accessory proteins.";
RL Virology 241:122-130(1998).
RN [8]
RP SUBUNIT.
RX PubMed=17942532; DOI=10.1128/jvi.01204-07;
RA Chattopadhyay S., Weller S.K.;
RT "Direct interaction between the N- and C-terminal portions of the herpes
RT simplex virus type 1 origin binding protein UL9 implies the formation of a
RT head-to-tail dimer.";
RL J. Virol. 81:13659-13667(2007).
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. {ECO:0000269|PubMed:7961904}.
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. {ECO:0000269|PubMed:17942532,
CC ECO:0000269|PubMed:7931156, ECO:0000269|PubMed:7961904,
CC ECO:0000269|PubMed:9454723}.
CC -!- INTERACTION:
CC P10193; P10226: UL42; NbExp=3; IntAct=EBI-8596799, EBI-1029310;
CC P10193; P09884: POLA1; Xeno; NbExp=4; IntAct=EBI-8596799, EBI-850026;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae OriBP family. {ECO:0000305}.
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DR EMBL; X14112; CAA32345.1; -; Genomic_DNA.
DR EMBL; M19120; AAA45822.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63471.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62231.1; -; Genomic_DNA.
DR PIR; B29890; WMBEU9.
DR SASBDB; P10193; -.
DR BioGRID; 971457; 2.
DR DIP; DIP-1095N; -.
DR IntAct; P10193; 2.
DR MINT; P10193; -.
DR PRIDE; P10193; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB.
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; 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 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Host nucleus;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..851
FT /note="Replication origin-binding protein"
FT /id="PRO_0000115866"
FT DOMAIN 68..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VARIANT 149
FT /note="R -> Q (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 204
FT /note="I -> T (in strain: Nonneuroinvasive mutant HF10 and
FT 17 syn+)"
FT VARIANT 280
FT /note="E -> D (in strain: Nonneuroinvasive mutant HF10 and
FT 17 syn+)"
FT VARIANT 668..669
FT /note="GP -> SH (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 745
FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 797
FT /note="A -> V (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 818
FT /note="S -> N (in strain: 17 syn+)"
SQ SEQUENCE 851 AA; 94262 MW; 961A133FE7A30CA7 CRC64;
MPFVGGAESG DPLGAGRPIG DDECEQYTSS VSLARMLYGG DLAEWVPRVH PKTTIERQQH
GPVTFPNASA PTARCVTVVR APMGSGKTTA LIRWLREAIH SPDTSVLVVS CRRSFTQTLA
TRFAESGLVD FVTYFSSTNY IMNDRPFHRL IVQVESLHRV GPNLLNNYDV LVLDEVMSTL
GQLYSPTMQQ LGRVDALMLR LLRICPRIIA MDATANAQLV DFLCGLRGEK NVHVVVGEYA
MPGFSARRCL FLPRLGTELL QAALRPPGPP SGPSPDASPE ARGATFFGEL EARLGGGDNI
CIFSSTVSFA EIVARFCRQF TDRVLLLHSL TPLGDVTTWG QYRVVIYTTV VTVGLSFDPL
HFDGMFAYVK PMNYGPDMVS VYQSLGRVRT LRKGELLIYM DGSGARSEPV FTPMLLNHVV
SSCGQWPAQF SQVTNLLCRR FKGRCDASAC DTSLGRGSRI YNKFRYKHYF ERCTLACLSD
SLNILHMLLT LNCIRVRFWG HDDTLTPKDF CLFLRGVHFD ALRAQRDLRE LRCRDPEASL
PAQAAETEEV GLFVEKYLRS DVAPAEIVAL MRNLNSLMGR TRFIYLALLE ACLRVPMATR
SSAIFRRIYD HYATGVIPTI NVTGELELVA LPPTLNVTPV WELLCLCSTM AARLHWDSAA
GGSGRTFGPD DVLDLLTPHY DRYMQLVFEL GHCNVTDGLL LSEEAVKRVA DALSGCPPRG
SVSETDHAVA LFKIIWGELF GVQMAKSTQT FPGAGRVKNL TKQTIVGLLD AHHIDHSACR
THRQLYALLM AHKREFAGAR FKLRVPAWGR CLRTHSSSAN PNADIILEAA LSELPTEAWP
MMQGAVNFST L