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Database: UniProt
Entry: OBP_HHV11
LinkDB: OBP_HHV11
Original site: 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   27-MAR-2024, entry version 112.
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; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
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; AH002360; 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; 3.
DR   DIP; DIP-1095N; -.
DR   IntAct; P10193; 2.
DR   MINT; 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; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 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
//
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