OBP_EHV1V
ID OBP_EHV1V Reviewed; 887 AA.
AC P84403; Q6S6V1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Replication origin-binding protein;
DE Short=OBP;
DE AltName: Full=OriBP;
GN OrderedLocusNames=53;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45937.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 DNA helicase/primase complex-associated protein and
CC the polymerase 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; AY464052; AAS45937.1; -; Genomic_DNA.
DR RefSeq; YP_053097.1; NC_001491.2.
DR GeneID; 2948557; -.
DR KEGG; vg:2948557; -.
DR Proteomes; UP000008296; 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.
FT CHAIN 1..887
FT /note="Replication origin-binding protein"
FT /id="PRO_0000115869"
FT DOMAIN 93..258
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 887 AA; 97276 MW; E43727EDA58C76BA CRC64;
MPSIGPIPTI PDEGSRGSSA TAAPRRAMAS YRDTTLGGRA EGVAFSAVED SYTSSVSLAR
MLYGGDLEEW VRHTRPGVSL EIQSRAPVRF PPPNNPSSRR VTVVRAPMGS GKTTALLKWL
GEALDAPDIS ALVVSCRRSF TRTLAKRFND AELPGFATYF TSTDYTMAGE PFRRLLVQIE
SLHRVDDNLL NNYDILVLDE VMSTIGQLYS PTMVHLNKVD ALLTRLLKTC PRVIAMDATA
NAQLVDFLAS ARGERSVHVI INSFAAPGFS QRDGTLLRTL GTDVLRAALG FVLVDDENGT
KVMETDSRPI SARLREVNSA GFFGRLMDRL VAGRNVCVFS STVSFSEIVA RFCSQFTDSI
LVLNSLRPSE DVAFWGGVRV LIYTTVVTVG LSFDTAHFHS MFAYVKPMSH GPDMVSVYQS
LGRVRELIHN ELLVYVDSSG ARAEPIFTPM LLNHVVSRQG GWPAEFSQVT DALCCQFKAR
CGPAYRTAST RGLALFVRFK YKHFFERCTL ASVGDSINIL YTLLESNQMR VAIEGCQFPL
TAAGFCDFLQ DLRLDAYAAR KEIKQLRGPG GIAATPTEVF ENDDVAVFIQ KYLRPGVAHD
EILALLVELN SPIVREQFVN VAVLGACLRL PAALESPEVF AGVYKHYASG VVPVISDAGA
LESVSITPDV NVLARWDLYK SCTRHARDLA WDPSRGGSGL DMSEDFITNT LSADYNRFQS
LLVEIAKCNV TPLEMLAAGA VRGVTTALSG RPKSRVPLSK GEHAVSLFKV LWEDVFGAKL
AKSTQTFPGG VRVKNLRKDE IVALLESVNV NHSECKTHRE LYALLMCNRK LFAGPRYKLR
APKWSRNLCF LELDNTGTCK TPLDAALADL APSAWPQVYG AVDFDAL