ID   YR001_MIMIV             Reviewed;         795 AA.
AC   Q5UP78;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Putative replication origin-binding protein;
DE            Short=OBP;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=MIMI_R1;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Probably involved in DNA replication. May bind the genome
CC       origin of replication (ori) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mimivirus R1 family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50276.1; -; Genomic_DNA.
DR   RefSeq; YP_003986475.1; NC_014649.1.
DR   SMR; Q5UP78; -.
DR   PRIDE; Q5UP78; -.
DR   GeneID; 9925578; -.
DR   KEGG; vg:9925578; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003450; Replication_origin-bd.
DR   Pfam; PF02399; Herpes_ori_bp; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..795
FT                   /note="Putative replication origin-binding protein"
FT                   /id="PRO_0000253219"
FT   DOMAIN          121..289
FT                   /note="Helicase ATP-binding"
FT   BINDING         134..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   795 AA;  93130 MW;  CD6A16B77AE28B7E CRC64;
     MTYVKKYHPT TKYYGIIHGE KYELQDVLFY SFNYSNREEV CPISGTAHKS NGFYVIETSK
     GYFMKCHSDK CKNKKAKYLG PADATDMFVK CANQIDQQYL IMKGGIADAP KEPVKDIIIN
     WLSNDKIKTL AVRSPMGTGK TTMIKKILDH YDNIKKILWI SHRQTLSKQI YGSFKNHGFV
     NYMDQKGNLF EHDRLIIQID SLKRIFKYDK DYNTVFKQYD LVIIDEIEGN MNHFMSPYLR
     KDSDFSVRQT FQKMLNCIDT AKKLLVLDAD LGMRSKLFID NFGKSIVVNN NYKPIQKIFE
     ITNDLSSFQE ILLADIKDGK NVCVVSMSAS YLDKLEPKFA GLKYVIHTSK SDDKLKNELE
     NVNYFWKKFQ ICCFSPTIEC GVDFNEKHFD KIYCYLKNGS KTCSQRSLLQ MVGRIRQLGN
     NKILCYYSGP TNIDADIYTY DDILGYFRHY EKINGRKVLE NVEYKKFIAN GEVTLKRVSA
     NISLFDHIHI YNEVEESNKN HSMFITVLFK LIQRAGHSMI FNTVEEPEEV EPDNNVISHA
     EILSMINETK YKISDLMKKQ SKNQLSRTEK LVLEKYFFMK NFGVKDSSNK DEFVKFHKKY
     ANKEITFKHF KRFFGYDNPN NSIDELKHLD IFVSNKKPPN NNNNNFLDEH NDSKDAVRDK
     IIVNFLNLIL DVKKNGYGPD DLGYTLTQDE HNTAVLTVAE QSMYFANEDK YRPLFNKNKG
     KFKEINEYNF KHYFKTVKAI LQSYGIDYYR GNRKRVNSRR EFEYSLSVDK QIRDIVDFKF
     GLSDTVDEFP NLFHK