ID   YR290_MIMIV             Reviewed;         548 AA.
AC   Q5UPX0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative ATP-dependent RNA helicase R290;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=MIMI_R290;
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 [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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAV50562.1; -; Genomic_DNA.
DR   RefSeq; YP_003986792.1; NC_014649.1.
DR   SMR; Q5UPX0; -.
DR   PRIDE; Q5UPX0; -.
DR   GeneID; 9924905; -.
DR   KEGG; vg:9924905; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00614; recQ_fam; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..548
FT                   /note="Putative ATP-dependent RNA helicase R290"
FT                   /id="PRO_0000253409"
FT   DOMAIN          38..206
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          231..376
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           150..153
FT                   /note="DEAH box"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   548 AA;  62737 MW;  95E7A086A2D57C6F CRC64;
     MDDYEKSKVL TKRYKKLKKL LKMVYGYDNF RPRQYEIINK VINGEDVCAI LMTSAGKSLC
     FQIPALYLDK PAIIISPLIS LMEDQRLILE KLGISSCCYN SNVENKAQMR KDIMQFKYKF
     IYVSPESVVH LKDLIVKLED FQGISLIAID EAHCISAYGF DFRTAYREIT FFKEILPNVP
     ILALTATATN IVAKDICKVL QLKTNEPIKA SFDRPNLYLE VRTKSKNPAN DIVPIINKYP
     NQSVIIYCLT KKETQKIADI LTVHKVVCGI YHAGLSNEHK TKTHTNFINN KIKIVVATIA
     FGMGINKPDV RVVIHYGAPK NIEGYYQEIG RAGRDGEKSY CYAFYNFQDF MIQRRFISQN
     NNPNYQKTQL ALLEQMKKYV TLRTCRRKIL LEYFDEETKE KCDFCDNCCG VHKNIVNENV
     TSKQNVQSEA KLIIELIESI PNRNFGVNMY INILRGSKNK AISPAIRKNK YYGLGSKHSS
     EWWKEVFDNL IKQGFLQSVS LKTGKFPIQV VKVTNKGVTW VSMADLGSLL DNIDNSVKLD
     PVEMVASV