ID   YR350_MIMIV             Reviewed;         817 AA.
AC   Q5UQU2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative ATP-dependent RNA helicase R350;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=MIMI_R350;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAV50619.1; -; Genomic_DNA.
DR   RefSeq; YP_003986853.1; NC_014649.1.
DR   SMR; Q5UQU2; -.
DR   GeneID; 9924969; -.
DR   KEGG; vg:9924969; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Virion.
FT   CHAIN           1..817
FT                   /note="Putative ATP-dependent RNA helicase R350"
FT                   /id="PRO_0000247395"
FT   DOMAIN          93..271
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          495..661
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           206..209
FT                   /note="DEAH box"
FT   COMPBIAS        7..29
FT                   /note="Polar residues"
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   817 AA;  95416 MW;  440D619A06E2A381 CRC64;
     MNRRNRSNDL NPEPSIENPN NQIAEEFPGN NSVYKSDGYV DLKNNGRLFP IWILKNFKQY
     KLPEIIRKEN EDPCNVQVKL ELRKYQEFVG QYLNPQGPYT SILLYHGLGS GKTASAINLM
     NILYNYDNGT NFIVLIKASL HNDPWMQDLK EWLGRDPSEQ NVDNVTKLDR YKNIHFVHYD
     SPFADSSFMS VIKTLDLSKP TMYIIDEAHN FIRNVYSNIN SKLGKRAKVI YEYIMKDKRE
     NKNTRIVLIS ATPAINTPFE LALMFNLLRP GIFPSSELDF NRTFVTESSY PILNPMKKNM
     FERRILGLVS YYIGATPDLY ARQELKYINL PMSAYQYDIY RIFEKLEAEI QERARRRGKQ
     SQLYRTYTRQ ACNFVFPYVN MNVNGELRPR PGKFRLSEKL ADDFSKGKNL DVPDTEKEIL
     NKYTKAIENY LNETERYFQN INKKDAENGR TIINDLDEFK KGFGTKFNSF LQYYQSEGPR
     SSLLTEMYNC SPKMLAIAFM TYISPGKVMI YSNYVVMEGI DVMKIYFRLI GFNDFTIARE
     YMGYCEYHGR IDPKDRVRIK NMFNDKNNVY GNKCKVIMLS PSATEGIQLL DIRQEHIMEP
     YWTEVRIQQV IGRGVRQCSH RDLPMSERIV DIYRYKVIKP ENLDPDDTVR QSTDEYVEDQ
     AKSKANLIES FLGAMKEAAV DCELFKEHNM MSQSYYCFKF PESAVTKTNV GPAYREDIKD
     DVKYDSGLNS KNSIVERIRV VKVNAVYQIN TDNNNPVYSS PTKYWYNKKT GMVYDFETHY
     PVGQVEFIDN LPNKLDKDTY IMRIDVIIPS ITGSVNT