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YL396_MIMIV
ID   YL396_MIMIV             Reviewed;         519 AA.
AC   Q5UQ46;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Putative ATP-dependent RNA helicase L396;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=MIMI_L396;
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; AAV50665.1; -; Genomic_DNA.
DR   RefSeq; YP_003986900.1; NC_014649.1.
DR   SMR; Q5UQ46; -.
DR   GeneID; 9925017; -.
DR   KEGG; vg:9925017; -.
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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..519
FT                   /note="Putative ATP-dependent RNA helicase L396"
FT                   /id="PRO_0000253412"
FT   DOMAIN          110..258
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          317..457
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           211..214
FT                   /note="DEAH box"
FT   BINDING         123..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   519 AA;  60347 MW;  B703EE1B717158E6 CRC64;
     MANNIKTKIT RFGYIVNKNL IDDETIKEIK SDLTVVPFKI NNYAPKYIKN EGFPLYVENG
     NYIGIPKYYG FDKLGEPDID KVSNYEYPVQ DMTYTGTLRP HQQMVSDKII KGMEEGGGGV
     LVMGCGSGKT NVAIYIACKF KLRTLFVVHK TFLRDQVIDR IKSNTNVKKV GIIQRKIVNY
     KHPFVVSMVQ SLAKINYNDE IFKDFGMIII DEVHHMGARN FSTVYQKISS KYMLGISAEY
     TRTDGMYKII NWYMGPILHL EEQKPNEMVI VKQFYYSTSN KERIKMKYIN GDTNKPNRSK
     MITNLFYIKR RNRFILYLIQ ELFDMGKNIL FLSGRLKQID LLYELLNNDE FTHGNVGKYI
     GGMKESSLKK SAMKQIILGS YDMASEGLDI EGLNVVILGT PKTSIKQSVG RILRKEVYEE
     HPIVIDIVDV DNDTFKKQSK SRNNYFQKQK YNIQKYYISE SLKQKYELWN DKEYIKKVLV
     EIPEIPDKQT QDMIKTNPNP KKKYQGPINI DELNFLEDD
 
 
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