ID   YL364_MIMIV             Reviewed;         536 AA.
AC   Q5UR22;
DT   25-JUL-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 L364;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=MIMI_L364;
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   -!- 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; AAV50633.1; -; Genomic_DNA.
DR   RefSeq; YP_003986868.1; NC_014649.1.
DR   SMR; Q5UR22; -.
DR   GeneID; 9924984; -.
DR   KEGG; vg:9924984; -.
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; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..536
FT                   /note="Putative ATP-dependent RNA helicase L364"
FT                   /id="PRO_0000247296"
FT   DOMAIN          47..214
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          338..486
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          502..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          288..334
FT                   /evidence="ECO:0000255"
FT   MOTIF           160..163
FT                   /note="DEAH box"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   536 AA;  61776 MW;  4BC1A367D4AA70CC CRC64;
     MDITASFLQD LVENKKAVPK IFSKTTLSNE TSAKLFPYQK NHVLNLISIL LKYFLVLDTS
     DTGVGKTYMA AAACRELGRK PIIVCPKTLI PNWASVLEFY GVKYYDIVNY ETLKNEKTYK
     DSNFRVRKRC PYIKKVDNDG DYLKPAFEWK VPRNAIIIFD ESHRCKDPST ENGKLLMSSK
     QLIQQNIPVM LLSATICESY SDMKIPFYLM NFIPHTRNFN EFVRTLKTKY PEYRVRNRQL
     DQAERKIAVE NAQTLIIFKE IKEYTSRIRI RDLGNQFPDN QWCAQQFLSD DSDKIAEAYE
     EIAELMRELE EKKTQCKNHL AKIQKLKQEI ELRKIPIFIE QTQLYLEQGK SVIIFVNYIN
     TMNILSAQLN IKCRICGDQT QDQRQESIAL FQANIEKIII CQIRAGGVGI SLHDLHGGHP
     RVTLLNFPDS ASDLLQALGR APRSGAKSPV LQRIILVANV EYEKNIMRSI NKKLANISAI
     NDGDLEGHKY QVNEGRRRQR RVLNEPVNNP IEEPVNDPVK DPVEDLTDNQ PNIVEV