ID   YR458_MIMIV             Reviewed;         524 AA.
AC   Q5UQD1;
DT   13-SEP-2005, 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 R458;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=MIMI_R458;
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: Putative ATP-dependent RNA helicase.
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. eIF4A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAV50724.1; -; Genomic_DNA.
DR   RefSeq; YP_003986965.1; NC_014649.1.
DR   SMR; Q5UQD1; -.
DR   PRIDE; Q5UQD1; -.
DR   GeneID; 9925083; -.
DR   KEGG; vg:9925083; -.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..524
FT                   /note="Putative ATP-dependent RNA helicase R458"
FT                   /id="PRO_0000054969"
FT   DOMAIN          125..338
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          373..524
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           268..271
FT                   /note="DEFD box"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   524 AA;  59563 MW;  F1B65C037BD75A22 CRC64;
     MNSDQENINS YNFESIKIGD YKCNVNRIPG DNLYLLSNFN DAEPKYDDKN GVHLEFNYKK
     IGESKTMRLN DGATSTVLIE GARNMNANEY FPKFVEKKKS FAEHLIRKTF AKGYESPSEI
     QALVVPELIQ RKDTLIQFKS GTGKTHAFLF GCLWGFDPDD DVLQYIFITS SHEVATQIYE
     QAVFLLPETA KIALCIGQKK SPNSFGNSGF KTPIGTSSLN HKPKSIKEER EEIRQAQIII
     CTMGRFYDIL CNKGWITTTR YLKAICVDEF DNIVASKTKQ RSSTVMNTED QMAEIIQKIE
     SEAPKNSENG AQRVFFSATV SPYAIKIANS YFRKYSPIIG EPFIVLLDSE DYTLEGIRQY
     YVQCSNYFEK KEIILDLLKQ CRIAQAIIFA NRIETANEIK KLLDEQEVPI SSAVFHGDLP
     AVTRKNIHKD FVENKIRLLI STDLTSRGLD VQGINVVFNF DMPDTLETYI HRVGRSGRYG
     RKGVSISLIL VNQNKNEMEK VEQIDNCSKQ SKMSQLPGDL STLL