YR563_MIMIV
ID YR563_MIMIV Reviewed; 573 AA.
AC Q7T6X3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Putative ATP-dependent RNA helicase R563;
DE EC=3.6.4.13;
GN OrderedLocusNames=MIMI_R563;
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; AAQ09587.2; -; Genomic_DNA.
DR RefSeq; YP_003987078.1; NC_014649.1.
DR SMR; Q7T6X3; -.
DR PRIDE; Q7T6X3; -.
DR GeneID; 9925199; -.
DR KEGG; vg:9925199; -.
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; 1.
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..573
FT /note="Putative ATP-dependent RNA helicase R563"
FT /id="PRO_0000244775"
FT DOMAIN 57..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 374..551
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 179..182
FT /note="DEAH box"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 573 AA; 66973 MW; 3FD7AF2FF32A06DD CRC64;
MSSRLSYVNV DDPNFYEFID EKYSKYKIPP KQKTFKQFCF PSKYEFQIPQ QFLAEYINPK
TPYKGLLIYH RIGAGKTCTA IKIAENFKNK SKIMIVVPAS LKGNFRSELR SLCADDHYLT
SKERSELKIL HPSSDEYKSI IKVSDDRIDK YYTIYSYNKF VDLIKQNKIN LTNTLLIIDE
VHNMISETGT YYESLYETIH SAPDNMRLVI MTATPIFDKP NEIALTMNLL VRNKQLPVGP
DFVSTFMDIR YNSKGPVYHV KNMDLFKEFV KGYVSYYRGA PPYVFPKSEL FFVRTKMSDL
QKTVYQKITG KEVKQTKVRD YVNENISNNF FIGTRMISNI VYPNEKVGLK GYNSLTDEDL
TIAKIREYSP KFLKILRKIK RCNGTVFVYS NFKEYGGIRV FARLLEFHRF KNYEFNGSGP
RRFAIWSGDQ DPIYKEEVKA VFNNKDNEFG SKIKVILGSS SIKEGVSFLR VQEVHIMEPY
WNFSRMEQII GRAIRFCSHK DVELDRQLVK VYIYLAVHPD IKMSIDERMM KMALDKKMIN
SAFEKALKEA AIDCELFKNA NVYPGEQDIQ CEQ