YL377_MIMIV
ID YL377_MIMIV Reviewed; 1147 AA.
AC Q5UQW0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Putative ATP-dependent RNA helicase L377;
DE EC=3.6.4.13;
GN OrderedLocusNames=MIMI_L377;
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).
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; AAV50646.1; -; Genomic_DNA.
DR PRIDE; Q5UQW0; -.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW Virion.
FT CHAIN 1..1147
FT /note="Putative ATP-dependent RNA helicase L377"
FT /id="PRO_0000253411"
FT DOMAIN 108..315
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 264..267
FT /note="DEAH box"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1147 AA; 133977 MW; 60DD5132F76A005A CRC64;
MKIMEDQINP INIRKQKDLD DNLEEITSEN SEIAPADIEK KMLENHAYPS PTQEDFQRAI
YVKRDFYIHS IPERKVLNTY DEIKEFRDNK CAGNFKLTES QTLLSNFINP NTPYRGLLMF
WGTGVGKSCG AIAIAEKFKH MVEKYGTKIH VLVPGPINKQ NFLNEIIKCT GETYTKMFQD
KTIVINEAEK NRIRKNALNV VNQYYRIMSY RSFYKKVLGE KIRDKVVTGN KVKLTSRKTE
TGEFERDISI DRIYSLDNTL LIVDEAHNIT GNGEGDAVKK IIDVSKNLKV VFLSATPMKN
LADSIVELIN YLRPKNYQME RDKIFTSQRG SEMDFKPGGR DYLRKMVRGY VSYLRGADPL
TFAERVDIGE IPPGLDFTKV TRCFMLPFQL GVYDNVIATQ DDSLDRNSEA VANFVFPGLS
KDRNSKNIEG YYGIKGMNEI RNQILNNSET LNRRIASTIL SEYEIEDPSN LMYLTDNNSV
ISGNIFNEKY LKHFSIKFYS ALQKINETVY GKRNSGLIFI YLNLVRVGIS IFQEVLLMNG
YLEYQENTNN YNLKRDTRCY FCDHKYGDHY NLPDDIPKHD FYPATFITVT GKSEEDIEQI
PEEKHRILNN VFNNVNNREG KYLKIVIGSR VMNEGITLRN IKEIYILDVH FNLGKVDQAI
GRGIRFCTHY GITNEKDPFP KVEVNKYVVS VKNGLSTEEQ LYKKAESKYK LIKQVERILQ
EEAIDCPLNR NGNIFPEEMK RYANCGTKDN PCPAICGYMP CEFKCGDKLL NAKYYDPDRA
VYKKITKSEL DYSTYNNALA SDEIDYSKAK IKEMYKLDFI YTLKDILRYV KKSYPVEKRE
MFDDFYVYQA LNDLIPITGN DFNNFHDTIA DKYNRPGYLI YINTYYIFQP FDENENIPMY
YRRIFTPPTI NKINVKDYIK NTPEYRQHKN LYQLDEEGPI DREYDFDSVQ DYYDSRDEFD
YVGIIDRESS KRKNGTNSSG DEFKIRRKRP KILSKKRETG IPSFLGAVCS TSKDKKYLAS
IMKKLNLDEN KSDSRMDICD RIKNKLFDLE KYSTNNMTYL IIPSNHPHIP FPLNLKDRVQ
YIIDQIKRET RSSINPEIKT IKTTGEFNDI DYIYYELYYD SSMDKYQDIL TLYGAKKINN
DWIIIIK