YL540_MIMIV
ID YL540_MIMIV Reviewed; 695 AA.
AC Q5UQ96;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Putative ATP-dependent RNA helicase L540;
DE EC=3.6.4.13;
GN OrderedLocusNames=MIMI_L540;
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; AAV50804.1; -; Genomic_DNA.
DR RefSeq; YP_003987055.1; NC_014649.1.
DR SMR; Q5UQ96; -.
DR GeneID; 9925174; -.
DR KEGG; vg:9925174; -.
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; IPR007502; Helicase-assoc_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; PF04408; HA2; 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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW Virion.
FT CHAIN 1..695
FT /note="Putative ATP-dependent RNA helicase L540"
FT /id="PRO_0000247281"
FT DOMAIN 53..219
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 247..434
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 164..167
FT /note="DEAH box"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 695 AA; 79556 MW; 12A49B7C1F544616 CRC64;
MASNLTFEDK IGILDPKGLR PNPLNNEPYS DDYKKLAMVW STYPAYSAAD RVLSALENYQ
LVFVTSSTGS GKSVLIPKLA LHYTNYNGRV VMTLPKRIIT LSAAIFSAKV SDVKLGESIG
YAYKGSDKSM YNDQNKIIYV TDGIFVMEYV RDPLLSKFNV VIIDEAHERR IQIDLILLFL
RTLLQSGNRP DLKVIIMSAT IDTDKYQKYF NSVDSTVIDI AGQPNHPIET HFMDKPVTSY
MKEGLELIED LIHQQIKKDM LFFITTSNEA LQLCRSIRPQ YPRVYCVEVY SDMDKNLKQY
AESRDKYLEL GNYDQKLVMA TNVAESSLTI DGLVYVIDSG YELSSRFDPE CYGQILEKKF
VSKAQALQRR GRVGRTEPGV CYHLLTKQQF DGLADYPTPD ILRQDITMDL IKIIQVSPNK
TYAEGINMMN QLMDPPLRSH INATRNLFDL YNVVDDNGIL TQVGIVATQF SSLPLNRILF
LIYAFELQCA REASIIVAMT EFLNGRVTNL FYKSDTICES NCEKQAANLL LEKLIQKRGD
HFTYLKIYQE FSKSTDQKSW ARKYGVRLDT INNIERTANQ YFYRILNLLR KPRLPNNKNT
LIDTSIDTPM DIQSRISSTD TKTNLLNALK KSHQHLTASK LKPTYSKENI TGKISRDSVL
NQIYKKNEIS KKKIIYDELS NINGKWEFRT VTIIS