VF509_ASFM2
ID VF509_ASFM2 Reviewed; 509 AA.
AC Q89576;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Putative ATP-dependent RNA helicase QP509L;
DE EC=3.6.4.13;
GN OrderedLocusNames=Mal-131; ORFNames=j11L;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8376971; DOI=10.1099/0022-1317-74-9-1969;
RA Baylis S.A., Twigg S.R.F., Vydelingum S., Dixon L.K., Smith G.L.;
RT "Three African swine fever virus genes encoding proteins with homology to
RT putative helicases of vaccinia virus.";
RL J. Gen. Virol. 74:1969-1974(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; X71982; CAA50831.1; -; Genomic_DNA.
DR EMBL; X72953; CAA51458.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JQ2211; JQ2211.
DR Proteomes; UP000000860; 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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Late protein; Nucleotide-binding.
FT CHAIN 1..509
FT /note="Putative ATP-dependent RNA helicase QP509L"
FT /id="PRO_0000373113"
FT DOMAIN 110..262
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 215..218
FT /note="DEAH box"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 509 AA; 58109 MW; 2F21873F9A3C5435 CRC64;
MEAILSFAGI GINYKKLQSK LQHDFGRFLK ALTITARALP GQPKHIAIRQ ETAFTLQGEY
IYFPILLRKQ FEMFNIVYTA HPVSLRTLPC VETEFPLFNY QQEMVDKIHK KLLPPYGRFY
LHLNTGLGKT RIAISIIQKL LYPTLVIVPT KAIQIQWIDE LTLLLPHLRV AAYNNAACKK
KDITSKEYDV IVGIINTLRK KPEAFFEPFG LVVLDEAHEL HSPENYKIFW KIQLSRILGL
SATPLDRPDG MDKIIIHHLG QPQRTVSPTT TFSGYVREIE YQGHPDFVKP VCINEKVSAI
ATIDKLLQDP SRIQLVVNET KRLYSLHTAE PQKWGTNEPY GIIIFVEFRK LLEIFYQALS
KEFKDVEIIV PEVALLCGGV SNTALSQAHS ASIILLTYGY GRRGISFKHM TSIIMATPRR
NNMEQILGRI TRQGSDEKKV RIVVDIKDTL SPLSSQVYDR HRIYKKKGYP IFKCSASYQQ
PYSSNEVLIW DPYNESCLAS TTTPPSPSK