ID   VF509_ASFB7             Reviewed;         509 AA.
AC   Q65191;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative ATP-dependent RNA helicase QP509L;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Ba71V-123; ORFNames=QP509L;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [2]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
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:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U18466; AAA65351.1; -; Genomic_DNA.
DR   RefSeq; NP_042815.1; NC_001659.2.
DR   GeneID; 22220352; -.
DR   KEGG; vg:22220352; -.
DR   Proteomes; UP000000624; 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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Late protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..509
FT                   /note="Putative ATP-dependent RNA helicase QP509L"
FT                   /id="PRO_0000373112"
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;  58103 MW;  4EC0E6D811A04A3C CRC64;
     MEAIISFAGI GINYKKLQSK LQHDFGRLLK ALTVTARALP GQPKHIAIRQ ETAFTLQGEY
     IYFPILLRKQ FEMFNMVYTT RPVSLRALPC VETEFPLFNY QQEMVDKIHK KLLSPYGRFY
     LHLNTGLGKT RIAISIIQKL LYPTLVIVPT KAIQIQWIDE LTLLLPHLRV AAYNNAACKK
     KDMTSKEYDV IVGIINTLRK KPEQFFEPFG LVVLDEAHEL HSPENYKIFW KIQLSRILGL
     SATPLDRPDG MDKIIIHHLG QPQRTVSPTT TFSGYVREIE YQGHPDFVSP VCINEKVSAI
     ATIDKLLQDP SRIQLVVNEA KRLYSLHTAE PHKWGTDEPY GIIIFVEFRK LLEIFYQALS
     KEFKDVQIVV PEVALLCGGV SNTALSQAHS ASIILLTYGY GRRGISFKHM TSIIMATPRR
     NNMEQILGRI TRQGSDEKKV RIVVDIKDTL SPLSSQVYDR HRIYKKKGYP IFKCSASYQQ
     PYSSNEVLIW DPYNESCLAC TTTPPSPSK