ID   VF509_ASFK5             Reviewed;         509 AA.
AC   P0C9B0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative ATP-dependent RNA helicase QP509L;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Ken-135;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561445;
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 [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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PRIDE; P0C9B0; -.
DR   Proteomes; UP000000861; 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_0000373116"
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;  58120 MW;  F286DF7FF2BBFEED CRC64;
     MEAIISFAGI GINYKKLQSK LQHDVGRFLR ALTITARALP GQPKHIAIRQ ETAFTLQGEY
     IYFPILLRKQ FEMFNMVYTA HPVSLRALPC VETEFPLFNY QQEMVDKIHK KLLSPYGRFY
     LHLNTGLGKT RIAISIIQKL LYPTLVIVPT KAIQIQWIDE LKLLLPHLRV AAYNNAACKK
     KDITSKEYDV IVGIINTLRK KPEPFFEPFG LVVLDEAHEL HSPENYKIFW KIQLSRILGL
     SATPLDRPDG MDKIILHHLG QPQRTVSPTT TFSGYVREIE YQGHPDFVKP VCINEKVSAI
     ATIDKLLQDP SRIQLVVNET KRLYSLHTAE PQKWGTNEPY GIIIFVEFRK LLEIFYQALS
     EEFKDVQIIV PEVALLCGGV SNTALSQAHS ASIILLTYGY GRRGISFKHM TSIIMATPRR
     NNMEQILGRI TRQGSDEKKV RIVVDIKDTL SPLSSQVYDR HRIYKKKGYP IFKCSASYQQ
     PYSSNEVLIW DPYNESCLAS TTTPPSPSK