ID   H962L_ASFK5             Reviewed;         963 AA.
AC   P0C9A4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Putative RNA Helicase B962L;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Ken-084;
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   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Virion {ECO:0000250|UniProtKB:Q89443}.
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9A4; -.
DR   Proteomes; UP000000861; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Host membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..963
FT                   /note="Putative RNA Helicase B962L"
FT                   /id="PRO_0000373106"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..229
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          253..459
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           167..170
FT                   /note="DEAH box"
FT   BINDING         56..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   963 AA;  109849 MW;  576F6EC8B7EAED4D CRC64;
     MGKPTLLEPG HLYNVPAEHK NDIPIHYIIT WIKQRLPEFG GSIPTSLADR VLIIKSRTGS
     GKSTALPVHV FRILRNENTH SFQKYLGRSV ICTQPRVLTA VTLAKDIGAS THYPDMILGQ
     TVGYQTKPLT EKPNRGLIYA TAGVLLAQLH TMTDDEIASR YAFMIIDEAH ERALGIDLML
     MYIKSMLERM LQRGSIGALR IPFVILTSAT IDTYKYSTYF GIGKENIILV EGRQFGVETH
     WPLYNTNNYI KTACETALTI HKENIHDRPT EADILIFMPG MGEIRFLSML LSHANMDLAK
     EKLPLMLILP IDSEAIAQEN EAYLGLKAEI KDLWVKNPLT AKVEKPLRRV IVSTVVAETG
     LTIETLKYVI DPGWNRSVET YYPEWAGGLI TRPAAQSRIE QRKGRVGRVF PGHFYPLYTK
     HVFEQIPAQQ YPEIITEGPG AIFLNIVVET IKKNKEGVFK VQEIDMLDPP PTDALASALE
     RAIVGGLLTR GEKGLQLTQL GDIASRFSFL SIEEARMCFS GYFWQAAISD IATILAVVSV
     VDKKLTNLLD SKQRNGAMLA EAVLAGIPPF LQNMDNAYSN IHLLLADDLL EGLFIFEGFQ
     HAIIYFINNK VNNLAKHLRE WCEKKMLKYS AMVQILARRE DILNELAVVG LNPFHQWQNR
     LASANAETFL KRVCTLKQCF YEAYRLNCFC YDEQRLLYTG RNGIHFSYQD TVIKNPSCIV
     TPKMMLSPVS KQYMEWRLEP SFVSVLDGFV NVDINFLLPR QEIPNILGGG VEDEEEEPPL
     PIQAFLHKYV KTNFHFSGKS FKELKMKPHQ TIKFPETTLI NIIPDIPKNV VQTYLEISVC
     HQYSFKRLIY CETFYTDMDD VQQENSVELI GLPMAAHHLT MHDFNKLYQL LKPDGFLIVY
     DFHKSQEAFW LHSLQDALGH HTIRRDMDFH TISEWETIFK ECGFTPMFNK QPSEHELFIV
     FKK