ID   H962L_ASFM2             Reviewed;         963 AA.
AC   Q8V9U2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative RNA Helicase B962L;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Mal-080; ORFNames=L09CL;
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].
RA   Roberts P.C., Lu Z., Rock D.L.;
RT   "Nucleotide sequence and analysis of 16.25 kilobase pairs of the African
RT   swine fever virus genome that span the central variable region.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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; L00966; AAL31320.1; -; Genomic_DNA.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; Q8V9U2; -.
DR   Proteomes; UP000000860; 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_0000373103"
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;  109832 MW;  C1137DAB22E2810F CRC64;
     MGKPTLLEPG HLYNVPAEHK NDIPIHYIIT WIKQRLPEFG GAIPTSLADR VLIIKSRTGS
     GKSTALPVHV FRILRNENTH SFQKYLGRSV ICTQPRVLTA VTLAKDIGAS THYPDMILGQ
     TVGYQTKPLT EKPNRGLIYA TAGVLLAQLH TMTDDEIASR YAFMIIDEAH ERALGIDLML
     MYIKSMLERM LQRGSIGALR IPFVILTSAT IDTHKYSTYF GIGKENIILV EGRQFGVETH
     WPLYNTNNYI KTACETALTI HKENIHDRPT EADILIFMPG MGEIRFLSTL LNNANMDLAK
     EKLPLMLILP IDSEAIAQEN EAYLGLKAEI KNLWVKNPLT AKVEKPLRRV IVSTVVAETG
     LTIETLKYVI DPGWNRSVET YYPEWAGGLI TRPAAQSRIE QRKGRVGRVF PGHFYPLYTK
     HVFEQIPAQQ YPEIITEGPG AIFLNIVVET IKKNKEGVFK AEEIDMLDPP PTDALASAIE
     RAIVGGLLTR GEKGLQLTQL GDIASRFSFL SIEEARMCFS GYFWQAAISD IAIILAVVSV
     VDKKLTNLLD SKQRNGAMLA EAVLAGIPPF LQHIDNAYTN IHLLLADDLL EGLFIFEGFQ
     HAIVYFINNK VNNLAKHLRE WCEKKMLKYS SMVQILARRE DILNELAIVG LNPFHQWQNR
     LASANAETFL KRVCTLKQCI YEAYRLNCFC YDEHRLLYTG RNGIHFSYHD TVIKNPSCIV
     TPRIMLAPVS KQYMEWRLEP SFVSVLDGFV NMDINFLLPR QEIPNILGGV EDEEEEEPPL
     PIQVFLHNYV KTHFHFSGKS FKELKMKPSQ MIKFPETTLI NMIPDIPKNV VQTYLEINVC
     HQYSFKRLIY CETFYTNMDD VQHENAVELI GLPMAAHHLT INDFNKLYRV LKPDGFLIVY
     DLHNSQEAYW LHSLQDALGH HTIRRDMDFH TITEWETIFK ECGFSPIFSK QPSEHELFIV
     FKK