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H962L_ASFB7
ID   H962L_ASFB7             Reviewed;         962 AA.
AC   Q89443;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative RNA helicase B962L;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Ba71V-072; ORFNames=B962L;
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 [GENOMIC DNA].
RX   PubMed=8262374; DOI=10.1016/0378-1119(93)90090-p;
RA   Yanez R.J., Rodriguez J.M., Boursnell M.E., Rodriguez J.F., Vinuela E.;
RT   "Two putative African swine fever virus helicases similar to yeast 'DEAH'
RT   pre-mRNA processing proteins and vaccinia virus ATPases D11L and D6R.";
RL   Gene 134:161-174(1993).
RN   [2]
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   [3]
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).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
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:0000269|PubMed:30185597}.
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; L10062; AAA42698.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65302.1; -; Genomic_DNA.
DR   PIR; JT0669; JT0669.
DR   RefSeq; NP_042766.1; NC_001659.2.
DR   SMR; Q89443; -.
DR   GeneID; 22220302; -.
DR   KEGG; vg:22220302; -.
DR   Proteomes; UP000000624; 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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Host membrane; Hydrolase; Late protein; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Virion.
FT   CHAIN           1..962
FT                   /note="Putative RNA helicase B962L"
FT                   /id="PRO_0000373102"
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   962 AA;  109630 MW;  EDA8F0CD02F3D2AC CRC64;
     MGKPTLLEPG HLYNVPAEHK NDVPIHYIIT WIKQRLPEFG GAIPTSLADR VLIIKSRTGS
     GKSTALPVHV FRILRNENTH SFQKYLGRSV ICTQPRVLTA VTLAKDIGAS THYPDMILGQ
     TVGYHTKPLT EKPNRGLIYA TAGVLLAQLH TMTDDEIASR YAFMIIDEAH ERALGIDLML
     MYIKSMLQRM LQRGSIGALR IPFVILTSAT IDTHKYSTYF GIGKENIILV EGRQYGVETH
     WPLYNTNNYI KTACETALTI HKENIHDRPT EADILIFMPG MAEIRFLSML LNNANMDLAK
     EKLPLMLILP IDSEAIAQEN EAYLGLKAEI KNLWVKNPLT AKVEKPLRRV IVSTVVAETG
     LTIETLKYVI DPGWNRSIET YYPEWAGGLI TRPAAQSRIE QRKGRVGRVF PGHFYPLYTK
     HVFEQIPAQQ YPEIITEGPG AIFLSIVVET IKKNKEGVFK AEEIDMLDPP PTDALASAIE
     RAIVAGLLTR GEKGLQLTQL GDIASRFSFL SIEEARMCFS GYFWQAAISD IATILAVVSV
     ADKKLTNLLD SKQRNGAMLA EAVLAGIPPF LQNIDNAYTN IHLLLADDLL EGLFIFEGFQ
     HAIVYFINNK VNNVAKHLRE WCEKKMLKYS SMVQILARRE DILNELAIVG LNPFHQWQNR
     LASANAETFL KRVCTLKQCM YEAYRLNCFC YDKHRLLYTG RNGIHFSYHD AVIKNPSCIV
     TPRIMLSPVS KQYMEWRLEP SFVSVLDGFV NVDINFLSPR QEIPNILGGV EDEEEEPPLP
     IQVFLHKYVK THFHFSGKSF KELKMKPSQM IKFPETTLIN MIPDIPKNVV QTYLEINVCH
     QYSFKRLIYC ETFYTDMDDV QHENSVELIG LPMAAHHLTI NDFNKLYHLL KPDGFLIVYD
     LHKGQEAFWL HSLQDALGHH TIRRDMDFHT IPEWETIFKE CGFTPIFSKQ PSEHELFIVF
     KK
 
 
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