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Database: UniProt
Entry: H962L_ASFP4
LinkDB: H962L_ASFP4
Original site: H962L_ASFP4 
ID   H962L_ASFP4             Reviewed;         962 AA.
AC   P0C9A2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Putative RNA Helicase B962L;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Pret-084;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus.
OX   NCBI_TaxID=561443;
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; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9A2; -.
DR   Proteomes; UP000000859; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044423; C:virion component; 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   CDD; cd17917; DEXHc_RHA-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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; Late protein; Membrane;
KW   Nucleotide-binding; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..962
FT                   /note="Putative RNA Helicase B962L"
FT                   /id="PRO_0000373104"
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;  109582 MW;  024D5DA7390B2961 CRC64;
     MGKPTLLEPG HLYNVPAEHK NDVPIHYIIT WIKQRLPEFG GAIPTSLADR VLIIKSRTGS
     GKSTALPVHV FRILRNENTH SFQKYLGRSV ICTQPRVLTA VTLAKDIGAS THYPDMILGQ
     TVGYQTKPLT EKPNRGLIYA TAGVLLAQLH TMTDDEIASR YAFMIIDEAH ERALGIDLML
     MYIKSMLERM 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 YDEHRLLYTG RNGIHFSYHD AVIKNPSCIV
     TPRIMLSPVS KQYMEWRLEP SFVSVLDGFV NVDINFLLPR QEIPNILGGA EDEEEEPPLP
     IQVFLHKYVK THFHFSGKSF KELKMKPGQT IKFPETTLIN MIPDIPKNVV QTYLEISVCH
     QYSFKRLIYC ETFYTDMDDV QHENSVELIG LPMAAHHLTI NDFNKLYHLL KPDGFLMVYD
     LHQSQEAFWL HSLQDALGHH TIRRDMDFHT IPEWETIFKE CGFTPIFSKQ PSEHELFIVF
     KK
//
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