ID D9MXA9_WNV Unreviewed; 511 AA.
AC D9MXA9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS West Nile virus (WNV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus nilense.
OX NCBI_TaxID=11082 {ECO:0000313|EMBL:ADK20367.1};
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=8495; Alligator.
OH NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH NCBI_TaxID=8782; Aves (birds).
OH NCBI_TaxID=53527; Culex.
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=34627; Hyalomma marginatum.
OH NCBI_TaxID=308735; Mansonia uniformis.
OH NCBI_TaxID=308737; Mimomyia.
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=34630; Rhipicephalus.
OH NCBI_TaxID=34861; Sciurus niger (Eastern fox squirrel).
RN [1] {ECO:0000313|EMBL:ADK20367.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3766 {ECO:0000313|EMBL:ADK20367.1};
RX PubMed=20579348;
RA Christofferson R.C., Roy A.F., Mores C.N.;
RT "Factors associated with mosquito pool positivity and the characterization
RT of the West Nile viruses found within Louisiana during 2007.";
RL Virol. J. 7:139-139(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
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DR EMBL; HM538811; ADK20367.1; -; Genomic_RNA.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
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:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd17931; DEXHc_viral_Ns3; 1.
DR CDD; cd18806; SF2_C_viral; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..148
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 159..324
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADK20367.1"
FT NON_TER 511
FT /evidence="ECO:0000313|EMBL:ADK20367.1"
SQ SEQUENCE 511 AA; 57407 MW; 95FC9C670AC8D9B0 CRC64;
TVLDLHPGAG KTRRILPQII KEAINRRLRT AVLAPTRVVA AEMAEALRGL PIRYQTSAVP
REHNGNEIVD VMCHATLTHR LMSPHRVPNY NLFVMDEAHF TDPASIAARG YISTKVELGE
AAAIFMTATP PGTSDPFPES NSPISDLQTE IPDRAWNSGY EWITEYTGKT VWFVPSVKMG
NEIALCLQRA GKKVVQLNRK SYETEYPKCK NDDWDFVITT DISEMGANFK ASRVIDSRKS
VKPTIITEGE GRVILGEPSA VTAASAAQRR GRIGRNPSQV GDEYCYGGHT NEDDSNFAHW
TEARIMLDNI NMPNGLIAQF YQPEREKVYT MDGEYRLRGE ERKNFLELLR TADLPVWLAY
KVAAAGVSYH DRRWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWIDA RVYSDHQALK
AFKDFASGKR SQIGLIEVLG KMPEHFMGKT WEAFDTMYVV ATAEKGGRAH RMALEELPDA
LQTIALIALL SVMTMGVFFL LMQRKGIGKI G
//