ID Q66472_9FLAV Unreviewed; 143 AA.
AC Q66472;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Nonstructural protein NS3 {ECO:0000313|EMBL:AAB03620.1};
DE Flags: Fragment;
OS dengue virus type 2.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus denguei;
OC Dengue virus.
OX NCBI_TaxID=11060 {ECO:0000313|EMBL:AAB03620.1};
RN [1] {ECO:0000313|EMBL:AAB03620.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9017828; DOI=10.1016/S0923-2516(97)81907-3;
RA Chow V.T., Yong R., Chan Y.C.;
RT "Sequence analyses of NS3 genes of recent Pakistan and Singapore strains of
RT dengue virus types 1 and 2.";
RL Res. Virol. 148:17-20(1997).
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=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91; Evidence={ECO:0000256|ARBA:ARBA00024468};
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DR EMBL; U60587; AAB03620.1; -; mRNA.
DR SMR; Q66472; -.
DR MEROPS; S07.001; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; 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 Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR001850; Flavi_NS3_S7.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 1..40
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAB03620.1"
FT NON_TER 143
FT /evidence="ECO:0000313|EMBL:AAB03620.1"
SQ SEQUENCE 143 AA; 15995 MW; F96A53333F2FAAD3 CRC64;
IVDKKGKVVG LYGNGVVTRS GTYVSAIAQT EKSIEDNPEI EDDIFRKKRL TIMDLHPGAG
KTKRYLPAIV REAIKRGLRT LILAPTRVVA AEMEEALRGL PIRYQTPAIR AEHTGREIVD
LMCHATFTMR LLSPVRVPNY NLI
//
