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Database: UniProt
Entry: B6VDH8_9FLAV
LinkDB: B6VDH8_9FLAV
Original site: B6VDH8_9FLAV 
ID   B6VDH8_9FLAV            Unreviewed;        87 AA.
AC   B6VDH8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Nonstructural protein 3 {ECO:0000313|EMBL:ACJ06081.1};
DE   Flags: Fragment;
OS   dengue virus type 3.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus denguei;
OC   Dengue virus.
OX   NCBI_TaxID=11069 {ECO:0000313|EMBL:ACJ06081.1};
RN   [1] {ECO:0000313|EMBL:ACJ06081.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=28D3/06 {ECO:0000313|EMBL:ACJ06081.1};
RA   Kukreti H., Chaudhary A., Mittal V., Lal S., Rai A.;
RT   "Correlation of NS3 gene sequences of Dengue virus type 3 with clinical
RT   disease severity.";
RL   Submitted (OCT-2008) 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         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; FJ375678; ACJ06081.1; -; Genomic_RNA.
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   Pfam; PF00949; Peptidase_S7; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PE   4: Predicted;
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..45
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000259|PROSITE:PS51528"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACJ06081.1"
FT   NON_TER         87
FT                   /evidence="ECO:0000313|EMBL:ACJ06081.1"
SQ   SEQUENCE   87 AA;  9494 MW;  D037339FF1F4F218 CRC64;
     TSGSPIINRE GKVVGLYGNG VVTKNGGYVS GIAQTNAEPD GPTPELEEEM FKKRNLTIMD
     LHPGSGKTRK YLPAIVREAI KRRLRTL
//
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