A0A7S9SKG3 · A0A7S9SKG3_9FLAV
- ProteinGenome polyprotein
- GenePOLY
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3390 (go to sequence)
- Protein existencePredicted
- Annotation score5/5
Function
function
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.
Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.
Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between RIGI and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles.
Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1524 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: H | ||||||
Active site | 1548 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: D | ||||||
Active site | 1608 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: S | ||||||
Binding site | 2546 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 2576 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 2577 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 2594 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 2595 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2621 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2622 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 2708 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 2927 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2931 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2936 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2939 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3202 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 3218 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3337 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus denguei > Dengue virus
Accessions
- Primary accessionA0A7S9SKG3
Subcellular Location
UniProt Annotation
GO Annotation
Host endoplasmic reticulum membrane ; Multi-pass membrane protein
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Virion membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 46-69 | Helical | ||||
Sequence: LVMAFIAFLRFLAIPPTAGVLARW | ||||||
Transmembrane | 247-272 | Helical | ||||
Sequence: FTILALFLAHYIGTSLTQKVVIFILL | ||||||
Transmembrane | 722-746 | Helical | ||||
Sequence: YTALFSGVSWVMKIGIGVLLTWIGL | ||||||
Transmembrane | 752-771 | Helical | ||||
Sequence: SMSFSCIAIGIITLYLGAVV | ||||||
Transmembrane | 1157-1175 | Helical | ||||
Sequence: MIAGVFFTFMLLLLGQITW | ||||||
Transmembrane | 1195-1218 | Helical | ||||
Sequence: MGVTYLALIATFKIQPFLALGFFL | ||||||
Transmembrane | 1316-1334 | Helical | ||||
Sequence: WLPMTVAAMGVPPLPLFIF | ||||||
Transmembrane | 1437-1464 | Helical | ||||
Sequence: ILTVLLKTALLIVSGIFPYSIPATLLVW | ||||||
Transmembrane | 2147-2166 | Helical | ||||
Sequence: LLLLGLMILLTGGAMLFLIS | ||||||
Transmembrane | 2173-2190 | Helical | ||||
Sequence: TSIGLICVIASSGMLWMA | ||||||
Transmembrane | 2196-2213 | Helical | ||||
Sequence: WIASAIVLEFFMMVLLIP | ||||||
Transmembrane | 2225-2242 | Helical | ||||
Sequence: QLAYVVIGILTLAAIIAA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 283↔310 | |||||
Sequence: CVGVGNRDFVEGLSGATWVDVVLEHGGC | ||||||
Disulfide bond | 340↔396 | |||||
Sequence: CIEGKITNITTDSRCPTQGEAVLPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTC | ||||||
Disulfide bond | 354↔385 | |||||
Sequence: CPTQGEAVLPEEQDQNYVCKHTYVDRGWGNGC | ||||||
Disulfide bond | 372↔401 | |||||
Sequence: CKHTYVDRGWGNGCGLFGKGSLVTCAKFQC | ||||||
Disulfide bond | 463↔563 | |||||
Sequence: CSPRTGLDFNEMILLIMKNKAWMVHRQWFFDLPLPWTSGATTETPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGHLKC | ||||||
Disulfide bond | 580↔611 | |||||
Sequence: CTNTFVLKKEVSETQHGTILIKVEYKGEDAPC |
Keywords
- PTM
Interaction
Subunit
Forms a heterodimer with serine protease NS3. May form homooligomers.
Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi.
Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1.
Interacts (via N-terminus) with serine protease NS3.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1344-1473 | Flavivirus NS2B | ||||
Sequence: SWPLNEGVMAVGLVSILASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTVLLKTALLIVSGIFPYSIPATLLVWHTWQKQTQR | ||||||
Domain | 1474-1651 | Peptidase S7 | ||||
Sequence: SGVLWDVPSPPETQKAELEEGVYRIKQQGILGKTQVGVGVQKEGVFHTMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGTFQTTTGEIGAIALDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPE | ||||||
Domain | 1654-1810 | Helicase ATP-binding | ||||
Sequence: EEMFKKRNLTIMDLHPGSGKTRKYLPAIVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEE | ||||||
Domain | 1805-1986 | Helicase C-terminal | ||||
Sequence: PIQDEEKDIPERSWNSGNEWITDFAGKTVWFVPSIKAGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGPMPVTVASAAQRRGRVGRNPQKENDQYIFTGXPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPE | ||||||
Domain | 2492-2753 | MRNA cap 0-1 NS5-type MT | ||||
Sequence: TGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGETTHHAVSRGSAKLQWFVERNMVIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGESSPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPAVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSSVNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRH | ||||||
Domain | 3017-3167 | RdRp catalytic | ||||
Sequence: GAMYADDTAGWDTRITEDDLHNEEKITQQMNPEHRLLANAIFKLTYQNKVVKVQRPTPTGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLVRQMEGEGVLSKADLENPHLPEKKIIQWLETKGVERLKRMAISGDDCVVKPIDDRFANA |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,390
- Mass (Da)377,938
- Last updated2021-06-02 v1
- ChecksumCFCE00AF58B04124