A0A0C4PNS1 · A0A0C4PNS1_9FLAV
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3427 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1551 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: H | ||||||
Active site | 1575 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: D | ||||||
Active site | 1635 | Charge relay system; for serine protease NS3 activity | ||||
Sequence: S | ||||||
Binding site | 2535 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2538 | GTP (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 2539 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 2541 | GTP (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 2546 | GTP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 2550 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 2578 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 2578 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 2608 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 2608 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 2609 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 2609 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 2626 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 2627 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2633 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2653 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2653 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2654 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 2654 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 2735 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 2737 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 2742 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 2962 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2966 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2971 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2974 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3239 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 3255 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3374 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Flasuviricetes > Amarillovirales > Flaviviridae > Orthoflavivirus > Orthoflavivirus ntayaense
Accessions
- Primary accessionA0A0C4PNS1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Peripheral membrane protein
Endoplasmic reticulum membrane ; Peripheral membrane protein
Host endoplasmic reticulum membrane ; Multi-pass membrane protein
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Host endoplasmic reticulum membrane ; Peripheral membrane protein
Membrane ; Multi-pass membrane protein
Membrane ; Peripheral membrane protein
Virion membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 742-763 | Helical | ||||
Sequence: LFGGMSWITQGLLGILMLWMGL | ||||||
Transmembrane | 770-790 | Helical | ||||
Sequence: ISITFLAVGGVLVFLATNVHA | ||||||
Transmembrane | 1178-1196 | Helical | ||||
Sequence: AMLMFLCALIFGGITYMDL | ||||||
Transmembrane | 1247-1263 | Helical | ||||
Sequence: VLVGIALSMLTLAMQDW | ||||||
Transmembrane | 1304-1325 | Helical | ||||
Sequence: LRIAGIDVVRIGLLIIGIMSLM | ||||||
Transmembrane | 1337-1363 | Helical | ||||
Sequence: GGLLIGLALAESGLISPLVYAGLTLAL | ||||||
Transmembrane | 1375-1393 | Helical | ||||
Sequence: EALTAVGLTFALAGGIAHF | ||||||
Transmembrane | 1399-1423 | Helical | ||||
Sequence: AIPLAVGGIMLVVAVVTGFTTDLWL | ||||||
Transmembrane | 2173-2191 | Helical | ||||
Sequence: ILLITMMALASCGVFLFFV | ||||||
Transmembrane | 2198-2216 | Helical | ||||
Sequence: KTGLGAMILMTATVLLWIA | ||||||
Transmembrane | 2222-2239 | Helical | ||||
Sequence: KIAGILLVSLLLMIVLIP | ||||||
Transmembrane | 2251-2268 | Helical | ||||
Sequence: HLAVFMIVVLLIVGAVAS | ||||||
Transmembrane | 2331-2350 | Helical | ||||
Sequence: YVNFSLMAVTAQAGALFGLG | ||||||
Transmembrane | 2362-2391 | Helical | ||||
Sequence: VPLLLLGCWGQFTMTSTLTTIVLLIVHYAF | ||||||
Transmembrane | 2440-2458 | Helical | ||||
Sequence: FGQVILIVVGVCAVFLKPG |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 292↔319 | |||||
Sequence: CLGMQNRDFVEGVNGVEWIDVVMEGGSC | ||||||
Disulfide bond | 349↔405 | |||||
Sequence: CYEPKITDVSTEPRCPTMGEAHNTKASSQDYVCKKGLTDRGWGNGCGLFGKGSIHTC | ||||||
Disulfide bond | 363↔394 | |||||
Sequence: CPTMGEAHNTKASSQDYVCKKGLTDRGWGNGC | ||||||
Disulfide bond | 381↔410 | |||||
Sequence: CKKGLTDRGWGNGCGLFGKGSIHTCAKFEC | ||||||
Disulfide bond | 479↔577 | |||||
Sequence: CEPRSGLDMSQFYVMTMNMKSWLVNRDWFHDLNLPWTGSAAGNWQNRESLVEFEEAHATKQSVVALASQEGALHAALAGAIPVKYTSSKLEMTSGHLKC | ||||||
Disulfide bond | 594↔625 | |||||
Sequence: CSNKFSLARNPTDTGHGTVVVKLSYAGSDGPC |
Keywords
- PTM
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1370-1500 | Flavivirus NS2B | ||||
Sequence: GWPVSEALTAVGLTFALAGGIAHFDEGNMAIPLAVGGIMLVVAVVTGFTTDLWLEKAGEMTWSEEAQITGSSQRYDVEIDSDGNMRLLNDPGIPFSVWALRTGLILLSAYNPYLLPVTLGAYWLTVKAPKR | ||||||
Domain | 1501-1678 | Peptidase S7 | ||||
Sequence: SGAIWDVPAPKERRKAEISTGVFRIMARGIFGKYQAGVGVMYEGVFHTMWHVTNGATIDVGDGCLVPYWASVREDLISYGGPWKLGKKWNGVDEVQVVVVQPGKPATNVQTKPGIFRTHAGEVGAVTLDYPTGTSGSPIIDKEGNIIGLYGNGILVGAGNFVSMISQGNRMEEEIPQV | ||||||
Domain | 1681-1837 | Helicase ATP-binding | ||||
Sequence: DDMLRKRQLTVLDLHPGSGKTRKVLPQIVKAAIEKRLRTAILAPTRVVAAEIAEALKEYPIRYLTPAVKREHTGTEIIDVMCHATLTARLLTPQRVPNYNLFVMDEAHFTDPASIAARGYISTKVDLGEAAAIFMTATPPGTRDAFPDSNSPIMDVE | ||||||
Domain | 1848-2013 | Helicase C-terminal | ||||
Sequence: GYDWITDYTGKTVWFVPSVKMGNEIAMCLTKAGKKVIQLNRKSFDNEYPKCKTGDWDFVVTTDISEMGANFGASRVIDSRKCIKPVIIEDGEGSVQLNGPVPITAASAAQRRGRVGRNPVQVGDEYHFAGPTSEDDHDFAHWKEAKILLDNINLPNGLVAQLYEPE | ||||||
Domain | 2523-2788 | MRNA cap 0-1 NS5-type MT | ||||
Sequence: GGGRGRMLGEMWKAQLNQLTRQEFMEYRRDGIIEVDRSAARKARREGNVTGGHPVSRGTAKLRWMVERGFVKPHGKVIDLGCGRGGWSYYCATLKLVQEVKGYTKGGPGHEEPVMMQSYGWNLVSLKSGVDVFYRPSEQSDTLLCDIGEASPVPEIEEARTVKVLQMVEEWLSRGVEDFCVKILCPYMPKVLKELEKMQLRWGGGLIRVPLSRNSNHEMYWVSGASGNITNSVNTVSQMLINRMNRTNRNGPKYEEDVHLGSGTRA | ||||||
Domain | 3052-3204 | RdRp catalytic | ||||
Sequence: GLMYADDTAGWDTRITKADLENESIVLEMMTPEHRALAEPLIKFAYMNKVVKVMRPGADGITVMDVISREDQRGSGQVVTYALNTFTNLCVQLIRCMEGEGLLKPEEVEKLERGKQRKIQDWLDKNGTERLASMAVSGDDCVVKPKDDRFATA |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,427
- Mass (Da)380,774
- Last updated2015-04-29 v1
- ChecksumE43988E0B7EEBA26
Keywords
- Technical term