UniProtKB - P26663 (POLG_HCVBK)
Genome polyprotein
Functioni
Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity).
Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (Probable). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity).
Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity).
Activates STAT3 leading to cellular transformation (By similarity).
Regulates the activity of cellular genes, including c-myc and c-fos (By similarity).
May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity).
Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity).
Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity).
Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity).
Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity).
Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).
By similarityCuratedForms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity).
Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity).
E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity).
APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity).
The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity).
E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity).
Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity).
By similarityForms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity).
Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity).
The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity).
This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (By similarity).
E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity).
APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity).
The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity).
E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity).
Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity).
Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity).
Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity).
These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity).
The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity).
By similarityIon channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity).
Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity).
Creates a pore in acidic organelles and releases Ca2+ and H+ in the cytoplasm of infected cells, leading to a productive viral infection (By similarity).
High levels of cytoplasmic Ca2+ may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity).
Targets also host mitochondria and induces mitochondrial depolarization (By similarity).
In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity).
By similarityCuratedCysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (Probable) (PubMed:11591719).
The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (PubMed:11591719).
Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity).
By similarity1 Publication1 PublicationDisplays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (PubMed:9614113).
NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity).
The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity).
The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity).
NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity).
Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity).
Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity).
Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity).
Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity).
By similarity1 PublicationPeptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity).
The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity).
The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity).
By similarityInduces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity).
This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity).
NS4B self-interaction contributes to its function in membranous web formation (By similarity).
Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3-mediated interferon signaling (By similarity).
Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity).
By similarityPhosphorylated protein that is indispensable for viral replication and assembly (By similarity).
Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity).
The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity).
Involved in RNA-binding and especially in binding to the viral genome (By similarity).
Zinc is essential for RNA-binding (By similarity).
Participates in the viral particle production as a result of its interaction with the viral mature core protein (By similarity).
Its interaction with host VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation (By similarity).
Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity).
Prevents BIN1-induced apoptosis (By similarity).
Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity).
Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity).
Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity).
By similarityRNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication.
By similarityMiscellaneous
Caution
Catalytic activityi
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphateBy similarityEC:3.6.1.15By similarity
- EC:3.6.4.13By similarity
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)PROSITE-ProRule annotation2 PublicationsEC:2.7.7.48PROSITE-ProRule annotation2 Publications
- Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.By similarity EC:3.4.21.98
Cofactori
Activity regulationi
Temperature dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 952 | For protease NS2 activity; shared with dimeric partnerPROSITE-ProRule annotation | 1 | |
Active sitei | 972 | For protease NS2 activity; shared with dimeric partnerPROSITE-ProRule annotation | 1 | |
Active sitei | 993 | For protease NS2 activity; shared with dimeric partnerPROSITE-ProRule annotation | 1 | |
Active sitei | 1083 | Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 1107 | Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 1123 | Zinc; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation3 Publications | 1 | |
Metal bindingi | 1125 | Zinc; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation3 Publications | 1 | |
Active sitei | 1165 | Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation2 Publications | 1 | |
Metal bindingi | 1171 | Zinc; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation2 Publications | 1 | |
Metal bindingi | 1175 | Zinc; structural; required for NS3 protease activityPROSITE-ProRule annotation2 Publications | 1 | |
Metal bindingi | 1237 | Magnesium; catalytic; for NS3 helicase activityBy similarity | 1 | |
Metal bindingi | 1317 | Magnesium; catalytic; for NS3 helicase activityBy similarity | 1 | |
Metal bindingi | 2011 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 2029 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 2031 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 2052 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 2639 | Magnesium; catalytic; for RNA-directed RNA polymerase activity2 Publications | 1 | |
Metal bindingi | 2737 | Magnesium; catalytic; for RNA-directed RNA polymerase activity2 Publications | 1 | |
Metal bindingi | 2738 | Magnesium; catalytic; for RNA-directed RNA polymerase activity2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1230 – 1237 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ATP hydrolysis activity Source: RHEA
- cysteine-type endopeptidase activity Source: InterPro
- identical protein binding Source: IntAct
- ion channel activity Source: UniProtKB-KW
- protease binding Source: AgBase
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
- serine-type endopeptidase activity Source: InterPro
- serine-type peptidase activity Source: AgBase
- SH3 domain binding Source: UniProtKB-KW
- structural molecule activity Source: InterPro
- zinc ion binding Source: InterPro
GO - Biological processi
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
- fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB-KW
- modulation by virus of host G1/S transition checkpoint Source: UniProtKB-KW
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- protein complex oligomerization Source: UniProtKB-KW
- suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity Source: UniProtKB-KW
- suppression by virus of host TRAF activity Source: UniProtKB-KW
- suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
- suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity Source: UniProtKB-KW
- transformation of host cell by virus Source: InterPro
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Enzyme and pathway databases
BRENDAi | 3.4.21.98, 17002 |
Protein family/group databases
MEROPSi | S29.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 11 chains: Alternative name(s): Capsid protp26663ein C p23 Alternative name(s): p21 Alternative name(s): gp32 gp35 Alternative name(s): NS1 gp68 gp70 Serine protease/helicase NS3 (EC:3.4.21.98By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity) Alternative name(s): Hepacivirin NS3 helicaseBy similarity NS3 proteaseBy similarity NS3P Viroporin p70 Alternative name(s): p8 Alternative name(s): p27 Alternative name(s): p56/58 RNA-directed RNA polymerase (EC:2.7.7.482 Publications) Alternative name(s): NS5B p68 |
Organismi | Hepatitis C virus genotype 1b (isolate BK) (HCV) |
Taxonomic identifieri | 11105 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Flasuviricetes › Amarillovirales › Flaviviridae › Hepacivirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Host endoplasmic reticulum membrane By similarity; Single-pass membrane protein Sequence analysis
- Host mitochondrion membrane By similarity; Single-pass type I membrane protein Sequence analysis Note: The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane.
- Virion By similarity
- Host cytoplasm By similarity
- Host nucleus By similarity
- Host lipid droplet 1 Publication Note: Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (PubMed:17188392).By similarity1 Publication
- Virion membrane Curated; Single-pass type I membrane protein Curated
- Host endoplasmic reticulum membrane ; Single-pass type I membrane protein By similarity Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity).By similarity
- Virion membrane Curated; Single-pass type I membrane protein Curated
- Host endoplasmic reticulum membrane ; Single-pass type I membrane protein By similarity
- Host lipid droplet By similarity Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity).By similarity
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
- Host mitochondrion By similarity
- Host cell membrane By similarity Note: The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity).By similarity
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
- Host lipid droplet By similarity Note: Probably present on the surface of lipid droplets.By similarity
- Host endoplasmic reticulum membrane Curated; Peripheral membrane protein Curated Note: NS3 is associated to the ER membrane through its binding to NS4A.Curated
- Host endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated Note: Host membrane insertion occurs after processing by the NS3 protease.
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity Note: A reorientation of the N-terminus into the ER lumen occurs post-translationally.By similarity
- Host endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
- host perinuclear region By similarity
- Host mitochondrion By similarity
- Host cytoplasm By similarity
- Host nucleus By similarity
- Host lipid droplet By similarity Note: Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity).By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum membrane ; Single-pass type IV membrane protein By similarity Note: Host membrane insertion occurs after processing by the NS3 protease.By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 190 – 358 | LumenalBy similarityAdd BLAST | 169 | |
Transmembranei | 359 – 379 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 380 – 725 | LumenalBy similarityAdd BLAST | 346 | |
Transmembranei | 726 – 746 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 747 – 757 | LumenalBy similarityAdd BLAST | 11 | |
Transmembranei | 758 – 778 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 779 – 781 | CytoplasmicBy similarity | 3 | |
Transmembranei | 782 – 803 | HelicalBy similarityAdd BLAST | 22 | |
Topological domaini | 804 – 813 | LumenalBy similarity | 10 | |
Transmembranei | 814 – 834 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 835 – 838 | CytoplasmicBy similarity | 4 | |
Transmembranei | 839 – 859 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 860 – 881 | LumenalBy similarityAdd BLAST | 22 | |
Transmembranei | 882 – 902 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 903 – 1657 | CytoplasmicBy similarityAdd BLAST | 755 | |
Transmembranei | 1658 – 1678 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1679 – 1805 | CytoplasmicSequence analysisAdd BLAST | 127 | |
Transmembranei | 1806 – 1826 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1827 – 1828 | LumenalSequence analysis | 2 | |
Transmembranei | 1829 – 1849 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1850 | CytoplasmicSequence analysis | 1 | |
Transmembranei | 1851 – 1871 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1872 – 1881 | LumenalSequence analysis | 10 | |
Transmembranei | 1882 – 1902 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1903 – 1972 | CytoplasmicSequence analysisAdd BLAST | 70 | |
Intramembranei | 1973 – 2003 | By similarityAdd BLAST | 31 | |
Topological domaini | 2004 – 2989 | CytoplasmicBy similarityAdd BLAST | 986 | |
Transmembranei | 2990 – 3010 | HelicalBy similarityAdd BLAST | 21 |
Keywords - Cellular componenti
Capsid protein, Host cell membrane, Host cytoplasm, Host endoplasmic reticulum, Host lipid droplet, Host membrane, Host mitochondrion, Host nucleus, Membrane, Viral envelope protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2194 | S → A: Loss of phosphorylation. 1 Publication | 1 | |
Mutagenesisi | 2322 | P → A: Complete loss of binding to GRB2. 1 Publication | 1 | |
Mutagenesisi | 2323 | P → A: Complete loss of binding to GRB2. 1 Publication | 1 | |
Mutagenesisi | 2326 | P → A: Complete loss of binding to GRB2. 1 Publication | 1 | |
Mutagenesisi | 2639 | D → C, G or N: Complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2644 | D → G or N: Complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2702 | G → D, L or R: Complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2705 | T → V: Almost complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2706 | T → C: Almost complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2706 | T → K: Complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2710 | N → K: Complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2736 | G → A or C: Almost complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2737 | D → E, H or N: Complete loss of RdRp activity. 1 Publication | 1 | |
Mutagenesisi | 2738 | D → H: Complete loss of RdRp activity. 1 Publication | 1 |
Keywords - Diseasei
OncogeneChemistry databases
ChEMBLi | CHEMBL6040 |
DrugBanki | DB08706, (2S)-({(5Z)-5-[(5-Ethyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl}amino)(4-fluorophenyl)acetic acid DB03605, (2s)-2-[(2,4-Dichloro-Benzoyl)-(3-Trifluoromethyl-Benzyl)-Amino]-3-Phenyl-Propionic Acid DB02331, (2s)-2-[(5-Benzofuran-2-Yl-Thiophen-2-Ylmethyl)-(2,4-Dichloro-Benzoyl)-Amino]-3-Phenyl-Propionic Acid DB07199, (2S,4S,5R)-1-(4-TERT-BUTYLBENZOYL)-2-ISOBUTYL-5-(1,3-THIAZOL-2-YL)PYRROLIDINE-2,4-DICARBOXYLIC ACID DB07200, (2S,4S,5R)-2-ISOBUTYL-5-(2-THIENYL)-1-[4-(TRIFLUOROMETHYL)BENZOYL]PYRROLIDINE-2,4-DICARBOXYLIC ACID DB07414, (5S)-1-benzyl-3-(1,1-dioxido-1,2-benzisothiazol-3-yl)-4-hydroxy-5-(1-methylethyl)-1,5-dihydro-2H-pyrrol-2-one DB08710, (5Z)-5-[(5-ethylfuran-2-yl)methylidene]-2-[[(S)-(4-fluorophenyl)-(2H-tetrazol-5-yl)methyl]amino]-1,3-thiazol-4-one DB08390, (6S)-6-CYCLOPENTYL-6-[2-(3-FLUORO-4-ISOPROPOXYPHENYL)ETHYL]-4-HYDROXY-5,6-DIHYDRO-2H-PYRAN-2-ONE DB08278, 1-(2-cyclopropylethyl)-3-(1,1-dioxo-2H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxy-2(1H)-quinolinone DB08701, 2-(3-BROMOPHENYL)-6-[(2-HYDROXYETHYL)AMINO]-1H-BENZO[DE]ISOQUINOLINE-1,3(2H)-DIONE DB04298, 3-(4-Amino-2-Tert-Butyl-5-Methyl-Phenylsulfanyl)-6-Cyclopentyl-4-Hydroxy-6-[2-(4-Hydroxy-Phenyl)-Ethyl]-5,6-Dihydro-Pyran-2-One DB07570, 3-CYCLOHEXYL-1-(2-MORPHOLIN-4-YL-2-OXOETHYL)-2-PHENYL-1H-INDOLE-6-CARBOXYLIC ACID DB08279, 3-{ISOPROPYL[(TRANS-4-METHYLCYCLOHEXYL)CARBONYL]AMINO}-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACID DB08581, 4-[(4-bromo-2-{[(3R,5S)-3,5-dimethylpiperidin-1-yl]carbonyl}phenyl)amino]-4-oxobutanoic acid DB08578, 4-[(5-bromopyridin-2-yl)amino]-4-oxobutanoic acid DB08580, 4-bromo-2-{[(2R)-2-(2-chlorobenzyl)pyrrolidin-1-yl]carbonyl}aniline DB08579, 4-bromo-2-{[(3R,5S)-3,5-dimethylpiperidin-1-yl]carbonyl}aniline DB08481, 4-Methyl-N-[5-(5-methyl-furan-2-ylmethylene)-4-oxo-thiazolidin-2-ylidene]-benzenesulfonamide DB06974, 5-hydroxy-4-(7-methoxy-1,1-dioxido-2H-1,2,4-benzothiadiazin-3-yl)-2-(3-methylbutyl)-6-phenylpyridazin-3(2H)-one DB07169, 5R-(3,4-DICHLOROPHENYLMETHYL)-3-(2-THIOPHENESULFONYLAMINO)-4-OXO-2-THIONOTHIAZOLIDINE DB11586, Asunaprevir DB04137, Guanosine-5'-Triphosphate DB08582, N-(4-bromo-2-{[(3R,5S)-3,5-dimethylpiperidin-1-yl]carbonyl}phenyl)-4-morpholin-4-yl-4-oxobutanamide DB08031, N-[(13-CYCLOHEXYL-6,7-DIHYDROINDOLO[1,2-D][1,4]BENZOXAZEPIN-10-YL)CARBONYL]-2-METHYL-L-ALANINE DB07062, N-{3-[4-Hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyrrolo[1,2-b]pyridazin-3-yl]-1,1-dioxido-2H-1,2,4-benzothiadiazin-7-yl}methanesulfonamide DB07238, Nesbuvir DB04005, Uridine 5'-triphosphate |
DrugCentrali | P26663 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostBy similarity | |||
ChainiPRO_0000450852 | 2 – 3010 | Genome polyproteinAdd BLAST | 3009 | |
ChainiPRO_0000037529 | 2 – 191 | Core protein precursorAdd BLAST | 190 | |
ChainiPRO_0000037530 | 2 – 177 | Mature core proteinAdd BLAST | 176 | |
PropeptideiPRO_0000037531 | 178 – 191 | ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityAdd BLAST | 14 | |
ChainiPRO_0000037532 | 192 – 383 | Envelope glycoprotein E1Add BLAST | 192 | |
ChainiPRO_0000037533 | 384 – 746 | Envelope glycoprotein E2Add BLAST | 363 | |
ChainiPRO_0000037534 | 747 – 809 | Viroporin p7Add BLAST | 63 | |
ChainiPRO_0000037535 | 810 – 1026 | Protease NS2PROSITE-ProRule annotationAdd BLAST | 217 | |
ChainiPRO_0000037536 | 1027 – 1657 | Serine protease/helicase NS3Add BLAST | 631 | |
ChainiPRO_0000037537 | 1658 – 1711 | Non-structural protein 4AAdd BLAST | 54 | |
ChainiPRO_0000037538 | 1712 – 1972 | Non-structural protein 4BAdd BLAST | 261 | |
ChainiPRO_0000037539 | 1973 – 2419 | Non-structural protein 5AAdd BLAST | 447 | |
ChainiPRO_0000037540 | 2420 – 3010 | RNA-directed RNA polymeraseAdd BLAST | 591 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine; by hostBy similarity | 1 | |
Modified residuei | 53 | Phosphoserine; by hostBy similarity | 1 | |
Modified residuei | 99 | Phosphoserine; by hostBy similarity | 1 | |
Modified residuei | 116 | Phosphoserine; by host PKABy similarity | 1 | |
Glycosylationi | 196 | N-linked (GlcNAc...) asparagine; by host1 Publication | 1 | |
Glycosylationi | 209 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 234 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 250 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 305 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 417 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 423 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 429 ↔ 552 | By similarity | ||
Glycosylationi | 430 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 448 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 452 ↔ 459 | By similarity | ||
Disulfide bondi | 486 ↔ 494 | By similarity | ||
Disulfide bondi | 503 ↔ 508 | By similarity | ||
Glycosylationi | 532 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 540 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 556 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 564 ↔ 569 | By similarity | ||
Glycosylationi | 576 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 581 ↔ 585 | By similarity | ||
Disulfide bondi | 597 ↔ 620 | By similarity | ||
Disulfide bondi | 607 ↔ 644 | By similarity | ||
Glycosylationi | 623 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 645 | N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 652 ↔ 677 | By similarity | ||
Lipidationi | 922 | S-palmitoyl cysteine; by hostBy similarity | 1 | |
Lipidationi | 1968 | S-palmitoyl cysteine; by hostBy similarity | 1 | |
Lipidationi | 1972 | S-palmitoyl cysteine; by hostBy similarity | 1 | |
Modified residuei | 2194 | Phosphoserine; by host; in p561 Publication | 1 | |
Modified residuei | 2197 | Phosphoserine; by host; in p58By similarity | 1 | |
Modified residuei | 2201 | Phosphoserine; by host; in p58By similarity | 1 | |
Modified residuei | 2204 | Phosphoserine; by host; in p58By similarity | 1 | |
Modified residuei | 2207 | Phosphoserine; by host; in p58By similarity | 1 | |
Modified residuei | 2210 | Phosphoserine; by host; in p58By similarity | 1 | |
Cross-linki | 2350 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 2448 | Phosphoserine; by hostBy similarity | 1 | |
Modified residuei | 2461 | Phosphoserine; by hostBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 177 – 178 | Cleavage; by host signal peptide peptidaseBy similarity | 2 | |
Sitei | 191 – 192 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 383 – 384 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 746 – 747 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 809 – 810 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 1026 – 1027 | Cleavage; by protease NS2PROSITE-ProRule annotation | 2 | |
Sitei | 1657 – 1658 | Cleavage; by serine protease/helicase NS3By similarity | 2 | |
Sitei | 1711 – 1712 | Cleavage; by serine protease/helicase NS3By similarity | 2 | |
Sitei | 1972 – 1973 | Cleavage; by serine protease/helicase NS3By similarity | 2 | |
Sitei | 2419 – 2420 | Cleavage; by serine protease/helicase NS3By similarity | 2 |
Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugationPTM databases
iPTMneti | P26663 |
Interactioni
Subunit structurei
Homooligomer (By similarity).
Interacts with E1 (via C-terminus) (By similarity).
Interacts with the non-structural protein 5A (By similarity).
Interacts (via N-terminus) with host STAT1 (via SH2 domain); this interaction results in decreased STAT1 phosphorylation and ubiquitin-mediated proteasome-dependent STAT1 degradation, leading to decreased IFN-stimulated gene transcription (By similarity).
Interacts with host STAT3; this interaction constitutively activates STAT3 (By similarity). Associates with host LTBR receptor (By similarity).
Interacts with host TNFRSF1A receptor and possibly induces apoptosis (By similarity).
Interacts with host HNRPK (By similarity).
Interacts with host YWHAE (By similarity).
Interacts with host UBE3A/E6AP (By similarity).
Interacts with host DDX3X (By similarity).
Interacts with host APOA2 (By similarity).
Interacts with host RXRA protein (By similarity).
Interacts with host SP110 isoform 3/Sp110b; this interaction sequesters the transcriptional corepressor SP110 away from the nucleus (By similarity).
Interacts with host CREB3 nuclear transcription protein; this interaction triggers cell transformation (By similarity).
Interacts with host ACY3 (By similarity).
Interacts with host C1QR1 (By similarity).
Interacts with host RBM24; this interaction, which enhances the interaction of the mature core protein with 5'-UTR, may inhibit viral translation and favor replication (By similarity).
Interacts (via N-terminus) with host EIF2AK2/PKR (via N-terminus); this interaction induces the autophosphorylation of EIF2AK2 (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).
By similarityForms a heterodimer with envelope glycoprotein E2 (By similarity).
Interacts with mature core protein (By similarity).
Interacts with protease NS2 (By similarity). The heterodimer E1/E2 interacts with host CLDN1; this interaction plays a role in viral entry into host cell (By similarity).
Interacts with host SPSB2 (via C-terminus) (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).
By similarityForms a heterodimer with envelope glycoprotein E1 (By similarity).
Interacts with host CD81 and SCARB1 receptors; these interactions play a role in viral entry into host cell (By similarity).
Interacts with host EIF2AK2/PKR; this interaction inhibits EIF2AK2 and probably allows the virus to evade the innate immune response (By similarity).
Interacts with host CD209/DC-SIGN and CLEC4M/DC-SIGNR (By similarity). Interact with host SPCS1; this interaction is essential for viral particle assembly (By similarity).
Interacts with protease NS2 (By similarity). The heterodimer E1/E2 interacts with host CLDN1; this interaction plays a role in viral entry into host cell (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).
Interacts with host SLC3A2/4F2hc; the interaction may facilitate viral entry into host cell (By similarity).
Interacts with human PLSCR1 (By similarity).
By similarityHomohexamer (By similarity). Homoheptamer (By similarity).
Interacts with protease NS2 (By similarity).
By similarityHomodimer (By similarity).
Interacts with host SPCS1; this interaction is essential for viral particle assembly (By similarity).
Interacts with envelope glycoprotein E1 (By similarity).
Interacts with envelope glycoprotein E2 (By similarity).
Interacts with viroporin p7 (By similarity).
Interacts with serine protease/helicase NS3 (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).
By similarityInteracts with protease NS2 (By similarity).
Interacts with non-structural protein 4A; this interaction stabilizes the folding of NS3 serine protease (PubMed:9568891, PubMed:10366511). NS3-NS4A interaction is essential for NS3 activation and allows membrane anchorage of the latter (PubMed:9568891). NS3/NS4A complex also prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity).
Interacts with host MAVS; this interaction leads to the cleavage and inhibition of host MAVS (By similarity).
Interacts with host TICAM1; this interaction leads to the cleavage and inhibition of host TICAM1 (By similarity).
Interacts with host TANK-binding kinase/TBK1; this interaction results in the inhibition of the association between TBK1 and IRF3, which leads to the inhibition of IRF3 activation (By similarity).
Interacts with host RBM24 (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).
By similarity2 PublicationsInteracts with NS3 serine protease; this interaction stabilizes the folding of NS3 serine protease (PubMed:9568891, PubMed:10366511). NS3-NS4A interaction is essential for NS3 activation and allows membrane anchorage of the latter (PubMed:9568891).
Interacts with non-structural protein 5A (via N-terminus) (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).
By similarity2 PublicationsMonomer (By similarity). Homodimer; dimerization is required for RNA-binding (By similarity).
Interacts with the mature core protein (By similarity).
Interacts (via N-terminus) with non-structural protein 4A (By similarity).
Interacts with non-structural protein 4B (By similarity).
Interacts with RNA-directed RNA polymerase (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity).
Interacts with host GRB2 (PubMed:10318918).
Interacts with host BIN1 (By similarity).
Interacts with host PIK3R1 (PubMed:12186904).
Interacts with host SRCAP (By similarity).
Interacts with host FKBP8 (By similarity).
Interacts with host VAPB (By similarity).
Interacts with host EIF2AK2/PKR; this interaction leads to disruption of EIF2AK2 dimerization by NS5A and probably allows the virus to evade the innate immune response (PubMed:9710605).
Interacts (via N-terminus) with host PACSIN2 (via N-terminus); this interaction attenuates protein kinase C alpha-mediated phosphorylation of PACSIN2 by disrupting the interaction between PACSIN2 and PRKCA (By similarity).
Interacts (via N-terminus) with host SRC kinase (via SH2 domain) (By similarity).
Interacts with most Src-family kinases (By similarity).
Interacts with host IFI27 and SKP2; promotes the ubiquitin-mediated proteasomal degradation of NS5A (By similarity).
Interacts with host GPS2 (By similarity).
Interacts with host TNFRSF21; this interaction allows the modulation by the virus of JNK, p38 MAPK, STAT3, and Akt signaling pathways in a DR6-dependent manner (By similarity).
Interacts (via N-terminus) with host CIDEB (via N-terminus); this interaction seems to regulate the association of HCV particles with APOE (By similarity).
Interacts with host CHKA/Choline Kinase-alpha; CHKA bridges host PI4KA and NS5A and potentiates NS5A-stimulated PI4KA activity, which then facilitates the targeting of the ternary complex to the ER for viral replication (By similarity).
Interacts with host SPSB2 (via C-terminus); this interaction targets NS5A for ubiquitination and degradation (By similarity).
Interacts with host RAB18; this interaction may promote the association of NS5A and other replicase components with lipid droplets (By similarity).
By similarity3 PublicationsHomooligomer.
Interacts with non-structural protein 5A (By similarity).
Interacts with host VAPB (By similarity).
Interacts with host PRK2/PKN2 (By similarity).
Interacts with host HNRNPA1 and SEPT6; these interactions facilitate the viral replication (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity).
By similarityBinary interactionsi
P26663
With | #Exp. | IntAct |
---|---|---|
Pkm [P52480] from Mus musculus. | 3 | EBI-6857429,EBI-647785 |
Sos1 [Q62245] from Mus musculus. | 2 | EBI-6857429,EBI-1693 |
Serine protease/helicase NS3 (PRO_0000037536)
With | #Exp. | IntAct |
---|---|---|
Non-structural protein 4A (PRO_0000037537) | 6 | EBI-6838571,EBI-6838576 |
TP53 [P04637] from Homo sapiens. | 9 | EBI-6838571,EBI-366083 |
RNA-directed RNA polymerase (PRO_0000037540)
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-6874437,EBI-6874437 |
Serine protease/helicase NS3 (PRO_0000037548) from Hepatitis C virus genotype 1b (isolate Con1). | 5 | EBI-6874437,EBI-6863741 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- protease binding Source: AgBase
- SH3 domain binding Source: UniProtKB-KW
Protein-protein interaction databases
IntActi | P26663, 6 interactors |
MINTi | P26663 |
Chemistry databases
BindingDBi | P26663 |
Structurei
Secondary structure
3D structure databases
BMRBi | P26663 |
SMRi | P26663 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P26663 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 903 – 1026 | Peptidase C18PROSITE-ProRule annotationAdd BLAST | 124 | |
Domaini | 1027 – 1208 | Peptidase S29PROSITE-ProRule annotationAdd BLAST | 182 | |
Domaini | 1217 – 1369 | Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST | 153 | |
Domaini | 2633 – 2751 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 119 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 75 | Disordered1 PublicationAdd BLAST | 74 | |
Regioni | 2 – 59 | Interaction with DDX3XBy similarityAdd BLAST | 58 | |
Regioni | 2 – 58 | Interaction with EIF2AK2/PKRBy similarityAdd BLAST | 57 | |
Regioni | 2 – 23 | Interaction with STAT1By similarityAdd BLAST | 22 | |
Regioni | 112 – 152 | Important for endoplasmic reticulum and mitochondrial localizationBy similarityAdd BLAST | 41 | |
Regioni | 122 – 173 | Interaction with APOA2By similarityAdd BLAST | 52 | |
Regioni | 164 – 167 | Important for lipid droplets localizationBy similarity | 4 | |
Regioni | 265 – 296 | Important for fusionBy similarityAdd BLAST | 32 | |
Regioni | 385 – 411 | HVR1By similarityAdd BLAST | 27 | |
Regioni | 474 – 482 | HVR2By similarity | 9 | |
Regioni | 480 – 494 | CD81-binding 11 PublicationAdd BLAST | 15 | |
Regioni | 544 – 552 | CD81-binding 21 Publication | 9 | |
Regioni | 660 – 671 | EIF2AK2/eIF2-alpha phosphorylation homology domain (PePHD)Add BLAST | 12 | |
Regioni | 904 – 1206 | Protease NS2-31 PublicationAdd BLAST | 303 | |
Regioni | 929 – 949 | Interaction with host SCPS1By similarityAdd BLAST | 21 | |
Regioni | 1486 – 1497 | RNA-binding1 PublicationAdd BLAST | 12 | |
Regioni | 1679 – 1690 | NS3-bindingBy similarityAdd BLAST | 12 | |
Regioni | 1833 – 1861 | Glycine zipperBy similarityAdd BLAST | 29 | |
Regioni | 1978 – 1998 | Membrane-bindingBy similarityAdd BLAST | 21 | |
Regioni | 2005 – 2221 | RNA-bindingBy similarityAdd BLAST | 217 | |
Regioni | 2120 – 2332 | Transcriptional activationSequence analysisAdd BLAST | 213 | |
Regioni | 2120 – 2208 | FKBP8-bindingBy similarityAdd BLAST | 89 | |
Regioni | 2135 – 2139 | Interaction with non-structural protein 4ABy similarity | 5 | |
Regioni | 2189 – 2441 | Interaction with host SKP2By similarityAdd BLAST | 253 | |
Regioni | 2210 – 2275 | EIF2AK2/PKR-binding1 PublicationAdd BLAST | 66 | |
Regioni | 2210 – 2249 | ISDR1 PublicationAdd BLAST | 40 | |
Regioni | 2249 – 2306 | NS4B-bindingSequence analysisAdd BLAST | 58 | |
Regioni | 2332 – 2441 | Interaction with host IFI27By similarityAdd BLAST | 110 | |
Regioni | 2351 – 2407 | DisorderedSequence analysisAdd BLAST | 57 | |
Regioni | 2354 – 2377 | V3Add BLAST | 24 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 5 – 13 | Nuclear localization signalBy similarity | 9 | |
Motifi | 38 – 43 | Nuclear localization signalBy similarity | 6 | |
Motifi | 58 – 64 | Nuclear localization signalBy similarity | 7 | |
Motifi | 66 – 71 | Nuclear localization signalBy similarity | 6 | |
Motifi | 1316 – 1319 | DECH boxBy similarity | 4 | |
Motifi | 2322 – 2325 | SH3-bindingSequence analysis | 4 | |
Motifi | 2326 – 2334 | Nuclear localization signalBy similarity | 9 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 47 – 69 | Basic and acidic residuesSequence analysisAdd BLAST | 23 | |
Compositional biasi | 2351 – 2369 | Polar residuesSequence analysisAdd BLAST | 19 |
Domaini
Sequence similaritiesi
Keywords - Domaini
SH3-binding, Transmembrane, Transmembrane helixFamily and domain databases
Gene3Di | 1.20.1280.150, 1 hit 2.20.25.210, 1 hit 2.20.25.220, 1 hit 2.30.30.710, 1 hit 2.40.10.10, 1 hit 3.30.70.270, 2 hits 3.40.50.300, 2 hits 4.10.710.10, 1 hit |
InterProi | View protein in InterPro IPR011492, DEAD_Flavivir IPR043502, DNA/RNA_pol_sf IPR002521, HCV_core_C IPR044896, HCV_core_chain_A IPR002522, HCV_core_N IPR002519, HCV_env IPR002531, HCV_NS1 IPR002518, HCV_NS2 IPR042205, HCV_NS2_C IPR042209, HCV_NS2_N IPR000745, HCV_NS4a IPR001490, HCV_NS4b IPR002868, HCV_NS5a IPR013193, HCV_NS5a_1B_dom IPR038568, HCV_NS5A_1B_sf IPR024350, HCV_NS5a_C IPR014001, Helicase_ATP-bd IPR001650, Helicase_C IPR013192, NS5A_1a IPR038170, NS5A_1a_sf IPR027417, P-loop_NTPase IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR004109, Peptidase_S29_NS3 IPR043128, Rev_trsase/Diguanyl_cyclase IPR007094, RNA-dir_pol_PSvirus IPR002166, RNA_pol_HCV |
Pfami | View protein in Pfam PF07652, Flavi_DEAD, 1 hit PF01543, HCV_capsid, 1 hit PF01542, HCV_core, 1 hit PF01539, HCV_env, 1 hit PF01560, HCV_NS1, 1 hit PF01538, HCV_NS2, 1 hit PF01006, HCV_NS4a, 1 hit PF01001, HCV_NS4b, 1 hit PF01506, HCV_NS5a, 1 hit PF08300, HCV_NS5a_1a, 1 hit PF08301, HCV_NS5a_1b, 1 hit PF12941, HCV_NS5a_C, 1 hit PF02907, Peptidase_S29, 1 hit PF00998, RdRP_3, 1 hit |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 2 hits SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51693, HCV_NS2_PRO, 1 hit PS51192, HELICASE_ATP_BIND_1, 1 hit PS51194, HELICASE_CTER, 1 hit PS51822, HV_PV_NS3_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRAPR
60 70 80 90 100
KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP
110 120 130 140 150
RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA
160 170 180 190 200
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTTPAS AYEVHNVSGI
210 220 230 240 250
YHVTNDCSNA SIVYEAADLI MHTPGCVPCV REGNSSRCWV ALTPTLAARN
260 270 280 290 300
VTIPTTTIRR HVDLLVGAAA FCSAMYVGDL CGSVFLVSQL FTFSPRRHVT
310 320 330 340 350
LQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG
360 370 380 390 400
AHWGVLAGLA YYSMAGNWAK VLIVMLLFAG VDGDTHVTGG AQAKTTNRLV
410 420 430 440 450
SMFASGPSQK IQLINTNGSW HINRTALNCN DSLQTGFLAA LFYTHSFNSS
460 470 480 490 500
GCPERMAQCR TIDKFDQGWG PITYAESSRS DQRPYCWHYP PPQCTIVPAS
510 520 530 540 550
EVCGPVYCFT PSPVVVGTTD RFGVPTYRWG ENETDVLLLN NTRPPQGNWF
560 570 580 590 600
GCTWMNSTGF TKTCGGPPCN IGGVGNNTLT CPTDCFRKHP EATYTKCGSG
610 620 630 640 650
PWLTPRCMVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL NAACNWTRGE
660 670 680 690 700
RCDLEDRDRP ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHQNIVDVQ
710 720 730 740 750
YLYGIGSAVV SFAIKWEYVL LLFLLLADAR VCACLWMMLL IAQAEAALEN
760 770 780 790 800
LVVLNSASVA GAHGILSFLV FFCAAWYIKG RLVPGATYAL YGVWPLLLLL
810 820 830 840 850
LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA RLIWWLQYFT
860 870 880 890 900
TRAEADLHVW IPPLNARGGR DAIILLMCAV HPELIFDITK LLIAILGPLM
910 920 930 940 950
VLQAGITRVP YFVRAQGLIH ACMLVRKVAG GHYVQMAFMK LGALTGTYIY
960 970 980 990 1000
NHLTPLRDWP RAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL
1010 1020 1030 1040 1050
PVSARRGKEI LLGPADSLEG RGLRLLAPIT AYSQQTRGLL GCIITSLTGR
1060 1070 1080 1090 1100
DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT VYHGAGSKTL AAPKGPITQM
1110 1120 1130 1140 1150
YTNVDQDLVG WPKPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG
1160 1170 1180 1190 1200
SLLSPRPVSY LKGSSGGPLL CPFGHAVGIF RAAVCTRGVA KAVDFVPVES
1210 1220 1230 1240 1250
METTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK
1260 1270 1280 1290 1300
VLVLNPSVAA TLGFGAYMSK AHGIDPNIRT GVRTITTGAP VTYSTYGKFL
1310 1320 1330 1340 1350
ADGGCSGGAY DIIICDECHS TDSTTILGIG TVLDQAETAG ARLVVLATAT
1360 1370 1380 1390 1400
PPGSVTVPHP NIEEVALSNT GEIPFYGKAI PIEAIRGGRH LIFCHSKKKC
1410 1420 1430 1440 1450
DELAAKLSGL GINAVAYYRG LDVSVIPTIG DVVVVATDAL MTGYTGDFDS
1460 1470 1480 1490 1500
VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRRGIYR
1510 1520 1530 1540 1550
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV
1560 1570 1580 1590 1600
CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP
1610 1620 1630 1640 1650
PPSWDQMWKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKYIMACMS
1660 1670 1680 1690 1700
ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV VIVGRIILSG RPAIVPDREL
1710 1720 1730 1740 1750
LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV
1760 1770 1780 1790 1800
ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
1810 1820 1830 1840 1850
LTTQSTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD
1860 1870 1880 1890 1900
ILAGYGAGVA GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA
1910 1920 1930 1940 1950
ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS
1960 1970 1980 1990 2000
LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FKTWLQSKLL
2010 2020 2030 2040 2050
PQLPGVPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK NGSMRIVGPK
2060 2070 2080 2090 2100
TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
2110 2120 2130 2140 2150
YVTGMTTDNV KCPCQVPAPE FFSEVDGVRL HRYAPACRPL LREEVTFQVG
2160 2170 2180 2190 2200
LNQYLVGSQL PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS
2210 2220 2230 2240 2250
SSASQLSAPS LKATCTTHHV SPDADLIEAN LLWRQEMGGN ITRVESENKV
2260 2270 2280 2290 2300
VVLDSFDPLR AEEDEREVSV PAEILRKSKK FPAAMPIWAR PDYNPPLLES
2310 2320 2330 2340 2350
WKDPDYVPPV VHGCPLPPIK APPIPPPRRK RTVVLTESSV SSALAELATK
2360 2370 2380 2390 2400
TFGSSESSAV DSGTATALPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL
2410 2420 2430 2440 2450
SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL
2460 2470 2480 2490 2500
RHHNMVYATT SRSAGLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK
2510 2520 2530 2540 2550
LLSVEEACKL TPPHSAKSKF GYGAKDVRNL SSKAVNHIHS VWKDLLEDTV
2560 2570 2580 2590 2600
TPIDTTIMAK NEVFCVQPEK GGRKPARLIV FPDLGVRVCE KMALYDVVST
2610 2620 2630 2640 2650
LPQVVMGSSY GFQYSPGQRV EFLVNTWKSK KNPMGFSYDT RCFDSTVTEN
2660 2670 2680 2690 2700
DIRVEESIYQ CCDLAPEARQ AIKSLTERLY IGGPLTNSKG QNCGYRRCRA
2710 2720 2730 2740 2750
SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVNGDDLV VICESAGTQE
2760 2770 2780 2790 2800
DAASLRVFTE AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV
2810 2820 2830 2840 2850
YYLTRDPTTP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS
2860 2870 2880 2890 2900
ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ IIERLHGLSA FSLHSYSPGE
2910 2920 2930 2940 2950
INRVASCLRK LGVPPLRVWR HRARSVRARL LSQGGRAATC GKYLFNWAVK
2960 2970 2980 2990 3000
TKLKLTPIPA ASRLDLSGWF VAGYSGGDIY HSLSRARPRW FMLCLLLLSV
3010
GVGIYLLPNR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M58335 Genomic RNA Translation: AAA72945.1 |
PIRi | A38465, GNWVTC |
Similar proteinsi
Cross-referencesi
Web resourcesi
Virus Pathogen Resource |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M58335 Genomic RNA Translation: AAA72945.1 |
PIRi | A38465, GNWVTC |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A1Q | X-ray | 2.40 | A/B/C | 1027-1215 | [»] | |
1BT7 | NMR | - | A | 1027-1206 | [»] | |
1C2P | X-ray | 1.90 | A/B | 2422-2989 | [»] | |
1CSJ | X-ray | 2.80 | A/B | 2420-2950 | [»] | |
1CU1 | X-ray | 2.50 | A/B | 1029-1657 | [»] | |
1GX5 | X-ray | 1.70 | A | 2420-2955 | [»] | |
1GX6 | X-ray | 1.85 | A | 2420-2950 | [»] | |
1JXP | X-ray | 2.20 | A/B | 1027-1206 | [»] | |
C/D | 1678-1691 | [»] | ||||
1NHU | X-ray | 2.00 | A/B | 2420-2989 | [»] | |
1NHV | X-ray | 2.90 | A/B | 2420-2989 | [»] | |
1NS3 | X-ray | 2.80 | A/B | 1029-1206 | [»] | |
C/D | 1678-1689 | [»] | ||||
1OS5 | X-ray | 2.20 | A | 2420-2989 | [»] | |
1QUV | X-ray | 2.50 | A | 2420-2989 | [»] | |
2AWZ | X-ray | 2.15 | A/B | 2420-2989 | [»] | |
2AX0 | X-ray | 2.00 | A/B | 2420-2989 | [»] | |
2AX1 | X-ray | 2.10 | A/B | 2420-2989 | [»] | |
2BRK | X-ray | 2.30 | A | 2420-2955 | [»] | |
2BRL | X-ray | 2.40 | A | 2420-2955 | [»] | |
2DXS | X-ray | 2.20 | A/B | 2420-2963 | [»] | |
2GIQ | X-ray | 1.65 | A/B | 2421-2981 | [»] | |
2GIR | X-ray | 1.90 | A/B | 2421-2981 | [»] | |
2HAI | X-ray | 1.58 | A | 2420-2988 | [»] | |
2HWH | X-ray | 2.30 | A/B | 2422-2989 | [»] | |
2HWI | X-ray | 2.00 | A/B | 2422-2989 | [»] | |
2I1R | X-ray | 2.20 | A/B | 2422-2989 | [»] | |
2JC0 | X-ray | 2.20 | A/B | 2420-2989 | [»] | |
2JC1 | X-ray | 2.00 | A/B | 2420-2989 | [»] | |
2O5D | X-ray | 2.20 | A/B | 2422-2989 | [»] | |
2WCX | X-ray | 2.00 | A | 2420-2955 | [»] | |
2WHO | X-ray | 2.00 | A/B | 2420-2955 | [»] | |
2WRM | X-ray | 1.95 | A | 2420-2955 | [»] | |
2XWY | X-ray | 2.53 | A | 2420-2955 | [»] | |
2ZKU | X-ray | 1.95 | A/B/C/D | 2420-2989 | [»] | |
3BR9 | X-ray | 2.30 | A/B | 2420-2989 | [»] | |
3BSA | X-ray | 2.30 | A/B | 2420-2989 | [»] | |
3BSC | X-ray | 2.65 | A/B | 2420-2989 | [»] | |
3CDE | X-ray | 2.10 | A/B | 2420-2989 | [»] | |
3CIZ | X-ray | 1.87 | A/B | 2421-2989 | [»] | |
3CJ0 | X-ray | 1.90 | A/B | 2421-2989 | [»] | |
3CJ2 | X-ray | 1.75 | A/B | 2421-2989 | [»] | |
3CJ3 | X-ray | 1.87 | A/B | 2421-2989 | [»] | |
3CJ4 | X-ray | 2.07 | A/B | 2421-2989 | [»] | |
3CJ5 | X-ray | 1.92 | A/B | 2421-2989 | [»] | |
3CO9 | X-ray | 2.10 | A/B | 2420-2989 | [»] | |
3CVK | X-ray | 2.31 | A/B | 2420-2989 | [»] | |
3CWJ | X-ray | 2.40 | A/B | 2420-2989 | [»] | |
3D28 | X-ray | 2.30 | A/B | 2420-2989 | [»] | |
3D5M | X-ray | 2.20 | A/B | 2420-2989 | [»] | |
3E51 | X-ray | 1.90 | A/B | 2420-2989 | [»] | |
3FQK | X-ray | 2.20 | A/B | 2421-2989 | [»] | |
3FRZ | X-ray | 1.86 | A | 2420-2989 | [»] | |
3G86 | X-ray | 2.20 | A/B | 2421-2989 | [»] | |
3GYN | X-ray | 2.15 | A/B | 2420-2989 | [»] | |
3H2L | X-ray | 1.90 | A/B | 2420-2989 | [»] | |
3H59 | X-ray | 2.10 | A/B | 2421-2989 | [»] | |
3H5S | X-ray | 2.00 | A/B | 2421-2989 | [»] | |
3H5U | X-ray | 1.95 | A/B | 2421-2989 | [»] | |
3H98 | X-ray | 1.90 | A/B | 2421-2989 | [»] | |
3IGV | X-ray | 2.60 | A/B | 2420-2989 | [»] | |
3MF5 | X-ray | 2.00 | A/B | 2421-2989 | [»] | |
3RVB | X-ray | 2.20 | A | 1186-1657 | [»] | |
3UA7 | X-ray | 1.50 | E/F | 2321-2331 | [»] | |
3UDL | X-ray | 2.17 | A/B/C/D | 2420-2989 | [»] | |
3VQS | X-ray | 1.90 | A/B/C/D | 2420-2989 | [»] | |
4A92 | X-ray | 2.73 | A/B | 1029-1657 | [»] | |
A/B | 1678-1690 | [»] | ||||
4B6E | X-ray | 2.46 | A/B | 1029-1657 | [»] | |
4B6F | X-ray | 2.89 | A/B | 1029-1657 | [»] | |
4B71 | X-ray | 2.50 | A/B | 1029-1657 | [»] | |
4B73 | X-ray | 2.50 | A/B | 1029-1657 | [»] | |
4B74 | X-ray | 2.18 | A/B | 1029-1657 | [»] | |
4B75 | X-ray | 2.53 | A/B | 1029-1655 | [»] | |
4B76 | X-ray | 2.14 | A/B | 1029-1657 | [»] | |
4DGV | X-ray | 1.80 | A | 412-423 | [»] | |
4DGY | X-ray | 1.80 | A | 412-423 | [»] | |
4EO6 | X-ray | 1.79 | A/B | 2422-2989 | [»] | |
4EO8 | X-ray | 1.80 | A/B | 2422-2989 | [»] | |
4IH5 | X-ray | 1.90 | A/B | 2421-2989 | [»] | |
4IH6 | X-ray | 2.20 | A/B | 2421-2989 | [»] | |
4IH7 | X-ray | 2.30 | A/B | 2421-2989 | [»] | |
4K8B | X-ray | 2.80 | C/D | 1678-1689 | [»] | |
4KAI | X-ray | 2.30 | A/B | 2420-2989 | [»] | |
4KB7 | X-ray | 1.85 | A/B | 2420-2989 | [»] | |
4KBI | X-ray | 2.06 | A/B | 2420-2989 | [»] | |
4KE5 | X-ray | 2.11 | A/B | 2420-2989 | [»] | |
4MIA | X-ray | 2.80 | A/B | 2421-2989 | [»] | |
4MIB | X-ray | 2.30 | A/B | 2421-2989 | [»] | |
4MK7 | X-ray | 2.80 | A/B | 2421-2989 | [»] | |
4MK8 | X-ray | 2.09 | A/B | 2421-2989 | [»] | |
4MK9 | X-ray | 2.05 | A/B | 2421-2989 | [»] | |
4MKA | X-ray | 2.05 | A/B | 2421-2989 | [»] | |
4MKB | X-ray | 1.90 | A/B | 2421-2989 | [»] | |
4TN2 | X-ray | 2.70 | A | 2422-2989 | [»] | |
4WXP | X-ray | 2.08 | A | 1206-1656 | [»] | |
5FPS | X-ray | 2.68 | A/B | 1029-1657 | [»] | |
5FPT | X-ray | 2.72 | A/B | 1029-1657 | [»] | |
5FPY | X-ray | 2.52 | A/B | 1029-1657 | [»] | |
5KZP | X-ray | 2.26 | A/B/C/D | 412-423 | [»] | |
5W2E | X-ray | 2.80 | A/B | 2422-2989 | [»] | |
6MVP | X-ray | 2.00 | A/B | 2420-2989 | [»] | |
6W4G | X-ray | 1.95 | A/B | 2421-2981 | [»] | |
8OHM | X-ray | 2.30 | A | 1216-1650 | [»] | |
BMRBi | P26663 | |||||
SMRi | P26663 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P26663, 6 interactors |
MINTi | P26663 |
Chemistry databases
BindingDBi | P26663 |
ChEMBLi | CHEMBL6040 |
DrugBanki | DB08706, (2S)-({(5Z)-5-[(5-Ethyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl}amino)(4-fluorophenyl)acetic acid DB03605, (2s)-2-[(2,4-Dichloro-Benzoyl)-(3-Trifluoromethyl-Benzyl)-Amino]-3-Phenyl-Propionic Acid DB02331, (2s)-2-[(5-Benzofuran-2-Yl-Thiophen-2-Ylmethyl)-(2,4-Dichloro-Benzoyl)-Amino]-3-Phenyl-Propionic Acid DB07199, (2S,4S,5R)-1-(4-TERT-BUTYLBENZOYL)-2-ISOBUTYL-5-(1,3-THIAZOL-2-YL)PYRROLIDINE-2,4-DICARBOXYLIC ACID DB07200, (2S,4S,5R)-2-ISOBUTYL-5-(2-THIENYL)-1-[4-(TRIFLUOROMETHYL)BENZOYL]PYRROLIDINE-2,4-DICARBOXYLIC ACID DB07414, (5S)-1-benzyl-3-(1,1-dioxido-1,2-benzisothiazol-3-yl)-4-hydroxy-5-(1-methylethyl)-1,5-dihydro-2H-pyrrol-2-one DB08710, (5Z)-5-[(5-ethylfuran-2-yl)methylidene]-2-[[(S)-(4-fluorophenyl)-(2H-tetrazol-5-yl)methyl]amino]-1,3-thiazol-4-one DB08390, (6S)-6-CYCLOPENTYL-6-[2-(3-FLUORO-4-ISOPROPOXYPHENYL)ETHYL]-4-HYDROXY-5,6-DIHYDRO-2H-PYRAN-2-ONE DB08278, 1-(2-cyclopropylethyl)-3-(1,1-dioxo-2H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxy-2(1H)-quinolinone DB08701, 2-(3-BROMOPHENYL)-6-[(2-HYDROXYETHYL)AMINO]-1H-BENZO[DE]ISOQUINOLINE-1,3(2H)-DIONE DB04298, 3-(4-Amino-2-Tert-Butyl-5-Methyl-Phenylsulfanyl)-6-Cyclopentyl-4-Hydroxy-6-[2-(4-Hydroxy-Phenyl)-Ethyl]-5,6-Dihydro-Pyran-2-One DB07570, 3-CYCLOHEXYL-1-(2-MORPHOLIN-4-YL-2-OXOETHYL)-2-PHENYL-1H-INDOLE-6-CARBOXYLIC ACID DB08279, 3-{ISOPROPYL[(TRANS-4-METHYLCYCLOHEXYL)CARBONYL]AMINO}-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACID DB08581, 4-[(4-bromo-2-{[(3R,5S)-3,5-dimethylpiperidin-1-yl]carbonyl}phenyl)amino]-4-oxobutanoic acid DB08578, 4-[(5-bromopyridin-2-yl)amino]-4-oxobutanoic acid DB08580, 4-bromo-2-{[(2R)-2-(2-chlorobenzyl)pyrrolidin-1-yl]carbonyl}aniline DB08579, 4-bromo-2-{[(3R,5S)-3,5-dimethylpiperidin-1-yl]carbonyl}aniline DB08481, 4-Methyl-N-[5-(5-methyl-furan-2-ylmethylene)-4-oxo-thiazolidin-2-ylidene]-benzenesulfonamide DB06974, 5-hydroxy-4-(7-methoxy-1,1-dioxido-2H-1,2,4-benzothiadiazin-3-yl)-2-(3-methylbutyl)-6-phenylpyridazin-3(2H)-one DB07169, 5R-(3,4-DICHLOROPHENYLMETHYL)-3-(2-THIOPHENESULFONYLAMINO)-4-OXO-2-THIONOTHIAZOLIDINE DB11586, Asunaprevir DB04137, Guanosine-5'-Triphosphate DB08582, N-(4-bromo-2-{[(3R,5S)-3,5-dimethylpiperidin-1-yl]carbonyl}phenyl)-4-morpholin-4-yl-4-oxobutanamide DB08031, N-[(13-CYCLOHEXYL-6,7-DIHYDROINDOLO[1,2-D][1,4]BENZOXAZEPIN-10-YL)CARBONYL]-2-METHYL-L-ALANINE DB07062, N-{3-[4-Hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyrrolo[1,2-b]pyridazin-3-yl]-1,1-dioxido-2H-1,2,4-benzothiadiazin-7-yl}methanesulfonamide DB07238, Nesbuvir DB04005, Uridine 5'-triphosphate |
DrugCentrali | P26663 |
Protein family/group databases
MEROPSi | S29.001 |
PTM databases
iPTMneti | P26663 |
Protocols and materials databases
ABCDi | P26663, 4 sequenced antibodies |
Organism-specific databases
euHCVdbi | M58335 |
Enzyme and pathway databases
BRENDAi | 3.4.21.98, 17002 |
Miscellaneous databases
EvolutionaryTracei | P26663 |
Family and domain databases
Gene3Di | 1.20.1280.150, 1 hit 2.20.25.210, 1 hit 2.20.25.220, 1 hit 2.30.30.710, 1 hit 2.40.10.10, 1 hit 3.30.70.270, 2 hits 3.40.50.300, 2 hits 4.10.710.10, 1 hit |
InterProi | View protein in InterPro IPR011492, DEAD_Flavivir IPR043502, DNA/RNA_pol_sf IPR002521, HCV_core_C IPR044896, HCV_core_chain_A IPR002522, HCV_core_N IPR002519, HCV_env IPR002531, HCV_NS1 IPR002518, HCV_NS2 IPR042205, HCV_NS2_C IPR042209, HCV_NS2_N IPR000745, HCV_NS4a IPR001490, HCV_NS4b IPR002868, HCV_NS5a IPR013193, HCV_NS5a_1B_dom IPR038568, HCV_NS5A_1B_sf IPR024350, HCV_NS5a_C IPR014001, Helicase_ATP-bd IPR001650, Helicase_C IPR013192, NS5A_1a IPR038170, NS5A_1a_sf IPR027417, P-loop_NTPase IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR004109, Peptidase_S29_NS3 IPR043128, Rev_trsase/Diguanyl_cyclase IPR007094, RNA-dir_pol_PSvirus IPR002166, RNA_pol_HCV |
Pfami | View protein in Pfam PF07652, Flavi_DEAD, 1 hit PF01543, HCV_capsid, 1 hit PF01542, HCV_core, 1 hit PF01539, HCV_env, 1 hit PF01560, HCV_NS1, 1 hit PF01538, HCV_NS2, 1 hit PF01006, HCV_NS4a, 1 hit PF01001, HCV_NS4b, 1 hit PF01506, HCV_NS5a, 1 hit PF08300, HCV_NS5a_1a, 1 hit PF08301, HCV_NS5a_1b, 1 hit PF12941, HCV_NS5a_C, 1 hit PF02907, Peptidase_S29, 1 hit PF00998, RdRP_3, 1 hit |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 2 hits SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51693, HCV_NS2_PRO, 1 hit PS51192, HELICASE_ATP_BIND_1, 1 hit PS51194, HELICASE_CTER, 1 hit PS51822, HV_PV_NS3_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_HCVBK | |
Accessioni | P26663Primary (citable) accession number: P26663 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 225 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families