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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus genotype 2a (isolate JFH-1) (HCV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).By similarity
E1 and E2 glycoproteins form a heterodimer that is involved in virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, but this binding is not sufficient for infection, some additional liver specific cofactors may be needed. The fusion function may possibly be carried by E1. E2 inhibits human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a 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. These interactions allow capture of circulating HCV particles by these cells and subsequent transmission to permissive cells. DCs act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection (By similarity).By similarity
P7 seems to be a heptameric ion channel protein (viroporin) and is inhibited by the antiviral drug amantadine. Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity (By similarity).By similarity
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation (By similarity).By similarity
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS (By similarity).By similarity
NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity).By similarity
NS5A is a component of the replication complex involved in RNA-binding. Its interaction with Human VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. Seems to inhibit apoptosis by interacting with BIN1 and FKBP8. The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity).By similarity
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity

Catalytic activityi

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'.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per NS3 protease domain.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per NS5A N-terminal domain.By similarity

Enzyme regulationi

Activity of auto-protease NS2-3 is dependent on zinc ions and completely inhibited by EDTA. Serine protease NS3 is also activated by zinc ions (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei956For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei976For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei997For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei1087Charge relay system; for serine protease NS3 activityBy similarity1
Active sitei1111Charge relay system; for serine protease NS3 activityBy similarity1
Metal bindingi1127ZincBy similarity1
Metal bindingi1129ZincBy similarity1
Active sitei1169Charge relay system; for serine protease NS3 activityBy similarity1
Metal bindingi1175ZincBy similarity1
Metal bindingi1179ZincBy similarity1
Metal bindingi2015ZincBy similarity1
Metal bindingi2033ZincBy similarity1
Metal bindingi2035ZincBy similarity1
Metal bindingi2056ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1234 – 1241ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, Apoptosis, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, G1/S host cell cycle checkpoint dysregulation by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host TRAFs by virus, Interferon antiviral system evasion, Ion transport, Modulation of host cell cycle by virus, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Viral nucleoprotein, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-5621480. Dectin-2 family.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 11 chains:
Alternative name(s):
Capsid protein C
p21
Alternative name(s):
gp32
gp35
Alternative name(s):
NS1
gp68
gp70
Protease NS2-3 (EC:3.4.22.-)
Short name:
p23
Alternative name(s):
Hepacivirin
NS3P
p70
Alternative name(s):
p8
Alternative name(s):
p27
Alternative name(s):
p56
Alternative name(s):
NS5B
p68
OrganismiHepatitis C virus genotype 2a (isolate JFH-1) (HCV)
Taxonomic identifieri356411 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008096 Componenti: Genome

Subcellular locationi

Core protein p21 :
Core protein p19 :
Envelope glycoprotein E1 :
  • Virion membrane Curated; Single-pass type I membrane protein Curated
  • Host endoplasmic reticulum membrane By similarity; 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. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E1 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.
Envelope glycoprotein E2 :
  • Virion membrane Curated; Single-pass type I membrane protein Curated
  • Host endoplasmic reticulum membrane By similarity; 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. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E2 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.
p7 :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 5A :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 168CytoplasmicSequence analysisAdd BLAST167
Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 358LumenalSequence analysisAdd BLAST169
Transmembranei359 – 379HelicalSequence analysisAdd BLAST21
Topological domaini380 – 729LumenalSequence analysisAdd BLAST350
Transmembranei730 – 750HelicalSequence analysisAdd BLAST21
Topological domaini751 – 761LumenalSequence analysisAdd BLAST11
Transmembranei762 – 782HelicalSequence analysisAdd BLAST21
Topological domaini783 – 786CytoplasmicSequence analysis4
Transmembranei787 – 807HelicalSequence analysisAdd BLAST21
Topological domaini808 – 817LumenalSequence analysis10
Transmembranei818 – 838HelicalSequence analysisAdd BLAST21
Topological domaini839 – 885CytoplasmicSequence analysisAdd BLAST47
Transmembranei886 – 906HelicalSequence analysisAdd BLAST21
Topological domaini907 – 932LumenalSequence analysisAdd BLAST26
Transmembranei933 – 953HelicalSequence analysisAdd BLAST21
Topological domaini954 – 1661CytoplasmicSequence analysisAdd BLAST708
Transmembranei1662 – 1682HelicalSequence analysisAdd BLAST21
Topological domaini1683 – 1809CytoplasmicSequence analysisAdd BLAST127
Transmembranei1810 – 1830HelicalSequence analysisAdd BLAST21
Topological domaini1831 – 1832LumenalSequence analysis2
Transmembranei1833 – 1853HelicalSequence analysisAdd BLAST21
Topological domaini1854CytoplasmicSequence analysis1
Transmembranei1855 – 1875HelicalSequence analysisAdd BLAST21
Topological domaini1876 – 1885LumenalSequence analysis10
Transmembranei1886 – 1906HelicalSequence analysisAdd BLAST21
Topological domaini1907 – 1976CytoplasmicSequence analysisAdd BLAST70
Intramembranei1977 – 2006By similarityAdd BLAST30
Topological domaini2007 – 3012CytoplasmicSequence analysisAdd BLAST1006
Transmembranei3013 – 3033HelicalBy similarityAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endoplasmic reticulum, Host lipid droplet, Host membrane, Host mitochondrion, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

Pathology & Biotechi

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00000455922 – 191Core protein p21Sequence analysisAdd BLAST190
ChainiPRO_00000455932 – 177Core protein p19By similarityAdd BLAST176
PropeptideiPRO_0000045594178 – 191ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityAdd BLAST14
ChainiPRO_0000045595192 – 383Envelope glycoprotein E1Sequence analysisAdd BLAST192
ChainiPRO_0000045596384 – 750Envelope glycoprotein E2Sequence analysisAdd BLAST367
ChainiPRO_0000045597751 – 813p7By similarityAdd BLAST63
ChainiPRO_0000045598814 – 1030Protease NS2-3PROSITE-ProRule annotationAdd BLAST217
ChainiPRO_00000455991031 – 1661Serine protease NS3Sequence analysisAdd BLAST631
ChainiPRO_00000456001662 – 1715Non-structural protein 4ASequence analysisAdd BLAST54
ChainiPRO_00000456011716 – 1976Non-structural protein 4BSequence analysisAdd BLAST261
ChainiPRO_00000456021977 – 2442Non-structural protein 5ASequence analysisAdd BLAST466
ChainiPRO_00000456032443 – 3033RNA-directed RNA polymeraseSequence analysisAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine; by hostBy similarity1
Modified residuei53Phosphoserine; by hostBy similarity1
Modified residuei99Phosphoserine; by hostBy similarity1
Modified residuei116Phosphoserine; by host PKABy similarity1
Glycosylationi196N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi209N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi234N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi305N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi417N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi423N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi430N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi448N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi477N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi534N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi542N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi558N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi578N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi627N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi649N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi1972S-palmitoyl cysteine; by hostBy similarity1
Lipidationi1976S-palmitoyl cysteine; by hostBy similarity1
Disulfide bondi2118 ↔ 2166By similarity
Modified residuei2198Phosphoserine; by host; in p56By similarity1
Modified residuei2201Phosphoserine; by host; in p58By similarity1
Modified residuei2205Phosphoserine; by host; in p58By similarity1
Modified residuei2208Phosphoserine; by host; in p58By similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases. The core protein is synthesized as a 21 kDa precursor which is retained in the ER membrane through the hydrophobic signal peptide. Cleavage by the signal peptidase releases the 19 kDa mature core protein. The other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity).By similarity
Envelope E1 and E2 glycoproteins are highly N-glycosylated.By similarity
Core protein is phosphorylated by host PKC and PKA.By similarity
NS5A is phosphorylated in a basal form termed p56. p58 is a hyperphosphorylated form of p56. p56 and p58 coexist in the cell in roughly equivalent amounts. Hyperphosphorylation is dependent on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1, MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for NS5A phosphorylation (By similarity).By similarity
NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions (By similarity).By similarity
The N-terminus of a fraction of NS4B molecules seems to be relocated post-translationally from the cytoplasm to the ER lumen, with a 5th transmembrane segment. The C-terminus of NS2 may be lumenal with a fourth transmembrane segment (By similarity).By similarity
Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei177 – 178Cleavage; by host signal peptidaseBy similarity2
Sitei191 – 192Cleavage; by host signal peptidaseSequence analysis2
Sitei383 – 384Cleavage; by host signal peptidaseSequence analysis2
Sitei750 – 751Cleavage; by host signal peptidaseBy similarity2
Sitei813 – 814Cleavage; by host signal peptidaseBy similarity2
Sitei1030 – 1031Cleavage; by protease NS2-3PROSITE-ProRule annotation2
Sitei1661 – 1662Cleavage; by serine protease NS3Sequence analysis2
Sitei1715 – 1716Cleavage; by serine protease NS3Sequence analysis2
Sitei1976 – 1977Cleavage; by serine protease NS3Sequence analysis2
Sitei2442 – 2443Cleavage; by serine protease NS3Sequence analysis2

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Core protein is a homomultimer that binds the C-terminal part of E1 and interacts with numerous cellular proteins. Interaction with human STAT1 SH2 domain seems to result in decreased STAT1 phosphorylation, leading to decreased IFN-stimulated gene transcription. In addition to blocking the formation of phosphorylated STAT1, the core protein also promotes ubiquitin-mediated proteasome-dependent degradation of STAT1. Interacts with, and constitutively activates human STAT3. Associates with human LTBR and TNFRSF1A receptors and possibly induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK, C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins. Interacts with human CREB3 nuclear transcription protein, triggering cell transformation. May interact with human p53. Also binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). E1 and E2 glycoproteins form a heterodimer that binds to human LDLR, CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR. p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing a pair of composite active sites at the dimerization interface. NS2 seems to interact with all other non-structural (NS) proteins. NS4A interacts with NS3 serine protease and stabilizes its folding. NS3-NS4A complex is essential for the activation of the latter and allows membrane anchorage of NS3. NS3 interacts with human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form homodimers and seem to interact with all other non-structural (NS) proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2, BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P279583EBI-6858513,EBI-8753518From a different organism.
ADARP552653EBI-6858501,EBI-2462104From a different organism.
AFPP027712EBI-6901449,EBI-722498From a different organism.
ANXA2P073555EBI-6927873,EBI-352622From a different organism.
CD81P600332EBI-6901449,EBI-712921From a different organism.
CYB5BO431695EBI-6928570,EBI-1058710From a different organism.
DDX3XO005719EBI-6674379,EBI-353779From a different organism.
DGAT1O759072EBI-6927873,EBI-3906527From a different organism.
FASNP493276EBI-6927928,EBI-356658From a different organism.
FN1P027513EBI-6927928,EBI-1220319From a different organism.
GORASP2Q9H8Y83EBI-6927928,EBI-739467From a different organism.
HACD3Q9P0352EBI-6927873,EBI-359013From a different organism.
HSPA8P111423EBI-6927928,EBI-351896From a different organism.
MAP3K11Q165845EBI-6927873,EBI-49961From a different organism.
MYCBP2O755923EBI-6927928,EBI-1043774From a different organism.
NUCB1Q028183EBI-6927928,EBI-2622179From a different organism.
OPTNQ96CV93EBI-6858501,EBI-748974From a different organism.
PARK2O602603EBI-6858513,EBI-716346From a different organism.
PI4KAP423565EBI-6927873,EBI-723050From a different organism.
PLK1P533504EBI-6927873,EBI-476768From a different organism.
PPIAP629372EBI-6927873,EBI-437708From a different organism.
PYM1Q9BRP84EBI-6858513,EBI-2352802From a different organism.
RAB18Q9NP725EBI-6927873,EBI-722247From a different organism.
RLFQ131292EBI-6927928,EBI-958266From a different organism.
SMC1AQ146833EBI-6927928,EBI-80690From a different organism.
SPCS1Q9Y6A94EBI-6901449,EBI-8852196From a different organism.
SSBP054552EBI-6858501,EBI-358037From a different organism.
TGFBR1P368975EBI-6858501,EBI-1027557From a different organism.
TMEM173Q86WV65EBI-6928570,EBI-2800345From a different organism.
VAPAQ9P0L03EBI-9096996,EBI-1059156From a different organism.
VAPBO952922EBI-9096996,EBI-1188298From a different organism.
WBP11Q9Y2W23EBI-6927928,EBI-714455From a different organism.

GO - Molecular functioni

  • transforming growth factor beta receptor binding Source: AgBase
  • ubiquitin protein ligase binding Source: AgBase

Protein-protein interaction databases

DIPiDIP-48925N.
IntActiQ99IB8. 345 interactors.
MINTiMINT-8361175.

Chemistry databases

BindingDBiQ99IB8.

Structurei

Secondary structure

13033
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi175 – 185Combined sources11
Helixi189 – 194Combined sources6
Helixi692 – 701Combined sources10
Turni702 – 706Combined sources5
Helixi710 – 714Combined sources5
Turni715 – 718Combined sources4
Helixi1719 – 1748Combined sources30
Beta strandi2444 – 2448Combined sources5
Helixi2467 – 2470Combined sources4
Helixi2476 – 2478Combined sources3
Beta strandi2479 – 2481Combined sources3
Helixi2484 – 2486Combined sources3
Helixi2487 – 2494Combined sources8
Helixi2504 – 2517Combined sources14
Helixi2527 – 2532Combined sources6
Turni2542 – 2544Combined sources3
Helixi2547 – 2552Combined sources6
Helixi2557 – 2570Combined sources14
Beta strandi2572 – 2574Combined sources3
Beta strandi2578 – 2582Combined sources5
Beta strandi2586 – 2588Combined sources3
Helixi2591 – 2593Combined sources3
Beta strandi2601 – 2604Combined sources4
Helixi2607 – 2629Combined sources23
Helixi2630 – 2632Combined sources3
Helixi2634 – 2636Combined sources3
Helixi2639 – 2651Combined sources13
Beta strandi2653 – 2663Combined sources11
Helixi2666 – 2669Combined sources4
Helixi2672 – 2684Combined sources13
Helixi2689 – 2701Combined sources13
Turni2702 – 2704Combined sources3
Beta strandi2706 – 2709Combined sources4
Beta strandi2715 – 2719Combined sources5
Helixi2729 – 2748Combined sources20
Beta strandi2754 – 2758Combined sources5
Beta strandi2761 – 2767Combined sources7
Helixi2771 – 2787Combined sources17
Beta strandi2792 – 2794Combined sources3
Beta strandi2799 – 2801Combined sources3
Helixi2802 – 2804Combined sources3
Beta strandi2810 – 2816Combined sources7
Helixi2818 – 2820Combined sources3
Beta strandi2822 – 2828Combined sources7
Helixi2831 – 2842Combined sources12
Beta strandi2846 – 2849Combined sources4
Helixi2850 – 2856Combined sources7
Turni2857 – 2859Combined sources3
Helixi2861 – 2865Combined sources5
Helixi2867 – 2878Combined sources12
Beta strandi2881 – 2883Combined sources3
Beta strandi2885 – 2889Combined sources5
Beta strandi2892 – 2896Combined sources5
Helixi2898 – 2900Combined sources3
Helixi2901 – 2909Combined sources9
Helixi2911 – 2914Combined sources4
Helixi2921 – 2934Combined sources14
Helixi2939 – 2955Combined sources17
Helixi2958 – 2967Combined sources10
Helixi2969 – 2971Combined sources3
Beta strandi2972 – 2974Combined sources3
Helixi2982 – 2986Combined sources5
Helixi2992 – 2996Combined sources5
Helixi2998 – 3000Combined sources3
Beta strandi3003 – 3005Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZQNMR-A684-719[»]
2LIFNMR-A171-195[»]
2LVGNMR-A1716-1755[»]
2XXDX-ray1.88A2443-3005[»]
2XYMX-ray1.77A2443-3005[»]
3I5KX-ray2.20A/B/C/D2443-3007[»]
4AEPX-ray1.80A2443-3013[»]
4AEXX-ray2.41A/B2443-3013[»]
4E76X-ray2.50A2443-2885[»]
A2896-3012[»]
4E78X-ray2.90A2443-2885[»]
A2896-3012[»]
4E7AX-ray3.00A2443-2885[»]
A2896-3012[»]
4J1VX-ray1.95E/F/G/H2284-2303[»]
4OBCX-ray2.50A2443-3012[»]
4WT9X-ray2.50A2443-2885[»]
A2896-3012[»]
4WTAX-ray2.80A2443-2885[»]
A2896-3012[»]
4WTCX-ray2.75A2443-2885[»]
A2896-3012[»]
4WTDX-ray2.70A2443-2885[»]
A2896-3012[»]
4WTEX-ray2.90A2443-2885[»]
A2896-3012[»]
4WTFX-ray2.65A2443-2885[»]
A2896-3012[»]
4WTGX-ray2.90A2443-2885[»]
A2896-3012[»]
4WTIX-ray2.80A2443-3012[»]
4WTJX-ray2.20A2443-3012[»]
4WTKX-ray2.50A2443-3012[»]
4WTLX-ray2.00A2443-3012[»]
4WTMX-ray2.15A2443-3012[»]
ProteinModelPortaliQ99IB8.
SMRiQ99IB8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99IB8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini907 – 1030Peptidase C18PROSITE-ProRule annotationAdd BLAST124
Domaini1221 – 1373Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini2656 – 2774RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 59Interaction with DDX3XBy similarityAdd BLAST58
Regioni2 – 23Interaction with STAT1By similarityAdd BLAST22
Regioni122 – 173Interaction with APOA2By similarityAdd BLAST52
Regioni150 – 159Mitochondrial targeting signalBy similarity10
Regioni164 – 167Important for lipid droplets localizationBy similarity4
Regioni265 – 296Fusion peptideSequence analysisAdd BLAST32
Regioni385 – 411HVR1By similarityAdd BLAST27
Regioni484 – 496CD81-binding 1Sequence analysisAdd BLAST13
Regioni524 – 555CD81-binding 2Sequence analysisAdd BLAST32
Regioni664 – 675PKR/eIF2-alpha phosphorylation homology domain (PePHD)By similarityAdd BLAST12
Regioni1683 – 1694NS3-binding (by NS4A)Sequence analysisAdd BLAST12
Regioni2124 – 2332Transcriptional activationSequence analysisAdd BLAST209
Regioni2124 – 2212FKBP8-bindingSequence analysisAdd BLAST89
Regioni2204 – 2250Basal phosphorylationBy similarityAdd BLAST47
Regioni2214 – 2275PKR-bindingSequence analysisAdd BLAST62
Regioni2249 – 2306NS4B-bindingSequence analysisAdd BLAST58
Regioni2351 – 2442Basal phosphorylationBy similarityAdd BLAST92

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi5 – 13Nuclear localization signalSequence analysis9
Motifi38 – 43Nuclear localization signalSequence analysis6
Motifi58 – 64Nuclear localization signalSequence analysis7
Motifi66 – 71Nuclear localization signalSequence analysis6
Motifi1320 – 1323DECH boxBy similarity4
Motifi2322 – 2325SH3-bindingSequence analysis4
Motifi2327 – 2335Nuclear localization signalSequence analysis9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1436 – 1439Poly-Val4
Compositional biasi2277 – 2327Pro-richAdd BLAST51
Compositional biasi2328 – 2331Poly-Arg4
Compositional biasi3018 – 3021Poly-Leu4

Domaini

The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins. Envelope E2 glycoprotein contain a highly variable region called hypervariable region 1 (HVR1). E2 also contains two segments involved in CD81-binding. HVR1 is implicated in the SCARB1-mediated cell entry. CD81-binding regions may be involved in sensitivity and/or resistance to IFN-alpha therapy (By similarity).By similarity
The N-terminus of NS5A acts as membrane anchor. The central part of NS5A seems to be intrinsically disordered and interacts with NS5B and host PKR (By similarity).By similarity
The SH3-binding domain of NS5A is involved in the interaction with human Bin1, GRB2 and Src-family kinases.By similarity
The N-terminal one-third of serine protease NS3 contains the protease activity. This region contains a zinc atom that does not belong to the active site, but may play a structural rather than a catalytic role. This region is essential for the activity of protease NS2-3, maybe by contributing to the folding of the latter. The helicase activity is located in the C-terminus of NS3 (By similarity).By similarity

Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 peptidase C18 domain.PROSITE-ProRule annotation
Contains 1 peptidase S29 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
IPR002518. HCV_NS2.
IPR000745. HCV_NS4a.
IPR001490. HCV_NS4b.
IPR002868. HCV_NS5a.
IPR013193. HCV_NS5a_1B_dom.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
[Graphical view]
PfamiPF07652. 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.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99IB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPE DVKFPGGGQI VGGVYLLPRR GPRLGVRTTR
60 70 80 90 100
KTSERSQPRG RRQPIPKDRR STGKAWGKPG RPWPLYGNEG LGWAGWLLSP
110 120 130 140 150
RGSRPSWGPT DPRHRSRNVG KVIDTLTCGF ADLMGYIPVV GAPLSGAARA
160 170 180 190 200
VAHGVRVLED GVNYATGNLP GFPFSIFLLA LLSCITVPVS AAQVKNTSSS
210 220 230 240 250
YMVTNDCSND SITWQLEAAV LHVPGCVPCE RVGNTSRCWV PVSPNMAVRQ
260 270 280 290 300
PGALTQGLRT HIDMVVMSAT FCSALYVGDL CGGVMLAAQV FIVSPQYHWF
310 320 330 340 350
VQECNCSIYP GTITGHRMAW DMMMNWSPTA TMILAYVMRV PEVIIDIVSG
360 370 380 390 400
AHWGVMFGLA YFSMQGAWAK VIVILLLAAG VDAGTTTVGG AVARSTNVIA
410 420 430 440 450
GVFSHGPQQN IQLINTNGSW HINRTALNCN DSLNTGFLAA LFYTNRFNSS
460 470 480 490 500
GCPGRLSACR NIEAFRIGWG TLQYEDNVTN PEDMRPYCWH YPPKPCGVVP
510 520 530 540 550
ARSVCGPVYC FTPSPVVVGT TDRRGVPTYT WGENETDVFL LNSTRPPQGS
560 570 580 590 600
WFGCTWMNST GFTKTCGAPP CRTRADFNAS TDLLCPTDCF RKHPDATYIK
610 620 630 640 650
CGSGPWLTPK CLVHYPYRLW HYPCTVNFTI FKIRMYVGGV EHRLTAACNF
660 670 680 690 700
TRGDRCDLED RDRSQLSPLL HSTTEWAILP CTYSDLPALS TGLLHLHQNI
710 720 730 740 750
VDVQYMYGLS PAITKYVVRW EWVVLLFLLL ADARVCACLW MLILLGQAEA
760 770 780 790 800
ALEKLVVLHA ASAANCHGLL YFAIFFVAAW HIRGRVVPLT TYCLTGLWPF
810 820 830 840 850
CLLLMALPRQ AYAYDAPVHG QIGVGLLILI TLFTLTPGYK TLLGQCLWWL
860 870 880 890 900
CYLLTLGEAM IQEWVPPMQV RGGRDGIAWA VTIFCPGVVF DITKWLLALL
910 920 930 940 950
GPAYLLRAAL THVPYFVRAH ALIRVCALVK QLAGGRYVQV ALLALGRWTG
960 970 980 990 1000
TYIYDHLTPM SDWAASGLRD LAVAVEPIIF SPMEKKVIVW GAETAACGDI
1010 1020 1030 1040 1050
LHGLPVSARL GQEILLGPAD GYTSKGWKLL APITAYAQQT RGLLGAIVVS
1060 1070 1080 1090 1100
MTGRDRTEQA GEVQILSTVS QSFLGTTISG VLWTVYHGAG NKTLAGLRGP
1110 1120 1130 1140 1150
VTQMYSSAEG DLVGWPSPPG TKSLEPCKCG AVDLYLVTRN ADVIPARRRG
1160 1170 1180 1190 1200
DKRGALLSPR PISTLKGSSG GPVLCPRGHV VGLFRAAVCS RGVAKSIDFI
1210 1220 1230 1240 1250
PVETLDVVTR SPTFSDNSTP PAVPQTYQVG YLHAPTGSGK STKVPVAYAA
1260 1270 1280 1290 1300
QGYKVLVLNP SVAATLGFGA YLSKAHGINP NIRTGVRTVM TGEAITYSTY
1310 1320 1330 1340 1350
GKFLADGGCA SGAYDIIICD ECHAVDATSI LGIGTVLDQA ETAGVRLTVL
1360 1370 1380 1390 1400
ATATPPGSVT TPHPDIEEVG LGREGEIPFY GRAIPLSCIK GGRHLIFCHS
1410 1420 1430 1440 1450
KKKCDELAAA LRGMGLNAVA YYRGLDVSII PAQGDVVVVA TDALMTGYTG
1460 1470 1480 1490 1500
DFDSVIDCNV AVTQAVDFSL DPTFTITTQT VPQDAVSRSQ RRGRTGRGRQ
1510 1520 1530 1540 1550
GTYRYVSTGE RASGMFDSVV LCECYDAGAA WYDLTPAETT VRLRAYFNTP
1560 1570 1580 1590 1600
GLPVCQDHLE FWEAVFTGLT HIDAHFLSQT KQAGENFAYL VAYQATVCAR
1610 1620 1630 1640 1650
AKAPPPSWDA MWKCLARLKP TLAGPTPLLY RLGPITNEVT LTHPGTKYIA
1660 1670 1680 1690 1700
TCMQADLEVM TSTWVLAGGV LAAVAAYCLA TGCVSIIGRL HVNQRVVVAP
1710 1720 1730 1740 1750
DKEVLYEAFD EMEECASRAA LIEEGQRIAE MLKSKIQGLL QQASKQAQDI
1760 1770 1780 1790 1800
QPAMQASWPK VEQFWARHMW NFISGIQYLA GLSTLPGNPA VASMMAFSAA
1810 1820 1830 1840 1850
LTSPLSTSTT ILLNIMGGWL ASQIAPPAGA TGFVVSGLVG AAVGSIGLGK
1860 1870 1880 1890 1900
VLVDILAGYG AGISGALVAF KIMSGEKPSM EDVINLLPGI LSPGALVVGV
1910 1920 1930 1940 1950
ICAAILRRHV GPGEGAVQWM NRLIAFASRG NHVAPTHYVT ESDASQRVTQ
1960 1970 1980 1990 2000
LLGSLTITSL LRRLHNWITE DCPIPCSGSW LRDVWDWVCT ILTDFKNWLT
2010 2020 2030 2040 2050
SKLFPKLPGL PFISCQKGYK GVWAGTGIMT TRCPCGANIS GNVRLGSMRI
2060 2070 2080 2090 2100
TGPKTCMNTW QGTFPINCYT EGQCAPKPPT NYKTAIWRVA ASEYAEVTQH
2110 2120 2130 2140 2150
GSYSYVTGLT TDNLKIPCQL PSPEFFSWVD GVQIHRFAPT PKPFFRDEVS
2160 2170 2180 2190 2200
FCVGLNSYAV GSQLPCEPEP DADVLRSMLT DPPHITAETA ARRLARGSPP
2210 2220 2230 2240 2250
SEASSSVSQL SAPSLRATCT THSNTYDVDM VDANLLMEGG VAQTEPESRV
2260 2270 2280 2290 2300
PVLDFLEPMA EEESDLEPSI PSECMLPRSG FPRALPAWAR PDYNPPLVES
2310 2320 2330 2340 2350
WRRPDYQPPT VAGCALPPPK KAPTPPPRRR RTVGLSESTI SEALQQLAIK
2360 2370 2380 2390 2400
TFGQPPSSGD AGSSTGAGAA ESGGPTSPGE PAPSETGSAS SMPPLEGEPG
2410 2420 2430 2440 2450
DPDLESDQVE LQPPPQGGGV APGSGSGSWS TCSEEDDTTV CCSMSYSWTG
2460 2470 2480 2490 2500
ALITPCSPEE EKLPINPLSN SLLRYHNKVY CTTSKSASQR AKKVTFDRTQ
2510 2520 2530 2540 2550
VLDAHYDSVL KDIKLAASKV SARLLTLEEA CQLTPPHSAR SKYGFGAKEV
2560 2570 2580 2590 2600
RSLSGRAVNH IKSVWKDLLE DPQTPIPTTI MAKNEVFCVD PAKGGKKPAR
2610 2620 2630 2640 2650
LIVYPDLGVR VCEKMALYDI TQKLPQAVMG ASYGFQYSPA QRVEYLLKAW
2660 2670 2680 2690 2700
AEKKDPMGFS YDTRCFDSTV TERDIRTEES IYQACSLPEE ARTAIHSLTE
2710 2720 2730 2740 2750
RLYVGGPMFN SKGQTCGYRR CRASGVLTTS MGNTITCYVK ALAACKAAGI
2760 2770 2780 2790 2800
VAPTMLVCGD DLVVISESQG TEEDERNLRA FTEAMTRYSA PPGDPPRPEY
2810 2820 2830 2840 2850
DLELITSCSS NVSVALGPRG RRRYYLTRDP TTPLARAAWE TVRHSPINSW
2860 2870 2880 2890 2900
LGNIIQYAPT IWVRMVLMTH FFSILMVQDT LDQNLNFEMY GSVYSVNPLD
2910 2920 2930 2940 2950
LPAIIERLHG LDAFSMHTYS HHELTRVASA LRKLGAPPLR VWKSRARAVR
2960 2970 2980 2990 3000
ASLISRGGKA AVCGRYLFNW AVKTKLKLTP LPEARLLDLS SWFTVGAGGG
3010 3020 3030
DIFHSVSRAR PRSLLFGLLL LFVGVGLFLL PAR
Length:3,033
Mass (Da):328,828
Last modified:January 23, 2007 - v3
Checksum:i7E5BEA79702AF95B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047639 Genomic RNA. Translation: BAB32872.1.

Cross-referencesi

Web resourcesi

euHCVdb

The European HCV database

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047639 Genomic RNA. Translation: BAB32872.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZQNMR-A684-719[»]
2LIFNMR-A171-195[»]
2LVGNMR-A1716-1755[»]
2XXDX-ray1.88A2443-3005[»]
2XYMX-ray1.77A2443-3005[»]
3I5KX-ray2.20A/B/C/D2443-3007[»]
4AEPX-ray1.80A2443-3013[»]
4AEXX-ray2.41A/B2443-3013[»]
4E76X-ray2.50A2443-2885[»]
A2896-3012[»]
4E78X-ray2.90A2443-2885[»]
A2896-3012[»]
4E7AX-ray3.00A2443-2885[»]
A2896-3012[»]
4J1VX-ray1.95E/F/G/H2284-2303[»]
4OBCX-ray2.50A2443-3012[»]
4WT9X-ray2.50A2443-2885[»]
A2896-3012[»]
4WTAX-ray2.80A2443-2885[»]
A2896-3012[»]
4WTCX-ray2.75A2443-2885[»]
A2896-3012[»]
4WTDX-ray2.70A2443-2885[»]
A2896-3012[»]
4WTEX-ray2.90A2443-2885[»]
A2896-3012[»]
4WTFX-ray2.65A2443-2885[»]
A2896-3012[»]
4WTGX-ray2.90A2443-2885[»]
A2896-3012[»]
4WTIX-ray2.80A2443-3012[»]
4WTJX-ray2.20A2443-3012[»]
4WTKX-ray2.50A2443-3012[»]
4WTLX-ray2.00A2443-3012[»]
4WTMX-ray2.15A2443-3012[»]
ProteinModelPortaliQ99IB8.
SMRiQ99IB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48925N.
IntActiQ99IB8. 345 interactors.
MINTiMINT-8361175.

Chemistry databases

BindingDBiQ99IB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

euHCVdbiAB047639.

Enzyme and pathway databases

ReactomeiR-HSA-5621480. Dectin-2 family.

Miscellaneous databases

EvolutionaryTraceiQ99IB8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
IPR002518. HCV_NS2.
IPR000745. HCV_NS4a.
IPR001490. HCV_NS4b.
IPR002868. HCV_NS5a.
IPR013193. HCV_NS5a_1B_dom.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
[Graphical view]
PfamiPF07652. 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.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_HCVJF
AccessioniPrimary (citable) accession number: Q99IB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Cell culture adaptation of the virus leads to mutations in NS5A, reducing its inhibitory effect on replication.By similarity
Core protein exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding.By similarity

Caution

The core gene probably also codes for alternative reading frame proteins (ARFPs). Many functions depicted for the core protein might belong to the ARFPs.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.