Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Genome polyprotein

Gene
N/A
Organism
Kunjin virus (strain MRM61C)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.By similarity
prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated.By similarity
Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes.By similarity
Non-structural protein 1 is involved in virus replication and regulation of the innate immune response.By similarity
Non-structural protein 2A may be involved viral RNA replication and capsid assembly.Curated
Non-structural protein 2B is a required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).PROSITE-ProRule annotation
Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase.By similarity
Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.By similarity
RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.PROSITE-ProRule annotation4 Publications

Catalytic activityi

Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1556Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1580Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1640Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2541mRNA capPROSITE-ProRule annotation1
Binding sitei2544mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2545mRNA capPROSITE-ProRule annotation1
Binding sitei2547mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2552mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2556mRNA capPROSITE-ProRule annotation1
Binding sitei2584S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2589Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2614S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2632S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2633S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2659S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2660S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2674Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2675S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2678mRNA capPROSITE-ProRule annotation1
Sitei2710Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2741mRNA capPROSITE-ProRule annotation1
Binding sitei2743mRNA capPROSITE-ProRule annotation1
Sitei2746Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2748S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1699 – 1706ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

Keywords - Biological processi

Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host JAK1 by virus, Inhibition of host TYK2 by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, 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, S-adenosyl-L-methionine

Protein family/group databases

MEROPSiS07.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
NS5
OrganismiKunjin virus (strain MRM61C)
Taxonomic identifieri11078 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostiCiconiiformes [TaxID: 8920]
Culex annulirostris (Common banded mosquito) [TaxID: 162997]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008379 Componenti: Genome

Subcellular locationi

Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation

  • Note: Remains non-covalently associated to NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 105CytoplasmicSequence analysisAdd BLAST104
Transmembranei106 – 126HelicalSequence analysisAdd BLAST21
Topological domaini127 – 248ExtracellularSequence analysisAdd BLAST122
Transmembranei249 – 269HelicalSequence analysisAdd BLAST21
Topological domaini270 – 273CytoplasmicSequence analysis4
Transmembranei274 – 290HelicalSequence analysisAdd BLAST17
Topological domaini291 – 743ExtracellularSequence analysisAdd BLAST453
Intramembranei744 – 763HelicalSequence analysisAdd BLAST20
Topological domaini764 – 770ExtracellularSequence analysis7
Intramembranei771 – 791HelicalSequence analysisAdd BLAST21
Topological domaini792 – 1142ExtracellularSequence analysisAdd BLAST351
Transmembranei1143 – 1163HelicalSequence analysisAdd BLAST21
Topological domaini1164 – 1216CytoplasmicSequence analysisAdd BLAST53
Transmembranei1217 – 1237HelicalSequence analysisAdd BLAST21
Topological domaini1238 – 1247LumenalSequence analysis10
Transmembranei1248 – 1268HelicalSequence analysisAdd BLAST21
Topological domaini1269 – 1296CytoplasmicSequence analysisAdd BLAST28
Transmembranei1297 – 1317HelicalSequence analysisAdd BLAST21
Topological domaini1318 – 1344LumenalSequence analysisAdd BLAST27
Transmembranei1345 – 1365HelicalSequence analysisAdd BLAST21
Topological domaini1366 – 1375CytoplasmicSequence analysis10
Transmembranei1376 – 1396HelicalSequence analysisAdd BLAST21
Topological domaini1397 – 1399LumenalSequence analysis3
Transmembranei1400 – 1420HelicalSequence analysisAdd BLAST21
Topological domaini1421 – 1477CytoplasmicSequence analysisAdd BLAST57
Intramembranei1478 – 1498HelicalSequence analysisAdd BLAST21
Topological domaini1499 – 2174CytoplasmicSequence analysisAdd BLAST676
Topological domaini2196 – 2200LumenalSequence analysis5
Intramembranei2201 – 2221HelicalSequence analysisAdd BLAST21
Topological domaini2222LumenalSequence analysis1
Topological domaini2244 – 2258CytoplasmicSequence analysisAdd BLAST15
Transmembranei2259 – 2279Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2280 – 2312LumenalSequence analysisAdd BLAST33
Intramembranei2313 – 2333HelicalSequence analysisAdd BLAST21
Topological domaini2334 – 2358LumenalSequence analysisAdd BLAST25
Intramembranei2359 – 2379HelicalSequence analysisAdd BLAST21
Topological domaini2380LumenalSequence analysis1
Transmembranei2381 – 2401HelicalSequence analysisAdd BLAST21
Topological domaini2402 – 2444CytoplasmicSequence analysisAdd BLAST43
Transmembranei2445 – 2465HelicalSequence analysisAdd BLAST21
Topological domaini2466 – 2470LumenalSequence analysis5
Transmembranei2471 – 2491HelicalSequence analysisAdd BLAST21
Topological domaini2492 – 3433CytoplasmicSequence analysisAdd BLAST942

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1292T → P: Restores induction of virus-specific membrane structures; when associated with N-1202. 1 Publication1
Mutagenesisi3181S → F: Increases STAT1 inhibitory function of NS5. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedSequence analysis
ChainiPRO_00004051362 – 3433Genome polyproteinAdd BLAST3432
ChainiPRO_00000377032 – 105Capsid protein CBy similarityAdd BLAST104
PropeptideiPRO_0000405137106 – 123ER anchor for the protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000405138124 – 290prMBy similarityAdd BLAST167
ChainiPRO_0000037704124 – 215Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037705216 – 290Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037706291 – 791Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037707792 – 1143Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377081144 – 1374Non-structural protein 2ABy similarityAdd BLAST231
ChainiPRO_00000377091375 – 1505Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377101506 – 2124Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000377112125 – 2250Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051392251 – 2273Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000377122274 – 2528Non-structural protein 4BBy similarityAdd BLAST255
ChainiPRO_00000377132529 – 3433RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi293 ↔ 320By similarity
Disulfide bondi350 ↔ 406By similarity
Disulfide bondi364 ↔ 395By similarity
Disulfide bondi382 ↔ 411By similarity
Disulfide bondi480 ↔ 578By similarity
Disulfide bondi595 ↔ 626By similarity
Glycosylationi921N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi966N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi998N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral protease NS3 and host cell enzymes yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature soluble protein C is released after cleavage by NS3 protease at a site upstream of this hydrophobic domain. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS3Sequence analysis2
Sitei123 – 124Cleavage; by host signal peptidaseBy similarity2
Sitei215 – 216Cleavage; by host furinSequence analysis2
Sitei290 – 291Cleavage; by host signal peptidaseSequence analysis2
Sitei791 – 792Cleavage; by host signal peptidaseSequence analysis2
Sitei1143 – 1144Cleavage; by hostSequence analysis2
Sitei1374 – 1375Cleavage; by viral protease NS3Sequence analysis2
Sitei1505 – 1506Cleavage; by autolysisSequence analysis2
Sitei2124 – 2125Cleavage; by autolysisSequence analysis2
Sitei2250 – 2251Cleavage; by viral protease NS3Sequence analysis2
Sitei2273 – 2274Cleavage; by host signal peptidaseSequence analysis2
Sitei2528 – 2529Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PeptideAtlasiP14335.

Interactioni

Subunit structurei

Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity.By similarity

Protein-protein interaction databases

IntActiP14335. 37 interactors.

Structurei

Secondary structure

13433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 38Combined sources13
Helixi44 – 56Combined sources13
Helixi63 – 69Combined sources7
Helixi74 – 95Combined sources22
Beta strandi1694 – 1697Combined sources4
Turni1703 – 1708Combined sources6
Helixi1709 – 1719Combined sources11
Beta strandi1724 – 1730Combined sources7
Helixi1731 – 1740Combined sources10
Beta strandi1763 – 1767Combined sources5
Helixi1768 – 1776Combined sources9
Beta strandi1777 – 1779Combined sources3
Beta strandi1785 – 1791Combined sources7
Helixi1797 – 1811Combined sources15
Beta strandi1816 – 1820Combined sources5
Beta strandi1839 – 1842Combined sources4
Beta strandi1851 – 1853Combined sources3
Helixi1855 – 1859Combined sources5
Beta strandi1864 – 1867Combined sources4
Helixi1871 – 1883Combined sources13
Beta strandi1888 – 1891Combined sources4
Beta strandi1909 – 1914Combined sources6
Beta strandi1926 – 1930Combined sources5
Beta strandi1937 – 1944Combined sources8
Beta strandi1946 – 1949Combined sources4
Helixi1957 – 1964Combined sources8
Beta strandi1977 – 1980Combined sources4
Helixi1992 – 2002Combined sources11
Helixi2007 – 2009Combined sources3
Helixi2016 – 2021Combined sources6
Turni2026 – 2029Combined sources4
Helixi2034 – 2044Combined sources11
Helixi2050 – 2058Combined sources9
Helixi2066 – 2069Combined sources4
Helixi2074 – 2076Combined sources3
Beta strandi2079 – 2084Combined sources6
Beta strandi2086 – 2088Combined sources3
Beta strandi2094 – 2096Combined sources3
Beta strandi2100 – 2103Combined sources4
Helixi2104 – 2106Combined sources3
Helixi2110 – 2121Combined sources12
Helixi2808 – 2815Combined sources8
Turni2819 – 2821Combined sources3
Beta strandi2831 – 2840Combined sources10
Helixi2853 – 2857Combined sources5
Helixi2860 – 2862Combined sources3
Turni2870 – 2872Combined sources3
Helixi2878 – 2885Combined sources8
Helixi2898 – 2915Combined sources18
Turni2916 – 2918Combined sources3
Helixi2926 – 2934Combined sources9
Helixi2951 – 2957Combined sources7
Helixi2959 – 2974Combined sources16
Helixi3004 – 3019Combined sources16
Helixi3021 – 3024Combined sources4
Turni3025 – 3028Combined sources4
Helixi3030 – 3033Combined sources4
Beta strandi3034 – 3036Combined sources3
Helixi3042 – 3052Combined sources11
Beta strandi3055 – 3058Combined sources4
Beta strandi3065 – 3067Combined sources3
Helixi3068 – 3070Combined sources3
Helixi3074 – 3080Combined sources7
Helixi3081 – 3086Combined sources6
Helixi3089 – 3099Combined sources11
Turni3100 – 3103Combined sources4
Beta strandi3104 – 3113Combined sources10
Helixi3115 – 3117Combined sources3
Beta strandi3119 – 3128Combined sources10
Helixi3134 – 3156Combined sources23
Beta strandi3164 – 3167Combined sources4
Helixi3172 – 3188Combined sources17
Beta strandi3191 – 3194Combined sources4
Beta strandi3197 – 3200Combined sources4
Helixi3205 – 3209Combined sources5
Helixi3212 – 3216Combined sources5
Turni3236 – 3238Combined sources3
Beta strandi3244 – 3250Combined sources7
Beta strandi3256 – 3261Combined sources6
Helixi3264 – 3271Combined sources8
Beta strandi3275 – 3278Combined sources4
Helixi3282 – 3298Combined sources17
Helixi3303 – 3315Combined sources13
Beta strandi3338 – 3340Combined sources3
Helixi3342 – 3350Combined sources9
Turni3351 – 3353Combined sources3
Helixi3366 – 3368Combined sources3
Helixi3374 – 3379Combined sources6
Helixi3387 – 3394Combined sources8
Helixi3396 – 3407Combined sources12
Helixi3416 – 3418Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SFKX-ray3.20A/B/C/D/E/F/G/H23-98[»]
2HCNX-ray2.35A2846-3433[»]
2HCSX-ray2.50A2846-3433[»]
2HFZX-ray3.00A2802-3433[»]
2OF6electron microscopy24.00A/B/C291-690[»]
2QEQX-ray3.10A/B1691-2124[»]
ProteinModelPortaliP14335.
SMRiP14335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14335.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1506 – 1683Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1686 – 1842Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1853 – 2018Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2529 – 2794mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3058 – 3210RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni388 – 401Involved in fusionAdd BLAST14
Regioni1428 – 1467Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1790 – 1793DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi281 – 284Poly-Leu4
Compositional biasi2678 – 2681Poly-Ser4

Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR026490. mRNA_cap_0/1_MeTrfase.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPGGPGK SRAVNMLKRG MPRVLSLTGL KRAMLSLIDG RGPTRFVLAL
60 70 80 90 100
LAFFRFTAIA PTRAVLDRWR SVNKQTAMKH LLSFKKELGT LTSAINRRSS
110 120 130 140 150
KQKKRGGKTG IAFMIGLIAG VGAVTLSNFQ GKVMMTVNAT DVTDIITIPP
160 170 180 190 200
AAGKNLCIVR AMDVGHMCDD TITYECPVLS AGNDPEDIDC WCTKLAVYVR
210 220 230 240 250
YGRCTKTRHS RRSRRSLTVQ THGESTLSNK KGAWMDSTKA TRYLVKTESW
260 270 280 290 300
ILRNPGYALV AAVIGWMLGS NTMQRVVFAV LLLLVAPAYS FNCLGMSNRD
310 320 330 340 350
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC
360 370 380 390 400
YLATVSELST KAACPTMGEA HNDKRADPSF VCKQGVVDRG WGNGCGLFGK
410 420 430 440 450
GSIDTCAKFA CSTKATGRTI LKENIKYEVA IFVHGPTTVE SHGNYFTQTG
460 470 480 490 500
AAQAGRFSIT PAAPSYTLKL GEYGEVTVDC EPRSGIDTSA YYVMTVGTKT
510 520 530 540 550
FLVHREWFMD LNLPWSSAES NVWRNRETLM EFEEPHATKQ SVIALGSQEG
560 570 580 590 600
ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFR
610 620 630 640 650
FLGTPADTGH GTVVLELQYT GTDGPCKIPI SSVASLNDLT PVGRLVTVNP
660 670 680 690 700
FVSVSTANAK VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTA
710 720 730 740 750
TLKGAQRLAA LGDTAWDFGS VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI
760 770 780 790 800
TQGLLGALLL WMGINARDRS IALTFLAVGG VLLFLSVNVH ADTGCAIDIS
810 820 830 840 850
RQELRCGSGV FIHNDVEAWI DRYKYYPETP QGLAKIIQKA HKEGVCGLRS
860 870 880 890 900
VSRLEHQMWE AVKDELNTLL KENGVDLSIV VEKQEGMYKS APRRLTATTE
910 920 930 940 950
KLEIGWKAWG KSILFAPELA NNTFVIDGPE TKECPTQNRA WNNLEVEDFG
960 970 980 990 1000
FGLTSTRMFL RVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRFNDT
1010 1020 1030 1040 1050
WKLERAVLGE VKSCTWPETH TLWGDGVLES DLIIPITLAG PRSNHNRRPG
1060 1070 1080 1090 1100
YKTQSQGPWD EGRVEIDFDY CPGTTVTLSE SCGHRGPATR TTTESGKLIT
1110 1120 1130 1140 1150
DWCCRSCTLP PLRYQTDNGC WYGMEIRPQR HDEKTLVQSQ VNAYNADMID
1160 1170 1180 1190 1200
PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
1210 1220 1230 1240 1250
VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL
1260 1270 1280 1290 1300
MLAAAFFQMA YYDARQILLW EMPDVLNSLA VAWMILRAIT FTTTSNVVVP
1310 1320 1330 1340 1350
LLALLTPGLR CLNLDVYRIL LLMVGIGSLI REKRSAAAKK KGASLLCLAL
1360 1370 1380 1390 1400
ASTGFFNPMI LAAGLVACDP NRKRGWPATE VMTAVGLMFA IVGGLAELDI
1410 1420 1430 1440 1450
DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWEGDA EITGSSERVD
1460 1470 1480 1490 1500
VRLDDDGNFQ LMNDPGAPWK IWMLRMACLA ISAYTPWAIL PSVVGFWITL
1510 1520 1530 1540 1550
QYTKRGGVLW DTPSPKEYKR GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV
1560 1570 1580 1590 1600
FHTLWHTTKG AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV
1610 1620 1630 1640 1650
QMIVVEPGKN VKNVQTKPGV FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD
1660 1670 1680 1690 1700
VIGLYGNGVI MPNGSYISAI VQGERMDEPV PAGFEPEMLR KKQITVLDLH
1710 1720 1730 1740 1750
PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA LRGLPIRYQT
1760 1770 1780 1790 1800
SAVAREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
1810 1820 1830 1840 1850
AARGYISTRV ELGEAAAIFM TATPPGTSDP FPESNAPISD LQTEIPDRAW
1860 1870 1880 1890 1900
NSGYEWITEY IGKTVWFVPS VKMGNEIALC LQRAGKKVIQ LNRKSYETEY
1910 1920 1930 1940 1950
PKCKNDDWDF VVTTDISEMG ANFKASRVID SRKSVKPTII TEGEGRVILG
1960 1970 1980 1990 2000
EPSAVTAASA AQRRGRTGRN PSQAGDEYCY GGHTNEDDSN CAHWTEARIM
2010 2020 2030 2040 2050
LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL ELLRTADLPV
2060 2070 2080 2090 2100
WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
2110 2120 2130 2140 2150
WIDARVYSDH QALKSFKDFA SGKRSQIGFI EVLGKMPEHF MGKTWEALDT
2160 2170 2180 2190 2200
MYVVATAEKG GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG
2210 2220 2230 2240 2250
IGKIGLGGVV LGAATFFCWM AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR
2260 2270 2280 2290 2300
SQTDNQLAVF LICVLTLVGA VAANEMGWLD KTKSDISGLF GQRIETKENF
2310 2320 2330 2340 2350
SIGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYITT SLTSINVQAS
2360 2370 2380 2390 2400
ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTSATL LFCHYAYMVP
2410 2420 2430 2440 2450
GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQVM
2460 2470 2480 2490 2500
LILVSLAALV VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC
2510 2520 2530 2540 2550
HIMRGGWLSC LSITWTLVKN MEKPGLKRGG AKGRTLGEVW KERLNQMTKE
2560 2570 2580 2590 2600
EFIRYRKEAI TEVDRSAAKH ARKERNITGG HPVSRGTAKL RWLVERRFLE
2610 2620 2630 2640 2650
PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE PQLVQSYGWN
2660 2670 2680 2690 2700
IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTL RVLEMVEDWL
2710 2720 2730 2740 2750
HRGPKEFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV
2760 2770 2780 2790 2800
SRASGNVVHS VNMTSQVLLG RMEKKTWKGP QYEEDVNLGS GTRAVGKPLL
2810 2820 2830 2840 2850
NSDTSKIKNR IERLRREYSS TWHHDENHPY RTWNYHGSYE VKPTGSASSL
2860 2870 2880 2890 2900
VNGVVRLLSK PWDTITNVTT MAMTDTTPFG QQRVFKEKVD TKAPEPPEGV
2910 2920 2930 2940 2950
KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG AMFEEQNQWR
2960 2970 2980 2990 3000
SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
3010 3020 3030 3040 3050
SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR
3060 3070 3080 3090 3100
EVGTRPGGRI YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE
3110 3120 3130 3140 3150
LTYRHKVVKV MRPAADGRTV MDVISREDQR GSGQVVTYAL NTFTNLAVQL
3160 3170 3180 3190 3200
VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL SENGEERLSR MAVSGDDCVV
3210 3220 3230 3240 3250
KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP FCSNHFTELI
3260 3270 3280 3290 3300
MKDGRTLVTP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
3310 3320 3330 3340 3350
HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW
3360 3370 3380 3390 3400
IEENEWMEDK TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI
3410 3420 3430
NQVRSIIGDE KYVDYMSSLK RYEDTTLVED TVL
Length:3,433
Mass (Da):381,369
Last modified:January 1, 1990 - v1
Checksum:iEE4B888A7D040B99
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti150P → T in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti820I → M in strain: Infectious clone pAKUNa and Infectious clone FLSDX. 1
Natural varianti943N → S in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti1041P → L in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti1202I → N in strain: Infectious clone pAKUN; blocks induction of virus-specific membrane structures. 1 Publication1
Natural varianti1318R → K in strain: Infectious clone pAKUN. 1
Natural varianti1967T → I in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti1974A → V in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1
Natural varianti2023Y → H in strain: Infectious clone pAKUN. 1
Natural varianti2062S → P in strain: Infectious clone pAKUN. 1
Natural varianti2339T → N in strain: Infectious clone pAKUN and Infectious clone FLSDX. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00246 Genomic RNA. Translation: BAA00176.1.
AY274504 Genomic RNA. Translation: AAP78941.1.
AY274505 Genomic RNA. Translation: AAP78942.1.
PIRiA28697. GNWVKV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00246 Genomic RNA. Translation: BAA00176.1.
AY274504 Genomic RNA. Translation: AAP78941.1.
AY274505 Genomic RNA. Translation: AAP78942.1.
PIRiA28697. GNWVKV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SFKX-ray3.20A/B/C/D/E/F/G/H23-98[»]
2HCNX-ray2.35A2846-3433[»]
2HCSX-ray2.50A2846-3433[»]
2HFZX-ray3.00A2802-3433[»]
2OF6electron microscopy24.00A/B/C291-690[»]
2QEQX-ray3.10A/B1691-2124[»]
ProteinModelPortaliP14335.
SMRiP14335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14335. 37 interactors.

Protein family/group databases

MEROPSiS07.001.

Proteomic databases

PeptideAtlasiP14335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP14335.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR026490. mRNA_cap_0/1_MeTrfase.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_KUNJM
AccessioniPrimary (citable) accession number: P14335
Secondary accession number(s): Q7T4P4, Q7T4P5, Q82983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.