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Protein

Genome polyprotein

Gene
N/A
Organism
Murray valley encephalitis virus (strain MVE-1-51) (MVEV)
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 (By similarity).PROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1554 – 15541Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1578 – 15781Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1638 – 16381Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2542 – 25421mRNA capPROSITE-ProRule annotation
Binding sitei2545 – 25451mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2546 – 25461mRNA capPROSITE-ProRule annotation
Binding sitei2548 – 25481mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2553 – 25531mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2557 – 25571mRNA capPROSITE-ProRule annotation
Binding sitei2585 – 25851S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2590 – 25901Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2615 – 26151S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2616 – 26161S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2633 – 26331S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2634 – 26341S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2660 – 26601S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2661 – 26611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2675 – 26751Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2676 – 26761S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2679 – 26791mRNA capPROSITE-ProRule annotation
Sitei2711 – 27111Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2742 – 27421mRNA capPROSITE-ProRule annotation
Binding sitei2744 – 27441mRNA capPROSITE-ProRule annotation
Sitei2747 – 27471Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2749 – 27491S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1697 – 17048ATPPROSITE-ProRule annotation

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, 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):
Non-structural protein 5
OrganismiMurray valley encephalitis virus (strain MVE-1-51) (MVEV)
Taxonomic identifieri301478 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus groupMurray Valley encephalitis virus
Virus hostiCulex annulirostris (Common banded mosquito) [TaxID: 162997]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008863 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 110109CytoplasmicSequence analysisAdd
BLAST
Transmembranei111 – 13121HelicalSequence analysisAdd
BLAST
Topological domaini132 – 251120ExtracellularSequence analysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence analysisAdd
BLAST
Topological domaini273 – 2775CytoplasmicSequence analysis
Transmembranei278 – 29215HelicalSequence analysisAdd
BLAST
Topological domaini293 – 745453ExtracellularSequence analysisAdd
BLAST
Intramembranei746 – 76621HelicalSequence analysisAdd
BLAST
Topological domaini767 – 7726ExtracellularSequence analysis
Intramembranei773 – 79321HelicalSequence analysisAdd
BLAST
Topological domaini794 – 1144351ExtracellularSequence analysisAdd
BLAST
Transmembranei1145 – 116521HelicalSequence analysisAdd
BLAST
Topological domaini1166 – 117611CytoplasmicSequence analysisAdd
BLAST
Transmembranei1177 – 119721HelicalSequence analysisAdd
BLAST
Topological domaini1198 – 121821LumenalSequence analysisAdd
BLAST
Transmembranei1219 – 123921HelicalSequence analysisAdd
BLAST
Topological domaini1240 – 124910CytoplasmicSequence analysis
Transmembranei1250 – 127021HelicalSequence analysisAdd
BLAST
Topological domaini1271 – 128616LumenalSequence analysisAdd
BLAST
Transmembranei1287 – 130721HelicalSequence analysisAdd
BLAST
Topological domaini1308 – 137366CytoplasmicSequence analysisAdd
BLAST
Transmembranei1374 – 139421HelicalSequence analysisAdd
BLAST
Topological domaini1395 – 13973LumenalSequence analysis
Transmembranei1398 – 141821HelicalSequence analysisAdd
BLAST
Topological domaini1419 – 147557CytoplasmicSequence analysisAdd
BLAST
Intramembranei1476 – 149621HelicalSequence analysisAdd
BLAST
Topological domaini1497 – 2172676CytoplasmicSequence analysisAdd
BLAST
Transmembranei2173 – 219321HelicalSequence analysisAdd
BLAST
Topological domaini2194 – 21974LumenalSequence analysis
Intramembranei2198 – 221821HelicalSequence analysisAdd
BLAST
Topological domaini2219 – 22202LumenalSequence analysis
Transmembranei2221 – 224121HelicalSequence analysisAdd
BLAST
Topological domaini2242 – 225615CytoplasmicSequence analysisAdd
BLAST
Transmembranei2257 – 227721Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2278 – 230932LumenalSequence analysisAdd
BLAST
Intramembranei2310 – 233021HelicalSequence analysisAdd
BLAST
Topological domaini2331 – 236636LumenalSequence analysisAdd
BLAST
Transmembranei2367 – 239428HelicalSequence analysisAdd
BLAST
Topological domaini2395 – 244652CytoplasmicSequence analysisAdd
BLAST
Transmembranei2447 – 246721HelicalSequence analysisAdd
BLAST
Topological domaini2468 – 249831LumenalSequence analysisAdd
BLAST
Transmembranei2499 – 251921HelicalSequence analysisAdd
BLAST
Topological domaini2520 – 3434915CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by hostSequence analysis
Chaini2 – 34343433Genome polyproteinPRO_0000405163Add
BLAST
Chaini2 – 105104Capsid protein CBy similarityPRO_0000037782Add
BLAST
Propeptidei106 – 12520ER anchor for the protein C, removed in mature form by serine protease NS3PRO_0000405164Add
BLAST
Chaini126 – 292167prMBy similarityPRO_0000405165Add
BLAST
Chaini126 – 21792Peptide prBy similarityPRO_0000037783Add
BLAST
Chaini218 – 29275Small envelope protein MBy similarityPRO_0000037784Add
BLAST
Chaini293 – 793501Envelope protein EBy similarityPRO_0000037785Add
BLAST
Chaini794 – 1145352Non-structural protein 1By similarityPRO_0000037786Add
BLAST
Chaini1146 – 1372227Non-structural protein 2ABy similarityPRO_0000037787Add
BLAST
Chaini1373 – 1503131Serine protease subunit NS2BBy similarityPRO_0000037788Add
BLAST
Chaini1504 – 2122619Serine protease NS3By similarityPRO_0000037789Add
BLAST
Chaini2123 – 2248126Non-structural protein 4ABy similarityPRO_0000037790Add
BLAST
Peptidei2249 – 227123Peptide 2kBy similarityPRO_0000405166Add
BLAST
Chaini2272 – 2529258Non-structural protein 4BBy similarityPRO_0000037791Add
BLAST
Chaini2530 – 3434905RNA-directed RNA polymerase NS5By similarityPRO_0000037792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi140 – 1401N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi295 ↔ 322By similarity
Disulfide bondi352 ↔ 408By similarity
Disulfide bondi366 ↔ 397By similarity
Disulfide bondi384 ↔ 413By similarity
Glycosylationi446 – 4461N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi482 ↔ 580By similarity
Disulfide bondi597 ↔ 628By similarity
Disulfide bondi797 ↔ 8081 Publication
Disulfide bondi848 ↔ 9361 Publication
Glycosylationi923 – 9231N-linked (GlcNAc...); by host1 Publication
Glycosylationi968 – 9681N-linked (GlcNAc...); by host1 Publication
Disulfide bondi972 ↔ 10161 Publication
Glycosylationi1000 – 10001N-linked (GlcNAc...) (high mannose); by host1 Publication
Glycosylationi2487 – 24871N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2493 – 24931N-linked (GlcNAc...); by hostSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei105 – 1062Cleavage; by viral protease NS3Sequence analysis
Sitei125 – 1262Cleavage; by host signal peptidaseBy similarity
Sitei217 – 2182Cleavage; by host furinBy similarity
Sitei292 – 2932Cleavage; by host signal peptidaseSequence analysis
Sitei793 – 7942Cleavage; by host signal peptidaseSequence analysis
Sitei1145 – 11462Cleavage; by hostBy similarity
Sitei1372 – 13732Cleavage; by viral protease NS3Sequence analysis
Sitei1503 – 15042Cleavage; by autolysisSequence analysis
Sitei2122 – 21232Cleavage; by autolysisSequence analysis
Sitei2248 – 22492Cleavage; by viral protease NS3Sequence analysis
Sitei2271 – 22722Cleavage; by host signal peptidaseSequence analysis
Sitei2529 – 25302Cleavage; by viral protease NS3Sequence analysis

Keywords - PTMi

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

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

Structurei

Secondary structure

1
3434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1423 – 14308Combined sources
Beta strandi1436 – 14405Combined sources
Beta strandi1523 – 15319Combined sources
Beta strandi1536 – 154510Combined sources
Beta strandi1548 – 15514Combined sources
Helixi1553 – 15564Combined sources
Beta strandi1564 – 15685Combined sources
Beta strandi1570 – 15745Combined sources
Turni1575 – 15784Combined sources
Beta strandi1579 – 15857Combined sources
Beta strandi1598 – 16025Combined sources
Beta strandi1610 – 16145Combined sources
Beta strandi1617 – 16193Combined sources
Beta strandi1622 – 16243Combined sources
Beta strandi1626 – 16294Combined sources
Helixi1635 – 16373Combined sources
Beta strandi1641 – 16433Combined sources
Beta strandi1649 – 165810Combined sources
Beta strandi1660 – 16623Combined sources
Beta strandi1664 – 16696Combined sources
Helixi1684 – 16874Combined sources
Beta strandi1692 – 16954Combined sources
Beta strandi1699 – 17013Combined sources
Turni1703 – 17064Combined sources
Helixi1707 – 171711Combined sources
Beta strandi1722 – 17287Combined sources
Helixi1729 – 173810Combined sources
Turni1739 – 17413Combined sources
Beta strandi1744 – 17463Combined sources
Beta strandi1761 – 17655Combined sources
Helixi1766 – 17738Combined sources
Beta strandi1775 – 17773Combined sources
Beta strandi1783 – 17897Combined sources
Helixi1795 – 180915Combined sources
Beta strandi1814 – 18185Combined sources
Beta strandi1836 – 18405Combined sources
Beta strandi1849 – 18513Combined sources
Helixi1853 – 18575Combined sources
Beta strandi1862 – 18654Combined sources
Helixi1869 – 188113Combined sources
Beta strandi1886 – 18894Combined sources
Turni1891 – 18933Combined sources
Helixi1894 – 19018Combined sources
Beta strandi1907 – 19115Combined sources
Helixi1913 – 19164Combined sources
Beta strandi1924 – 19285Combined sources
Beta strandi1935 – 19384Combined sources
Beta strandi1944 – 19474Combined sources
Beta strandi1950 – 19523Combined sources
Helixi1955 – 19628Combined sources
Beta strandi1974 – 19785Combined sources
Helixi1990 – 199910Combined sources
Turni2005 – 20073Combined sources
Helixi2014 – 20163Combined sources
Turni2024 – 20274Combined sources
Helixi2031 – 204212Combined sources
Helixi2048 – 20558Combined sources
Turni2056 – 20583Combined sources
Helixi2064 – 20674Combined sources
Helixi2072 – 20743Combined sources
Beta strandi2078 – 20814Combined sources
Beta strandi2098 – 21014Combined sources
Helixi2102 – 21043Combined sources
Helixi2108 – 211811Combined sources
Helixi2537 – 254610Combined sources
Helixi2550 – 25578Combined sources
Turni2558 – 25603Combined sources
Beta strandi2562 – 25643Combined sources
Helixi2566 – 25683Combined sources
Turni2571 – 25766Combined sources
Beta strandi2578 – 25803Combined sources
Beta strandi2584 – 25863Combined sources
Helixi2587 – 259610Combined sources
Beta strandi2604 – 26096Combined sources
Helixi2615 – 26206Combined sources
Beta strandi2626 – 26327Combined sources
Helixi2650 – 26523Combined sources
Beta strandi2653 – 26564Combined sources
Helixi2661 – 26633Combined sources
Beta strandi2670 – 26745Combined sources
Helixi2683 – 270119Combined sources
Beta strandi2706 – 27138Combined sources
Helixi2718 – 273114Combined sources
Beta strandi2734 – 27363Combined sources
Beta strandi2748 – 27514Combined sources
Helixi2758 – 277114Combined sources
Turni2772 – 27743Combined sources
Beta strandi2782 – 27843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PX2X-ray2.00A/B2530-2798[»]
2PX4X-ray2.20A2530-2798[»]
2PX5X-ray2.30A/B2530-2798[»]
2PX8X-ray2.20A/B2530-2798[»]
2PXAX-ray2.30A/B2530-2798[»]
2PXCX-ray2.80A2530-2798[»]
2V8OX-ray1.90A1681-2122[»]
2WV9X-ray2.75A1421-1465[»]
A1504-2122[»]
ProteinModelPortaliP05769.
SMRiP05769. Positions 27-97, 293-691, 1422-1464, 1513-2122, 2532-2796, 2803-3426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1504 – 1681178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1684 – 1840157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1851 – 2016166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2530 – 2795266mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3059 – 3211153RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1426 – 146540Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1788 – 17914DEAH box

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.

P05769-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MSKKPGGPGK PRVVNMLKRG IPRVFPLVGV KRVVMNLLDG RGPIRFVLAL
60 70 80 90 100
LAFFRFTALA PTKALMRRWK SVNKTTAMKH LTSFKKELGT LIDVVNKRGK
110 120 130 140 150
KQKKRGGSET SVLMLIFMLI GFAAALKLST FQGKIMMTVN ATDIADVIAI
160 170 180 190 200
PTPKGPNQCW IRAIDIGFMC DDTITYECPK LESGNDPEDI DCWCDKQAVY
210 220 230 240 250
VNYGRCTRAR HSKRSRRSIT VQTHGESTLV NKKDAWLDST KATRYLTKTE
260 270 280 290 300
NWIIRNPGYA LVAVVLGWML GSNTGQKVIF TVLLLLVAPA YSFNCLGMSS
310 320 330 340 350
RDFIEGASGA TWVDLVLEGD SCITIMAADK PTLDIRMMNI EATNLALVRN
360 370 380 390 400
YCYAATVSDV STVSNCPTTG ESHNTKRADH NYLCKRGVTD RGWGNGCGLF
410 420 430 440 450
GKGSIDTCAK FTCSNSAAGR LILPEDIKYE VGVFVHGSTD STSHGNYSTQ
460 470 480 490 500
IGANQAVRFT ISPNAPAITA KMGDYGEVTV ECEPRSGLNT EAYYVMTIGT
510 520 530 540 550
KHFLVHREWF NDLLLPWTSP ASTEWRNREI LVEFEEPHAT KQSVVALGSQ
560 570 580 590 600
EGALHQALAG AIPVEFSSST LKLTSGHLKC RVKMEKLKLK GTTYGMCTEK
610 620 630 640 650
FTFSKNPADT GHGTVVLELQ YTGSDGPCKI PISSVASLND MTPVGRMVTA
660 670 680 690 700
NPYVASSTAN AKVLVEIEPP FGDSYIVVGR GDKQINHHWH KEGSSIGKAF
710 720 730 740 750
STTLKGAQRL AALGDTAWDF GSVGGVFNSI GKAVHQVFGG AFRTLFGGMS
760 770 780 790 800
WISPGLLGAL LLWMGVNARD KSIALAFLAT GGVLLFLATN VHADTGCAID
810 820 830 840 850
ITRRELKCGS GIFIHNDVEA WIDRYKYLPE TPKQLAKVVE NAHKSGICGI
860 870 880 890 900
RSVNRFEHQM WESVRDELNA LLKENAIDLS VVVEKQKGMY RAAPNRLRLT
910 920 930 940 950
VEELDIGWKA WGKSLLFAAE LANSTFVVDG PETAECPNSK RAWNSFEIED
960 970 980 990 1000
FGFGITSTRG WLKLREENTS ECDSTIIGTA VKGNHAVHSD LSYWIESGLN
1010 1020 1030 1040 1050
GTWKLERAIF GEVKSCTWPE THTLWGDAVE ETELIIPVTL AGPRSKHNRR
1060 1070 1080 1090 1100
EGYKVQVQGP WDEEDIKLDF DYCPGTTVTV SEHCGKRGPS VRTTTDSGKL
1110 1120 1130 1140 1150
VTDWCCRSCT LPPLRFTTAS GCWYGMEIRP MKHDESTLVK SRVQAFNGDM
1160 1170 1180 1190 1200
IDPFQLGLLV MFLATQEVLR KRWTARLTLP AAVGALLVLL LGGITYTDLV
1210 1220 1230 1240 1250
RYLILVGSAF AESNNGGDVI HLALIAVFKV QPAFLVASLT RSRWTNQENL
1260 1270 1280 1290 1300
VLVLGAAFFQ MAASDLELTI PGLLNSAATA WMVLRAMAFP STSAIAMPML
1310 1320 1330 1340 1350
AMLAPGMRML HLDTYRIVLL LIGICSLLNE RRRSVEKKKG AVLIGLALTS
1360 1370 1380 1390 1400
TGYFSPTIMA AGLMICNPNK KRGWPATEVL TAVGLMFAIV GGLAELDIDS
1410 1420 1430 1440 1450
MSVPFTIAGL MLVSYVISGK ATDMWLERAA DVSWEAGAAI TGTSERLDVQ
1460 1470 1480 1490 1500
LDDDGDFHLL NDPGVPWKIW VLRMTCLSVA AITPRAILPS AFGYWLTLKY
1510 1520 1530 1540 1550
TKRGGVFWDT PSPKVYPKGD TTPGVYRIMA RGILGRYQAG VGVMHEGVFH
1560 1570 1580 1590 1600
TLWHTTRGAA IMSGEGRLTP YWGNVKEDRV TYGGPWKLDQ KWNGVDDVQM
1610 1620 1630 1640 1650
IVVEPGKPAI NVQTKPGIFK TAHGEIGAVS LDYPIGTSGS PIVNSNGEII
1660 1670 1680 1690 1700
GLYGNGVILG NGAYVSAIVQ GERVEEPVPE AYNPEMLKKR QLTVLDLHPG
1710 1720 1730 1740 1750
AGKTRRILPQ IIKDAIQKRL RTAVLAPTRV VAAEMAEALR GLPVRYLTPA
1760 1770 1780 1790 1800
VQREHSGNEI VDVMCHATLT HRLMSPLRVP NYNLFVMDEA HFTDPASIAA
1810 1820 1830 1840 1850
RGYIATRVEA GEAAAIFMTA TPPGTSDPFP DTNSPVHDVS SEIPDRAWSS
1860 1870 1880 1890 1900
GFEWITDYAG KTVWFVASVK MSNEIAQCLQ RAGKRVIQLN RKSYDTEYPK
1910 1920 1930 1940 1950
CKNGDWDFVI TTDISEMGAN FGASRVIDCR KSVKPTILDE GEGRVILSVP
1960 1970 1980 1990 2000
SAITSASAAQ RRGRVGRNPS QIGDEYHYGG GTSEDDTMLA HWTEAKILLD
2010 2020 2030 2040 2050
NIHLPNGLVA QLYGPERDKT YTMDGEYRLR GEERKTFLEL IKTADLPVWL
2060 2070 2080 2090 2100
AYKVASNGIQ YNDRKWCFDG PRSNIILEDN NEVEIITRIG ERKVLKPRWL
2110 2120 2130 2140 2150
DARVYSDHQS LKWFKDFAAG KRSAIGFFEV LGRMPEHFAG KTREALDTMY
2160 2170 2180 2190 2200
LVATSEKGGK AHRMALEELP DALETITLIA ALGVMTAGFF LLMMQRKGIG
2210 2220 2230 2240 2250
KLGLGALVLV VATFFLWMSD VSGTKIAGVL LLALLMMVVL IPEPEKQRSQ
2260 2270 2280 2290 2300
TDNQLAVFLI CVLLVVGLVA ANEYGMLERT KTDIRNLFGK SLIEENEVHI
2310 2320 2330 2340 2350
PPFDFFTLDL KPATAWALYG GSTVVLTPLI KHLVTSQYVT TSLASINAQA
2360 2370 2380 2390 2400
GSLFTLPKGI PFTDFDLSVA LVFLGCWGQV TLTTLIMATI LVTLHYGYLL
2410 2420 2430 2440 2450
PGWQAEALRA AQKRTAAGIM KNAVVDGIVA TDVPELERTT PQMQKRLGQI
2460 2470 2480 2490 2500
LLVLASVAAV CVNPRITTIR EAGILCTAAA LTLWDNNASA AWNSTTATGL
2510 2520 2530 2540 2550
CHVMRGSWIA GASIAWTLIK NAEKPAFKRG RAGGRTLGEQ WKEKLNAMGK
2560 2570 2580 2590 2600
EEFFSYRKEA ILEVDRTEAR RARREGNKVG GHPVSRGTAK LRWLVERRFV
2610 2620 2630 2640 2650
QPIGKVVDLG CGRGGWSYYA ATMKNVQEVR GYTKGGPGHE EPMLMQSYGW
2660 2670 2680 2690 2700
NIVTMKSGVD VFYKPSEISD TLLCDIGESS PSAEIEEQRT LRILEMVSDW
2710 2720 2730 2740 2750
LSRGPKEFCI KILCPYMPKV IEKLESLQRR FGGGLVRVPL SRNSNHEMYW
2760 2770 2780 2790 2800
VSGASGNIVH AVNMTSQVLI GRMDKKIWKG PKYEEDVNLG SGTRAVGKGV
2810 2820 2830 2840 2850
QHTDYKRIKS RIEKLKEEYA ATWHTDDNHP YRTWTYHGSY EVKPSGSAST
2860 2870 2880 2890 2900
LVNGVVRLLS KPWDAITGVT TMAMTDTTPF GQQRVFKEKV DTKAPEPPQG
2910 2920 2930 2940 2950
VKTVMDETTN WLWAYLARNK KARLCTREEF VKKVNSHAAL GAMFEEQNQW
2960 2970 2980 2990 3000
KNAREAVEDP KFWEMVDEER ECHLRGECRT CIYNMMGKRE KKPGEFGKAK
3010 3020 3030 3040 3050
GSRAIWFMWL GARFLEFEAL GFLNEDHWMS RENSGGGVEG AGIQKLGYIL
3060 3070 3080 3090 3100
RDVAQKPGGK IYADDTAGWD TRITQADLEN EAKVLELMEG EQRTLARAII
3110 3120 3130 3140 3150
ELTYRHKVVK VMRPAAGGKT VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ
3160 3170 3180 3190 3200
LVRLMEAEAV IGPDDIESIE RKKKFAVRTW LFENAEERVQ RMAVSGDDCV
3210 3220 3230 3240 3250
VKPLDDRFST ALHFLNAMSK VRKDIQEWKP SQGWYDWQQV PFCSNHFQEV
3260 3270 3280 3290 3300
IMKDGRTLVV PCRGQDELIG RARISPGSGW NVRDTACLAK AYAQMWLVLY
3310 3320 3330 3340 3350
FHRRDLRLMA NAICSSVPVD WVPTGRTTWS IHGKGEWMTT EDMLSVWNRV
3360 3370 3380 3390 3400
WILENEWMED KTTVSDWTEV PYVGKREDIW CGSLIGTRTR ATWAENIYAA
3410 3420 3430
INQVRSVIGK EKYVDYVQSL RRYEETHVSE DRVL
Length:3,434
Mass (Da):380,577
Last modified:December 21, 2004 - v2
Checksum:i20D7110791C567A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151L → V in CAA27184 (PubMed:3009829).Curated
Sequence conflicti754 – 7541P → Q in CAA27184 (PubMed:3009829).Curated
Sequence conflicti960 – 9601G → V in CAA27184 (PubMed:3009829).Curated
Sequence conflicti1485 – 14851R → W in CAA27184 (PubMed:3009829).Curated
Sequence conflicti1779 – 17791V → G in CAA27184 (PubMed:3009829).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161266 Genomic RNA. Translation: AAF05296.1.
X03467 Unassigned RNA. Translation: CAA27184.1.
PIRiA24635. GNWVMV.
RefSeqiNP_051124.1. NC_000943.1.

Genome annotation databases

GeneIDi1489715.
KEGGivg:1489715.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161266 Genomic RNA. Translation: AAF05296.1.
X03467 Unassigned RNA. Translation: CAA27184.1.
PIRiA24635. GNWVMV.
RefSeqiNP_051124.1. NC_000943.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PX2X-ray2.00A/B2530-2798[»]
2PX4X-ray2.20A2530-2798[»]
2PX5X-ray2.30A/B2530-2798[»]
2PX8X-ray2.20A/B2530-2798[»]
2PXAX-ray2.30A/B2530-2798[»]
2PXCX-ray2.80A2530-2798[»]
2V8OX-ray1.90A1681-2122[»]
2WV9X-ray2.75A1421-1465[»]
A1504-2122[»]
ProteinModelPortaliP05769.
SMRiP05769. Positions 27-97, 293-691, 1422-1464, 1513-2122, 2532-2796, 2803-3426.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489715.
KEGGivg:1489715.

Miscellaneous databases

EvolutionaryTraceiP05769.

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_MVEV5
AccessioniPrimary (citable) accession number: P05769
Secondary accession number(s): Q9Q9F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.