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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)DescriptionActionsGraphical viewLength
Active sitei1554Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1578Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1638Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2542mRNA capPROSITE-ProRule annotation1
Binding sitei2545mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2546mRNA capPROSITE-ProRule annotation1
Binding sitei2548mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2553mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2557mRNA capPROSITE-ProRule annotation1
Binding sitei2585S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2590Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2616S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2633S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2634S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2660S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2661S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2675Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2676S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2679mRNA capPROSITE-ProRule annotation1
Sitei2711Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2742mRNA capPROSITE-ProRule annotation1
Binding sitei2744mRNA capPROSITE-ProRule annotation1
Sitei2747Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2749S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1697 – 1704ATPPROSITE-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, 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)DescriptionActionsGraphical viewLength
Topological domaini2 – 110CytoplasmicSequence analysisAdd BLAST109
Transmembranei111 – 131HelicalSequence analysisAdd BLAST21
Topological domaini132 – 251ExtracellularSequence analysisAdd BLAST120
Transmembranei252 – 272HelicalSequence analysisAdd BLAST21
Topological domaini273 – 277CytoplasmicSequence analysis5
Transmembranei278 – 292HelicalSequence analysisAdd BLAST15
Topological domaini293 – 745ExtracellularSequence analysisAdd BLAST453
Intramembranei746 – 766HelicalSequence analysisAdd BLAST21
Topological domaini767 – 772ExtracellularSequence analysis6
Intramembranei773 – 793HelicalSequence analysisAdd BLAST21
Topological domaini794 – 1144ExtracellularSequence analysisAdd BLAST351
Transmembranei1145 – 1165HelicalSequence analysisAdd BLAST21
Topological domaini1166 – 1176CytoplasmicSequence analysisAdd BLAST11
Transmembranei1177 – 1197HelicalSequence analysisAdd BLAST21
Topological domaini1198 – 1218LumenalSequence analysisAdd BLAST21
Transmembranei1219 – 1239HelicalSequence analysisAdd BLAST21
Topological domaini1240 – 1249CytoplasmicSequence analysis10
Transmembranei1250 – 1270HelicalSequence analysisAdd BLAST21
Topological domaini1271 – 1286LumenalSequence analysisAdd BLAST16
Transmembranei1287 – 1307HelicalSequence analysisAdd BLAST21
Topological domaini1308 – 1373CytoplasmicSequence analysisAdd BLAST66
Transmembranei1374 – 1394HelicalSequence analysisAdd BLAST21
Topological domaini1395 – 1397LumenalSequence analysis3
Transmembranei1398 – 1418HelicalSequence analysisAdd BLAST21
Topological domaini1419 – 1475CytoplasmicSequence analysisAdd BLAST57
Intramembranei1476 – 1496HelicalSequence analysisAdd BLAST21
Topological domaini1497 – 2172CytoplasmicSequence analysisAdd BLAST676
Transmembranei2173 – 2193HelicalSequence analysisAdd BLAST21
Topological domaini2194 – 2197LumenalSequence analysis4
Intramembranei2198 – 2218HelicalSequence analysisAdd BLAST21
Topological domaini2219 – 2220LumenalSequence analysis2
Transmembranei2221 – 2241HelicalSequence analysisAdd BLAST21
Topological domaini2242 – 2256CytoplasmicSequence analysisAdd BLAST15
Transmembranei2257 – 2277Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2278 – 2309LumenalSequence analysisAdd BLAST32
Intramembranei2310 – 2330HelicalSequence analysisAdd BLAST21
Topological domaini2331 – 2366LumenalSequence analysisAdd BLAST36
Transmembranei2367 – 2394HelicalSequence analysisAdd BLAST28
Topological domaini2395 – 2446CytoplasmicSequence analysisAdd BLAST52
Transmembranei2447 – 2467HelicalSequence analysisAdd BLAST21
Topological domaini2468 – 2498LumenalSequence analysisAdd BLAST31
Transmembranei2499 – 2519HelicalSequence analysisAdd BLAST21
Topological domaini2520 – 3434CytoplasmicSequence analysisAdd BLAST915

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostSequence analysis
ChainiPRO_00004051632 – 3434Genome polyproteinAdd BLAST3433
ChainiPRO_00000377822 – 105Capsid protein CBy similarityAdd BLAST104
PropeptideiPRO_0000405164106 – 125ER anchor for the protein C, removed in mature form by serine protease NS3Add BLAST20
ChainiPRO_0000405165126 – 292prMBy similarityAdd BLAST167
ChainiPRO_0000037783126 – 217Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037784218 – 292Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037785293 – 793Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037786794 – 1145Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377871146 – 1372Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000377881373 – 1503Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377891504 – 2122Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000377902123 – 2248Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051662249 – 2271Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000377912272 – 2529Non-structural protein 4BBy similarityAdd BLAST258
ChainiPRO_00000377922530 – 3434RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi140N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi295 ↔ 322By similarity
Disulfide bondi352 ↔ 408By similarity
Disulfide bondi366 ↔ 397By similarity
Disulfide bondi384 ↔ 413By similarity
Glycosylationi446N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi482 ↔ 580By similarity
Disulfide bondi597 ↔ 628By similarity
Disulfide bondi797 ↔ 8081 Publication
Disulfide bondi848 ↔ 9361 Publication
Glycosylationi923N-linked (GlcNAc...); by host1 Publication1
Glycosylationi968N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi972 ↔ 10161 Publication
Glycosylationi1000N-linked (GlcNAc...) (high mannose); by host1 Publication1
Glycosylationi2487N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2493N-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
Sitei125 – 126Cleavage; by host signal peptidaseBy similarity2
Sitei217 – 218Cleavage; by host furinBy similarity2
Sitei292 – 293Cleavage; by host signal peptidaseSequence analysis2
Sitei793 – 794Cleavage; by host signal peptidaseSequence analysis2
Sitei1145 – 1146Cleavage; by hostBy similarity2
Sitei1372 – 1373Cleavage; by viral protease NS3Sequence analysis2
Sitei1503 – 1504Cleavage; by autolysisSequence analysis2
Sitei2122 – 2123Cleavage; by autolysisSequence analysis2
Sitei2248 – 2249Cleavage; by viral protease NS3Sequence analysis2
Sitei2271 – 2272Cleavage; by host signal peptidaseSequence analysis2
Sitei2529 – 2530Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP05769.

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

13434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1423 – 1430Combined sources8
Beta strandi1436 – 1440Combined sources5
Beta strandi1523 – 1531Combined sources9
Beta strandi1536 – 1545Combined sources10
Beta strandi1548 – 1551Combined sources4
Helixi1553 – 1556Combined sources4
Beta strandi1564 – 1568Combined sources5
Beta strandi1570 – 1574Combined sources5
Turni1575 – 1578Combined sources4
Beta strandi1579 – 1585Combined sources7
Beta strandi1598 – 1602Combined sources5
Beta strandi1610 – 1614Combined sources5
Beta strandi1617 – 1619Combined sources3
Beta strandi1622 – 1624Combined sources3
Beta strandi1626 – 1629Combined sources4
Helixi1635 – 1637Combined sources3
Beta strandi1641 – 1643Combined sources3
Beta strandi1649 – 1658Combined sources10
Beta strandi1660 – 1662Combined sources3
Beta strandi1664 – 1669Combined sources6
Helixi1684 – 1687Combined sources4
Beta strandi1692 – 1695Combined sources4
Beta strandi1699 – 1701Combined sources3
Turni1703 – 1706Combined sources4
Helixi1707 – 1717Combined sources11
Beta strandi1722 – 1728Combined sources7
Helixi1729 – 1738Combined sources10
Turni1739 – 1741Combined sources3
Beta strandi1744 – 1746Combined sources3
Beta strandi1761 – 1765Combined sources5
Helixi1766 – 1773Combined sources8
Beta strandi1775 – 1777Combined sources3
Beta strandi1783 – 1789Combined sources7
Helixi1795 – 1809Combined sources15
Beta strandi1814 – 1818Combined sources5
Beta strandi1836 – 1840Combined sources5
Beta strandi1849 – 1851Combined sources3
Helixi1853 – 1857Combined sources5
Beta strandi1862 – 1865Combined sources4
Helixi1869 – 1881Combined sources13
Beta strandi1886 – 1889Combined sources4
Turni1891 – 1893Combined sources3
Helixi1894 – 1901Combined sources8
Beta strandi1907 – 1911Combined sources5
Helixi1913 – 1916Combined sources4
Beta strandi1924 – 1928Combined sources5
Beta strandi1935 – 1938Combined sources4
Beta strandi1944 – 1947Combined sources4
Beta strandi1950 – 1952Combined sources3
Helixi1955 – 1962Combined sources8
Beta strandi1974 – 1978Combined sources5
Helixi1990 – 1999Combined sources10
Turni2005 – 2007Combined sources3
Helixi2014 – 2016Combined sources3
Turni2024 – 2027Combined sources4
Helixi2031 – 2042Combined sources12
Helixi2048 – 2055Combined sources8
Turni2056 – 2058Combined sources3
Helixi2064 – 2067Combined sources4
Helixi2072 – 2074Combined sources3
Beta strandi2078 – 2081Combined sources4
Beta strandi2098 – 2101Combined sources4
Helixi2102 – 2104Combined sources3
Helixi2108 – 2118Combined sources11
Helixi2537 – 2546Combined sources10
Helixi2550 – 2557Combined sources8
Turni2558 – 2560Combined sources3
Beta strandi2562 – 2564Combined sources3
Helixi2566 – 2568Combined sources3
Turni2571 – 2576Combined sources6
Beta strandi2578 – 2580Combined sources3
Beta strandi2584 – 2586Combined sources3
Helixi2587 – 2596Combined sources10
Beta strandi2604 – 2609Combined sources6
Helixi2615 – 2620Combined sources6
Beta strandi2626 – 2632Combined sources7
Helixi2650 – 2652Combined sources3
Beta strandi2653 – 2656Combined sources4
Helixi2661 – 2663Combined sources3
Beta strandi2670 – 2674Combined sources5
Helixi2683 – 2701Combined sources19
Beta strandi2706 – 2713Combined sources8
Helixi2718 – 2731Combined sources14
Beta strandi2734 – 2736Combined sources3
Beta strandi2748 – 2751Combined sources4
Helixi2758 – 2771Combined sources14
Turni2772 – 2774Combined sources3
Beta strandi2782 – 2784Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1504 – 1681Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1684 – 1840Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1851 – 2016Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2530 – 2795mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3059 – 3211RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni1426 – 1465Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1788 – 1791DEAH box4

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

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti115L → V in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti754P → Q in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti960G → V in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti1485R → W in CAA27184 (PubMed:3009829).Curated1
Sequence conflicti1779V → G in CAA27184 (PubMed:3009829).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Proteomic databases

PRIDEiP05769.

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: November 2, 2016
This is version 154 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.