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Protein

Genome polyprotein

Gene
N/A
Organism
St. louis encephalitis virus (strain MS1-7)
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
Binding sitei2537mRNA capPROSITE-ProRule annotation1
Binding sitei2540mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2541mRNA capPROSITE-ProRule annotation1
Binding sitei2543mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2548mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2552mRNA capPROSITE-ProRule annotation1
Binding sitei2580S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2585Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2610S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2628S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2655S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2656S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2670Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2671S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2674mRNA capPROSITE-ProRule annotation1
Sitei2706Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2737mRNA capPROSITE-ProRule annotation1
Binding sitei2739mRNA capPROSITE-ProRule annotation1
Sitei2742Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2744S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1693 – 1700ATPPROSITE-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

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):
NS5
OrganismiSt. louis encephalitis virus (strain MS1-7)
Taxonomic identifieri11081 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostiAgelaius tricolor (Tricolored blackbird) [TaxID: 9191]
Cardinalis cardinalis (Northern cardinal) [TaxID: 98964]
Carpodacus mexicanus (House finch) (Haemorhous mexicanus) [TaxID: 30427]
Columba livia (Rock dove) [TaxID: 8932]
Culex nigripalpus [TaxID: 42429]
Culex pipiens (House mosquito) [TaxID: 7175]
Culex quinquefasciatus (Southern house mosquito) (Culex pungens) [TaxID: 7176]
Culex tarsalis (Encephalitis mosquito) [TaxID: 7177]
Cyanocitta cristata (Blue jay) [TaxID: 28727]
Euphagus cyanocephalus (Brewer's blackbird) [TaxID: 84817]
Homo sapiens (Human) [TaxID: 9606]
Mimus polyglottos (Northern mockingbird) [TaxID: 60713]
Passer domesticus (House sparrow) (Fringilla domestica) [TaxID: 48849]
Turdus migratorius (American robin) [TaxID: 9188]
Zenaida macroura (Mourning dove) [TaxID: 47245]

Subcellular locationi

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

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 108CytoplasmicSequence analysisAdd BLAST107
Transmembranei109 – 129HelicalSequence analysisAdd BLAST21
Topological domaini130 – 247ExtracellularSequence analysisAdd BLAST118
Transmembranei248 – 268HelicalSequence analysisAdd BLAST21
Topological domaini269 – 273CytoplasmicSequence analysis5
Transmembranei274 – 290HelicalSequence analysisAdd BLAST17
Topological domaini291 – 741ExtracellularSequence analysisAdd BLAST451
Intramembranei742 – 762HelicalSequence analysisAdd BLAST21
Topological domaini763 – 768ExtracellularSequence analysis6
Intramembranei769 – 789HelicalSequence analysisAdd BLAST21
Topological domaini790 – 1138ExtracellularSequence analysisAdd BLAST349
Transmembranei1139 – 1159HelicalSequence analysisAdd BLAST21
Topological domaini1160 – 1214CytoplasmicSequence analysisAdd BLAST55
Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21
Topological domaini1236 – 1245LumenalSequence analysis10
Transmembranei1246 – 1266HelicalSequence analysisAdd BLAST21
Topological domaini1267 – 1304CytoplasmicSequence analysisAdd BLAST38
Transmembranei1305 – 1325HelicalSequence analysisAdd BLAST21
Topological domaini1326 – 1339LumenalSequence analysisAdd BLAST14
Transmembranei1340 – 1360HelicalSequence analysisAdd BLAST21
Topological domaini1361 – 1369CytoplasmicSequence analysis9
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Topological domaini1391 – 1393LumenalSequence analysis3
Transmembranei1394 – 1414HelicalSequence analysisAdd BLAST21
Topological domaini1415 – 1471CytoplasmicSequence analysisAdd BLAST57
Intramembranei1472 – 1492HelicalSequence analysisAdd BLAST21
Topological domaini1493 – 2167CytoplasmicSequence analysisAdd BLAST675
Transmembranei2168 – 2188HelicalSequence analysisAdd BLAST21
Topological domaini2189 – 2193LumenalSequence analysis5
Intramembranei2194 – 2214HelicalSequence analysisAdd BLAST21
Topological domaini2215LumenalSequence analysis1
Transmembranei2216 – 2236HelicalSequence analysisAdd BLAST21
Topological domaini2237 – 2251CytoplasmicSequence analysisAdd BLAST15
Transmembranei2252 – 2272Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2273 – 2308LumenalSequence analysisAdd BLAST36
Intramembranei2309 – 2329HelicalSequence analysisAdd BLAST21
Topological domaini2330 – 2354LumenalSequence analysisAdd BLAST25
Intramembranei2355 – 2375HelicalSequence analysisAdd BLAST21
Topological domaini2376LumenalSequence analysis1
Transmembranei2377 – 2397HelicalSequence analysisAdd BLAST21
Topological domaini2398 – 2440CytoplasmicSequence analysisAdd BLAST43
Transmembranei2441 – 2461HelicalSequence analysisAdd BLAST21
Topological domaini2462 – 2466LumenalSequence analysis5
Transmembranei2467 – 2487HelicalSequence analysisAdd BLAST21
Topological domaini2488 – ›3412CytoplasmicSequence analysisAdd BLAST›925

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_00004051432 – ›3412Genome polyproteinAdd BLAST›3411
ChainiPRO_00000377352 – 103Capsid protein CBy similarityAdd BLAST102
PropeptideiPRO_0000405144104 – 121ER anchor for the protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000405145122 – 288prMBy similarityAdd BLAST167
ChainiPRO_0000037736122 – 213Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037737214 – 288Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037738289 – 789Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037739790 – 1141Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377401142 – 1368Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000377411369 – 1499Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377421500 – 2117Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00004051462118 – 2243Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051472244 – 2266Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004051482267 – 2524Non-structural protein 4BBy similarityAdd BLAST258
ChainiPRO_00004051492525 – ›3412RNA-directed RNA polymerase NS5By similarityAdd BLAST›888

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi136N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi291 ↔ 318By similarity
Disulfide bondi348 ↔ 404By similarity
Disulfide bondi362 ↔ 393By similarity
Disulfide bondi380 ↔ 409By similarity
Disulfide bondi478 ↔ 576By similarity
Disulfide bondi593 ↔ 624By similarity
Glycosylationi919N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi964N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi996N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2335N-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
Sitei103 – 104Cleavage; by viral protease NS3Sequence analysis2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei213 – 214Cleavage; by host furinBy similarity2
Sitei288 – 289Cleavage; by host signal peptidaseSequence analysis2
Sitei789 – 790Cleavage; by host signal peptidaseSequence analysis2
Sitei1141 – 1142Cleavage; by hostBy similarity2
Sitei1368 – 1369Cleavage; by viral protease NS3Sequence analysis2
Sitei1499 – 1500Cleavage; by autolysisSequence analysis2
Sitei2117 – 2118Cleavage; by autolysisSequence analysis2
Sitei2243 – 2244Cleavage; by viral protease NS3Sequence analysis2
Sitei2266 – 2267Cleavage; by host signal peptidaseSequence analysis2
Sitei2524 – 2525Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP09732.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FG0X-ray3.90A289-695[»]
ProteinModelPortaliP09732.
SMRiP09732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1500 – 1677Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1680 – 1836Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1847 – 2011Helicase C-terminalPROSITE-ProRule annotationAdd BLAST165
Domaini2525 – 2790mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3054 – 3206RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST42
Regioni1422 – 1461Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1784 – 1787DEAH 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: Fragment.

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

P09732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPGKPGR NRVVNMLKRG VSRVNPLTGL KRILGSLLDG RGPVRFILAI
60 70 80 90 100
LTFFRFTALQ PTEALKRRWR AVDKRTALKH LNGFKRDLGS MLDTINRRPS
110 120 130 140 150
KKRGGTRSLL GLAALIGLAS SLQLSTYQGK VLMSINKTDA QSAINIPSAN
160 170 180 190 200
GANTCIVRAL DVGVMCKNDI TYLCPVLSAG NDPEDIDCWC DVEEVWVHYG
210 220 230 240 250
RCTRMGHSRR SRRSISVQHH GDSTLATKNT PWLDTVKTTK YLTKVENWVL
260 270 280 290 300
RNPGYALVAL AIGWMLGSNN TQRVVFVIML MLIAPAYSFN CLGTSNRDFV
310 320 330 340 350
EGASGATWID LVLEGGSCVT VMAPEKPTLD FKVMKMEATE LATVREYCYE
360 370 380 390 400
ATLDTLSTVA RCPTTGEAHN TKRSDPTFVC KRDVVDRGWG NGCGLFGKGS
410 420 430 440 450
IDTCAKFTCK NKATGKTILR ENIKYEVAIF VHGSTDSTSH GNYFEQIGKN
460 470 480 490 500
QAARFTISPQ APSFTANMGE YGTVTIDCEA RSGINTEDYY VFTVKEKSWL
510 520 530 540 550
VNRDWFHDLN LPWTSPATTD WRNRETLVEF EEPHATKQTV VALGSQEGAL
560 570 580 590 600
HTALAGAIPA TVSSSTLTLQ SGHLKCRAKL DKVKIKGTTY GMCDSAFTFS
610 620 630 640 650
KNPADTGHGT VIVELQYTGS NGPCRVPISV TANLMDLTPV GRLVTVNPFI
660 670 680 690 700
STGGANNKVM IEVEPPFGDS YIVVGRGTTQ INYHWHKEGS SIGKALATTW
710 720 730 740 750
KGAQRLAVLG DTAWDFGSIG GVFNSIGKAV HQVFGGAFRT LFGGMSWITQ
760 770 780 790 800
GLLGALLLWM GLQARDRSIS LTLLAVGGIL IFLATSVQAD SGCAIDLQRR
810 820 830 840 850
ELKCGGGIFV YNDVEKWKSD YKYFPLTPTG LAHVIQEAHA NGICGIRSTS
860 870 880 890 900
RLEHLMWENI QRELNAIFED NEIDLSVVVQ EDPKYYKRAP RRLKKLEDEL
910 920 930 940 950
DYGWKKWGKT LFVEPRLGNN TFVVDGPETK ECPTANRAWN SFKVEDFGFG
960 970 980 990 1000
MVFTRLWLTI REENTTECDS AIIGTAIKGD RAVHSDLSYW IESKKNETWQ
1010 1020 1030 1040 1050
LERAVMGEVK SCTWPETHTL WGDGVVESEM IIPVTLGGPK SHHNKRNGYH
1060 1070 1080 1090 1100
TQTKGPWSEG EITLDFDYCP GTTVTVTEHC GNRGASLRTT TASGKLVTDW
1110 1120 1130 1140 1150
CCRSCSLPPL RYTTKDGCWY GMEIRPVKEE EAKLVKSRVT AGVAGGMEPF
1160 1170 1180 1190 1200
QLGLLVAFIA TQEVLKRRWT GKLTLTSLAV CLALLIFGNL TYMDLVRYLV
1210 1220 1230 1240 1250
LVGTAFAEMN TGGDVIHLAL VAVFKVQPAF LAGLFLRMQW SNQENILMVI
1260 1270 1280 1290 1300
GAAFLQMAAN DLKLEVLPIL NAMSIAWMLI RAMKEGKVAM YALPILCALT
1310 1320 1330 1340 1350
PGMRMAGLDV IRCLLLIIGI VTLLNERRES VAKKKGGYLL AAALCQAGVC
1360 1370 1380 1390 1400
SPLIMMGGLI LAHPNGKRSW PASEVLTGVG LMCALAGGLL EFEETSMVVP
1410 1420 1430 1440 1450
FAIAGLMYIT YTVSGKAAEM WIEKAADITW EQNAEITGTS PRLDVDLDSH
1460 1470 1480 1490 1500
GNFKLLNDPG APVHLFALRF ILLGLSARFH WFIPFGVLGF WLLGKHSKRG
1510 1520 1530 1540 1550
GALWDVPSPK VYPKCETKPG IYRIMTRGIL GTFQAGVGVM HEGVFHTMWH
1560 1570 1580 1590 1600
ATEGAVLRNG EGRLDPYAGD VRNDLISYGG PWKLSATWDG TEEVQMIAVA
1610 1620 1630 1640 1650
PGKPAINVQT TPGVFKTPFG TIGAVTLDFP KGTSGSPIIN KKGEIIGLYG
1660 1670 1680 1690 1700
NGVLIGQGEY VSGIIQGERT EEPIPDAYNE EMLRKRKLTV LELHPGAGKT
1710 1720 1730 1740 1750
RKVLPQIIKD CIQKRLRTAV LAPTRVVACE IAEALKGLPI RYLTPAVRNE
1760 1770 1780 1790 1800
HQGNEIVDVM CHATLTQKLL TPTRVPNYQV YIMDEAHFID PASIAARGYI
1810 1820 1830 1840 1850
STKVELGEAA AIFMTATPPG TNDPFPDSNS PILDVEAQVP DKAWSTGYEW
1860 1870 1880 1890 1900
ITNFTGRTVW FVPSVKSGNE IAICLQKAGK RVIQLNRKSF DTEYPKTKNN
1910 1920 1930 1940 1950
EWDFVVTTDI SEMGANFGAH RVIDSRKCVK PVILEDDDRV ILNGPMAITS
1960 1970 1980 1990 2000
ASAAQRRGRI GRNPSQIGDE YHYGGATNED DHDLANWTEA KILLDNIYLP
2010 2020 2030 2040 2050
NGLVAQMYQP ERDKVFTMDG EFRLRGEERK NFVELMRNGD LPVWLAYKVA
2060 2070 2080 2090 2100
SNGHSYQDRS WCFTGQTNNT ILEDNNEVEV FTKTGDRKIL RPKWMDARVC
2110 2120 2130 2140 2150
CDYQALKSFK EFAAGKRSAL GMMEVMGRMP NHFWEKTVAA ADTLYLLGTS
2160 2170 2180 2190 2200
EANSRAHKEA LAELPDSLET LLLIGMLCVM SMGTFIFLMN RKGVGKMGLG
2210 2220 2230 2240 2250
AFVMTLATAL LWAAEVPGTQ IAGVLLIVFL LMIVLIPEPE KQRSQTDNQL
2260 2270 2280 2290 2300
AVFLICIMTL MGVVAANEMG LLEKTKSDIA KLFGSQPGSV GFATRTTPWD
2310 2320 2330 2340 2350
ISLDIKPATA WALYAAATMV MTPLIKHLIT TQYVNFSLTA IASQAGVLLG
2360 2370 2380 2390 2400
LTNGMPFTAM DLSVPLLVLG CWNQMTLPSL AVAVMLLAIH YAFMIPGWQA
2410 2420 2430 2440 2450
EAMRAAQRRT AAGIMKNAVV DGIVATDIPD LSPATPMTEK KMGQILLIAA
2460 2470 2480 2490 2500
AVLAVLVRPG ICSIKEFGVL GSAALVTLIE GTAGVVWNCT TAVGLCNLMR
2510 2520 2530 2540 2550
GGWLAGMSIT WTVYKNVDKP KGKRGGGKGA TLGEIWKSRL NQLTRAEFMA
2560 2570 2580 2590 2600
YRKDGIVEVD RAPARKARRE GRLTGGHPVS RGSAKLRWIT ERGFVKPMGK
2610 2620 2630 2640 2650
VVDLGCGRGG WSYYCATLKH VQEVKGFTKG GPGHEEPQLM QSYGWNLVHM
2660 2670 2680 2690 2700
KSGVDVFHKP AEPADTVLCD IGESNPSCEV EEARTARVLD MVEEWLKKGA
2710 2720 2730 2740 2750
TEFCIKVLCP YTPKIIEKLE KLQRKYGGGL VRVPLSRNST HEMYWVSGAA
2760 2770 2780 2790 2800
GNIIHAVSMT SQVLMGRMDK QNRSGPRYEE DVNLGSGTRS VGKLTEKPDL
2810 2820 2830 2840 2850
RKVGERIRRL REEYQQTWTY DHNNPYRTWN YHGSYEVKPT GSASSMVNGV
2860 2870 2880 2890 2900
VRLLSKPWDM ITNVTTMAMT DTTPFGQQRV FKEKVDTKAP EPPLGVAQIM
2910 2920 2930 2940 2950
DVTTDWLWDF VAREKKPRVC TPEEFKAKVN SHAALGAMFE EQNQWSSARE
2960 2970 2980 2990 3000
AVEDPKFWEM VDEEREAHLK GECHTCIYNM MGKREKKTGE FGKAKGSRAI
3010 3020 3030 3040 3050
WYMWLGARFL EFEALGFLNE DHWMSRENSY GGVEGKGLQK LGYILQEISQ
3060 3070 3080 3090 3100
IPGGKMYADD TAGWDTRITK EDLKNEAKIT KRMEERHRKL AEAIIDLTYR
3110 3120 3130 3140 3150
HKVVKVMRPG PDGKTYMDVI SREDQRGSGQ VVTYALNTFT NLAVQLIRCM
3160 3170 3180 3190 3200
EAEGVVDEDD ITRVRLGRLA KAVEWLRKNG PERLSRMAVS GDDCVVKPID
3210 3220 3230 3240 3250
DRFATALHFL NNMSKIRKDI QEWKPSTGWH NWQEVPFCSH HFNELMLKDG
3260 3270 3280 3290 3300
RTIVVPCRSQ DELIGRARIS PGAGWNVKET ACLSKSYAQM WLLMYFHRRD
3310 3320 3330 3340 3350
LRMMANAICS AVPVNWVPTG RTTWSIHGKG EWMTTEDMLS VWNRVWIEEN
3360 3370 3380 3390 3400
EYMKDKTPLA AWNDIPYLGK REDIWCGSLI GTRTRATWAE NIYAPIMQIR
3410
NLIGEEEYRD YM
Length:3,412
Mass (Da):378,483
Last modified:February 8, 2011 - v2
Checksum:iF89336D9D434A11F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei34121

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti47I → M.1
Natural varianti164V → I.1
Natural varianti168N → D.1
Natural varianti249 – 250VL → FC.2
Natural varianti346E → K.1
Natural varianti444F → S.1
Natural varianti604A → T.1
Natural varianti796D → S.1
Natural varianti843I → Y.1
Natural varianti955R → Q.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF158050 Genomic RNA. Translation: ABN11812.1.
M16614 Genomic RNA. Translation: AAA47786.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF158050 Genomic RNA. Translation: ABN11812.1.
M16614 Genomic RNA. Translation: AAA47786.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FG0X-ray3.90A289-695[»]
ProteinModelPortaliP09732.
SMRiP09732.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

Proteomic databases

PRIDEiP09732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_STEVM
AccessioniPrimary (citable) accession number: P09732
Secondary accession number(s): A3EZ58
, Q88781, Q88782, Q88783, Q88784, Q88785, Q88786, Q88787, Q88788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 8, 2011
Last modified: November 2, 2016
This is version 127 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, 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.