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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei2537 – 25371mRNA capPROSITE-ProRule annotation
Binding sitei2540 – 25401mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2541 – 25411mRNA capPROSITE-ProRule annotation
Binding sitei2543 – 25431mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2548 – 25481mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2552 – 25521mRNA capPROSITE-ProRule annotation
Binding sitei2580 – 25801S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2585 – 25851Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2610 – 26101S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2611 – 26111S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2628 – 26281S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2629 – 26291S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2655 – 26551S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2656 – 26561S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2670 – 26701Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2671 – 26711S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2674 – 26741mRNA capPROSITE-ProRule annotation
Sitei2706 – 27061Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2737 – 27371mRNA capPROSITE-ProRule annotation
Binding sitei2739 – 27391mRNA capPROSITE-ProRule annotation
Sitei2742 – 27421Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2744 – 27441S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1693 – 17008ATPPROSITE-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

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 108107CytoplasmicSequence analysisAdd
BLAST
Transmembranei109 – 12921HelicalSequence analysisAdd
BLAST
Topological domaini130 – 247118ExtracellularSequence analysisAdd
BLAST
Transmembranei248 – 26821HelicalSequence analysisAdd
BLAST
Topological domaini269 – 2735CytoplasmicSequence analysis
Transmembranei274 – 29017HelicalSequence analysisAdd
BLAST
Topological domaini291 – 741451ExtracellularSequence analysisAdd
BLAST
Intramembranei742 – 76221HelicalSequence analysisAdd
BLAST
Topological domaini763 – 7686ExtracellularSequence analysis
Intramembranei769 – 78921HelicalSequence analysisAdd
BLAST
Topological domaini790 – 1138349ExtracellularSequence analysisAdd
BLAST
Transmembranei1139 – 115921HelicalSequence analysisAdd
BLAST
Topological domaini1160 – 121455CytoplasmicSequence analysisAdd
BLAST
Transmembranei1215 – 123521HelicalSequence analysisAdd
BLAST
Topological domaini1236 – 124510LumenalSequence analysis
Transmembranei1246 – 126621HelicalSequence analysisAdd
BLAST
Topological domaini1267 – 130438CytoplasmicSequence analysisAdd
BLAST
Transmembranei1305 – 132521HelicalSequence analysisAdd
BLAST
Topological domaini1326 – 133914LumenalSequence analysisAdd
BLAST
Transmembranei1340 – 136021HelicalSequence analysisAdd
BLAST
Topological domaini1361 – 13699CytoplasmicSequence analysis
Transmembranei1370 – 139021HelicalSequence analysisAdd
BLAST
Topological domaini1391 – 13933LumenalSequence analysis
Transmembranei1394 – 141421HelicalSequence analysisAdd
BLAST
Topological domaini1415 – 147157CytoplasmicSequence analysisAdd
BLAST
Intramembranei1472 – 149221HelicalSequence analysisAdd
BLAST
Topological domaini1493 – 2167675CytoplasmicSequence analysisAdd
BLAST
Transmembranei2168 – 218821HelicalSequence analysisAdd
BLAST
Topological domaini2189 – 21935LumenalSequence analysis
Intramembranei2194 – 221421HelicalSequence analysisAdd
BLAST
Topological domaini2215 – 22151LumenalSequence analysis
Transmembranei2216 – 223621HelicalSequence analysisAdd
BLAST
Topological domaini2237 – 225115CytoplasmicSequence analysisAdd
BLAST
Transmembranei2252 – 227221Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2273 – 230836LumenalSequence analysisAdd
BLAST
Intramembranei2309 – 232921HelicalSequence analysisAdd
BLAST
Topological domaini2330 – 235425LumenalSequence analysisAdd
BLAST
Intramembranei2355 – 237521HelicalSequence analysisAdd
BLAST
Topological domaini2376 – 23761LumenalSequence analysis
Transmembranei2377 – 239721HelicalSequence analysisAdd
BLAST
Topological domaini2398 – 244043CytoplasmicSequence analysisAdd
BLAST
Transmembranei2441 – 246121HelicalSequence analysisAdd
BLAST
Topological domaini2462 – 24665LumenalSequence analysis
Transmembranei2467 – 248721HelicalSequence analysisAdd
BLAST
Topological domaini2488 – ›3412›925CytoplasmicSequence 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 – ›3412›3411Genome polyproteinPRO_0000405143Add
BLAST
Chaini2 – 103102Capsid protein CBy similarityPRO_0000037735Add
BLAST
Propeptidei104 – 12118ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000405144Add
BLAST
Chaini122 – 288167prMBy similarityPRO_0000405145Add
BLAST
Chaini122 – 21392Peptide prBy similarityPRO_0000037736Add
BLAST
Chaini214 – 28875Small envelope protein MBy similarityPRO_0000037737Add
BLAST
Chaini289 – 789501Envelope protein EBy similarityPRO_0000037738Add
BLAST
Chaini790 – 1141352Non-structural protein 1By similarityPRO_0000037739Add
BLAST
Chaini1142 – 1368227Non-structural protein 2ABy similarityPRO_0000037740Add
BLAST
Chaini1369 – 1499131Serine protease subunit NS2BBy similarityPRO_0000037741Add
BLAST
Chaini1500 – 2117618Serine protease NS3By similarityPRO_0000037742Add
BLAST
Chaini2118 – 2243126Non-structural protein 4ABy similarityPRO_0000405146Add
BLAST
Peptidei2244 – 226623Peptide 2kBy similarityPRO_0000405147Add
BLAST
Chaini2267 – 2524258Non-structural protein 4BBy similarityPRO_0000405148Add
BLAST
Chaini2525 – ›3412›888RNA-directed RNA polymerase NS5By similarityPRO_0000405149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi291 ↔ 318By similarity
Disulfide bondi348 ↔ 404By similarity
Disulfide bondi362 ↔ 393By similarity
Disulfide bondi380 ↔ 409By similarity
Disulfide bondi478 ↔ 576By similarity
Disulfide bondi593 ↔ 624By similarity
Glycosylationi919 – 9191N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi964 – 9641N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi996 – 9961N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2335 – 23351N-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
Sitei103 – 1042Cleavage; by viral protease NS3Sequence analysis
Sitei121 – 1222Cleavage; by host signal peptidaseBy similarity
Sitei213 – 2142Cleavage; by host furinBy similarity
Sitei288 – 2892Cleavage; by host signal peptidaseSequence analysis
Sitei789 – 7902Cleavage; by host signal peptidaseSequence analysis
Sitei1141 – 11422Cleavage; by hostBy similarity
Sitei1368 – 13692Cleavage; by viral protease NS3Sequence analysis
Sitei1499 – 15002Cleavage; by autolysisSequence analysis
Sitei2117 – 21182Cleavage; by autolysisSequence analysis
Sitei2243 – 22442Cleavage; by viral protease NS3Sequence analysis
Sitei2266 – 22672Cleavage; by host signal peptidaseSequence analysis
Sitei2524 – 25252Cleavage; 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

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1500 – 1677178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1680 – 1836157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1847 – 2011165Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2525 – 2790266mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3054 – 3206153RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1422 – 146140Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1784 – 17874DEAH 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: 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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei3412 – 34121

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471I → M.
Natural varianti164 – 1641V → I.
Natural varianti168 – 1681N → D.
Natural varianti249 – 2502VL → FC.
Natural varianti346 – 3461E → K.
Natural varianti444 – 4441F → S.
Natural varianti604 – 6041A → T.
Natural varianti796 – 7961D → S.
Natural varianti843 – 8431I → Y.
Natural varianti955 – 9551R → Q.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4FG0X-ray3.90A289-695[»]
ProteinModelPortaliP09732.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.

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: September 7, 2016
This is version 125 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.