UniProtKB - P27395 (POLG_JAEV1)
Genome polyprotein
Functioni
Miscellaneous
Catalytic activityi
- EC:2.7.7.48PROSITE-ProRule annotation
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphate1 PublicationEC:3.6.1.151 Publication
- EC:3.6.4.131 Publication
- a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteinePROSITE-ProRule annotationEC:2.1.1.56PROSITE-ProRule annotation
- a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteinePROSITE-ProRule annotationEC:2.1.1.56PROSITE-ProRule annotation
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H+ + S-adenosyl-L-homocysteinePROSITE-ProRule annotationEC:2.1.1.57PROSITE-ProRule annotation
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H+ + S-adenosyl-L-homocysteinePROSITE-ProRule annotationEC:2.1.1.57PROSITE-ProRule annotation
- 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.1 Publication EC:3.4.21.91
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 1555 | Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1579 | Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1639 | Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation | 1 | |
Sitei | 1962 | Involved in NS3 ATPase and RTPase activitiesBy similarity | 1 | |
Sitei | 1965 | Involved in NS3 ATPase and RTPase activitiesBy similarity | 1 | |
Sitei | 2540 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Sitei | 2543 | mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Sitei | 2544 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Sitei | 2546 | mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Sitei | 2551 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Sitei | 2555 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Binding sitei | 2583 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Active sitei | 2588 | For 2'-O-MTase activityBy similarity | 1 | |
Sitei | 2588 | Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 2613 | S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Binding sitei | 2614 | S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Binding sitei | 2631 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Binding sitei | 2632 | S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Binding sitei | 2658 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Binding sitei | 2659 | S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Active sitei | 2673 | For 2'-O-MTase activityBy similarity | 1 | |
Sitei | 2673 | Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 2674 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Sitei | 2677 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Active sitei | 2709 | For 2'-O-MTase activityBy similarity | 1 | |
Sitei | 2709 | Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation | 1 | |
Sitei | 2740 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Sitei | 2742 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Active sitei | 2745 | For 2'-O-MTase activityBy similarity | 1 | |
Sitei | 2745 | Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 2747 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Metal bindingi | 2967 | Zinc 11 Publication | 1 | |
Metal bindingi | 2971 | Zinc 1; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 2976 | Zinc 11 Publication | 1 | |
Metal bindingi | 2979 | Zinc 11 Publication | 1 | |
Metal bindingi | 3244 | Zinc 2; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 3260 | Zinc 21 Publication | 1 | |
Metal bindingi | 3379 | Zinc 21 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1698 – 1705 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- double-stranded RNA binding Source: InterPro
- metal ion binding Source: UniProtKB-KW
- mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
- mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB-EC
- protein dimerization activity Source: InterPro
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
- serine-type endopeptidase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
- fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB-KW
- suppression by virus of host STAT1 activity Source: UniProtKB-KW
- suppression by virus of host STAT2 activity Source: UniProtKB-KW
- suppression by virus of host TYK2 activity Source: UniProtKB-KW
- suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Enzyme and pathway databases
BRENDAi | 3.6.4.12, 2787 3.6.4.13, 2787 |
Protein family/group databases
MEROPSi | S07.003 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved 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 Serine protease NS3 (EC:3.4.21.911 Publication, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication) Alternative name(s): Flavivirin protease NS3 catalytic subunit Non-structural protein 3 RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation) Alternative name(s): Non-structural protein 5 |
Organismi | Japanese encephalitis virus (strain SA-14) (JEV) |
Taxonomic identifieri | 11073 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Flasuviricetes › Amarillovirales › Flaviviridae › Flavivirus › |
Virus hosti | Ardeidae (herons) [TaxID: 8899] Bos taurus (Bovine) [TaxID: 9913] Culex gelidus [TaxID: 308713] Culex tritaeniorhynchus (Mosquito) [TaxID: 7178] Equus caballus (Horse) [TaxID: 9796] Homo sapiens (Human) [TaxID: 9606] Sus scrofa (Pig) [TaxID: 9823] |
Proteomesi |
|
Subcellular locationi
- Host endoplasmic reticulum membrane Sequence analysis; Multi-pass membrane protein Sequence analysis
- Virion By similarity
- Host nucleus By similarity
- Host cytoplasm By similarity
- host perinuclear region By similarity
- Secreted By similarity
- Virion membrane By similarity; Multi-pass membrane protein By similarity
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis Note: ER membrane retention is mediated by the transmembrane domains.By similarity
- Virion membrane Curated; Multi-pass membrane protein By similarity
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis Note: ER membrane retention is mediated by the transmembrane domains.By similarity
- Secreted By similarity
- Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side By similarity Note: Located in RE-derived vesicles hosting the replication complex.By similarity
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
- Host endoplasmic reticulum membrane ; Multi-pass membrane protein By similarity
- Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation Note: Remains non-covalently associated to serine protease subunit NS2B.PROSITE-ProRule annotation
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity Note: Located in RE-associated vesicles hosting the replication complex.By similarity
- Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity Note: Located in RE-derived vesicles hosting the replication complex.By similarity
- Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side By similarity
- Host nucleus 1 Publication Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles.By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 109 | CytoplasmicSequence analysisAdd BLAST | 108 | |
Transmembranei | 110 – 130 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 131 – 253 | ExtracellularSequence analysisAdd BLAST | 123 | |
Transmembranei | 254 – 274 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 275 – 279 | CytoplasmicSequence analysis | 5 | |
Transmembranei | 280 – 294 | HelicalCuratedAdd BLAST | 15 | |
Topological domaini | 295 – 746 | ExtracellularSequence analysisAdd BLAST | 452 | |
Transmembranei | 747 – 767 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 768 – 773 | CytoplasmicSequence analysis | 6 | |
Transmembranei | 774 – 794 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 795 – 1219 | ExtracellularSequence analysisAdd BLAST | 425 | |
Transmembranei | 1220 – 1240 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1241 – 1250 | CytoplasmicSequence analysis | 10 | |
Transmembranei | 1251 – 1271 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1272 | LumenalSequence analysis | 1 | |
Transmembranei | 1273 – 1293 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1294 – 1309 | CytoplasmicSequence analysisAdd BLAST | 16 | |
Transmembranei | 1310 – 1330 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1331 – 1341 | LumenalSequence analysisAdd BLAST | 11 | |
Transmembranei | 1342 – 1362 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1363 – 1374 | CytoplasmicSequence analysisAdd BLAST | 12 | |
Transmembranei | 1375 – 1395 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1396 – 1398 | LumenalSequence analysis | 3 | |
Transmembranei | 1399 – 1419 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1420 – 1476 | CytoplasmicSequence analysisAdd BLAST | 57 | |
Intramembranei | 1477 – 1497 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1498 – 2173 | CytoplasmicSequence analysisAdd BLAST | 676 | |
Transmembranei | 2174 – 2194 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2195 – 2199 | LumenalSequence analysis | 5 | |
Intramembranei | 2200 – 2220 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2221 | LumenalSequence analysis | 1 | |
Transmembranei | 2222 – 2242 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2243 – 2257 | CytoplasmicSequence analysisAdd BLAST | 15 | |
Transmembranei | 2258 – 2278 | Helical; Note=Signal for NS4BSequence analysisAdd BLAST | 21 | |
Topological domaini | 2279 – 2311 | LumenalSequence analysisAdd BLAST | 33 | |
Intramembranei | 2312 – 2332 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2333 – 2368 | LumenalSequence analysisAdd BLAST | 36 | |
Transmembranei | 2369 – 2389 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2390 – 2444 | CytoplasmicSequence analysisAdd BLAST | 55 | |
Transmembranei | 2445 – 2465 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2466 – 2469 | LumenalSequence analysis | 4 | |
Transmembranei | 2470 – 2490 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2491 – 3432 | CytoplasmicSequence analysisAdd BLAST | 942 |
GO - Cellular componenti
- extracellular region Source: UniProtKB-SubCell
- host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
- host cell nucleus Source: UniProtKB-SubCell
- host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
- viral capsid Source: UniProtKB-KW
- viral envelope Source: UniProtKB-KW
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, Viral envelope protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1379 | E → A: No effect on human SPCS1 binding. 1 Publication | 1 | |
Mutagenesisi | 1385 | G → A: Reduces human SPCS1 binding. 1 Publication | 1 | |
Mutagenesisi | 1405 | P → A: Slightly reduces human SPCS1 binding. 1 Publication | 1 | |
Mutagenesisi | 1410 | G → A: Slightly reduces human SPCS1 binding. 1 Publication | 1 | |
Mutagenesisi | 1420 | G → A: Slightly reduces human SPCS1 binding. 1 Publication | 1 | |
Mutagenesisi | 1485 | P → A: Reduces SPCS1 human binding. 1 Publication | 1 | |
Mutagenesisi | 1488 | I → A: Slightly reduces human SPCS1 binding. 1 Publication | 1 | |
Mutagenesisi | 1703 | G → A: Complete loss of both the ATPase and helicase activities. 1 Publication | 1 | |
Mutagenesisi | 1704 | K → D, E, H, N, Q or R: Complete loss of both the ATPase and helicase activities. 1 Publication | 1 | |
Mutagenesisi | 1705 | T → A: Complete loss of both the ATPase and helicase activities. 1 Publication | 1 | |
Mutagenesisi | 1961 | Q → A: 80% loss of ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 1962 | R → A: 90% loss of ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 1965 | R → A: Complete loss of ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 1968 | R → A: Complete loss of ATPase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000405188 | 1 – 3432 | Genome polyproteinAdd BLAST | 3432 | |
ChainiPRO_0000037836 | 1 – 105 | Capsid protein CAdd BLAST | 105 | |
PropeptideiPRO_0000405189 | 106 – 127 | ER anchor for the capsid protein C, removed in mature form by serine protease NS3Add BLAST | 22 | |
ChainiPRO_0000405190 | 128 – 294 | Protein prMAdd BLAST | 167 | |
ChainiPRO_0000037837 | 128 – 219 | Peptide prAdd BLAST | 92 | |
ChainiPRO_0000037838 | 220 – 294 | Small envelope protein MBy similarityAdd BLAST | 75 | |
ChainiPRO_0000037839 | 295 – 794 | Envelope protein EAdd BLAST | 500 | |
ChainiPRO_0000037840 | 795 – 1146 | Non-structural protein 1Add BLAST | 352 | |
ChainiPRO_0000037841 | 1147 – 1373 | Non-structural protein 2AAdd BLAST | 227 | |
ChainiPRO_0000037842 | 1374 – 1504 | Serine protease subunit NS2BAdd BLAST | 131 | |
ChainiPRO_0000037843 | 1505 – 2123 | Serine protease NS3Add BLAST | 619 | |
ChainiPRO_0000037844 | 2124 – 2249 | Non-structural protein 4AAdd BLAST | 126 | |
PeptideiPRO_0000405191 | 2250 – 2272 | Peptide 2kAdd BLAST | 23 | |
ChainiPRO_0000037845 | 2273 – 2527 | Non-structural protein 4BAdd BLAST | 255 | |
ChainiPRO_0000037846 | 2528 – 3432 | RNA-directed RNA polymerase NS5Add BLAST | 905 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 142 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 297 ↔ 324 | By similarity | ||
Disulfide bondi | 354 ↔ 415 | By similarity | ||
Disulfide bondi | 354 ↔ 410 | By similarity | ||
Disulfide bondi | 368 ↔ 399 | By similarity | ||
Disulfide bondi | 386 ↔ 415 | By similarity | ||
Disulfide bondi | 386 ↔ 410 | By similarity | ||
Glycosylationi | 448 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Disulfide bondi | 484 ↔ 581 | By similarity | ||
Disulfide bondi | 598 ↔ 629 | By similarity | ||
Disulfide bondi | 798 ↔ 809 | By similarity | ||
Disulfide bondi | 849 ↔ 937 | By similarity | ||
Glycosylationi | 924 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 973 ↔ 1017 | By similarity | ||
Glycosylationi | 1001 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 1074 ↔ 1123 | By similarity | ||
Disulfide bondi | 1085 ↔ 1106 | By similarity | ||
Disulfide bondi | 1107 ↔ 1110 | By similarity | ||
Modified residuei | 2583 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 105 – 106 | Cleavage; by viral protease NS3By similarity | 2 | |
Sitei | 127 – 128 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 219 – 220 | Cleavage; by host furinBy similarity | 2 | |
Sitei | 294 – 295 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 794 – 795 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 1146 – 1147 | Cleavage; by hostBy similarity | 2 | |
Sitei | 1373 – 1374 | Cleavage; by viral protease NS3By similarity | 2 | |
Sitei | 1504 – 1505 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 2123 – 2124 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 2249 – 2250 | Cleavage; by viral protease NS3By similarity | 2 | |
Sitei | 2272 – 2273 | Cleavage; by host signal peptidaseBy similarity | 2 | |
Sitei | 2527 – 2528 | Cleavage; by viral protease NS3By similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
PRIDEi | P27395 |
Interactioni
Subunit structurei
Capsid protein C: Homodimer.
Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway. Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi.
Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1: Homohexamer when secreted. NS1 interacts with NS4B.
Interacts with host complement protein CFH; this interaction leads to the degradation of C3. Non-structural protein 2A:
Interacts (via N-terminus) with serine protease NS3. Non-structural protein 2B:
Forms a heterodimer with serine protease NS3 (PubMed:7897348). May form homooligomers.
Interacts with human SPCS1 (PubMed:29593046). Serine protease NS3:
Forms a heterodimer with NS2B (PubMed:7897348).
Interacts with NS4B.
Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Non-structural protein 4B:
Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer.
Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation.
Interacts with serine protease NS3.
By similarity2 PublicationsGO - Molecular functioni
- protein dimerization activity Source: InterPro
Structurei
Secondary structure
3D structure databases
SMRi | P27395 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P27395 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1505 – 1682 | Peptidase S7PROSITE-ProRule annotationAdd BLAST | 178 | |
Domaini | 1685 – 1841 | Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST | 157 | |
Domaini | 1852 – 2017 | Helicase C-terminalPROSITE-ProRule annotationAdd BLAST | 166 | |
Domaini | 2528 – 2793 | mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST | 266 | |
Domaini | 3057 – 3209 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 153 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 15 | Interaction with host EXOC1By similarityAdd BLAST | 14 | |
Regioni | 37 – 72 | Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST | 36 | |
Regioni | 392 – 405 | Fusion peptideBy similarityAdd BLAST | 14 | |
Regioni | 1374 – 1423 | Interaction with human SPCS11 PublicationAdd BLAST | 50 | |
Regioni | 1427 – 1466 | Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST | 40 | |
Regioni | 1458 – 1505 | Interaction with human SPCS11 PublicationAdd BLAST | 48 | |
Regioni | 1689 – 1692 | Important for RNA-bindingBy similarity | 4 | |
Regioni | 2168 – 2172 | Regulates the ATPase activity of NS3 helicaseBy similarity | 5 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1789 – 1792 | DEAH boxPROSITE-ProRule annotation | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
CDDi | cd12149, Flavi_E_C, 1 hit |
Gene3Di | 1.10.10.930, 1 hit 1.10.8.970, 1 hit 1.20.1280.260, 1 hit 2.40.10.10, 1 hit 2.60.260.50, 1 hit 2.60.40.350, 1 hit 2.60.98.10, 1 hit 3.30.387.10, 1 hit 3.30.67.10, 1 hit |
InterProi | View protein in InterPro IPR011492, DEAD_Flavivir IPR043502, DNA/RNA_pol_sf IPR000069, Env_glycoprot_M_flavivir IPR038302, Env_glycoprot_M_sf_flavivir IPR013755, Flav_gly_cen_dom_subdom1 IPR001122, Flavi_capsidC IPR037172, Flavi_capsidC_sf IPR027287, Flavi_E_Ig-like IPR026470, Flavi_E_Stem/Anchor_dom IPR038345, Flavi_E_Stem/Anchor_dom_sf IPR001157, Flavi_NS1 IPR000752, Flavi_NS2A IPR000487, Flavi_NS2B IPR000404, Flavi_NS4A IPR001528, Flavi_NS4B IPR002535, Flavi_propep IPR038688, Flavi_propep_sf IPR000336, Flavivir/Alphavir_Ig-like_sf IPR001850, Flavivirus_NS3_S7 IPR014412, Gen_Poly_FLV IPR011998, Glycoprot_cen/dimer IPR036253, Glycoprot_cen/dimer_sf IPR038055, Glycoprot_E_dimer_dom IPR013756, GlyE_cen_dom_subdom2 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 IPR043504, Peptidase_S1_PA_chymotrypsin IPR000208, RNA-dir_pol_flavivirus IPR007094, RNA-dir_pol_PSvirus IPR002877, rRNA_MeTrfase_FtsJ_dom IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF01003, 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 |
PIRSFi | PIRSF003817, Gen_Poly_FLV, 1 hit |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit SM00490, HELICc, 1 hit |
SUPFAMi | SSF101257, SSF101257, 1 hit SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 2 hits SSF53335, SSF53335, 1 hit SSF56672, SSF56672, 1 hit SSF56983, SSF56983, 1 hit SSF81296, SSF81296, 1 hit |
TIGRFAMsi | TIGR04240, flavi_E_stem, 1 hit |
PROSITEi | View protein in PROSITE PS51527, 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 |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL
60 70 80 90 100
ITFFKFTALA PTKALLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR
110 120 130 140 150
KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI
160 170 180 190 200
VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE
210 220 230 240 250
VYVQYGRCTR TRHSKRSRRS VSVQTHGESS LVNKKEAWLD STKATRYLMK
260 270 280 290 300
TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM
310 320 330 340 350
GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV
360 370 380 390 400
RSYCYHASVT DISTVARCPT TGEAHNEKRA DSSYVCKQGF TDRGWGNGCG
410 420 430 440 450
LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS
460 470 480 490 500
AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV
510 520 530 540 550
GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEGAH ATKQSVVALG
560 570 580 590 600
SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE
610 620 630 640 650
KFSFAKNPVD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT
660 670 680 690 700
VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA
710 720 730 740 750
FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGRAVHQVFG GAFRTLFGGM
760 770 780 790 800
SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI
810 820 830 840 850
DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG
860 870 880 890 900
VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM
910 920 930 940 950
TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE
960 970 980 990 1000
DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY
1010 1020 1030 1040 1050
NDTWKLERAV FGEVKSCTWP ETHTLWGDDV EESELIIPHT IAGPKSKHNR
1060 1070 1080 1090 1100
REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCSKRGP SVRTTTDSGK
1110 1120 1130 1140 1150
LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVMHDETTLV RSQVDAFKGE
1160 1170 1180 1190 1200
MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGVLLVL MLGGITYTDL
1210 1220 1230 1240 1250
ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN
1260 1270 1280 1290 1300
VILVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV
1310 1320 1330 1340 1350
LALLTPGMRA LYLDTYRIIL LVIGICSLLH ERKKTMAKKK GAVLLGLALT
1360 1370 1380 1390 1400
STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE
1410 1420 1430 1440 1450
SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV
1460 1470 1480 1490 1500
KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK
1510 1520 1530 1540 1550
TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF
1560 1570 1580 1590 1600
HTLWHTTRGA AIMSGEGKLT PYWGSVREDR IAYGGPWRFD RKWNGTDDVQ
1610 1620 1630 1640 1650
VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI
1660 1670 1680 1690 1700
IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP
1710 1720 1730 1740 1750
GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS
1760 1770 1780 1790 1800
AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA
1810 1820 1830 1840 1850
ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS
1860 1870 1880 1890 1900
SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP
1910 1920 1930 1940 1950
KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN
1960 1970 1980 1990 2000
PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML
2010 2020 2030 2040 2050
DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW
2060 2070 2080 2090 2100
LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW
2110 2120 2130 2140 2150
LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM
2160 2170 2180 2190 2200
YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI
2210 2220 2230 2240 2250
GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS
2260 2270 2280 2290 2300
QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG
2310 2320 2330 2340 2350
LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS
2360 2370 2380 2390 2400
LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG
2410 2420 2430 2440 2450
WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL
2460 2470 2480 2490 2500
IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH
2510 2520 2530 2540 2550
VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE
2560 2570 2580 2590 2600
FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP
2610 2620 2630 2640 2650
IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL
2660 2670 2680 2690 2700
VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH
2710 2720 2730 2740 2750
RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS
2760 2770 2780 2790 2800
GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH
2810 2820 2830 2840 2850
SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV
2860 2870 2880 2890 2900
NGVVELMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK
2910 2920 2930 2940 2950
EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST
2960 2970 2980 2990 3000
AREAVDDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS
3010 3020 3030 3040 3050
RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD
3060 3070 3080 3090 3100
IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL
3110 3120 3130 3140 3150
TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV
3160 3170 3180 3190 3200
RLMEAEGVIG PQHLEQLPRK TKIAVRTWLF ENGEERVTRM AISGDDCVVK
3210 3220 3230 3240 3250
PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM
3260 3270 3280 3290 3300
KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH
3310 3320 3330 3340 3350
RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLQVWNRVWI
3360 3370 3380 3390 3400
EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN
3410 3420 3430
QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Sequence cautioni
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M55506 Genomic RNA Translation: AAA46248.1 M55506 Genomic RNA Translation: AAA46249.1 Different initiation. |
PIRi | A35519, GNWVJS |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M55506 Genomic RNA Translation: AAA46248.1 M55506 Genomic RNA Translation: AAA46249.1 Different initiation. |
PIRi | A35519, GNWVJS |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2Z83 | X-ray | 1.80 | A | 1685-2123 | [»] | |
3P54 | X-ray | 2.10 | A | 295-700 | [»] | |
4HDG | X-ray | 2.38 | A/B | 2799-3432 | [»] | |
4HDH | X-ray | 2.28 | A/B | 2799-3432 | [»] | |
4K6M | X-ray | 2.60 | A/B | 2528-3432 | [»] | |
4MTP | X-ray | 3.65 | A/B/C/D | 2799-3432 | [»] | |
5MV1 | X-ray | 2.25 | A | 295-700 | [»] | |
5MV2 | X-ray | 2.10 | A | 295-700 | [»] | |
5O19 | X-ray | 2.10 | A | 965-1146 | [»] | |
5O36 | X-ray | 2.60 | A | 965-1158 | [»] | |
5OW2 | X-ray | 1.98 | A/B | 1-105 | [»] | |
5WSN | electron microscopy | 4.30 | B/D/F | 220-293 | [»] | |
5YWO | electron microscopy | 4.70 | B/D/F | 220-293 | [»] | |
5YWP | electron microscopy | 4.60 | B/D/F | 220-293 | [»] | |
SMRi | P27395 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | S07.003 |
Proteomic databases
PRIDEi | P27395 |
Enzyme and pathway databases
BRENDAi | 3.6.4.12, 2787 3.6.4.13, 2787 |
Miscellaneous databases
EvolutionaryTracei | P27395 |
Family and domain databases
CDDi | cd12149, Flavi_E_C, 1 hit |
Gene3Di | 1.10.10.930, 1 hit 1.10.8.970, 1 hit 1.20.1280.260, 1 hit 2.40.10.10, 1 hit 2.60.260.50, 1 hit 2.60.40.350, 1 hit 2.60.98.10, 1 hit 3.30.387.10, 1 hit 3.30.67.10, 1 hit |
InterProi | View protein in InterPro IPR011492, DEAD_Flavivir IPR043502, DNA/RNA_pol_sf IPR000069, Env_glycoprot_M_flavivir IPR038302, Env_glycoprot_M_sf_flavivir IPR013755, Flav_gly_cen_dom_subdom1 IPR001122, Flavi_capsidC IPR037172, Flavi_capsidC_sf IPR027287, Flavi_E_Ig-like IPR026470, Flavi_E_Stem/Anchor_dom IPR038345, Flavi_E_Stem/Anchor_dom_sf IPR001157, Flavi_NS1 IPR000752, Flavi_NS2A IPR000487, Flavi_NS2B IPR000404, Flavi_NS4A IPR001528, Flavi_NS4B IPR002535, Flavi_propep IPR038688, Flavi_propep_sf IPR000336, Flavivir/Alphavir_Ig-like_sf IPR001850, Flavivirus_NS3_S7 IPR014412, Gen_Poly_FLV IPR011998, Glycoprot_cen/dimer IPR036253, Glycoprot_cen/dimer_sf IPR038055, Glycoprot_E_dimer_dom IPR013756, GlyE_cen_dom_subdom2 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 IPR043504, Peptidase_S1_PA_chymotrypsin IPR000208, RNA-dir_pol_flavivirus IPR007094, RNA-dir_pol_PSvirus IPR002877, rRNA_MeTrfase_FtsJ_dom IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF01003, 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 |
PIRSFi | PIRSF003817, Gen_Poly_FLV, 1 hit |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit SM00490, HELICc, 1 hit |
SUPFAMi | SSF101257, SSF101257, 1 hit SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 2 hits SSF53335, SSF53335, 1 hit SSF56672, SSF56672, 1 hit SSF56983, SSF56983, 1 hit SSF81296, SSF81296, 1 hit |
TIGRFAMsi | TIGR04240, flavi_E_stem, 1 hit |
PROSITEi | View protein in PROSITE PS51527, 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_JAEV1 | |
Accessioni | P27395Primary (citable) accession number: P27395 Secondary accession number(s): Q82920 Q82928 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | August 1, 1992 | |
Last modified: | October 7, 2020 | |
This is version 165 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families