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Protein

Genome polyprotein

Gene
N/A
Organism
Tick-borne encephalitis virus European subtype (strain Neudoerfl) (NEUV) (Neudoerfl virus)
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
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. Inhibits host SCRIB and prevents activation of downstream JAK-STAT signaling pathway (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1543Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1567Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1627Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Binding sitei2524mRNA capPROSITE-ProRule annotation1
Binding sitei2527mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2528mRNA capPROSITE-ProRule annotation1
Binding sitei2530mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2535mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2539mRNA capPROSITE-ProRule annotation1
Binding sitei2567S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2572Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2597S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2598S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2616S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2642S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2643S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2657Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2658S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2661mRNA capPROSITE-ProRule annotation1
Sitei2694Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2725mRNA capPROSITE-ProRule annotation1
Binding sitei2727mRNA capPROSITE-ProRule annotation1
Sitei2730Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2732S-adenosyl-L-methioninePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1688 – 1695ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

Keywords - Biological processi

Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Protein family/group databases

MEROPSiS07.001.
TCDBi1.G.3.1.1. the viral pore-forming membrane fusion protein-3 (vmfp3) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
Non-structural protein 5
OrganismiTick-borne encephalitis virus European subtype (strain Neudoerfl) (NEUV) (Neudoerfl virus)
Taxonomic identifieri11088 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirustick-borne encephalitis virus group
Virus hostiIxodes persulcatus (Taiga tick) [TaxID: 34615]
Ixodes ricinus (Common tick) [TaxID: 34613]
Proteomesi
  • UP000007402 Componenti: Genome

Subcellular locationi

Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation

  • Note: Remains non-covalently associated to NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 98CytoplasmicSequence analysisAdd BLAST98
Transmembranei99 – 119HelicalSequence analysisAdd BLAST21
Topological domaini120 – 242ExtracellularSequence analysisAdd BLAST123
Transmembranei243 – 260HelicalSequence analysisAdd BLAST18
Topological domaini261CytoplasmicSequence analysis1
Transmembranei262 – 280HelicalSequence analysisAdd BLAST19
Topological domaini281 – 727ExtracellularSequence analysisAdd BLAST447
Intramembranei728 – 748HelicalSequence analysisAdd BLAST21
Topological domaini749 – 759ExtracellularSequence analysisAdd BLAST11
Intramembranei760 – 780HelicalSequence analysisAdd BLAST21
Topological domaini781 – 1132ExtracellularSequence analysisAdd BLAST352
Transmembranei1133 – 1153HelicalSequence analysisAdd BLAST21
Topological domaini1154 – 1158CytoplasmicSequence analysis5
Transmembranei1159 – 1179HelicalSequence analysisAdd BLAST21
Topological domaini1180 – 1187LumenalSequence analysis8
Transmembranei1188 – 1208HelicalSequence analysisAdd BLAST21
Topological domaini1209 – 1293CytoplasmicSequence analysisAdd BLAST85
Transmembranei1294 – 1314HelicalSequence analysisAdd BLAST21
Topological domaini1315 – 1327LumenalSequence analysisAdd BLAST13
Transmembranei1328 – 1348HelicalSequence analysisAdd BLAST21
Topological domaini1349 – 1359CytoplasmicSequence analysisAdd BLAST11
Transmembranei1360 – 1378HelicalSequence analysisAdd BLAST19
Topological domaini1379 – 1382LumenalSequence analysis4
Transmembranei1383 – 1403HelicalSequence analysisAdd BLAST21
Topological domaini1404 – 1454CytoplasmicSequence analysisAdd BLAST51
Intramembranei1455 – 1475HelicalSequence analysisAdd BLAST21
Topological domaini1476 – 2160CytoplasmicSequence analysisAdd BLAST685
Transmembranei2161 – 2181HelicalSequence analysisAdd BLAST21
Topological domaini2182 – 2189LumenalSequence analysis8
Intramembranei2190 – 2210HelicalSequence analysisAdd BLAST21
Topological domaini2211LumenalSequence analysis1
Transmembranei2212 – 2232HelicalSequence analysisAdd BLAST21
Topological domaini2233 – 2244CytoplasmicSequence analysisAdd BLAST12
Transmembranei2245 – 2265Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2266 – 2299LumenalSequence analysisAdd BLAST34
Intramembranei2300 – 2320HelicalSequence analysisAdd BLAST21
Topological domaini2321 – 2343LumenalSequence analysisAdd BLAST23
Intramembranei2344 – 2364HelicalSequence analysisAdd BLAST21
Topological domaini2365 – 2368LumenalSequence analysis4
Transmembranei2369 – 2389HelicalSequence analysisAdd BLAST21
Topological domaini2390 – 2432CytoplasmicSequence analysisAdd BLAST43
Transmembranei2433 – 2453HelicalSequence analysisAdd BLAST21
Topological domaini2454 – 2477LumenalSequence analysisAdd BLAST24
Transmembranei2478 – 2498HelicalSequence analysisAdd BLAST21
Topological domaini2499 – 3414CytoplasmicSequence analysisAdd BLAST916

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
ChainiPRO_00004051751 – 3414Genome polyproteinAdd BLAST3414
ChainiPRO_00000378151 – 96Capsid protein CBy similarityAdd BLAST96
PropeptideiPRO_000040517697 – 117ER anchor for the protein C, removed in mature form by serine protease NS3By similarityAdd BLAST21
ChainiPRO_0000405177118 – 280prMBy similarityAdd BLAST163
ChainiPRO_0000037816118 – 205Peptide prBy similarityAdd BLAST88
ChainiPRO_0000037817206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037818281 – 776Envelope protein EBy similarityAdd BLAST496
ChainiPRO_0000037819777 – 1128Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000378201129 – 1358Non-structural protein 2ABy similarityAdd BLAST230
ChainiPRO_00000378211359 – 1489Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000378221490 – 2110Serine protease NS3By similarityAdd BLAST621
ChainiPRO_00000378232111 – 2236Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004051782237 – 2259Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000378242260 – 2511Non-structural protein 4BBy similarityAdd BLAST252
ChainiPRO_00000378252512 – 3414RNA-directed RNA polymerase NS5By similarityAdd BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi144N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi283 ↔ 310
Disulfide bondi340 ↔ 396
Disulfide bondi354 ↔ 385
Disulfide bondi372 ↔ 401
Glycosylationi434N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi466 ↔ 570
Disulfide bondi587 ↔ 618
Glycosylationi861N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi983N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi999N-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
Sitei96 – 97Cleavage; by viral protease NS3Sequence analysis2
Sitei117 – 118Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinBy similarity2
Sitei280 – 281Cleavage; by host signal peptidaseSequence analysis2
Sitei776 – 777Cleavage; by host signal peptidaseSequence analysis2
Sitei1128 – 1129Cleavage; by hostSequence analysis2
Sitei1358 – 1359Cleavage; by viral protease NS3Sequence analysis2
Sitei1489 – 1490Cleavage; by autolysisSequence analysis2
Sitei2110 – 2111Cleavage; by autolysisSequence analysis2
Sitei2236 – 2237Cleavage; by viral protease NS3Sequence analysis2
Sitei2259 – 2260Cleavage; by host signal peptidaseSequence analysis2
Sitei2511 – 2512Cleavage; by viral protease NS3Sequence analysis2

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. NS5 interacts with human SCRIB (via PDZ domain); this interaction inhibits STAT1 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

Structurei

Secondary structure

13414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi282 – 285Combined sources4
Beta strandi290 – 294Combined sources5
Beta strandi300 – 306Combined sources7
Beta strandi311 – 315Combined sources5
Beta strandi318 – 332Combined sources15
Beta strandi334 – 352Combined sources19
Helixi363 – 366Combined sources4
Beta strandi370 – 380Combined sources11
Helixi381 – 383Combined sources3
Beta strandi389 – 401Combined sources13
Beta strandi406 – 411Combined sources6
Turni414 – 416Combined sources3
Beta strandi418 – 425Combined sources8
Beta strandi441 – 446Combined sources6
Beta strandi451 – 455Combined sources5
Helixi457 – 459Combined sources3
Beta strandi460 – 467Combined sources8
Helixi468 – 470Combined sources3
Beta strandi477 – 482Combined sources6
Beta strandi491 – 496Combined sources6
Helixi497 – 501Combined sources5
Helixi518 – 521Combined sources4
Beta strandi522 – 524Combined sources3
Beta strandi534 – 536Combined sources3
Helixi541 – 547Combined sources7
Turni548 – 550Combined sources3
Beta strandi553 – 557Combined sources5
Beta strandi560 – 562Combined sources3
Beta strandi567 – 573Combined sources7
Beta strandi591 – 600Combined sources10
Beta strandi602 – 604Combined sources3
Beta strandi606 – 612Combined sources7
Beta strandi616 – 619Combined sources4
Beta strandi622 – 626Combined sources5
Beta strandi636 – 641Combined sources6
Beta strandi643 – 645Combined sources3
Beta strandi651 – 655Combined sources5
Beta strandi658 – 665Combined sources8
Beta strandi668 – 674Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N6Gelectron microscopy16.00A/B/C281-675[»]
1NA4electron microscopy-A/B/C281-675[»]
1SVBX-ray1.90A281-675[»]
1URZX-ray2.70A/B/C/D/E/F281-681[»]
ProteinModelPortaliP14336.
SMRiP14336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14336.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1490 – 1669Peptidase S7PROSITE-ProRule annotationAdd BLAST180
Domaini1675 – 1831Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1841 – 2000Helicase C-terminalPROSITE-ProRule annotationAdd BLAST160
Domaini2512 – 2776mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3040 – 3189RdRp catalyticPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 68Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST45
Regioni378 – 391Involved in fusionAdd BLAST14
Regioni1410 – 1449Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1779 – 1782DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1970 – 1973Poly-Asp4
Compositional biasi2201 – 2204Poly-Leu4

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. 1 hit.
3.30.387.10. 1 hit.
3.30.67.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_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.
IPR013756. GlyE_cen_dom_subdom2.
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.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR04240. flavi_E_stem. 1 hit.
PROSITEiPS51527. FLAVIVIRUS_NS2B. 1 hit.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51591. RNA_CAP01_NS5_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV
60 70 80 90 100
AGTARNPVLK AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD
110 120 130 140 150
WMSWLLVITL LGMTLAATVR KERDGSTVIR AEGKDAATQV RVENGTCVIL
160 170 180 190 200
ATDMGSWCDD SLSYECVTID QGEEPVDVDC FCRNVDGVYL EYGRCGKQEG
210 220 230 240 250
SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW VWKNKLLALA
260 270 280 290 300
MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
310 320 330 340 350
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSDTKV
360 370 380 390 400
AARCPTMGPA TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA
410 420 430 440 450
CEAKKKATGH VYDANKIVYT VKVEPHTGDY VAANETHSGR KTASFTISSE
460 470 480 490 500
KTILTMGEYG DVSLLCRVAS GVDLAQTVIL ELDKTVEHLP TAWQVHRDWF
510 520 530 540 550
NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ TGVLLKALAG
560 570 580 590 600
VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD
610 620 630 640 650
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG
660 670 680 690 700
FIEMQLPPGD NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA
710 720 730 740 750
WDFGSAGGFL SSIGKAVHTV LGGAFNSIFG GVGFLPKLLL GVALAWLGLN
760 770 780 790 800
MRNPTMSMSF LLAGGLVLAM TLGVGADVGC AVDTERMELR CGEGLVVWRE
810 820 830 840 850
VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE MAMWRSSVTE
860 870 880 890 900
LNLALAEGEA NLTVVVDKFD PTDYRGGVPG LLKKGKDIKV SWKSWGHSMI
910 920 930 940 950
WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE
960 970 980 990 1000
PTHECDTGVM GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC
1010 1020 1030 1040 1050
SWPASHTIDN ADVVDSELFL PASLAGPRSW YNRIPGYSEQ VKGPWKYTPI
1060 1070 1080 1090 1100
RVIREECPGT TVTINAKCDK RGASVRSTTE SGKVIPEWCC RACTMPPVTF
1110 1120 1130 1140 1150
RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP GIVALFVVLE
1160 1170 1180 1190 1200
YIIRRRPSTG TTVVWGGIVV LALLVTGMVR IESLVRYVVA VGITFHLELG
1210 1220 1230 1240 1250
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPG
1260 1270 1280 1290 1300
ASLEEFWKWG DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG
1310 1320 1330 1340 1350
LVCFLSVASA CSVWRLLKGH REQKGLTWVV PLAGLLGGEG SGIRLLAFWE
1360 1370 1380 1390 1400
LSAHRGRRSF SEPLTVVGVM LTLASGMMRH TSQEALCALA VASFLLLMLV
1410 1420 1430 1440 1450
LGTRKMQLVA EWSGCVEWYP ELVNEGGEVS LRVRQDAMGN FHLTELEKEE
1460 1470 1480 1490 1500
RMMAFWLIAG LAASAIHWSG ILGVMGLWTL TEMLRSSRRS DLVFSGQGGR
1510 1520 1530 1540 1550
ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL
1560 1570 1580 1590 1600
SIDDAVAGPY WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH
1610 1620 1630 1640 1650
QCQPGELILD TGRKLGAIPI DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE
1660 1670 1680 1690 1700
TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK GQITVLDMHP GSGKTHRVLP
1710 1720 1730 1740 1750
ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP AVSDQQAGGA
1760 1770 1780 1790 1800
IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
1810 1820 1830 1840 1850
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPDGEWR DGFDWITEYE
1860 1870 1880 1890 1900
GRTAWFVPSI AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV
1910 1920 1930 1940 1950
VTTDISEMGA NLDVSRVIDG RTNIKPEEVD GKVELTGTRR VTTASAAQRR
1960 1970 1980 1990 2000
GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK EAQILLDNIT TLRGPVATFY
2010 2020 2030 2040 2050
GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH VAANVSSVTD
2060 2070 2080 2090 2100
RSWTWEGPEA NAVDEASGDL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
2110 2120 2130 2140 2150
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM
2160 2170 2180 2190 2200
RMAERDAPEA FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS
2210 2220 2230 2240 2250
LLLLWAGGVG YGNMAGVALI FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL
2260 2270 2280 2290 2300
CSLAGLVAAN EMGFLEKTKA DLSTALWSER EEPRPWSEWT NVDIQPARSW
2310 2320 2330 2340 2350
GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL GGGAPFFGVA
2360 2370 2380 2390 2400
GHVMTLGVVS LIGATPTSLM VGVGLAALHL AIVVSGLEAE LTQRAHKVFF
2410 2420 2430 2440 2450
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLATVLC LMSVVMNRTV
2460 2470 2480 2490 2500
ASITEASAVG LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH
2510 2520 2530 2540 2550
RLWLRASGGR RGGSEGDTLG DLWKRRLNNC TREEFFVYRR TGILETERDK
2560 2570 2580 2590 2600
ARELLRRGET NVGLAVSRGT AKLAWLEERG YATLKGEVVD LGCGRGGWSY
2610 2620 2630 2640 2650
YAASRPAVMS VRAYTIGGKG HEAPKMVTSL GWNLIKFRSG MDVFSMQPHR
2660 2670 2680 2690 2700
ADTVMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR
2710 2720 2730 2740 2750
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR
2760 2770 2780 2790 2800
KLLARFGDQR GPTKVPELDL GVGTRCVVLA EDKVKEQDVQ ERIRALREQY
2810 2820 2830 2840 2850
SETWHMDEEH PYRTWQYWGS YRTAPTGSAA SLINGVVKLL SWPWNAREDV
2860 2870 2880 2890 2900
VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP GTRVIMRAVN DWILERLAQK
2910 2920 2930 2940 2950
SKPRMCSREE FIAKVKSNAA LGAWSDEQNR WASAREAVED PAFWRLVDEE
2960 2970 2980 2990 3000
RERHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
3010 3020 3030 3040 3050
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLNGG LFYADDTAGW
3060 3070 3080 3090 3100
DTKVTNADLE DEEQILRYME GEHKQLATTI MQKAYHAKVV KVARPSRDGG
3110 3120 3130 3140 3150
CIMDVITRRD QRGSGQVVTY ALNTLTNIKV QLIRMMEGEG VIEAADAHNP
3160 3170 3180 3190 3200
RLLRVERWLK EHGEERLGRM LVSGDDCVVR PLDDRFGKAL YFLNDMAKTR
3210 3220 3230 3240 3250
KDIGEWEHSA GFSSWEEVPF CSHHFHELVM KDGRTLVVPC RDQDELVGRA
3260 3270 3280 3290 3300
RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPADWV
3310 3320 3330 3340 3350
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE RVMEWRDVPY
3360 3370 3380 3390 3400
LPKAQDMLCS SLVGRRERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR
3410
HDLHWELRLE SSII
Length:3,414
Mass (Da):378,322
Last modified:May 30, 2000 - v4
Checksum:i35DBCE014B310B79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27495 Genomic RNA. Translation: AAA86870.1.
PIRiA31052. GNWVNE.
RefSeqiNP_043135.1. NC_001672.1.

Genome annotation databases

GeneIDi1489719.
KEGGivg:1489719.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27495 Genomic RNA. Translation: AAA86870.1.
PIRiA31052. GNWVNE.
RefSeqiNP_043135.1. NC_001672.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N6Gelectron microscopy16.00A/B/C281-675[»]
1NA4electron microscopy-A/B/C281-675[»]
1SVBX-ray1.90A281-675[»]
1URZX-ray2.70A/B/C/D/E/F281-681[»]
ProteinModelPortaliP14336.
SMRiP14336.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.001.
TCDBi1.G.3.1.1. the viral pore-forming membrane fusion protein-3 (vmfp3) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489719.
KEGGivg:1489719.

Miscellaneous databases

EvolutionaryTraceiP14336.

Family and domain databases

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 1 hit.
3.30.387.10. 1 hit.
3.30.67.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_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.
IPR013756. GlyE_cen_dom_subdom2.
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.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 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_TBEVW
AccessioniPrimary (citable) accession number: P14336
Secondary accession number(s): Q88493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.