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P14335 (POLG_KUNJM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 13 chains:

  1. Peptide 2k
  2. Capsid protein C
    Alternative name(s):
    Core protein
  3. prM
  4. Peptide pr
  5. Small envelope protein M
    Alternative name(s):
    Matrix protein
  6. Envelope protein E
  7. Non-structural protein 1
    Short name=NS1
  8. Non-structural protein 2A
    Short name=NS2A
  9. Serine protease subunit NS2B
    Alternative name(s):
    Flavivirin protease NS2B regulatory subunit
    Non-structural protein 2B
  10. Serine protease NS3
    EC=3.4.21.91
    EC=3.6.1.15
    EC=3.6.4.13
    Alternative name(s):
    Flavivirin protease NS3 catalytic subunit
    Non-structural protein 3
  11. Non-structural protein 4A
    Short name=NS4A
  12. Non-structural protein 4B
    Short name=NS4B
  13. RNA-directed RNA polymerase NS5
    EC=2.1.1.56
    EC=2.1.1.57
    EC=2.7.7.48
    Alternative name(s):
    NS5
OrganismKunjin virus (strain MRM61C) [Complete proteome]
Taxonomic identifier11078 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostCiconiiformes [TaxID: 8920]
Culex annulirostris (Common banded mosquito) [TaxID: 162997]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length3433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity. Ref.4 Ref.5 Ref.7 Ref.8

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. Ref.4 Ref.5 Ref.7 Ref.8

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. Ref.4 Ref.5 Ref.7 Ref.8

Non-structural protein 1 is involved in virus replication and regulation of the innate immune response By similarity. Ref.4 Ref.5 Ref.7 Ref.8

Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential. Ref.4 Ref.5 Ref.7 Ref.8

Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity. Ref.4 Ref.5 Ref.7 Ref.8

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. Ref.4 Ref.5 Ref.7 Ref.8

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. Ref.4 Ref.5 Ref.7 Ref.8

Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter By similarity. Ref.4 Ref.5 Ref.7 Ref.8

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. Ref.4 Ref.5 Ref.7 Ref.8

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 JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway. Ref.4 Ref.5 Ref.7 Ref.8

Catalytic activity

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).

NTP + H2O = NDP + phosphate.

ATP + H2O = ADP + phosphate.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

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).

Subunit structure

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.

Subcellular location

Capsid protein C: Virion Potential Ref.3.

Peptide pr: Secreted By similarity Ref.3.

Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.3.

Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.3.

Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity Ref.3.

Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.3.

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.3.

Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity. Ref.3

Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex. Ref.3

Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.3.

RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus By similarity. Note: Located in RE-associated vesicles hosting the replication complex. Ref.3

Post-translational modification

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.

Sequence similarities

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 mRNA cap 0-1 NS5-type MT domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processActivation 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
Inhibition of host JAK1 by virus
Inhibition of host TYK2 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
   Cellular componentCapsid protein
Host endoplasmic reticulum
Host membrane
Host nucleus
Membrane
Secreted
Viral envelope protein
Virion
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
S-adenosyl-L-methionine
   Molecular functionHelicase
Hydrolase
Methyltransferase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Serine protease
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host JAK1 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host TYK2 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

mRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

mRNA (nucleoside-2'-O-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 34333432Genome polyprotein
PRO_0000405136
Chain2 – 105104Capsid protein C By similarity
PRO_0000037703
Propeptide106 – 12318ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000405137
Chain124 – 290167prM By similarity
PRO_0000405138
Chain124 – 21592Peptide pr By similarity
PRO_0000037704
Chain216 – 29075Small envelope protein M By similarity
PRO_0000037705
Chain291 – 791501Envelope protein E By similarity
PRO_0000037706
Chain792 – 1143352Non-structural protein 1 By similarity
PRO_0000037707
Chain1144 – 1374231Non-structural protein 2A By similarity
PRO_0000037708
Chain1375 – 1505131Serine protease subunit NS2B By similarity
PRO_0000037709
Chain1506 – 2124619Serine protease NS3 By similarity
PRO_0000037710
Chain2125 – 2250126Non-structural protein 4A By similarity
PRO_0000037711
Peptide2251 – 227323Peptide 2k By similarity
PRO_0000405139
Chain2274 – 2528255Non-structural protein 4B By similarity
PRO_0000037712
Chain2529 – 3433905RNA-directed RNA polymerase NS5 By similarity
PRO_0000037713

Regions

Topological domain2 – 105104Cytoplasmic Potential
Transmembrane106 – 12621Helical; Potential
Topological domain127 – 248122Extracellular Potential
Transmembrane249 – 26921Helical; Potential
Topological domain270 – 2734Cytoplasmic Potential
Transmembrane274 – 29017Helical; Potential
Topological domain291 – 743453Extracellular Potential
Intramembrane744 – 76320Helical; Potential
Topological domain764 – 7707Extracellular Potential
Intramembrane771 – 79121Helical; Potential
Topological domain792 – 1142351Extracellular Potential
Transmembrane1143 – 116321Helical; Potential
Topological domain1164 – 121653Cytoplasmic Potential
Transmembrane1217 – 123721Helical; Potential
Topological domain1238 – 124710Lumenal Potential
Transmembrane1248 – 126821Helical; Potential
Topological domain1269 – 129628Cytoplasmic Potential
Transmembrane1297 – 131721Helical; Potential
Topological domain1318 – 134427Lumenal Potential
Transmembrane1345 – 136521Helical; Potential
Topological domain1366 – 137510Cytoplasmic Potential
Transmembrane1376 – 139621Helical; Potential
Topological domain1397 – 13993Lumenal Potential
Transmembrane1400 – 142021Helical; Potential
Topological domain1421 – 147757Cytoplasmic Potential
Intramembrane1478 – 149821Helical; Potential
Topological domain1499 – 2174676Cytoplasmic Potential
Topological domain2196 – 22005Lumenal Potential
Intramembrane2201 – 222121Helical; Potential
Topological domain22221Lumenal Potential
Topological domain2244 – 225815Cytoplasmic Potential
Transmembrane2259 – 227921Helical; Note=Signal for NS4B; Potential
Topological domain2280 – 231233Lumenal Potential
Intramembrane2313 – 233321Helical; Potential
Topological domain2334 – 235825Lumenal Potential
Intramembrane2359 – 237921Helical; Potential
Topological domain23801Lumenal Potential
Transmembrane2381 – 240121Helical; Potential
Topological domain2402 – 244443Cytoplasmic Potential
Transmembrane2445 – 246521Helical; Potential
Topological domain2466 – 24705Lumenal Potential
Transmembrane2471 – 249121Helical; Potential
Topological domain2492 – 3433942Cytoplasmic Potential
Domain1506 – 1683178Peptidase S7
Domain1686 – 1842157Helicase ATP-binding
Domain1853 – 2018166Helicase C-terminal
Domain2529 – 2794266mRNA cap 0-1 NS5-type MT
Domain3058 – 3210153RdRp catalytic
Nucleotide binding1699 – 17068ATP Potential
Region33 – 7442Hydrophobic; homodimerization of capsid protein C By similarity
Region388 – 40114Involved in fusion
Region1428 – 146740Interacts with and activates NS3 protease By similarity
Motif1790 – 17934DEAH box
Compositional bias281 – 2844Poly-Leu
Compositional bias2678 – 26814Poly-Ser

Sites

Active site15561Charge relay system; for serine protease NS3 activity By similarity
Active site15801Charge relay system; for serine protease NS3 activity By similarity
Active site16401Charge relay system; for serine protease NS3 activity By similarity
Binding site25411mRNA cap By similarity
Binding site25441mRNA cap; via carbonyl oxygen By similarity
Binding site25451mRNA cap By similarity
Binding site25471mRNA cap; via carbonyl oxygen By similarity
Binding site25561mRNA cap By similarity
Binding site25841S-adenosyl-L-methionine By similarity
Binding site26141S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26151S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26321S-adenosyl-L-methionine By similarity
Binding site26331S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26591S-adenosyl-L-methionine By similarity
Binding site26601S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26781mRNA cap By similarity
Binding site27411mRNA cap By similarity
Binding site27431mRNA cap By similarity
Binding site27481S-adenosyl-L-methionine By similarity
Site105 – 1062Cleavage; by viral protease NS3 Potential
Site123 – 1242Cleavage; by host signal peptidase By similarity
Site215 – 2162Cleavage; by host furin Potential
Site290 – 2912Cleavage; by host signal peptidase Potential
Site791 – 7922Cleavage; by host signal peptidase Potential
Site1143 – 11442Cleavage; by host Potential
Site1374 – 13752Cleavage; by viral protease NS3 Potential
Site1505 – 15062Cleavage; by autolysis Potential
Site2124 – 21252Cleavage; by autolysis Potential
Site2250 – 22512Cleavage; by viral protease NS3 Potential
Site2273 – 22742Cleavage; by host signal peptidase Potential
Site2528 – 25292Cleavage; by viral protease NS3 Potential
Site25521mRNA cap binding By similarity
Site25891Essential for 2'-O-methyltransferase activity By similarity
Site26741Essential for 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Site26751S-adenosyl-L-methionine binding By similarity
Site27101Essential for 2'-O-methyltransferase activity By similarity
Site27461Essential for 2'-O-methyltransferase activity By similarity

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...); by host Potential
Glycosylation9211N-linked (GlcNAc...); by host Potential
Glycosylation9661N-linked (GlcNAc...); by host Potential
Glycosylation9981N-linked (GlcNAc...); by host Potential
Disulfide bond293 ↔ 320 By similarity
Disulfide bond350 ↔ 406 By similarity
Disulfide bond364 ↔ 395 By similarity
Disulfide bond382 ↔ 411 By similarity
Disulfide bond480 ↔ 578 By similarity
Disulfide bond595 ↔ 626 By similarity

Natural variations

Natural variant1501P → T in strain: Infectious clone pAKUN and Infectious clone FLSDX.
Natural variant8201I → M in strain: Infectious clone pAKUNa and Infectious clone FLSDX.
Natural variant9431N → S in strain: Infectious clone pAKUN and Infectious clone FLSDX.
Natural variant10411P → L in strain: Infectious clone pAKUN and Infectious clone FLSDX.
Natural variant12021I → N in strain: Infectious clone pAKUN; blocks induction of virus-specific membrane structures. Ref.4
Natural variant13181R → K in strain: Infectious clone pAKUN.
Natural variant19671T → I in strain: Infectious clone pAKUN and Infectious clone FLSDX.
Natural variant19741A → V in strain: Infectious clone pAKUN and Infectious clone FLSDX.
Natural variant20231Y → H in strain: Infectious clone pAKUN.
Natural variant20621S → P in strain: Infectious clone pAKUN.
Natural variant23391T → N in strain: Infectious clone pAKUN and Infectious clone FLSDX.

Experimental info

Mutagenesis12921T → P: Restores induction of virus-specific membrane structures; when associated with N-1202. Ref.4
Mutagenesis31811S → F: Increases STAT1 inhibitory function of NS5. Ref.8

Secondary structure

.......................................................................................................................................................................... 3433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14335 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: EE4B888A7D040B99

FASTA3,433381,369
        10         20         30         40         50         60 
MSKKPGGPGK SRAVNMLKRG MPRVLSLTGL KRAMLSLIDG RGPTRFVLAL LAFFRFTAIA 

        70         80         90        100        110        120 
PTRAVLDRWR SVNKQTAMKH LLSFKKELGT LTSAINRRSS KQKKRGGKTG IAFMIGLIAG 

       130        140        150        160        170        180 
VGAVTLSNFQ GKVMMTVNAT DVTDIITIPP AAGKNLCIVR AMDVGHMCDD TITYECPVLS 

       190        200        210        220        230        240 
AGNDPEDIDC WCTKLAVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLSNK KGAWMDSTKA 

       250        260        270        280        290        300 
TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFAV LLLLVAPAYS FNCLGMSNRD 

       310        320        330        340        350        360 
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC YLATVSELST 

       370        380        390        400        410        420 
KAACPTMGEA HNDKRADPSF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CSTKATGRTI 

       430        440        450        460        470        480 
LKENIKYEVA IFVHGPTTVE SHGNYFTQTG AAQAGRFSIT PAAPSYTLKL GEYGEVTVDC 

       490        500        510        520        530        540 
EPRSGIDTSA YYVMTVGTKT FLVHREWFMD LNLPWSSAES NVWRNRETLM EFEEPHATKQ 

       550        560        570        580        590        600 
SVIALGSQEG ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFR 

       610        620        630        640        650        660 
FLGTPADTGH GTVVLELQYT GTDGPCKIPI SSVASLNDLT PVGRLVTVNP FVSVSTANAK 

       670        680        690        700        710        720 
VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTA TLKGAQRLAA LGDTAWDFGS 

       730        740        750        760        770        780 
VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI TQGLLGALLL WMGINARDRS IALTFLAVGG 

       790        800        810        820        830        840 
VLLFLSVNVH ADTGCAIDIS RQELRCGSGV FIHNDVEAWI DRYKYYPETP QGLAKIIQKA 

       850        860        870        880        890        900 
HKEGVCGLRS VSRLEHQMWE AVKDELNTLL KENGVDLSIV VEKQEGMYKS APRRLTATTE 

       910        920        930        940        950        960 
KLEIGWKAWG KSILFAPELA NNTFVIDGPE TKECPTQNRA WNNLEVEDFG FGLTSTRMFL 

       970        980        990       1000       1010       1020 
RVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRFNDT WKLERAVLGE VKSCTWPETH 

      1030       1040       1050       1060       1070       1080 
TLWGDGVLES DLIIPITLAG PRSNHNRRPG YKTQSQGPWD EGRVEIDFDY CPGTTVTLSE 

      1090       1100       1110       1120       1130       1140 
SCGHRGPATR TTTESGKLIT DWCCRSCTLP PLRYQTDNGC WYGMEIRPQR HDEKTLVQSQ 

      1150       1160       1170       1180       1190       1200 
VNAYNADMID PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY 

      1210       1220       1230       1240       1250       1260 
VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL MLAAAFFQMA 

      1270       1280       1290       1300       1310       1320 
YYDARQILLW EMPDVLNSLA VAWMILRAIT FTTTSNVVVP LLALLTPGLR CLNLDVYRIL 

      1330       1340       1350       1360       1370       1380 
LLMVGIGSLI REKRSAAAKK KGASLLCLAL ASTGFFNPMI LAAGLVACDP NRKRGWPATE 

      1390       1400       1410       1420       1430       1440 
VMTAVGLMFA IVGGLAELDI DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWEGDA 

      1450       1460       1470       1480       1490       1500 
EITGSSERVD VRLDDDGNFQ LMNDPGAPWK IWMLRMACLA ISAYTPWAIL PSVVGFWITL 

      1510       1520       1530       1540       1550       1560 
QYTKRGGVLW DTPSPKEYKR GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV FHTLWHTTKG 

      1570       1580       1590       1600       1610       1620 
AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV QMIVVEPGKN VKNVQTKPGV 

      1630       1640       1650       1660       1670       1680 
FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD VIGLYGNGVI MPNGSYISAI VQGERMDEPV 

      1690       1700       1710       1720       1730       1740 
PAGFEPEMLR KKQITVLDLH PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA 

      1750       1760       1770       1780       1790       1800 
LRGLPIRYQT SAVAREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI 

      1810       1820       1830       1840       1850       1860 
AARGYISTRV ELGEAAAIFM TATPPGTSDP FPESNAPISD LQTEIPDRAW NSGYEWITEY 

      1870       1880       1890       1900       1910       1920 
IGKTVWFVPS VKMGNEIALC LQRAGKKVIQ LNRKSYETEY PKCKNDDWDF VVTTDISEMG 

      1930       1940       1950       1960       1970       1980 
ANFKASRVID SRKSVKPTII TEGEGRVILG EPSAVTAASA AQRRGRTGRN PSQAGDEYCY 

      1990       2000       2010       2020       2030       2040 
GGHTNEDDSN CAHWTEARIM LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL 

      2050       2060       2070       2080       2090       2100 
ELLRTADLPV WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR 

      2110       2120       2130       2140       2150       2160 
WIDARVYSDH QALKSFKDFA SGKRSQIGFI EVLGKMPEHF MGKTWEALDT MYVVATAEKG 

      2170       2180       2190       2200       2210       2220 
GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG IGKIGLGGVV LGAATFFCWM 

      2230       2240       2250       2260       2270       2280 
AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR SQTDNQLAVF LICVLTLVGA VAANEMGWLD 

      2290       2300       2310       2320       2330       2340 
KTKSDISGLF GQRIETKENF SIGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYITT 

      2350       2360       2370       2380       2390       2400 
SLTSINVQAS ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTSATL LFCHYAYMVP 

      2410       2420       2430       2440       2450       2460 
GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQVM LILVSLAALV 

      2470       2480       2490       2500       2510       2520 
VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC HIMRGGWLSC LSITWTLVKN 

      2530       2540       2550       2560       2570       2580 
MEKPGLKRGG AKGRTLGEVW KERLNQMTKE EFIRYRKEAI TEVDRSAAKH ARKERNITGG 

      2590       2600       2610       2620       2630       2640 
HPVSRGTAKL RWLVERRFLE PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE 

      2650       2660       2670       2680       2690       2700 
PQLVQSYGWN IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTL RVLEMVEDWL 

      2710       2720       2730       2740       2750       2760 
HRGPKEFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV SRASGNVVHS 

      2770       2780       2790       2800       2810       2820 
VNMTSQVLLG RMEKKTWKGP QYEEDVNLGS GTRAVGKPLL NSDTSKIKNR IERLRREYSS 

      2830       2840       2850       2860       2870       2880 
TWHHDENHPY RTWNYHGSYE VKPTGSASSL VNGVVRLLSK PWDTITNVTT MAMTDTTPFG 

      2890       2900       2910       2920       2930       2940 
QQRVFKEKVD TKAPEPPEGV KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG 

      2950       2960       2970       2980       2990       3000 
AMFEEQNQWR SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG 

      3010       3020       3030       3040       3050       3060 
SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR EVGTRPGGRI 

      3070       3080       3090       3100       3110       3120 
YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE LTYRHKVVKV MRPAADGRTV 

      3130       3140       3150       3160       3170       3180 
MDVISREDQR GSGQVVTYAL NTFTNLAVQL VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL 

      3190       3200       3210       3220       3230       3240 
SENGEERLSR MAVSGDDCVV KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP 

      3250       3260       3270       3280       3290       3300 
FCSNHFTELI MKDGRTLVTP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF 

      3310       3320       3330       3340       3350       3360 
HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW IEENEWMEDK 

      3370       3380       3390       3400       3410       3420 
TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI NQVRSIIGDE KYVDYMSSLK 

      3430 
RYEDTTLVED TVL 

« Hide

References

[1]"Nucleotide and complete amino acid sequences of Kunjin virus: definitive gene order and characteristics of the virus-specified proteins."
Coia G., Parker M.D., Speight G., Byrne M.E., Westaway E.G.
J. Gen. Virol. 69:1-21(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential role for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication."
Liu W.J., Chen H.B., Khromykh A.A.
J. Virol. 77:7804-7813(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Infectious clone FLSDX and Infectious clone pAKUN.
[3]"Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A."
Mackenzie J.M., Khromykh A.A., Jones M.K., Westaway E.G.
Virology 245:203-215(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION OF NON-STRUCTURAL PROTEIN 2A, NON-STRUCTURAL PROTEIN 4A.
[4]"Role of nonstructural protein NS2A in flavivirus assembly."
Leung J.Y., Pijlman G.P., Kondratieva N., Hyde J., Mackenzie J.M., Khromykh A.A.
J. Virol. 82:4731-4741(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 2A, MUTAGENESIS OF THR-1292, CHARACTERIZATION OF VARIANT ASN-1202.
[5]"The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex."
Gillespie L.K., Hoenen A., Morgan G., Mackenzie J.M.
J. Virol. 84:10438-10447(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 4A.
[6]"West Nile virus core protein; tetramer structure and ribbon formation."
Dokland T., Walsh M., Mackenzie J.M., Khromykh A.A., Ee K.H., Wang S.
Structure 12:1157-1163(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-98.
[7]"West Nile virus inhibits the signal transduction pathway of alpha interferon."
Guo J.T., Hayashi J., Seeger C.
J. Virol. 79:1343-1350(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
[8]"The NS5 protein of the virulent West Nile virus NY99 strain is a potent antagonist of type I interferon-mediated JAK-STAT signaling."
Laurent-Rolle M., Boer E.F., Lubick K.J., Wolfinbarger J.B., Carmody A.B., Rockx B., Liu W., Ashour J., Shupert W.L., Holbrook M.R., Barrett A.D., Mason P.W., Bloom M.E., Garcia-Sastre A., Khromykh A.A., Best S.M.
J. Virol. 84:3503-3515(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5, MUTAGENESIS OF SER-3181.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00246 Genomic RNA. Translation: BAA00176.1.
AY274504 Genomic RNA. Translation: AAP78941.1.
AY274505 Genomic RNA. Translation: AAP78942.1.
PIRGNWVKV. A28697.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SFKX-ray3.20A/B/C/D/E/F/G/H23-98[»]
2HCNX-ray2.35A2846-3433[»]
2HCSX-ray2.50A2846-3433[»]
2HFZX-ray3.00A2802-3433[»]
2OF6electron microscopy24.00A/B/C291-690[»]
2QEQX-ray3.10A/B1691-2124[»]
ProteinModelPortalP14335.
SMRP14335. Positions 25-97, 291-693, 1424-1467, 1506-2124, 2534-2795, 2802-3427.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS07.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.350. 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.
InterProIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
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.
IPR027287. Flavovir_Ig-like.
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.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF01003. 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.
PF00271. Helicase_C. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsTIGR04240. flavi_E_stem. 1 hit.
PROSITEPS51527. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP14335.

Entry information

Entry namePOLG_KUNJM
AccessionPrimary (citable) accession number: P14335
Secondary accession number(s): Q7T4P4, Q7T4P5, Q82983
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 11, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references