Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P06935 (POLG_WNV)

Last modified February 9, 2010. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Genome polyprotein
Cleaved into the following 10 chains:
    1- Recommended name:
            Protein C
        Alternative name(s):
            Core protein
            Capsid protein
    2- Recommended name:
            Small envelope protein M
        Alternative name(s):
            Matrix protein
    3- Recommended name:
            Envelope protein E
    4- Recommended name:
            Non-structural protein 1
                Short name=NS1
    5- Recommended name:
            Non-structural protein 2A
                Short name=NS2A
    6- Recommended name:
            Serine protease subunit NS2B
        Alternative name(s):
            Non-structural protein 2B
            Flavivirin protease NS2B regulatory subunit
    7- Recommended name:
            Serine protease/NTPase/helicase NS3
              EC=3.4.21.91
              EC=3.6.1.15
              EC=3.6.1.-
        Alternative name(s):
            Flavivirin protease NS3 catalytic subunit
            Non-structural protein 3
    8- Recommended name:
            Non-structural protein 4A
                Short name=NS4A
    9- Recommended name:
            Non-structural protein 4B
                Short name=NS4B
    10- Recommended name:
            Methyltransferase/RNA-directed RNA polymerase NS5
              EC=2.7.7.48
              EC=2.1.1.56
              EC=2.1.1.57
        Alternative name(s):
            NS5
OrganismWest Nile virus (WNV) [Complete proteome]
Taxonomic identifier11082 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Japanese encephalitis virus group
Virus hostAedes [TaxID: 7158]
Aves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Amblyomma variegatum (Tropical bont tick) [TaxID: 34610]
Hyalomma marginatum [TaxID: 34627]
Rhipicephalus [TaxID: 34630]
Culex [TaxID: 53527]
Mansonia uniformis [TaxID: 308735]
Mimomyia [TaxID: 308737]

Hide | Top

Protein attributes

Sequence length3430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

The small proteins NS2A, NS4A and NS4B are hydrophobic, suggesting a possible membrane-related function.

Non-structural protein 2B is a required cofactor for the serine protease function of NS3.

Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, cleaves the polyprotein 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.

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.

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

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

Subunit structure

NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter By similarity.

Subcellular location

Protein C: Virion Potential. Host membrane; Single-pass membrane protein Potential.

Small envelope protein M: Virion Potential. Host membrane; Single-pass membrane protein Potential.

Envelope protein E: Virion Potential. Host membrane; Multi-pass membrane protein Potential.

Non-structural protein 4A: Host membrane; Single-pass membrane protein Potential.

Non-structural protein 4B: Host membrane; Multi-pass membrane protein Potential.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins By similarity.

Miscellaneous

The virion of this virus is a nucleocapsid covered by a lipoprotein envelope. The envelope contains two proteins: the protein M and glycoprotein E. The nucleocapsid is a complex of protein C and mRNA. 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 By similarity.

Sequence similarities

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

Hide | Top

Ontologies

Keywords
   Biological processRNA replication
   Cellular componentCapsid protein
Core protein
Envelope protein
Host membrane
Membrane
Virion
   DomainTransmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
Methyltransferase
Nucleotidyltransferase
RNA-directed RNA polymerase
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processRNA metabolic process

Inferred from electronic annotation. Source: InterPro

methylation

Inferred from electronic annotation. Source: InterPro

transcription, RNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: UniProtKB-KW

   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

methyltransferase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB3P051062EBI-981051,EBI-702847From a different organism.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host Potential
Chain2 – 123122Protein C
PRO_0000037743
Propeptide124 – 21592
PRO_0000037744
Chain216 – 29075Small envelope protein M
PRO_0000037745
Chain291 – 787497Envelope protein E
PRO_0000037746
Chain788 – 1139352Non-structural protein 1
PRO_0000037747
Chain1140 – 1370231Non-structural protein 2A
PRO_0000037748
Chain1371 – 1501131Serine protease subunit NS2B
PRO_0000037749
Chain1502 – 2120619Serine protease/NTPase/helicase NS3
PRO_0000037750
Chain2121 – 2269149Non-structural protein 4A
PRO_0000037751
Chain2270 – 2525256Non-structural protein 4B
PRO_0000037752
Chain2526 – 3430905Methyltransferase/RNA-directed RNA polymerase NS5
PRO_0000037753

Regions

Transmembrane46 – 6621 Potential
Transmembrane106 – 12621 Potential
Transmembrane249 – 26921 Potential
Transmembrane276 – 29217 Potential
Transmembrane740 – 76021 Potential
Transmembrane767 – 78721 Potential
Transmembrane1139 – 115921 Potential
Transmembrane1171 – 119121 Potential
Transmembrane1213 – 123321 Potential
Transmembrane1244 – 126421 Potential
Transmembrane1279 – 130123 Potential
Transmembrane1341 – 136121 Potential
Transmembrane1372 – 139221 Potential
Transmembrane1396 – 141621 Potential
Transmembrane1474 – 149421 Potential
Transmembrane2171 – 219121 Potential
Transmembrane2197 – 221721 Potential
Transmembrane2219 – 223921 Potential
Transmembrane2255 – 227521 Potential
Transmembrane2310 – 233021 Potential
Transmembrane2356 – 237621 Potential
Transmembrane2378 – 239821 Potential
Transmembrane2442 – 246221 Potential
Domain1508 – 1679172Peptidase S7
Domain1682 – 1838157Helicase ATP-binding
Domain1849 – 2014166Helicase C-terminal
Domain3055 – 3207153RdRp catalytic
Nucleotide binding1695 – 17028ATP Potential
Region388 – 40114Involved in fusion
Motif1786 – 17894DEAH box

Sites

Active site15521Charge relay system By similarity
Active site15761Charge relay system By similarity
Active site16361Charge relay system By similarity
Active site25861For 2'-O-methyltransferase activity
Active site26711For 2'-O-methyltransferase and N-7 methyltransferase activity
Active site27071For 2'-O-methyltransferase activity
Active site27431For 2'-O-methyltransferase activity

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...); by host Potential
Glycosylation9171N-linked (GlcNAc...); by host Potential
Glycosylation9621N-linked (GlcNAc...); by host Potential
Glycosylation9941N-linked (GlcNAc...); by host Potential
Glycosylation23361N-linked (GlcNAc...); by host Potential
Glycosylation24891N-linked (GlcNAc...); by host Potential
Disulfide bond293 ↔ 320 Ref.5
Disulfide bond350 ↔ 406 Ref.5
Disulfide bond364 ↔ 395 Ref.5
Disulfide bond382 ↔ 411 Ref.5
Disulfide bond476 ↔ 574 Ref.5
Disulfide bond591 ↔ 622 Ref.5

Experimental info

Mutagenesis25861K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity.
Mutagenesis26711D → A: Lethal for the virus. Complete loss of 2'-O and N-7 methyltransferase activies.
Mutagenesis27071K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity.
Mutagenesis27431E → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity.

Secondary structure

1 .......................................... 3430
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P06935-1 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: 42D71B7CB12DC45B

FASTA3,430380,110
        10         20         30         40         50         60 
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA 

        70         80         90        100        110        120 
PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST KQKKRGGTAG FTILLGLIAC 

       130        140        150        160        170        180 
AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT AAGKNLCIVR AMDVGYLCED TITYECPVLA 

       190        200        210        220        230        240 
AGNDPEDIDC WCTKSSVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA 

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

       310        320        330        340        350        360 
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC YLASVSDLST 

       370        380        390        400        410        420 
RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CTTKATGWII 

       430        440        450        460        470        480 
QKENIKYEVA IFVHGPTTVE SHGKIGATQA GRFSITPSAP SYTLKLGEYG EVTVDCEPRS 

       490        500        510        520        530        540 
GIDTSAYYVM SVGEKSFLVH REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA 

       550        560        570        580        590        600 
LGSQEGALHQ ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART 

       610        620        630        640        650        660 
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV ATANSKVLIE 

       670        680        690        700        710        720 
LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG AQRLAALGDT AWDFGSVGGV 

       730        740        750        760        770        780 
FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL LGALLLWMGI NARDRSIAMT FLAVGGVLLF 

       790        800        810        820        830        840 
LSVNVHADTG CAIDIGRQEL RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG 

       850        860        870        880        890        900 
VCGLRSVSRL EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM 

       910        920        930        940        950        960 
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT STRMFLRIRE 

       970        980        990       1000       1010       1020 
TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE RAVLGEVKSC TWPETHTLWG 

      1030       1040       1050       1060       1070       1080 
DGVLESDLII PITLAGPRSN HNRRPGYKTQ NQGPWDEGRV EIDFDYCPGT TVTISDSCEH 

      1090       1100       1110       1120       1130       1140 
RGPAARTTTE SGKLITDWCC RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY 

      1150       1160       1170       1180       1190       1200 
NADMIDPFQL GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV 

      1210       1220       1230       1240       1250       1260 
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA AFFQMAYYDA 

      1270       1280       1290       1300       1310       1320 
KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL LTPGLKCLNL DVYRILLLMV 

      1330       1340       1350       1360       1370       1380 
GVGSLIKEKR SSAAKKKGAC LICLALASTG VFNPMILAAG LMACDPNRKR GWPATEVMTA 

      1390       1400       1410       1420       1430       1440 
VGLMFAIVGG LAELDIDSMA IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG 

      1450       1460       1470       1480       1490       1500 
SSERVDVRLD DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK 

      1510       1520       1530       1540       1550       1560 
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL WHTTKGAALM 

      1570       1580       1590       1600       1610       1620 
SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV VEPGKNVKNV QTKPGVFKTP 

      1630       1640       1650       1660       1670       1680 
EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL YGNGVIMPNG SYISAIVQGE RMEEPAPAGF 

      1690       1700       1710       1720       1730       1740 
EPEMLRKKQI TVLDLHPGAG KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL 

      1750       1760       1770       1780       1790       1800 
PIRYQTSAVH REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG 

      1810       1820       1830       1840       1850       1860 
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY EWITEYVGKT 

      1870       1880       1890       1900       1910       1920 
VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK NDDWDFVITT DISEMGANFK 

      1930       1940       1950       1960       1970       1980 
ASRVIDSRKS VKPTIIEEGD GRVILGEPSA ITAASAAQRR GRIGRNPSQV GDEYCYGGHT 

      1990       2000       2010       2020       2030       2040 
NEDDSNFAHW TEARIMLDNI NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR 

      2050       2060       2070       2080       2090       2100 
TADLPVWLAY KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA 

      2110       2120       2130       2140       2150       2160 
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV ATAEKGGRAH 

      2170       2180       2190       2200       2210       2220 
RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI GLGGVILGAA TFFCWMAEVP 

      2230       2240       2250       2260       2270       2280 
GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD NQLAVFLICV LTLVGAVAAN EMGWLDKTKN 

      2290       2300       2310       2320       2330       2340 
DIGSLLGHRP EARETTLGVE SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT 

      2350       2360       2370       2380       2390       2400 
SINVQASALF TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ 

      2410       2420       2430       2440       2450       2460 
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL VSMAAVVVNP 

      2470       2480       2490       2500       2510       2520 
SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM RGGWLSCLSI MWTLIKNMEK 

      2530       2540       2550       2560       2570       2580 
PGLKRGGAKG RTLGEVWKER LNHMTKEEFT RYRKEAITEV DRSAAKHARR EGNITGGHPV 

      2590       2600       2610       2620       2630       2640 
SRGTAKLRWL VERRFLEPVG KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL 

      2650       2660       2670       2680       2690       2700 
VQSYGWNIVT MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG 

      2710       2720       2730       2740       2750       2760 
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA SGNIVHSVNM 

      2770       2780       2790       2800       2810       2820 
TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD TSKIKNRIER LKKEYSSTWH 

      2830       2840       2850       2860       2870       2880 
QDANHPYRTW NYHGSYEVKP TGSASSLVNG VVRLLSKPWD TITNVTTMAM TDTTPFGQQR 

      2890       2900       2910       2920       2930       2940 
VFKEKVDTKA PEPPEGVKYV LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF 

      2950       2960       2970       2980       2990       3000 
EEQNQWKNAR EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA 

      3010       3020       3030       3040       3050       3060 
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG TKPGGKVYAD 

      3070       3080       3090       3100       3110       3120 
DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY RHKVVKVMRP AADGKTVMDV 

      3130       3140       3150       3160       3170       3180 
ISREDQRGSG QVVTYALNTF TNLAVQLVRM MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN 

      3190       3200       3210       3220       3230       3240 
GEERLSRMAV SGDDCVVKPL DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS 

      3250       3260       3270       3280       3290       3300 
NHFTELIMKD GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR 

      3310       3320       3330       3340       3350       3360 
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE NEWMEDKTPV 

      3370       3380       3390       3400       3410       3420 
ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV RSVIGEEKYV DYMSSLRRYE 

      3430 
DTIVVEDTVL

« Hide

Hide | Top

References

[1]"Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins."
Castle E., Leidner U., Nowak T., Wengler G., Wengler G.
Virology 149:10-26(1986) [PubMed: 3753811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"An infectious clone of the West Nile flavivirus."
Yamshchikov V.F., Wengler G., Perelygin A.A., Brinton M.A., Compans R.W.
Virology 281:294-304(2001) [PubMed: 11277701] [Abstract]
Cited for: SEQUENCE REVISION TO 1908; 2018-2036; 2242 AND 2859-2860.
[3]"Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins."
Castle E., Nowak T., Leidner U., Wengler G., Wengler G.
Virology 145:227-236(1985) [PubMed: 2992152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-291.
[4]"Sequence analysis of the membrane protein V3 of the flavivirus West Nile virus and of its gene."
Wengler G., Castle E., Leidner U., Nowak T., Wengler G.
Virology 147:264-274(1985) [PubMed: 3855247] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 255-854.
[5]"Analysis of disulfides present in the membrane proteins of the West Nile flavivirus."
Nowak T., Wengler G.
Virology 156:127-137(1987) [PubMed: 3811228] [Abstract]
Cited for: DISULFIDE BONDS IN E PROTEIN.
[6]"Structure and function of flavivirus NS5 methyltransferase."
Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A., Shi P.-Y., Li H.
J. Virol. 81:3891-3903(2007) [PubMed: 17267492] [Abstract]
Cited for: FUNCTION AS METHYLTRANSFERASE, MUTAGENESIS OF LYS-2586; ASP-2671; LYS-2707 AND GLU-2743.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12294 Genomic RNA. Translation: AAA48498.2.
PIRGNWVWV. A25256.
RefSeqNP_041724.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FP7X-ray1.68A1420-1466[»]
B1517-1688[»]
2G05model-D1675-2120[»]
2G2Gmodel-D1675-2120[»]
2GGVX-ray1.80A1419-1463[»]
B1503-1679[»]
2IJOX-ray2.30A1419-1465[»]
B1502-1685[»]
2P5PX-ray2.80A/B/C585-701[»]
3E90X-ray2.45A/C1420-1463[»]
B/D1502-1685[»]
3I50X-ray3.00E291-688[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP06935. 1 interaction.

Genome annotation databases

GeneID912267.

Enzyme and pathway databases

BRENDA2.7.7.48. 271356.
3.4.21.91. 271356.

Family and domain databases

InterProIPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR000069. Env_glycoprot_M_flavivir.
IPR013756. Flav_glyE_cen_dom_subdom2.
IPR013754. Flav_glyE_dim.
IPR001122. Flavi_capsidC.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flv_glyE_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR014756. Ig_E-set.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
Gene3DG3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit.
G3DSA:2.60.98.10. Flav_glyE_dim. 1 hit.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
PfamPF01003. Flavi_capsid. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
PROSITEPS00690. DEAH_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP06935.

Hide | Top

Entry information

Entry namePOLG_WNV
AccessionPrimary (citable) accession number: P06935
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 24, 2003
Last modified: February 9, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents