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P04517 (POLG_TEV) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 10 chains:

  1. P1 proteinase
    EC=3.4.-.-
    Alternative name(s):
    N-terminal protein
  2. Helper component proteinase
    Short name=HC-pro
    EC=3.4.22.45
  3. Protein P3
  4. 6 kDa protein 1
    Short name=6K1
  5. Cytoplasmic inclusion protein
    Short name=CI
    EC=3.6.4.-
  6. 6 kDa protein 2
    Short name=6K2
  7. Viral genome-linked protein
    Alternative name(s):
    VPg
  8. Nuclear inclusion protein A
    Short name=NI-a
    Short name=NIa
    EC=3.4.22.44
    Alternative name(s):
    49 kDa proteinase
    Short name=49 kDa-Pro
    NIa-pro
  9. Nuclear inclusion protein B
    Short name=NI-b
    Short name=NIb
    EC=2.7.7.48
    Alternative name(s):
    RNA-directed RNA polymerase
  10. Capsid protein
    Short name=CP
    Alternative name(s):
    Coat protein
OrganismTobacco etch virus (TEV) [Complete proteome]
Taxonomic identifier12227 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostCapsicum annuum (Bell pepper) [TaxID: 4072]
Cassia [TaxID: 53851]
Datura stramonium (Jimsonweed) (Common thornapple) [TaxID: 4076]
Nicotiana tabacum (Common tobacco) [TaxID: 4097]
Physalis [TaxID: 24663]
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]

Protein attributes

Sequence length3054 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: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. Ref.7 Ref.8

Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication. Ref.7 Ref.8

Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. Ref.7 Ref.8

Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication. Ref.7 Ref.8

Both 6K peptides are indispensable for virus replication By similarity. Ref.7 Ref.8

Nuclear inclusion protein A: has RNA-binding and proteolytic activities. Ref.7 Ref.8

Catalytic activity

Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.

Subunit structure

Nuclear inclusion protein A protease is a dimer; disulfide-linked. Ref.10 Ref.11

Subcellular location

Capsid protein: Virion Potential.

Domain

The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.

Post-translational modification

VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.

Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI By similarity.

Sequence similarities

Belongs to the potyviridae genome polyprotein family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase C4 domain.

Contains 1 peptidase C6 domain.

Contains 1 peptidase S30 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processViral RNA replication
   Cellular componentCapsid protein
Helical capsid protein
Virion
   Coding sequence diversityRibosomal frameshifting
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Suppressor of RNA silencing
Thiol protease
Transferase
   PTMCovalent protein-RNA linkage
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from electronic annotation. Source: GOC

RNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

transcription, RNA-templated

Inferred from electronic annotation. Source: GOC

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthelical viral capsid

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 binding

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]
Isoform Genome polyprotein (identifier: P04517-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by conventional translation.
Isoform P3N-PIPO polyprotein (identifier: P0CK09-1)

The sequence of this isoform can be found in the external entry P0CK09.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting in P3 ORF.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 30543054Genome polyprotein
PRO_0000420026
Chain1 – 304304P1 proteinase Potential
PRO_0000040450
Chain305 – 763459Helper component proteinase Potential
PRO_0000040451
Chain764 – 1110347Protein P3 By similarity
PRO_0000040452
Chain1111 – 1163536 kDa protein 1 By similarity
PRO_0000040453
Chain1164 – 1796633Cytoplasmic inclusion protein
PRO_0000040454
Chain1797 – 1849536 kDa protein 2
PRO_0000040455
Chain1850 – 2037188Viral genome-linked protein By similarity
PRO_0000040456
Chain2038 – 2279242Nuclear inclusion protein A By similarity
PRO_0000040457
Chain2280 – 2791512Nuclear inclusion protein B
PRO_0000040458
Chain2792 – 3054263Capsid protein
PRO_0000040459

Regions

Domain1234 – 1386153Helicase ATP-binding
Domain1401 – 1564164Helicase C-terminal
Domain2038 – 2255218Peptidase C4
Domain2521 – 2641121RdRp catalytic
Nucleotide binding1247 – 12548ATP Potential
Motif358 – 3614Involved in interaction with stylet and aphid transmission
Motif615 – 6173Involved in virions binding and aphid transmission By similarity
Motif1336 – 13394DECH box
Motif1889 – 18968Nuclear localization signal Potential

Sites

Active site2141For P1 proteinase activity Ref.4 Ref.5 Ref.6 Ref.11
Active site2231For P1 proteinase activity Potential
Active site2561For P1 proteinase activity Ref.4 Ref.5 Ref.6 Ref.11
Active site6491For helper component proteinase activity Ref.4 Ref.5 Ref.6 Ref.11
Active site7221For helper component proteinase activity Ref.4 Ref.5 Ref.6 Ref.11
Active site20831For nuclear inclusion protein A activity Ref.4 Ref.5 Ref.6 Ref.11
Active site21181For nuclear inclusion protein A activity Ref.4 Ref.5 Ref.6 Ref.11
Active site21881For nuclear inclusion protein A activity Ref.4 Ref.5 Ref.6 Ref.11
Site304 – 3052Cleavage; by P1 proteinase Potential
Site763 – 7642Cleavage; by HC-pro
Site1110 – 11112Cleavage; by NIa-pro By similarity
Site1163 – 11642Cleavage; by NIa-pro By similarity
Site1796 – 17972Cleavage; by NIa-pro By similarity
Site1849 – 18502Cleavage; by NIa-pro By similarity
Site2037 – 20382Cleavage; by NIa-pro By similarity
Site2279 – 22802Cleavage; by NIa-pro By similarity
Site2791 – 27922Cleavage; by NIa-pro By similarity

Amino acid modifications

Modified residue19111O-(5'-phospho-RNA)-tyrosine By similarity
Disulfide bond2167Interchain Ref.10 Ref.11

Experimental info

Mutagenesis2141H → A: Complete loss of proteolytic activity of P1 proteinase. Ref.6
Mutagenesis2561S → A: Complete loss of proteolytic activity of P1 proteinase. Ref.6
Mutagenesis3141F → L: Complete loss of aphid transmission. Ref.7
Mutagenesis3581K → E: Complete loss of interaction with stylet and aphid transmission; no effect on virion binding. Ref.7
Mutagenesis6101S → T: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6191H → S: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6251S → T: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6271D → E: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6321D → E: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6491C → S: Complete loss of proteolytic activity of HC-pro. Ref.4
Mutagenesis6751D → E: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6891D → E: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6941C → S: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis6981S → T: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7151D → E: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7161H → S: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7221H → S: Complete loss of proteolytic activity of HC-pro. Ref.4
Mutagenesis7251D → E: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7261S → T: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7291S → T: No effect on proteolytic activity of HC-pro.
Mutagenesis7351H → S: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7431S → T: No effect on proteolytic activity of HC-pro. Ref.4
Mutagenesis7551S → T: No effect on proteolytic activity of HC-pro. Ref.4

Secondary structure

...................................................... 3054
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Genome polyprotein [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 0AF9A3626960B5CE

FASTA3,054346,164
        10         20         30         40         50         60 
MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH KPVIFGEDYI 

        70         80         90        100        110        120 
TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN NKRNRRRKVA KTYVGRDSIV 

       130        140        150        160        170        180 
EKIVVPHTER KVDTTAAVED ICNEATTQLV HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV 

       190        200        210        220        230        240 
RKRHMQVEII SKKSVRARVK RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR 

       250        260        270        280        290        300 
FKNERVDQSK LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS 

       310        320        330        340        350        360 
MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT QALSPCGKIT 

       370        380        390        400        410        420 
CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA EKLLTRFLQQ KSLVNTNLTA 

       430        440        450        460        470        480 
CVSVKQLIGD RKQAPFTHVL AVSEILFKGN KLTGADLEEA STHMLEIARF LNNRTENMRI 

       490        500        510        520        530        540 
GHLGSFRNKI SSKAHVNNAL MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK 

       550        560        570        580        590        600 
YVIRKHIRGS RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV 

       610        620        630        640        650        660 
TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY MNIFFALLVN 

       670        680        690        700        710        720 
VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL YPDVLRAELP RILVDHDNKT 

       730        740        750        760        770        780 
MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH SGLESEMKTY NVGGMNRDVV TQGAIEMLIK 

       790        800        810        820        830        840 
SIYKPHLMKQ LLEEEPYIIV LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS 

       850        860        870        880        890        900 
ALAQKLTLAD LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL 

       910        920        930        940        950        960 
REGGYAVTSE KVHEMLEKNY VKALKDAWDE LTWLEKFSAI RHSRKLLKFG RKPLIMKNTV 

       970        980        990       1000       1010       1020 
DCGGHIDLSV KSLFKFHLEL LKGTISRAVN GGARKVRVAK NAMTKGVFLK IYSMLPDVYK 

      1030       1040       1050       1060       1070       1080 
FITVSSVLSL LLTFLFQIDC MIRAHREAKV AAQLQKESEW DNIINRTFQY SKLENPIGYR 

      1090       1100       1110       1120       1130       1140 
STAEERLQSE HPEAFEYYKF CIGKEDLVEQ AKQPEIAYFE KIIAFITLVL MAFDAERSDG 

      1150       1160       1170       1180       1190       1200 
VFKILNKFKG ILSSTEREII YTQSLDDYVT TFDDNMTINL ELNMDELHKT SLPGVTFKQW 

      1210       1220       1230       1240       1250       1260 
WNNQISRGNV KPHYRTEGHF MEFTRDTAAS VASEISHSPA RDFLVRGAVG SGKSTGLPYH 

      1270       1280       1290       1300       1310       1320 
LSKRGRVLML EPTRPLTDNM HKQLRSEPFN CFPTLRMRGK STFGSSPITV MTSGFALHHF 

      1330       1340       1350       1360       1370       1380 
ARNIAEVKTY DFVIIDECHV NDASAIAFRN LLFEHEFEGK VLKVSATPPG REVEFTTQFP 

      1390       1400       1410       1420       1430       1440 
VKLKIEEALS FQEFVSLQGT GANADVISCG DNILVYVASY NDVDSLGKLL VQKGYKVSKI 

      1450       1460       1470       1480       1490       1500 
DGRTMKSGGT EIITEGTSVK KHFIVATNII ENGVTIDIDV VVDFGTKVVP VLDVDNRAVQ 

      1510       1520       1530       1540       1550       1560 
YNKTVVSYGE RIQKLGRVGR HKEGVALRIG QTNKTLVEIP EMVATEAAFL CFMYNLPVTT 

      1570       1580       1590       1600       1610       1620 
QSVSTTLLEN ATLLQARTMA QFELSYFYTI NFVRFDGSMH PVIHDKLKRF KLHTCETFLN 

      1630       1640       1650       1660       1670       1680 
KLAIPNKGLS SWLTSGEYKR LGYIAEDAGI RIPFVCKEIP DSLHEEIWHI VVAHKGDSGI 

      1690       1700       1710       1720       1730       1740 
GRLTSVQAAK VVYTLQTDVH SIARTLACIN RRIADEQMKQ SHFEAATGRA FSFTNYSIQS 

      1750       1760       1770       1780       1790       1800 
IFDTLKANYA TKHTKENIAV LQQAKDQLLE FSNLAKDQDV TGIIQDFNHL ETIYLQSDSE 

      1810       1820       1830       1840       1850       1860 
VAKHLKLKSH WNKSQITRDI IIALSVLIGG GWMLATYFKD KFNEPVYFQG KKNQKHKLKM 

      1870       1880       1890       1900       1910       1920 
REARGARGQY EVAAEPEALE HYFGSAYNNK GKRKGTTRGM GAKSRKFINM YGFDPTDFSY 

      1930       1940       1950       1960       1970       1980 
IRFVDPLTGH TIDESTNAPI DLVQHEFGKV RTRMLIDDEI EPQSLSTHTT IHAYLVNSGT 

      1990       2000       2010       2020       2030       2040 
KKVLKVDLTP HSSLRASEKS TAIMGFPERE NELRQTGMAV PVAYDQLPPK NEDLTFEGES 

      2050       2060       2070       2080       2090       2100 
LFKGPRDYNP ISSTICHLTN ESDGHTTSLY GIGFGPFIIT NKHLFRRNNG TLLVQSLHGV 

      2110       2120       2130       2140       2150       2160 
FKVKNTTTLQ QHLIDGRDMI IIRMPKDFPP FPQKLKFREP QREERICLVT TNFQTKSMSS 

      2170       2180       2190       2200       2210       2220 
MVSDTSCTFP SSDGIFWKHW IQTKDGQCGS PLVSTRDGFI VGIHSASNFT NTNNYFTSVP 

      2230       2240       2250       2260       2270       2280 
KNFMELLTNQ EAQQWVSGWR LNADSVLWGG HKVFMSKPEE PFQPVKEATQ LMNELVYSQG 

      2290       2300       2310       2320       2330       2340 
EKRKWVVEAL SGNLRPVAEC PSQLVTKHVV KGKCPLFELY LQLNPEKEAY FKPMMGAYKP 

      2350       2360       2370       2380       2390       2400 
SRLNREAFLK DILKYASEIE IGNVDCDLLE LAISMLVTKL KALGFPTVNY ITDPEEIFSA 

      2410       2420       2430       2440       2450       2460 
LNMKAAMGAL YKGKKKEALS ELTLDEQEAM LKASCLRLYT GKLGIWNGSL KAELRPIEKV 

      2470       2480       2490       2500       2510       2520 
ENNKTRTFTA APIDTLLAGK VCVDDFNNQF YDLNIKAPWT VGMTKFYQGW NELMEALPSG 

      2530       2540       2550       2560       2570       2580 
WVYCDADGSQ FDSSLTPFLI NAVLKVRLAF MEEWDIGEQM LRNLYTEIVY TPILTPDGTI 

      2590       2600       2610       2620       2630       2640 
IKKHKGNNSG QPSTVVDNTL MVIIAMLYTC EKCGINKEEI VYYVNGDDLL IAIHPDKAER 

      2650       2660       2670       2680       2690       2700 
LSRFKESFGE LGLKYEFDCT TRDKTQLWFM SHRALERDGM YIPKLEEERI VSILEWDRSK 

      2710       2720       2730       2740       2750       2760 
EPSHRLEAIC ASMIEAWGYD KLVEEIRNFY AWVLEQAPYS QLAEEGKAPY LAETALKFLY 

      2770       2780       2790       2800       2810       2820 
TSQHGTNSEI EEYLKVLYDY DIPTTENLYF QSGTVDAGAD AGKKKDQKDD KVAEQASKDR 

      2830       2840       2850       2860       2870       2880 
DVNAGTSGTF SVPRINAMAT KLQYPRMRGE VVVNLNHLLG YKPQQIDLSN ARATHEQFAA 

      2890       2900       2910       2920       2930       2940 
WHQAVMTAYG VNEEQMKILL NGFMVWCIEN GTSPNLNGTW VMMDGEDQVS YPLKPMVENA 

      2950       2960       2970       2980       2990       3000 
QPTLRQIMTH FSDLAEAYIE MRNRERPYMP RYGLQRNITD MSLSRYAFDF YELTSKTPVR 

      3010       3020       3030       3040       3050 
AREAHMQMKA AAVRNSGTRL FGLDGNVGTA EEDTERHTAH DVNRNMHTLL GVRQ 

« Hide

Isoform P3N-PIPO polyprotein [UniParc].

See P0CK09.

References

[1]"The nucleotide sequence of the coding region of tobacco etch virus genomic RNA: evidence for the synthesis of a single polyprotein."
Allison R., Johnston R.E., Dougherty W.G.
Virology 154:9-20(1986)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Sequence determination of the capsid protein gene and flanking regions of tobacco etch virus: evidence for synthesis and processing of a polyprotein in potyvirus genome expression."
Allison R.F., Sorenson J.C., Kelly M.E., Armstrong F.B., Dougherty W.G.
Proc. Natl. Acad. Sci. U.S.A. 82:3969-3972(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2344-3054.
[3]"A second proteinase encoded by a plant potyvirus genome."
Carrigton J.C., Cary S.M., Parks T.D., Dougherty W.G.
EMBO J. 8:365-370(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROTEASES.
[4]"Identification of essential residues in potyvirus proteinase HC-Pro by site-directed mutagenesis."
Oh C.-S., Carrington J.C.
Virology 173:692-699(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES OF HELPER COMPONENT PROTEINASE, MUTAGENESIS OF SER-610; HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675; ASP-689; CYS-694; SER-698; ASP-715; HIS-716; HIS-722; ASP-725; SER-726; HIS-735; SER-743 AND SER-755.
[5]"Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase."
Dougherty W.G., Parks T.D., Cary S.M., Bazan J.F., Fletterick R.J.
Virology 172:302-310(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A.
[6]"The 35-kDa protein from the N-terminus of the potyviral polyprotein functions as a third virus-encoded proteinase."
Verchot J., Koonin E.V., Carrington J.C.
Virology 185:527-535(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES OF P1 PROTEINASE, MUTAGENESIS OF HIS-214 AND SER-256.
[7]"Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets."
Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C., Baker J., Pirone T.P.
J. Gen. Virol. 79:3119-3122(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF HELPER COMPONENT PROTEINASE, MUTAGENESIS OF PHE-314 AND LYS-358.
[8]"Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro."
Kasschau K.D., Carrington J.C.
Virology 285:71-81(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF HELPER COMPONENT PROTEINASE.
[9]"Potyvirus proteins: a wealth of functions."
Urcuqui-Inchima S., Haenni A.L., Bernardi F.
Virus Res. 74:157-175(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[10]"Structural basis for the substrate specificity of tobacco etch virus protease."
Phan J., Zdanov A., Evdokimov A.G., Tropea J.E., Peters H.K. III, Kapust R.B., Li M., Wlodawer A., Waugh D.S.
J. Biol. Chem. 277:50564-50572(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2038-2794, SUBUNIT, DISULFIDE BOND.
[11]"Crystal structure of tobacco etch virus protease shows the protein C terminus bound within the active site."
Nunn C.M., Jeeves M., Cliff M.J., Urquhart G.T., George R.R., Chao L.H., Tscuchia Y., Djordjevic S.
J. Mol. Biol. 350:145-155(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2038-2279, SUBUNIT, DISULFIDE BOND, ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15239 Genomic RNA. Translation: AAA47910.1.
M11458 Genomic RNA. Translation: AAA47909.1.
M11216 Genomic RNA. Translation: AAA47908.1. Sequence problems.
PIRGNBVEV. A04207.
RefSeqNP_062908.1. NC_001555.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVBX-ray2.20A/B2038-2273[»]
C/D2785-2794[»]
1LVMX-ray1.80A/B2038-2258[»]
E2267-2273[»]
1Q31X-ray2.70A/B2038-2279[»]
ProteinModelPortalP04517.
SMRP04517. Positions 2038-2258.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC04.004.

Proteomic databases

PRIDEP04517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1502321.

Family and domain databases

InterProIPR011492. DEAD_Flavivir.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR002540. Pept_S30_P1_potyvir.
IPR001456. Peptidase_C6.
IPR001592. Poty_coat.
IPR001730. Potyv_NIa-pro_dom.
IPR013648. PP_Potyviridae.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF07652. Flavi_DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00863. Peptidase_C4. 1 hit.
PF00851. Peptidase_C6. 1 hit.
PF01577. Peptidase_S30. 1 hit.
PF00767. Poty_coat. 1 hit.
PF08440. Poty_PP. 1 hit.
PF00680. RdRP_1. 1 hit.
[Graphical view]
PRINTSPR00966. NIAPOTYPTASE.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51436. POTYVIRUS_NIA_PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04517.
PMAP-CutDBP04517.

Entry information

Entry namePOLG_TEV
AccessionPrimary (citable) accession number: P04517
Secondary accession number(s): Q88500 expand/collapse secondary AC list , Q88501, Q88502, Q88504, Q88505, Q88506, Q89773
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 19, 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