P04517 (POLG_TEV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 10 chains: P1 proteinase EC=3.4.-.- Alternative name(s): N-terminal protein Helper component proteinase Short name=HC-pro EC=3.4.22.45 Protein P3 6 kDa protein 1 Short name=6K1 Cytoplasmic inclusion protein Short name=CI EC=3.6.4.- 6 kDa protein 2 Short name=6K2 Viral genome-linked protein Alternative name(s): VPg 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 Nuclear inclusion protein B Short name=NI-b Short name=NIb EC=2.7.7.48 Alternative name(s): RNA-directed RNA polymerase Capsid protein Short name=CP Alternative name(s): Coat protein
Organism	Tobacco etch virus (TEV) [Complete proteome]
Taxonomic identifier	12227 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Potyviridae › Potyvirus
Virus host	Capsicum 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 length	3054 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: a 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 process	Viral RNA replication
Cellular component	Virion
Coding sequence diversity	Ribosomal frameshifting
Ligand	ATP-binding Nucleotide-binding
Molecular function	Capsid protein Helicase Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Suppressor of RNA silencing Thiol protease Transferase
PTM	Covalent protein-RNA linkage Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular_component	viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3054

3054

Genome polyprotein

PRO_0000420026

Chain

1 – 304

304

P1 proteinase Potential

PRO_0000040450

Chain

305 – 763

459

Helper component proteinase Potential

PRO_0000040451

Chain

764 – 1110

347

Protein P3 By similarity

PRO_0000040452

Chain

1111 – 1163

53

6 kDa protein 1 By similarity

PRO_0000040453

Chain

1164 – 1796

633

Cytoplasmic inclusion protein

PRO_0000040454

Chain

1797 – 1849

53

6 kDa protein 2

PRO_0000040455

Chain

1850 – 2037

188

Viral genome-linked protein By similarity

PRO_0000040456

Chain

2038 – 2279

242

Nuclear inclusion protein A By similarity

PRO_0000040457

Chain

2280 – 2791

512

Nuclear inclusion protein B

PRO_0000040458

Chain

2792 – 3054

263

Capsid protein

PRO_0000040459

Regions

Domain

1234 – 1386

153

Helicase ATP-binding

Domain

1401 – 1564

164

Helicase C-terminal

Domain

2038 – 2255

218

Peptidase C4

Domain

2521 – 2641

121

RdRp catalytic

Nucleotide binding

1247 – 1254

8

ATP Potential

Motif

358 – 361

4

Involved in interaction with stylet and aphid transmission

Motif

615 – 617

3

Involved in virions binding and aphid transmission By similarity

Motif

1336 – 1339

4

DECH box

Motif

1889 – 1896

8

Nuclear localization signal Potential

Sites

Active site

214

1

For P1 proteinase activity Ref.4 Ref.5 Ref.6 Ref.11

Active site

223

1

For P1 proteinase activity Potential

Active site

256

1

For P1 proteinase activity Ref.4 Ref.5 Ref.6 Ref.11

Active site

649

1

For helper component proteinase activity Ref.4 Ref.5 Ref.6 Ref.11

Active site

722

1

For helper component proteinase activity Ref.4 Ref.5 Ref.6 Ref.11

Active site

2083

1

For nuclear inclusion protein A activity Ref.4 Ref.5 Ref.6 Ref.11

Active site

2118

1

For nuclear inclusion protein A activity Ref.4 Ref.5 Ref.6 Ref.11

Active site

2188

1

For nuclear inclusion protein A activity Ref.4 Ref.5 Ref.6 Ref.11

Site

304 – 305

2

Cleavage; by P1 proteinase Potential

Site

763 – 764

2

Cleavage; by HC-pro

Site

1110 – 1111

2

Cleavage; by NIa-pro By similarity

Site

1163 – 1164

2

Cleavage; by NIa-pro By similarity

Site

1796 – 1797

2

Cleavage; by NIa-pro By similarity

Site

1849 – 1850

2

Cleavage; by NIa-pro By similarity

Site

2037 – 2038

2

Cleavage; by NIa-pro By similarity

Site

2279 – 2280

2

Cleavage; by NIa-pro By similarity

Site

2791 – 2792

2

Cleavage; by NIa-pro By similarity

Amino acid modifications

Modified residue

1911

1

O-(5'-phospho-RNA)-tyrosine By similarity

Disulfide bond

2167

Interchain Ref.10 Ref.11

Experimental info

Mutagenesis

214

1

H → A: Complete loss of proteolytic activity of P1 proteinase. Ref.6

Mutagenesis

256

1

S → A: Complete loss of proteolytic activity of P1 proteinase. Ref.6

Mutagenesis

314

1

F → L: Complete loss of aphid transmission. Ref.7

Mutagenesis

358

1

K → E: Complete loss of interaction with stylet and aphid transmission; no effect on virion binding. Ref.7

Mutagenesis

610

1

S → T: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

619

1

H → S: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

625

1

S → T: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

627

1

D → E: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

632

1

D → E: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

649

1

C → S: Complete loss of proteolytic activity of HC-pro. Ref.4

Mutagenesis

675

1

D → E: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

689

1

D → E: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

694

1

C → S: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

698

1

S → T: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

715

1

D → E: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

716

1

H → S: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

722

1

H → S: Complete loss of proteolytic activity of HC-pro. Ref.4

Mutagenesis

725

1

D → E: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

726

1

S → T: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

729

1

S → T: No effect on proteolytic activity of HC-pro.

Mutagenesis

735

1

H → S: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

743

1

S → T: No effect on proteolytic activity of HC-pro. Ref.4

Mutagenesis

755

1

S → T: No effect on proteolytic activity of HC-pro. Ref.4

Secondary structure

1

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3054

Helix Strand Turn

Details...

Helix

2049 – 2053

5

Beta strand

2055 – 2064

10

Beta strand

2066 – 2074

9

Beta strand

2077 – 2080

4

Helix

2082 – 2085

4

Beta strand

2089 – 2096

8

Beta strand

2099 – 2104

6

Helix

2106 – 2108

3

Beta strand

2110 – 2113

4

Beta strand

2120 – 2123

4

Beta strand

2145 – 2152

8

Beta strand

2154 – 2157

4

Beta strand

2159 – 2162

4

Turn

2172 – 2175

4

Beta strand

2176 – 2179

4

Beta strand

2191 – 2194

4

Turn

2195 – 2197

3

Beta strand

2200 – 2207

8

Beta strand

2209 – 2211

3

Beta strand

2214 – 2218

5

Helix

2223 – 2228

6

Beta strand

2236 – 2238

3

Beta strand

2243 – 2248

6

Beta strand

2251 – 2256

6

Beta strand

2276 – 2278

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Genome polyprotein [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 0AF9A3626960B5CE	FASTA	3,054	346,164
	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
	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.

PIR

GNBVEV. A04207.

RefSeq

NP_062908.1. NC_001555.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LVB	X-ray	2.20	A/B	2038-2273	[»]
			C/D	2785-2794	[»]
1LVM	X-ray	1.80	A/B	2038-2258	[»]
			E	2267-2273	[»]
1Q31	X-ray	2.70	A/B	2038-2279	[»]

ProteinModelPortal

P04517.

SMR

P04517. Positions 2038-2258.

ModBase

Search...

Protein family/group databases

MEROPS

C04.004.

Proteomic databases

PRIDE

P04517.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR011492. DEAD_Flavivir.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
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]

Pfam

PF07652. 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]

PRINTS

PR00966. NIAPOTYPTASE.

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS51192. 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]

ProtoNet

Search...

Other

EvolutionaryTrace

P04517.

PMAP-CutDB

P04517.

Entry information

Entry name

POLG_TEV

Accession

Primary (citable) accession number: P04517
Secondary accession number(s): Q88500 , Q88501, Q88502, Q88504, Q88505, Q88506, Q89773

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program