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P04517

- POLG_TEV

UniProt

P04517 - POLG_TEV

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Protein

Genome polyprotein

Gene
N/A
Organism
Tobacco etch virus (TEV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.
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.
Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.
Both 6K peptides are indispensable for virus replication.By similarity
Nuclear inclusion protein A: has RNA-binding and proteolytic activities.

Catalytic activityi

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).PROSITE-ProRule annotation
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei214 – 2141For P1 proteinase activity
Active sitei223 – 2231For P1 proteinase activitySequence Analysis
Active sitei256 – 2561For P1 proteinase activity
Sitei304 – 3052Cleavage; by P1 proteinaseSequence Analysis
Active sitei649 – 6491For helper component proteinase activity
Active sitei722 – 7221For helper component proteinase activity
Sitei763 – 7642Cleavage; by HC-pro
Sitei1110 – 11112Cleavage; by NIa-proBy similarity
Sitei1163 – 11642Cleavage; by NIa-proBy similarity
Sitei1796 – 17972Cleavage; by NIa-proBy similarity
Sitei1849 – 18502Cleavage; by NIa-proBy similarity
Sitei2037 – 20382Cleavage; by NIa-proBy similarity
Active sitei2083 – 20831For nuclear inclusion protein A activity
Active sitei2118 – 21181For nuclear inclusion protein A activity
Active sitei2188 – 21881For nuclear inclusion protein A activity
Sitei2279 – 22802Cleavage; by NIa-proBy similarity
Sitei2791 – 27922Cleavage; by NIa-proBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1247 – 12548ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. cysteine-type endopeptidase activity Source: InterPro
  4. RNA binding Source: InterPro
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. structural molecule activity Source: InterPro

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. transcription, DNA-templated Source: InterPro
  3. viral RNA genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Suppressor of RNA silencing, Thiol protease, Transferase

Keywords - Biological processi

Viral RNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Protein family/group databases

MEROPSiC04.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 10 chains:
Alternative name(s):
N-terminal protein
Helper component proteinase (EC:3.4.22.45)
Short name:
HC-pro
6 kDa protein 1
Short name:
6K1
6 kDa protein 2
Short name:
6K2
Alternative name(s):
VPg
Nuclear inclusion protein A (EC:3.4.22.44)
Short name:
NI-a
Short name:
NIa
Alternative name(s):
49 kDa proteinase
Short name:
49 kDa-Pro
NIa-pro
Nuclear inclusion protein B (EC:2.7.7.48)
Short name:
NI-b
Short name:
NIb
Alternative name(s):
RNA-directed RNA polymerase
Capsid protein
Short name:
CP
Alternative name(s):
Coat protein
OrganismiTobacco etch virus (TEV)
Taxonomic identifieri12227 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiCapsicum 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]
ProteomesiUP000007404: Genome

Subcellular locationi

GO - Cellular componenti

  1. helical viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141H → A: Complete loss of proteolytic activity of P1 proteinase. 1 Publication
Mutagenesisi256 – 2561S → A: Complete loss of proteolytic activity of P1 proteinase. 1 Publication
Mutagenesisi314 – 3141F → L: Complete loss of aphid transmission. 1 Publication
Mutagenesisi358 – 3581K → E: Complete loss of interaction with stylet and aphid transmission; no effect on virion binding. 1 Publication
Mutagenesisi610 – 6101S → T: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi619 – 6191H → S: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi625 – 6251S → T: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi627 – 6271D → E: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi632 – 6321D → E: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi649 – 6491C → S: Complete loss of proteolytic activity of HC-pro. 1 Publication
Mutagenesisi675 – 6751D → E: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi689 – 6891D → E: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi694 – 6941C → S: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi698 – 6981S → T: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi715 – 7151D → E: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi716 – 7161H → S: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi722 – 7221H → S: Complete loss of proteolytic activity of HC-pro. 1 Publication
Mutagenesisi725 – 7251D → E: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi726 – 7261S → T: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi729 – 7291S → T: No effect on proteolytic activity of HC-pro.
Mutagenesisi735 – 7351H → S: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi743 – 7431S → T: No effect on proteolytic activity of HC-pro. 1 Publication
Mutagenesisi755 – 7551S → T: No effect on proteolytic activity of HC-pro. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30543054Genome polyproteinPRO_0000420026Add
BLAST
Chaini1 – 304304P1 proteinaseSequence AnalysisPRO_0000040450Add
BLAST
Chaini305 – 763459Helper component proteinaseSequence AnalysisPRO_0000040451Add
BLAST
Chaini764 – 1110347Protein P3By similarityPRO_0000040452Add
BLAST
Chaini1111 – 1163536 kDa protein 1By similarityPRO_0000040453Add
BLAST
Chaini1164 – 1796633Cytoplasmic inclusion proteinPRO_0000040454Add
BLAST
Chaini1797 – 1849536 kDa protein 2PRO_0000040455Add
BLAST
Chaini1850 – 2037188Viral genome-linked proteinBy similarityPRO_0000040456Add
BLAST
Chaini2038 – 2279242Nuclear inclusion protein ABy similarityPRO_0000040457Add
BLAST
Chaini2280 – 2791512Nuclear inclusion protein BPRO_0000040458Add
BLAST
Chaini2792 – 3054263Capsid proteinPRO_0000040459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1911 – 19111O-(5'-phospho-RNA)-tyrosineBy similarity
Disulfide bondi2167 – 2167Interchain2 Publications

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiP04517.

Miscellaneous databases

PMAP-CutDBP04517.

Interactioni

Subunit structurei

Nuclear inclusion protein A protease is a dimer; disulfide-linked.2 Publications

Structurei

Secondary structure

1
3054
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2038 – 20403
Helixi2049 – 20524
Beta strandi2055 – 20628
Beta strandi2065 – 207410
Beta strandi2077 – 20804
Helixi2082 – 20865
Beta strandi2089 – 20968
Beta strandi2099 – 21046
Helixi2106 – 21083
Beta strandi2109 – 21135
Beta strandi2120 – 21234
Beta strandi2145 – 21528
Beta strandi2154 – 21574
Beta strandi2159 – 21624
Beta strandi2169 – 21713
Turni2172 – 21754
Beta strandi2176 – 21794
Beta strandi2191 – 21944
Turni2195 – 21973
Beta strandi2200 – 22089
Beta strandi2209 – 22113
Beta strandi2213 – 22186
Helixi2223 – 22286
Helixi2230 – 22323
Beta strandi2235 – 22384
Beta strandi2243 – 22486
Beta strandi2251 – 22566
Beta strandi2276 – 22783
Beta strandi2788 – 27903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVBX-ray2.20A/B2038-2273[»]
C/D2785-2794[»]
1LVMX-ray1.80A/B2038-2258[»]
E2267-2273[»]
1Q31X-ray2.70A/B2038-2279[»]
ProteinModelPortaliP04517.
SMRiP04517. Positions 2038-2258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1234 – 1386153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1401 – 1564164Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2038 – 2255218Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2521 – 2641121RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi358 – 3614Involved in interaction with stylet and aphid transmission
Motifi615 – 6173Involved in virions binding and aphid transmissionBy similarity
Motifi1336 – 13394DECH box
Motifi1889 – 18968Nuclear localization signalSequence Analysis

Domaini

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.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 peptidase C4 domain.PROSITE-ProRule annotation
Contains 1 peptidase C6 domain.Curated
Contains 1 peptidase S30 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. 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]
PfamiPF07652. 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]
PRINTSiPR00966. NIAPOTYPTASE.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Isoform Genome polyprotein (identifier: P04517-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH
60 70 80 90 100
KPVIFGEDYI TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN
110 120 130 140 150
NKRNRRRKVA KTYVGRDSIV EKIVVPHTER KVDTTAAVED ICNEATTQLV
160 170 180 190 200
HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV RKRHMQVEII SKKSVRARVK
210 220 230 240 250
RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR FKNERVDQSK
260 270 280 290 300
LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS
310 320 330 340 350
MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT
360 370 380 390 400
QALSPCGKIT CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA
410 420 430 440 450
EKLLTRFLQQ KSLVNTNLTA CVSVKQLIGD RKQAPFTHVL AVSEILFKGN
460 470 480 490 500
KLTGADLEEA STHMLEIARF LNNRTENMRI GHLGSFRNKI SSKAHVNNAL
510 520 530 540 550
MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK YVIRKHIRGS
560 570 580 590 600
RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV
610 620 630 640 650
TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY
660 670 680 690 700
MNIFFALLVN VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL
710 720 730 740 750
YPDVLRAELP RILVDHDNKT MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH
760 770 780 790 800
SGLESEMKTY NVGGMNRDVV TQGAIEMLIK SIYKPHLMKQ LLEEEPYIIV
810 820 830 840 850
LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS ALAQKLTLAD
860 870 880 890 900
LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL
910 920 930 940 950
REGGYAVTSE KVHEMLEKNY VKALKDAWDE LTWLEKFSAI RHSRKLLKFG
960 970 980 990 1000
RKPLIMKNTV DCGGHIDLSV KSLFKFHLEL LKGTISRAVN GGARKVRVAK
1010 1020 1030 1040 1050
NAMTKGVFLK IYSMLPDVYK FITVSSVLSL LLTFLFQIDC MIRAHREAKV
1060 1070 1080 1090 1100
AAQLQKESEW DNIINRTFQY SKLENPIGYR STAEERLQSE HPEAFEYYKF
1110 1120 1130 1140 1150
CIGKEDLVEQ AKQPEIAYFE KIIAFITLVL MAFDAERSDG VFKILNKFKG
1160 1170 1180 1190 1200
ILSSTEREII YTQSLDDYVT TFDDNMTINL ELNMDELHKT SLPGVTFKQW
1210 1220 1230 1240 1250
WNNQISRGNV KPHYRTEGHF MEFTRDTAAS VASEISHSPA RDFLVRGAVG
1260 1270 1280 1290 1300
SGKSTGLPYH LSKRGRVLML EPTRPLTDNM HKQLRSEPFN CFPTLRMRGK
1310 1320 1330 1340 1350
STFGSSPITV MTSGFALHHF ARNIAEVKTY DFVIIDECHV NDASAIAFRN
1360 1370 1380 1390 1400
LLFEHEFEGK VLKVSATPPG REVEFTTQFP VKLKIEEALS FQEFVSLQGT
1410 1420 1430 1440 1450
GANADVISCG DNILVYVASY NDVDSLGKLL VQKGYKVSKI DGRTMKSGGT
1460 1470 1480 1490 1500
EIITEGTSVK KHFIVATNII ENGVTIDIDV VVDFGTKVVP VLDVDNRAVQ
1510 1520 1530 1540 1550
YNKTVVSYGE RIQKLGRVGR HKEGVALRIG QTNKTLVEIP EMVATEAAFL
1560 1570 1580 1590 1600
CFMYNLPVTT QSVSTTLLEN ATLLQARTMA QFELSYFYTI NFVRFDGSMH
1610 1620 1630 1640 1650
PVIHDKLKRF KLHTCETFLN KLAIPNKGLS SWLTSGEYKR LGYIAEDAGI
1660 1670 1680 1690 1700
RIPFVCKEIP DSLHEEIWHI VVAHKGDSGI GRLTSVQAAK VVYTLQTDVH
1710 1720 1730 1740 1750
SIARTLACIN RRIADEQMKQ SHFEAATGRA FSFTNYSIQS IFDTLKANYA
1760 1770 1780 1790 1800
TKHTKENIAV LQQAKDQLLE FSNLAKDQDV TGIIQDFNHL ETIYLQSDSE
1810 1820 1830 1840 1850
VAKHLKLKSH WNKSQITRDI IIALSVLIGG GWMLATYFKD KFNEPVYFQG
1860 1870 1880 1890 1900
KKNQKHKLKM REARGARGQY EVAAEPEALE HYFGSAYNNK GKRKGTTRGM
1910 1920 1930 1940 1950
GAKSRKFINM YGFDPTDFSY IRFVDPLTGH TIDESTNAPI DLVQHEFGKV
1960 1970 1980 1990 2000
RTRMLIDDEI EPQSLSTHTT IHAYLVNSGT KKVLKVDLTP HSSLRASEKS
2010 2020 2030 2040 2050
TAIMGFPERE NELRQTGMAV PVAYDQLPPK NEDLTFEGES LFKGPRDYNP
2060 2070 2080 2090 2100
ISSTICHLTN ESDGHTTSLY GIGFGPFIIT NKHLFRRNNG TLLVQSLHGV
2110 2120 2130 2140 2150
FKVKNTTTLQ QHLIDGRDMI IIRMPKDFPP FPQKLKFREP QREERICLVT
2160 2170 2180 2190 2200
TNFQTKSMSS MVSDTSCTFP SSDGIFWKHW IQTKDGQCGS PLVSTRDGFI
2210 2220 2230 2240 2250
VGIHSASNFT NTNNYFTSVP KNFMELLTNQ EAQQWVSGWR LNADSVLWGG
2260 2270 2280 2290 2300
HKVFMSKPEE PFQPVKEATQ LMNELVYSQG EKRKWVVEAL SGNLRPVAEC
2310 2320 2330 2340 2350
PSQLVTKHVV KGKCPLFELY LQLNPEKEAY FKPMMGAYKP SRLNREAFLK
2360 2370 2380 2390 2400
DILKYASEIE IGNVDCDLLE LAISMLVTKL KALGFPTVNY ITDPEEIFSA
2410 2420 2430 2440 2450
LNMKAAMGAL YKGKKKEALS ELTLDEQEAM LKASCLRLYT GKLGIWNGSL
2460 2470 2480 2490 2500
KAELRPIEKV ENNKTRTFTA APIDTLLAGK VCVDDFNNQF YDLNIKAPWT
2510 2520 2530 2540 2550
VGMTKFYQGW NELMEALPSG WVYCDADGSQ FDSSLTPFLI NAVLKVRLAF
2560 2570 2580 2590 2600
MEEWDIGEQM LRNLYTEIVY TPILTPDGTI IKKHKGNNSG QPSTVVDNTL
2610 2620 2630 2640 2650
MVIIAMLYTC EKCGINKEEI VYYVNGDDLL IAIHPDKAER LSRFKESFGE
2660 2670 2680 2690 2700
LGLKYEFDCT TRDKTQLWFM SHRALERDGM YIPKLEEERI VSILEWDRSK
2710 2720 2730 2740 2750
EPSHRLEAIC ASMIEAWGYD KLVEEIRNFY AWVLEQAPYS QLAEEGKAPY
2760 2770 2780 2790 2800
LAETALKFLY TSQHGTNSEI EEYLKVLYDY DIPTTENLYF QSGTVDAGAD
2810 2820 2830 2840 2850
AGKKKDQKDD KVAEQASKDR DVNAGTSGTF SVPRINAMAT KLQYPRMRGE
2860 2870 2880 2890 2900
VVVNLNHLLG YKPQQIDLSN ARATHEQFAA WHQAVMTAYG VNEEQMKILL
2910 2920 2930 2940 2950
NGFMVWCIEN GTSPNLNGTW VMMDGEDQVS YPLKPMVENA QPTLRQIMTH
2960 2970 2980 2990 3000
FSDLAEAYIE MRNRERPYMP RYGLQRNITD MSLSRYAFDF YELTSKTPVR
3010 3020 3030 3040 3050
AREAHMQMKA AAVRNSGTRL FGLDGNVGTA EEDTERHTAH DVNRNMHTLL

GVRQ

Note: Produced by conventional translation.

Length:3,054
Mass (Da):346,164
Last modified:August 13, 1987 - v1
Checksum:i0AF9A3626960B5CE
GO
Isoform P3N-PIPO polyprotein (identifier: P0CK09-1) [UniParc]FASTAAdd to Basket

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.

Length:1,016
Mass (Da):115,451
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15239 Genomic RNA. Translation: AAA47910.1.
M11458 Genomic RNA. Translation: AAA47909.1.
M11216 Genomic RNA. Translation: AAA47908.1. Sequence problems.
PIRiA04207. GNBVEV.
RefSeqiNP_062908.1. NC_001555.1. [P04517-1]

Genome annotation databases

GeneIDi1502321.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15239 Genomic RNA. Translation: AAA47910.1 .
M11458 Genomic RNA. Translation: AAA47909.1 .
M11216 Genomic RNA. Translation: AAA47908.1 . Sequence problems.
PIRi A04207. GNBVEV.
RefSeqi NP_062908.1. NC_001555.1. [P04517-1 ]

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P04517.
SMRi P04517. Positions 2038-2258.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C04.004.

Proteomic databases

PRIDEi P04517.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1502321.

Miscellaneous databases

EvolutionaryTracei P04517.
PMAP-CutDB P04517.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011492. 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 ]
Pfami 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 ]
PRINTSi PR00966. NIAPOTYPTASE.
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiPOLG_TEV
AccessioniPrimary (citable) accession number: P04517
Secondary accession number(s): Q88500
, Q88501, Q88502, Q88504, Q88505, Q88506, Q89773
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 1, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3