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P04517

- POLG_TEV

UniProt

P04517 - POLG_TEV

Protein

Genome polyprotein

Gene
N/A
Organism
Tobacco etch virus (TEV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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

    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

    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

    MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH     50
    KPVIFGEDYI TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN 100
    NKRNRRRKVA KTYVGRDSIV EKIVVPHTER KVDTTAAVED ICNEATTQLV 150
    HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV RKRHMQVEII SKKSVRARVK 200
    RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR FKNERVDQSK 250
    LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS 300
    MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT 350
    QALSPCGKIT CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA 400
    EKLLTRFLQQ KSLVNTNLTA CVSVKQLIGD RKQAPFTHVL AVSEILFKGN 450
    KLTGADLEEA STHMLEIARF LNNRTENMRI GHLGSFRNKI SSKAHVNNAL 500
    MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK YVIRKHIRGS 550
    RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV 600
    TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY 650
    MNIFFALLVN VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL 700
    YPDVLRAELP RILVDHDNKT MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH 750
    SGLESEMKTY NVGGMNRDVV TQGAIEMLIK SIYKPHLMKQ LLEEEPYIIV 800
    LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS ALAQKLTLAD 850
    LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL 900
    REGGYAVTSE KVHEMLEKNY VKALKDAWDE LTWLEKFSAI RHSRKLLKFG 950
    RKPLIMKNTV DCGGHIDLSV KSLFKFHLEL LKGTISRAVN GGARKVRVAK 1000
    NAMTKGVFLK IYSMLPDVYK FITVSSVLSL LLTFLFQIDC MIRAHREAKV 1050
    AAQLQKESEW DNIINRTFQY SKLENPIGYR STAEERLQSE HPEAFEYYKF 1100
    CIGKEDLVEQ AKQPEIAYFE KIIAFITLVL MAFDAERSDG VFKILNKFKG 1150
    ILSSTEREII YTQSLDDYVT TFDDNMTINL ELNMDELHKT SLPGVTFKQW 1200
    WNNQISRGNV KPHYRTEGHF MEFTRDTAAS VASEISHSPA RDFLVRGAVG 1250
    SGKSTGLPYH LSKRGRVLML EPTRPLTDNM HKQLRSEPFN CFPTLRMRGK 1300
    STFGSSPITV MTSGFALHHF ARNIAEVKTY DFVIIDECHV NDASAIAFRN 1350
    LLFEHEFEGK VLKVSATPPG REVEFTTQFP VKLKIEEALS FQEFVSLQGT 1400
    GANADVISCG DNILVYVASY NDVDSLGKLL VQKGYKVSKI DGRTMKSGGT 1450
    EIITEGTSVK KHFIVATNII ENGVTIDIDV VVDFGTKVVP VLDVDNRAVQ 1500
    YNKTVVSYGE RIQKLGRVGR HKEGVALRIG QTNKTLVEIP EMVATEAAFL 1550
    CFMYNLPVTT QSVSTTLLEN ATLLQARTMA QFELSYFYTI NFVRFDGSMH 1600
    PVIHDKLKRF KLHTCETFLN KLAIPNKGLS SWLTSGEYKR LGYIAEDAGI 1650
    RIPFVCKEIP DSLHEEIWHI VVAHKGDSGI GRLTSVQAAK VVYTLQTDVH 1700
    SIARTLACIN RRIADEQMKQ SHFEAATGRA FSFTNYSIQS IFDTLKANYA 1750
    TKHTKENIAV LQQAKDQLLE FSNLAKDQDV TGIIQDFNHL ETIYLQSDSE 1800
    VAKHLKLKSH WNKSQITRDI IIALSVLIGG GWMLATYFKD KFNEPVYFQG 1850
    KKNQKHKLKM REARGARGQY EVAAEPEALE HYFGSAYNNK GKRKGTTRGM 1900
    GAKSRKFINM YGFDPTDFSY IRFVDPLTGH TIDESTNAPI DLVQHEFGKV 1950
    RTRMLIDDEI EPQSLSTHTT IHAYLVNSGT KKVLKVDLTP HSSLRASEKS 2000
    TAIMGFPERE NELRQTGMAV PVAYDQLPPK NEDLTFEGES LFKGPRDYNP 2050
    ISSTICHLTN ESDGHTTSLY GIGFGPFIIT NKHLFRRNNG TLLVQSLHGV 2100
    FKVKNTTTLQ QHLIDGRDMI IIRMPKDFPP FPQKLKFREP QREERICLVT 2150
    TNFQTKSMSS MVSDTSCTFP SSDGIFWKHW IQTKDGQCGS PLVSTRDGFI 2200
    VGIHSASNFT NTNNYFTSVP KNFMELLTNQ EAQQWVSGWR LNADSVLWGG 2250
    HKVFMSKPEE PFQPVKEATQ LMNELVYSQG EKRKWVVEAL SGNLRPVAEC 2300
    PSQLVTKHVV KGKCPLFELY LQLNPEKEAY FKPMMGAYKP SRLNREAFLK 2350
    DILKYASEIE IGNVDCDLLE LAISMLVTKL KALGFPTVNY ITDPEEIFSA 2400
    LNMKAAMGAL YKGKKKEALS ELTLDEQEAM LKASCLRLYT GKLGIWNGSL 2450
    KAELRPIEKV ENNKTRTFTA APIDTLLAGK VCVDDFNNQF YDLNIKAPWT 2500
    VGMTKFYQGW NELMEALPSG WVYCDADGSQ FDSSLTPFLI NAVLKVRLAF 2550
    MEEWDIGEQM LRNLYTEIVY TPILTPDGTI IKKHKGNNSG QPSTVVDNTL 2600
    MVIIAMLYTC EKCGINKEEI VYYVNGDDLL IAIHPDKAER LSRFKESFGE 2650
    LGLKYEFDCT TRDKTQLWFM SHRALERDGM YIPKLEEERI VSILEWDRSK 2700
    EPSHRLEAIC ASMIEAWGYD KLVEEIRNFY AWVLEQAPYS QLAEEGKAPY 2750
    LAETALKFLY TSQHGTNSEI EEYLKVLYDY DIPTTENLYF QSGTVDAGAD 2800
    AGKKKDQKDD KVAEQASKDR DVNAGTSGTF SVPRINAMAT KLQYPRMRGE 2850
    VVVNLNHLLG YKPQQIDLSN ARATHEQFAA WHQAVMTAYG VNEEQMKILL 2900
    NGFMVWCIEN GTSPNLNGTW VMMDGEDQVS YPLKPMVENA QPTLRQIMTH 2950
    FSDLAEAYIE MRNRERPYMP RYGLQRNITD MSLSRYAFDF YELTSKTPVR 3000
    AREAHMQMKA AAVRNSGTRL FGLDGNVGTA EEDTERHTAH DVNRNMHTLL 3050
    GVRQ 3054

    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