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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.2 Publications
Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.2 Publications
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.2 Publications
Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.2 Publications
Both 6K peptides are indispensable for virus replication By similarity.2 Publications
Nuclear inclusion protein A: has RNA-binding and proteolytic activities.2 Publications

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).
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 activity4 Publications
Active sitei223 – 2231For P1 proteinase activity Reviewed prediction
Active sitei256 – 2561For P1 proteinase activity4 Publications
Sitei304 – 3052Cleavage; by P1 proteinase Reviewed prediction
Active sitei649 – 6491For helper component proteinase activity4 Publications
Active sitei722 – 7221For helper component proteinase activity4 Publications
Sitei763 – 7642Cleavage; by HC-pro
Sitei1110 – 11112Cleavage; by NIa-pro By similarity
Sitei1163 – 11642Cleavage; by NIa-pro By similarity
Sitei1796 – 17972Cleavage; by NIa-pro By similarity
Sitei1849 – 18502Cleavage; by NIa-pro By similarity
Sitei2037 – 20382Cleavage; by NIa-pro By similarity
Active sitei2083 – 20831For nuclear inclusion protein A activity4 Publications
Active sitei2118 – 21181For nuclear inclusion protein A activity4 Publications
Active sitei2188 – 21881For nuclear inclusion protein A activity4 Publications
Sitei2279 – 22802Cleavage; by NIa-pro By similarity
Sitei2791 – 27922Cleavage; by NIa-pro By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1247 – 12548ATP Reviewed prediction

GO - Molecular functioni

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

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

Chain Capsid protein : Virion Reviewed prediction

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 polyprotein
PRO_0000420026Add
BLAST
Chaini1 – 304304P1 proteinase Reviewed prediction
PRO_0000040450Add
BLAST
Chaini305 – 763459Helper component proteinase Reviewed prediction
PRO_0000040451Add
BLAST
Chaini764 – 1110347Protein P3 By similarity
PRO_0000040452Add
BLAST
Chaini1111 – 1163536 kDa protein 1 By similarity
PRO_0000040453Add
BLAST
Chaini1164 – 1796633Cytoplasmic inclusion protein
PRO_0000040454Add
BLAST
Chaini1797 – 1849536 kDa protein 2
PRO_0000040455Add
BLAST
Chaini1850 – 2037188Viral genome-linked protein By similarity
PRO_0000040456Add
BLAST
Chaini2038 – 2279242Nuclear inclusion protein A By similarity
PRO_0000040457Add
BLAST
Chaini2280 – 2791512Nuclear inclusion protein B
PRO_0000040458Add
BLAST
Chaini2792 – 3054263Capsid protein
PRO_0000040459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1911 – 19111O-(5'-phospho-RNA)-tyrosine By 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.
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.

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiP04517.

Miscellaneous databases

PMAP-CutDBiP04517.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP04517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1234 – 1386153Helicase ATP-binding
Add
BLAST
Domaini1401 – 1564164Helicase C-terminal
Add
BLAST
Domaini2038 – 2255218Peptidase C4
Add
BLAST
Domaini2521 – 2641121RdRp catalytic
Add
BLAST

Motif

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

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

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...

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-CutDBi 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: May 14, 2014
This is version 144 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

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