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Protein

Genome polyprotein

Gene
N/A
Organism
Tobacco etch virus (TEV)
Status
Reviewed-Annotation score: -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 similarity2 Publications
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)DescriptionActionsGraphical viewLength
Active sitei214For P1 proteinase activityPROSITE-ProRule annotation1
Active sitei223For P1 proteinase activityPROSITE-ProRule annotation1
Active sitei256For P1 proteinase activityPROSITE-ProRule annotation1
Active sitei649For helper component proteinase activityPROSITE-ProRule annotation1
Active sitei722For helper component proteinase activityPROSITE-ProRule annotation1
Active sitei2083For nuclear inclusion protein A activity1
Active sitei2118For nuclear inclusion protein A activity1
Active sitei2188For nuclear inclusion protein A activity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1247 – 1254ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Thiol protease, Transferase
Biological processViral RNA replication
LigandATP-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 virusesssRNA 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]
Proteomesi
  • UP000007404 Componenti: Genome
  • UP000201712 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi214H → A: Complete loss of proteolytic activity of P1 proteinase. 1 Publication1
Mutagenesisi256S → A: Complete loss of proteolytic activity of P1 proteinase. 1 Publication1
Mutagenesisi314F → L: Complete loss of aphid transmission. 1 Publication1
Mutagenesisi358K → E: Complete loss of interaction with stylet and aphid transmission; no effect on virion binding. 1 Publication1
Mutagenesisi610S → T: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi619H → S: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi625S → T: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi627D → E: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi632D → E: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi649C → S: Complete loss of proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi675D → E: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi689D → E: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi694C → S: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi698S → T: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi715D → E: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi716H → S: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi722H → S: Complete loss of proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi725D → E: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi726S → T: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi729S → T: No effect on proteolytic activity of HC-pro. 1
Mutagenesisi735H → S: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi743S → T: No effect on proteolytic activity of HC-pro. 1 Publication1
Mutagenesisi755S → T: No effect on proteolytic activity of HC-pro. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004200261 – 3054Genome polyproteinAdd BLAST3054
ChainiPRO_00000404501 – 304P1 proteinaseSequence analysisAdd BLAST304
ChainiPRO_0000040451305 – 763Helper component proteinaseSequence analysisAdd BLAST459
ChainiPRO_0000040452764 – 1110Protein P3By similarityAdd BLAST347
ChainiPRO_00000404531111 – 11636 kDa protein 1By similarityAdd BLAST53
ChainiPRO_00000404541164 – 1796Cytoplasmic inclusion proteinAdd BLAST633
ChainiPRO_00000404551797 – 18496 kDa protein 2Add BLAST53
ChainiPRO_00000404561850 – 2037Viral genome-linked proteinBy similarityAdd BLAST188
ChainiPRO_00000404572038 – 2279Nuclear inclusion protein ABy similarityAdd BLAST242
ChainiPRO_00000404582280 – 2791Nuclear inclusion protein BAdd BLAST512
ChainiPRO_00000404592792 – 3054Capsid proteinAdd BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1911O-(5'-phospho-RNA)-tyrosineBy similarity1
Disulfide bondi2167Interchain2 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei304 – 305Cleavage; by P1 proteinasePROSITE-ProRule annotation2
Sitei763 – 764Cleavage; by autolysisPROSITE-ProRule annotation2
Sitei1110 – 1111Cleavage; by NIa-proBy similarity2
Sitei1163 – 1164Cleavage; by NIa-proBy similarity2
Sitei1796 – 1797Cleavage; by NIa-proBy similarity2
Sitei1849 – 1850Cleavage; by NIa-proBy similarity2
Sitei2037 – 2038Cleavage; by NIa-proBy similarity2
Sitei2279 – 2280Cleavage; by NIa-proBy similarity2
Sitei2791 – 2792Cleavage; by NIa-proBy similarity2

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

13054
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP04517
SMRiP04517
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04517

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini163 – 304Peptidase S30PROSITE-ProRule annotationAdd BLAST142
Domaini641 – 763Peptidase C6PROSITE-ProRule annotationAdd BLAST123
Domaini1234 – 1386Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini1401 – 1564Helicase C-terminalPROSITE-ProRule annotationAdd BLAST164
Domaini2038 – 2255Peptidase C4PROSITE-ProRule annotationAdd BLAST218
Domaini2521 – 2641RdRp catalyticPROSITE-ProRule annotationAdd BLAST121

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi358 – 361Involved in interaction with stylet and aphid transmission4
Motifi615 – 617Involved in virions binding and aphid transmissionBy similarity3
Motifi1336 – 1339DECH box4
Motifi1889 – 1896Nuclear localization signalSequence analysis8

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

Phylogenomic databases

OrthoDBiVOG0900003L

Family and domain databases

InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR001456 HC-pro
IPR031159 HC_PRO_CPD_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR002540 Pept_S30_P1_potyvir
IPR009003 Peptidase_S1_PA
IPR001592 Poty_coat
IPR001730 Potyv_NIa-pro_dom
IPR039560 Potyvirid-P3
IPR013648 PP_Potyviridae
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
PfamiView protein in 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
PF13608 Potyvirid-P3, 1 hit
PF00680 RdRP_1, 1 hit
PRINTSiPR00966 NIAPOTYPTASE
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51744 HC_PRO_CPD, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51436 POTYVIRUS_NIA_PRO, 1 hit
PS51871 PV_P1_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

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. AlignAdd to basket
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:
EMBLi
GenBanki
DDBJi
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
KEGGivg:1502321

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LVBX-ray2.20A/B2038-2273[»]
C/D2785-2794[»]
1LVMX-ray1.80A/B2038-2258[»]
C/D2786-2794[»]
E2267-2273[»]
1Q31X-ray2.70A/B2038-2279[»]
ProteinModelPortaliP04517
SMRiP04517
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC04.004

Proteomic databases

PRIDEiP04517

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1502321
KEGGivg:1502321

Phylogenomic databases

OrthoDBiVOG0900003L

Miscellaneous databases

EvolutionaryTraceiP04517
PMAP-CutDBiP04517

Family and domain databases

InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR001456 HC-pro
IPR031159 HC_PRO_CPD_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR002540 Pept_S30_P1_potyvir
IPR009003 Peptidase_S1_PA
IPR001592 Poty_coat
IPR001730 Potyv_NIa-pro_dom
IPR039560 Potyvirid-P3
IPR013648 PP_Potyviridae
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
PfamiView protein in 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
PF13608 Potyvirid-P3, 1 hit
PF00680 RdRP_1, 1 hit
PRINTSiPR00966 NIAPOTYPTASE
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51744 HC_PRO_CPD, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51436 POTYVIRUS_NIA_PRO, 1 hit
PS51871 PV_P1_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_TEV
AccessioniPrimary (citable) accession number: P04517
Secondary accession number(s): Q88500
, Q88501, Q88502, Q88504, Q88505, Q88506, Q89773
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 7, 2018
This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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