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P09814

- POLG_TVMV

UniProt

P09814 - POLG_TVMV

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Protein

Genome polyprotein

Gene
N/A
Organism
Tobacco vein mottling virus (TVMV)
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 (By similarity).By similarity
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 sitei183 – 1831For P1 proteinase activityBy similarity
Active sitei192 – 1921For P1 proteinase activitySequence Analysis
Active sitei225 – 2251For P1 proteinase activityBy similarity
Sitei274 – 2752Cleavage; by P1 proteinaseSequence Analysis
Active sitei617 – 6171For helper component proteinase activityBy similarity
Active sitei690 – 6901For helper component proteinase activityBy similarity
Sitei731 – 7322Cleavage; by HC-proSequence Analysis
Sitei1078 – 10792Cleavage; by NIa-proBy similarity
Sitei1130 – 11312Cleavage; by NIa-proBy similarity
Sitei1765 – 17662Cleavage; by NIa-proBy similarity
Sitei1818 – 18192Cleavage; by NIa-proBy similarity
Sitei2001 – 20022Cleavage; by NIa-proBy similarity
Active sitei2047 – 20471For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2082 – 20821For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2152 – 21521For nuclear inclusion protein A activityPROSITE-ProRule annotation
Sitei2242 – 22432Cleavage; by NIa-proBy similarity
Sitei2758 – 27592Cleavage; by NIa-proBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1215 – 12228ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. helicase activity Source: UniProtKB-KW
  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

MEROPSiC04.003.

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 vein mottling virus (TVMV)
Taxonomic identifieri12228 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiNicotiana tabacum (Common tobacco) [TaxID: 4097]
Rumex [TaxID: 3618]
ProteomesiUP000007549: 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30233023Genome polyproteinPRO_0000420031Add
BLAST
Chaini1 – 274274P1 proteinaseSequence AnalysisPRO_0000040483Add
BLAST
Chaini275 – 731457Helper component proteinaseSequence AnalysisPRO_0000040484Add
BLAST
Chaini732 – 1078347Protein P3By similarityPRO_0000040485Add
BLAST
Chaini1079 – 1130526 kDa protein 1By similarityPRO_0000040486Add
BLAST
Chaini1131 – 1765635Cytoplasmic inclusion proteinBy similarityPRO_0000040487Add
BLAST
Chaini1766 – 1818536 kDa protein 2By similarityPRO_0000040488Add
BLAST
Chaini1819 – 2001183Viral genome-linked proteinBy similarityPRO_0000040489Add
BLAST
Chaini2002 – 2242241Nuclear inclusion protein ABy similarityPRO_0000040490Add
BLAST
Chaini2243 – 2758516Nuclear inclusion protein BBy similarityPRO_0000040491Add
BLAST
Chaini2759 – 3023265Capsid proteinBy similarityPRO_0000040492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1878 – 18781O-(5'-phospho-RNA)-tyrosine
Modified residuei1878 – 18781O-UMP-tyrosine; transient1 Publication

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.
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, Phosphoprotein

Miscellaneous databases

PMAP-CutDBP09814.

Structurei

Secondary structure

1
3023
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2013 – 20164
Beta strandi2019 – 20268
Beta strandi2029 – 203810
Beta strandi2041 – 20444
Helixi2046 – 20494
Beta strandi2055 – 20606
Beta strandi2063 – 20697
Helixi2070 – 20723
Beta strandi2075 – 20773
Beta strandi2080 – 20823
Beta strandi2084 – 20874
Beta strandi2110 – 21178
Beta strandi2122 – 21309
Beta strandi2138 – 21436
Beta strandi2155 – 21584
Turni2159 – 21613
Beta strandi2164 – 21729
Turni2173 – 21753
Beta strandi2178 – 21825
Helixi2187 – 21915
Helixi2206 – 22083
Beta strandi2754 – 27574

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MMGX-ray1.70A/B2002-2242[»]
C/D2753-2760[»]
ProteinModelPortaliP09814.
SMRiP09814. Positions 2010-2221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1202 – 1354153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1367 – 1532166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2002 – 2218217Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2484 – 2608125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi325 – 3284Involved in interaction with stylet and aphid transmissionBy similarity
Motifi583 – 5853Involved in virions binding and aphid transmissionBy similarity
Motifi1304 – 13074DEFH box
Motifi1856 – 18638Nuclear 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.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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.
IPR014014. RNA_helicase_DEAD_Q_motif.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00270. 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.
PS51195. Q_MOTIF. 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: P09814-1) [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
MAATMIFGSF THDLLGKAMS TIHSAVTAEK DIFSSIKERL ERKRHGKICR
60 70 80 90 100
MKNGSIYIKA ASSTKVEKIN AAAKKLADDK AAFLKAQPTI VDKIIVNEKI
110 120 130 140 150
QVVEAEEVHK REDVQTVFFK KTKKRAPKLR ATCSSSGLDN LYNAVANIAK
160 170 180 190 200
ASSLRVEVIH KKRVCGEFKQ TRFGRALFID VAHAKGHRRR IDCRMHRREQ
210 220 230 240 250
RTMHMFMRKT TKTEVRSKHL RKGDSGIVLL TQKIKGHLSG VRDEFFIVRG
260 270 280 290 300
TCDDSLLEAR ARFSQSITLR ATHFSTGDIF WKGFNASFQE QKAIGLDHTC
310 320 330 340 350
TSDLPVEACG HVAALMCQSL FPCGKITCKR CIANLSNLDF DTFSELQGDR
360 370 380 390 400
AMRILDVMRA RFPSFTHTIR FLHDLFTQRR VTNPNTAAFR EILRLIGDRN
410 420 430 440 450
EAPFAHVNRL NEILLLGSKA NPDSLAKASD SLLELARYLN NRTENIRNGS
460 470 480 490 500
LKHFRNKISS KAHSNLALSC DNQLDQNGNF LWGLAGIAAK RFLNNYFETI
510 520 530 540 550
DPEQGYDKYV IRKNPNGERK LAIGNFIIST NLEKLRDQLE GESIARVGIT
560 570 580 590 600
EECVSRKDGN YRYPCCCVTL EDGSPMYSEL KMPTKNHLVI GNSGDPKYLD
610 620 630 640 650
LPGEISNLMY IAKEGYCYIN IFLAMLVNVD EANAKDFTKR VRDESVQKLG
660 670 680 690 700
KWPSLIDVAT ECALLSTYYP AAASAELPRL LVDHAQKTIH VVDSYGSLNT
710 720 730 740 750
GYHILKANTV SQLEKFASNT LESPMAQYKV GGLVYSENND ASAVKALTQA
760 770 780 790 800
IFRPDVLSEL IEKEPYLMVF ALVSPGILMA MSNSGALEFG ISKWISSDHS
810 820 830 840 850
LVRMASILKT LASKVSVADT LALQKHIMRQ NANFLCGELI NGFQKKKSYT
860 870 880 890 900
HATRFLLMIS EENEMDDPVL NAGYRVLEAS SHEIMEKTYL ALLETSWSDL
910 920 930 940 950
SLYGKFKSIW FTRKHFGRYK AELFPKEQTD LQGRYSNSLR FHYQSTLKRL
960 970 980 990 1000
RNKGSLCRER FLESISSARR RTTCAVFSLL HKAFPDVLKF INTLVIVSLS
1010 1020 1030 1040 1050
MQIYYMLVAI IHEHRAAKIK SAQLEERVLE DKTMLLYDDF KAKLPEGSFE
1060 1070 1080 1090 1100
EFLEYTRQRD KEVYEYLMME TTEIVEFQAK NTGQASLERI IAFVSLTLML
1110 1120 1130 1140 1150
FDNERSDCVY KILTKFKGIL GSVENNVRFQ SLDTIVPTQE EKNMVIDFEL
1160 1170 1180 1190 1200
DSDTAHTPQM QEQTFSDWWS NQIANNRVVP HYRTEGYFMQ FTRNTASAVS
1210 1220 1230 1240 1250
HQIAHNEHKD IILMGAVGSG KSTGLPTNLC KFGGVLLLEP TRPLAENVTK
1260 1270 1280 1290 1300
QMRGSPFFAS PTLRMRNLST FGSSPITVMT TGFALHFFAN NVKEFDRYQF
1310 1320 1330 1340 1350
IIFDEFHVLD SNAIAFRNLC HEYSYNGKII KVSATPPGRE CDLTTQYPVE
1360 1370 1380 1390 1400
LLIEEQLSLR DFVDAQGTDA HADVVKKGDN ILVYVASYNE VDQLSKMLNE
1410 1420 1430 1440 1450
RGFLVTKVDG RTMKLGGVEI ITKGSSIKKH FIVATNIIEN GVTLDVDVVV
1460 1470 1480 1490 1500
DFGLKVVPNL DSDNRLVSYC KIPISLGERI QRFGRVGRNK PGVALRIGET
1510 1520 1530 1540 1550
IKGLVEIPSM IATEAAFLCF VYGLPVTTQN VSTSILSQVS VRQARVMCQF
1560 1570 1580 1590 1600
ELPIFYTAHL VRYDGAMHPA IHNALKRFKL RDSEINLNTL AIPTSSSKTW
1610 1620 1630 1640 1650
YTGKCYKQLV GRLDIPDEIK IPFYTKEVPE KVPEQIWDVM VKFSSDAGFG
1660 1670 1680 1690 1700
RMTSAAACKV AYTLQTDIHS IQRTVQIIDR LLENEMKKRN HFNLVVNQSC
1710 1720 1730 1740 1750
SSHFMSLSSI MASLRAHYAK NHTGQNIEIL QKAKAQLLEF SNLAIDPSTT
1760 1770 1780 1790 1800
EALRDFGYLE AVRFQSESEM ARGLKLSGHW KWSLISRDLI VVSGVGIGLG
1810 1820 1830 1840 1850
CMLWQFFKEK MHEPVKFQGK SRRRLQFRKA RDDKMGYIMH GEGDTIEHFF
1860 1870 1880 1890 1900
GAAYTKKGKS KGKTHGAGTK AHKFVNMYGV SPDEYSYVRY LDPVTGATLD
1910 1920 1930 1940 1950
ESPMTDLNIV QEHFGEIRRE AILADAMSPQ QRNKGIQAYF VRNSTMPILK
1960 1970 1980 1990 2000
VDLTPHIPLK VCESNNIAGF PEREGELRRT GPTETLPFDA LPPEKQEVAF
2010 2020 2030 2040 2050
ESKALLKGVR DFNPISACVW LLENSSDGHS ERLFGIGFGP YIIANQHLFR
2060 2070 2080 2090 2100
RNNGELTIKT MHGEFKVKNS TQLQMKPVEG RDIIVIKMAK DFPPFPQKLK
2110 2120 2130 2140 2150
FRQPTIKDRV CMVSTNFQQK SVSSLVSESS HIVHKEDTSF WQHWITTKDG
2160 2170 2180 2190 2200
QCGSPLVSII DGNILGIHSL THTTNGSNYF VEFPEKFVAT YLDAADGWCK
2210 2220 2230 2240 2250
NWKFNADKIS WGSFTLVEDA PEDDFMAKKT VAAIMDDLVR TQGEKRKWML
2260 2270 2280 2290 2300
EAAHTNIQPV AHLQSQLVTK HIVKGRCKMF ALYLQENADA RDFFKSFMGA
2310 2320 2330 2340 2350
YGPSHLNKEA YIKDIMKYSK QIVVGSVDCD TFESSLKVLS RKMKEWGFEN
2360 2370 2380 2390 2400
LEYVTDEQTI KNALNMDAAV GALYSGKKKQ YFEDLSDDAV ANLVQKSCLR
2410 2420 2430 2440 2450
LFKNKLGVWN GSLKAELRPF EKLIENKTRT FTAAPIETLL GGKVCVDDFN
2460 2470 2480 2490 2500
NHFYSKHIQC PWSVGMTKFY GGWNELLGKL PDGWVYCDAD GSQFDSSLSP
2510 2520 2530 2540 2550
YLINAVLRLR LSSMEEWDVG QKMLQNLYTE IVYTPISTPD GTIVKKFKGN
2560 2570 2580 2590 2600
NSGQPSTVVD NTLMVVLAMY YALSKLGVDI NSQEDVCKFF ANGDDLIIAI
2610 2620 2630 2640 2650
SPELEHVLDG FQQHFSDLGL NYDFSSRTRD KKELWFMSHR ALSKDGILIP
2660 2670 2680 2690 2700
KLEPERIVSI LEWDRSAEPH HRLEAICASM IEAWGYTDLL QNIRRFYKWT
2710 2720 2730 2740 2750
IEQEPYRSLA EQGLAPYLSE VALRRLYTSQ IATDNELTDY YKEILANNEF
2760 2770 2780 2790 2800
LRETVRFQSD TVDAGKDKAR DQKLADKPTL AIDRTKDKDV NTGTSGTFSI
2810 2820 2830 2840 2850
PRLKKAAMNM KLPKVGGSSV VNLDHLLTYK PAQEFVVNTR ATHSQFKAWH
2860 2870 2880 2890 2900
TNVMAELELN EEQMKIVLNG FMIWCIENGT SPNISGVWTM MDGDEQVEYP
2910 2920 2930 2940 2950
IEPMVKHANP SLRQIMKHFS NLAEAYIRMR NSEQVYIPRY GLQRGLVDRN
2960 2970 2980 2990 3000
LAPFAFDFFE VNGATPVRAR EAHAQMKAAA LRNSQQRMFC LDGSVSGQEE
3010 3020
NTERHTVDDV NAQMHHLLGV KGV

Note: Produced by conventional translation.

Length:3,023
Mass (Da):342,285
Last modified:May 30, 2000 - v2
Checksum:i299FDED15C0E5B87
GO
Isoform P3N-PIPO polyprotein (identifier: P0CK10-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P0CK10.
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:977
Mass (Da):109,980
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04083 Genomic RNA. Translation: CAA27720.1.
PIRiA23647. GNVSTV.
RefSeqiNP_056867.1. NC_001768.1. [P09814-1]

Genome annotation databases

GeneIDi1494056.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04083 Genomic RNA. Translation: CAA27720.1 .
PIRi A23647. GNVSTV.
RefSeqi NP_056867.1. NC_001768.1. [P09814-1 ]

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MMG X-ray 1.70 A/B 2002-2242 [» ]
C/D 2753-2760 [» ]
ProteinModelPortali P09814.
SMRi P09814. Positions 2010-2221.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C04.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1494056.

Miscellaneous databases

PMAP-CutDB P09814.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
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.
IPR014014. RNA_helicase_DEAD_Q_motif.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00270. 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.
PS51195. Q_MOTIF. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Shaw J.G.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "A tyrosine residue in the small nuclear inclusion protein of tobacco vein mottling virus links the VPg to the viral RNA."
    Murphy J.F., Rychlik W., Rhoads R.E., Hunt A.G., Shaw J.G.
    J. Virol. 65:511-513(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1874-1888, COVALENT RNA-LINKAGE AT TYR-1878 OF VPG, URIDYLYLATION AT TYR-1878.
  4. Cited for: REVIEW.

Entry informationi

Entry nameiPOLG_TVMV
AccessioniPrimary (citable) accession number: P09814
Secondary accession number(s): Q84898
, Q84899, Q84900, Q84901, Q84902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

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