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Protein

Genome polyprotein

Gene
N/A
Organism
Turnip mosaic virus (strain Quebec) (TuMV)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity
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 sitei270 – 2701For P1 proteinase activityBy similarity
Active sitei279 – 2791For P1 proteinase activitySequence analysis
Active sitei313 – 3131For P1 proteinase activityBy similarity
Active sitei706 – 7061For helper component proteinase activityPROSITE-ProRule annotation
Active sitei779 – 7791For helper component proteinase activityPROSITE-ProRule annotation
Active sitei2161 – 21611For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2196 – 21961For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2266 – 22661For nuclear inclusion protein A activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1313 – 13208ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

MEROPSiC04.001.

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
OrganismiTurnip mosaic virus (strain Quebec) (TuMV)
Taxonomic identifieri36396 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiAlliaria [TaxID: 126269]
Brassica [TaxID: 3705]
Calanthe [TaxID: 38206]
Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris) [TaxID: 3719]
Hesperis matronalis [TaxID: 264418]
Stellaria media (Common chickweed) (Alsine media) [TaxID: 13274]
Trifolium hybridum (Alsike clover) [TaxID: 74517]
Proteomesi
  • UP000008263 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31633163Genome polyproteinPRO_0000420030Add
BLAST
Chaini1 – 362362P1 proteinaseSequence analysisPRO_0000040473Add
BLAST
Chaini363 – 820458Helper component proteinaseSequence analysisPRO_0000040474Add
BLAST
Chaini821 – 1175355Protein P3By similarityPRO_0000040475Add
BLAST
Chaini1176 – 1227526 kDa protein 1By similarityPRO_0000040476Add
BLAST
Chaini1228 – 1870643Cytoplasmic inclusion proteinBy similarityPRO_0000040477Add
BLAST
Chaini1871 – 1923536 kDa protein 2By similarityPRO_0000040478Add
BLAST
Chaini1924 – 2115192Viral genome-linked proteinBy similarityPRO_0000040479Add
BLAST
Chaini2116 – 2358243Nuclear inclusion protein ABy similarityPRO_0000040480Add
BLAST
Chaini2359 – 2875517Nuclear inclusion protein BBy similarityPRO_0000040481Add
BLAST
Chaini2876 – 3163288Capsid proteinBy similarityPRO_0000040482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1986 – 19861O-(5'-phospho-RNA)-tyrosineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei362 – 3632Cleavage; by P1 proteinaseSequence analysis
Sitei820 – 8212Cleavage; by autolysisPROSITE-ProRule annotation
Sitei1175 – 11762Cleavage; by NIa-proBy similarity
Sitei1227 – 12282Cleavage; by NIa-proBy similarity
Sitei1870 – 18712Cleavage; by NIa-proBy similarity
Sitei2115 – 21162Cleavage; by NIa-proBy similarity
Sitei2358 – 23592Cleavage; by NIa-proBy similarity
Sitei2875 – 28762Cleavage; by NIa-proBy similarity

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Structurei

3D structure databases

DisProtiDP00560.
ProteinModelPortaliQ02597.
SMRiQ02597. Positions 2124-2337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini698 – 820123Peptidase C6PROSITE-ProRule annotationAdd
BLAST
Domaini1300 – 1452153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1471 – 1630160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2116 – 2334219Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2600 – 2724125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4174Involved in interaction with stylet and aphid transmissionBy similarity
Motifi672 – 6743Involved in virions binding and aphid transmissionBy similarity
Motifi1402 – 14054DECH box
Motifi1964 – 19718Nuclear 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.PROSITE-ProRule annotationCurated
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.
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.
IPR013648. PP_Potyviridae.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[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.
PROSITEiPS51744. HC_PRO_CPD. 1 hit.
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]

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: Q02597-1) [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
MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK
60 70 80 90 100
LYTVRFGSLD PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS
110 120 130 140 150
SAVLRMHEEA NKERALFLDW EASLKRRSYG IAENEKVVMT TRGVSKIVPR
160 170 180 190 200
SSRAMKQKRA RERRRAQQPI ILKWEPKLSG FSIGGGFSAS AIEAEEVRTK
210 220 230 240 250
WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS ANIEYIGKKP
260 270 280 290 300
IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG
310 320 330 340 350
TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK
360 370 380 390 400
ITKTMSLKIV HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE
410 420 430 440 450
VAALMCLAMF PCGKITCPDC VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS
460 470 480 490 500
YPRFKHAVQI LDRYEQSLSS ANENYQDFAE IQSISDGVEK AAFPHVNKLN
510 520 530 540 550
AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL KSFRNKVSQK
560 570 580 590 600
AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
610 620 630 640 650
RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF
660 670 680 690 700
VHACCCVTTE SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI
710 720 730 740 750
AKEGYCYINI FLAMLVNVKE SQAKEFTKVV RDKLVSELGK WPTLLDVATA
760 770 780 790 800
CYFLKVFYPD VANAELPRML VDHKTKIIHV VDSYGSLSTG YHVLKTNTVE
810 820 830 840 850
QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI KRLVKGVYRP
860 870 880 890 900
KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL
910 920 930 940 950
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN
960 970 980 990 1000
RFMGMLLHMA EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWS
1010 1020 1030 1040 1050
ERCVIRYYPS KQAIFTQKDL PMQSEADLGG RYSESVISSY EWSKQQAKGV
1060 1070 1080 1090 1100
KDSVVNKLRS SMSWTSSKVS NSVCRTINYL VPDVFKFMNV LVCISLLIKM
1110 1120 1130 1140 1150
TAEANHIITT QRRLKLDIEE TERKKIEWEL AFHHNILTHS ASQHPTLDEF
1160 1170 1180 1190 1200
TAYIAEKAPH LSEHIEPEEK EVVHQAKRQS EQELERVIAF VALVLMMFDA
1210 1220 1230 1240 1250
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN EIEDDLNERN LFVDFELSSD
1260 1270 1280 1290 1300
SEMLQQLPAE KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK
1310 1320 1330 1340 1350
IAHESDKDIL LMGAVGSGKS TGLPYHLSRK GNVLLLEPTR PLAENVHKQL
1360 1370 1380 1390 1400
SQAPFHQNTT LRMRGLTAFG SAPISVMTSG FALNYFANNR SRIEEFDFVI
1410 1420 1430 1440 1450
FDECHVHDAN AMAMRCLIHE CDYSGKIIKV SATPPGREVE FSTQYPVSIS
1460 1470 1480 1490 1500
TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD
1510 1520 1530 1540 1550
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF
1560 1570 1580 1590 1600
GTKVLPYLDT DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTER
1610 1620 1630 1640 1650
GLSEVPSCIA TEAALKCFTY GLPVITNNVS TSILGNVTVK QARTMSVFEI
1660 1670 1680 1690 1700
TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD SEIVLTKLAI PNRGVNAGSQ
1710 1720 1730 1740 1750
PVSMHDSVQM LKIGVTLRIP FMCRDIPEKL HLDMWDVVVK FKGDAGFGRL
1760 1770 1780 1790 1800
SSSASKVAYT LQTDVNSIQR TVTIIDTLIA EERRKQEYFK TVTSNCVSSS
1810 1820 1830 1840 1850
NFSLQSITNA IKSRMMKDHP CENISVLEGA KSQLLEFRNL NSDHSFVTKT
1860 1870 1880 1890 1900
DGISRSFMRD YGALEAVNHQ STNEMSKFLQ LKGKWNKTLI TRDVLVICGV
1910 1920 1930 1940 1950
LGGGVWMVVQ HFRSKVSEPV THEAKGKKQR QKLKFRNARD NKMGREVYGD
1960 1970 1980 1990 2000
DDTIEHFFGD AYTKKGKSKG RTRGIGHKNR KFINMYGFDP EDFSAVRFVD
2010 2020 2030 2040 2050
PLTGATLDDN PFTDITLVQK HFGDIRMDLL GEDELDSNEI RMNKTIQAYY
2060 2070 2080 2090 2100
MNNKTGKALK VDLTPHIPLK VCDLHATIAG FPERENELRQ TGKAQPINID
2110 2120 2130 2140 2150
EVPRANNELV PVDHESNSMF RGLRDYNPIS NNICHLTNVS DGASNSLYGV
2160 2170 2180 2190 2200
GFGPLILTNR HLFERNNGEL IIKSRHGEFV IKNTTQLHLL PIPDRDLLLI
2210 2220 2230 2240 2250
RLPKDVPPFP QKLGFRQPEK GERICMVGSN FQTKSITSIV SETSTIMPVE
2260 2270 2280 2290 2300
NSQFWKHWIS TKDGQCGSPM VSTKDGKILG LHSLANFQNS INYFAAFPDD
2310 2320 2330 2340 2350
FTEKYLHTIE AHEWVKHWKY NTSAISWGSL NIQASQPVSL FKVSKLISDL
2360 2370 2380 2390 2400
DSTAVYAQTQ QNRWMFEQLT GNLKAIAHCP SQLVTKHTVK GKCQMFDLYL
2410 2420 2430 2440 2450
KLHDEAREYF QPMLGQYQKS KLNREAYAKD LLKYATPIEA GNIDCDLFEK
2460 2470 2480 2490 2500
TVEIVISDLR GYGFETCNYV TDENDIFEAL NMKSAVGALY KGKKKDYFAE
2510 2520 2530 2540 2550
FTPEVKEEIL KQSCERLFLG KMGVWNGSLK AELRPLEKVE ANKTRTFTAA
2560 2570 2580 2590 2600
PLDTLLGGKV CVDDFNNQFY DHNLRAPWDV GMTKFYCGWD RLLESLPDGW
2610 2620 2630 2640 2650
VYCDADGSQF DSSLSPYLIN AVLNIRLGFM EEWDVGEVML RNLYTEIVYT
2660 2670 2680 2690 2700
PISTPDGTLV KKFKGNNSGQ PSTVVDNTLM VILAVNYSLK KGGIPSELRD
2710 2720 2730 2740 2750
SIIRFFVNGD DLLLSVHPEY EYILDTMADN FRELGLKYTF DSRTREKGDL
2760 2770 2780 2790 2800
WFMSHQGHRR EGIWIPKLEP ERIVSILEWD RSKEPCHRLE AICAAMIESW
2810 2820 2830 2840 2850
GYDKLTHEIR KFYAWMIEQA PFSSLAQEGK APYIAETALR KLYLDKEPAQ
2860 2870 2880 2890 2900
EDLTQYLQAI FEDYEDGVEA CVYHQAGETL DADLTEEQKQ AEKEKKEREK
2910 2920 2930 2940 2950
AEKERERQKQ LAFKKGKDVA QEEGKRDKEV NAGTSGTFSV PRLKSLTSKM
2960 2970 2980 2990 3000
RVPRYEKRVA LNLDHLILYT PEQTDLSNTR STRKQFDTWF EGVMADYELT
3010 3020 3030 3040 3050
EDKMQIILNG LRVWCIENGT SPNINGMWVM MDGDDQVEFP IKPLIDHAKP
3060 3070 3080 3090 3100
TFRQIMAHFS DVAEAYIEKR NQDRPYMPRY GLQRNLTDMS LARYAFDFYE
3110 3120 3130 3140 3150
MTSRTPIRAR EAHIQMKAAA LRGANNNLFG LDGNVGTTVE NTERHTTEDV
3160
NRNMHNLLGV QGL
Note: Produced by conventional translation.
Length:3,163
Mass (Da):357,822
Last modified:June 1, 1994 - v2
Checksum:i61B0F73B58DF6D59
GO
Isoform P3N-PIPO polyprotein (identifier: P0CK12-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P0CK12.
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:1,052
Mass (Da):117,956
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2862 – 28621E → G in BAA01452 (PubMed:2254757).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10927 Genomic RNA. Translation: BAA01725.1.
D10601 Genomic RNA. Translation: BAA01452.1.
PIRiJQ1895.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10927 Genomic RNA. Translation: BAA01725.1.
D10601 Genomic RNA. Translation: BAA01452.1.
PIRiJQ1895.

3D structure databases

DisProtiDP00560.
ProteinModelPortaliQ02597.
SMRiQ02597. Positions 2124-2337.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC04.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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.
IPR013648. PP_Potyviridae.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[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.
PROSITEiPS51744. HC_PRO_CPD. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

  1. "The complete nucleotide sequence of turnip mosaic potyvirus RNA."
    Nicolas O., Laliberte J.F.
    J. Gen. Virol. 73:2785-2793(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Sequence of the 3'-terminal region of turnip mosaic virus RNA and the capsid protein gene."
    Tremblay M.F., Nicolas O., Sinha R., Lazure C., Laliberte J.F.
    J. Gen. Virol. 71:2769-2772(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1534-3163, PARTIAL PROTEIN SEQUENCE.
  3. Cited for: REVIEW.

Entry informationi

Entry nameiPOLG_TUMVQ
AccessioniPrimary (citable) accession number: Q02597
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 1, 1994
Last modified: October 14, 2015
This is version 133 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

Complete proteome, Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.