DP00560: Genome polyprotein [Isoform Genome polyprotein]FASTA viewXML view

General information
DisProt:DP00560
Name:Genome polyprotein [Isoform Genome polyprotein]
Synonym(s):POLG_TUMVQ
1. P1 proteinase [cleavage product 1]
N-terminal protein
2. Helper component proteinase [cleavage product 2]
HC-pro
3. Protein P3 [cleavage product 3]
4. 6 kDa protein 1 [cleavage product 4]
6K1
5. Cytoplasmic inclusion protein [cleavage product 5]
CI
6. 6 kDa protein 2 [cleavage product 6]
6K2
7. Viral genome-linked protein [cleavage product 7]
VPg
8. Nuclear inclusion protein A [cleavage product 8]
NI-a or NIa or NIa-pro
49 kDa proteinase or 49 kDa-Pro
9. Nuclear inclusion protein B [cleavage product 9]
NI-b or NIb
RNA-directed RNA polymerase
10. Coat protein [cleavage product 10]
CP
First appeared in release:Release 5.4 (10/14/2010)
UniProt:Q02597
UniGene: 
SwissProt: POLG_TUMVQ
TrEMBL:  
NCBI (GI):  
Source organism:Turnip mosaic virus (strain Quebec) (TuMV)
Sequence length:3163
Percent disordered:-1%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK LYTVRFGSLD - 60
PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS SAVLRMHEEA NKERALFLDW - 120
EASLKRRSYG IAENEKVVMT TRGVSKIVPR SSRAMKQKRA RERRRAQQPI ILKWEPKLSG - 180
FSIGGGFSAS AIEAEEVRTK WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS - 240
ANIEYIGKKP IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG - 300
TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK ITKTMSLKIV - 360
HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC - 420
VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE - 480
IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL - 540
KSFRNKVSQK AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET - 600
RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF VHACCCVTTE - 660
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE - 720
SQAKEFTKVV RDKLVSELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV - 780
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI - 840
KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL - 900
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN RFMGMLLHMA - 960
EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWS ERCVIRYYPS KQAIFTQKDL - 1020
PMQSEADLGG RYSESVISSY EWSKQQAKGV KDSVVNKLRS SMSWTSSKVS NSVCRTINYL - 1080
VPDVFKFMNV LVCISLLIKM TAEANHIITT QRRLKLDIEE TERKKIEWEL AFHHNILTHS - 1140
ASQHPTLDEF TAYIAEKAPH LSEHIEPEEK EVVHQAKRQS EQELERVIAF VALVLMMFDA - 1200
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN EIEDDLNERN LFVDFELSSD SEMLQQLPAE - 1260
KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDKDIL LMGAVGSGKS - 1320
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG - 1380
FALNYFANNR SRIEEFDFVI FDECHVHDAN AMAMRCLIHE CDYSGKIIKV SATPPGREVE - 1440
FSTQYPVSIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD - 1500
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT - 1560
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTER GLSEVPSCIA TEAALKCFTY - 1620
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD - 1680
SEIVLTKLAI PNRGVNAGSQ PVSMHDSVQM LKIGVTLRIP FMCRDIPEKL HLDMWDVVVK - 1740
FKGDAGFGRL SSSASKVAYT LQTDVNSIQR TVTIIDTLIA EERRKQEYFK TVTSNCVSSS - 1800
NFSLQSITNA IKSRMMKDHP CENISVLEGA KSQLLEFRNL NSDHSFVTKT DGISRSFMRD - 1860
YGALEAVNHQ STNEMSKFLQ LKGKWNKTLI TRDVLVICGV LGGGVWMVVQ HFRSKVSEPV - 1920
THEAKGKKQR QKLKFRNARD NKMGREVYGD DDTIEHFFGD AYTKKGKSKG RTRGIGHKNR - 1980
KFINMYGFDP EDFSAVRFVD PLTGATLDDN PFTDITLVQK HFGDIRMDLL GEDELDSNEI - 2040
RMNKTIQAYY MNNKTGKALK VDLTPHIPLK VCDLHATIAG FPERENELRQ TGKAQPINID - 2100
EVPRANNELV PVDHESNSMF RGLRDYNPIS NNICHLTNVS DGASNSLYGV GFGPLILTNR - 2160
HLFERNNGEL IIKSRHGEFV IKNTTQLHLL PIPDRDLLLI RLPKDVPPFP QKLGFRQPEK - 2220
GERICMVGSN FQTKSITSIV SETSTIMPVE NSQFWKHWIS TKDGQCGSPM VSTKDGKILG - 2280
LHSLANFQNS INYFAAFPDD FTEKYLHTIE AHEWVKHWKY NTSAISWGSL NIQASQPVSL - 2340
FKVSKLISDL DSTAVYAQTQ QNRWMFEQLT GNLKAIAHCP SQLVTKHTVK GKCQMFDLYL - 2400
KLHDEAREYF QPMLGQYQKS KLNREAYAKD LLKYATPIEA GNIDCDLFEK TVEIVISDLR - 2460
GYGFETCNYV TDENDIFEAL NMKSAVGALY KGKKKDYFAE FTPEVKEEIL KQSCERLFLG - 2520
KMGVWNGSLK AELRPLEKVE ANKTRTFTAA PLDTLLGGKV CVDDFNNQFY DHNLRAPWDV - 2580
GMTKFYCGWD RLLESLPDGW VYCDADGSQF DSSLSPYLIN AVLNIRLGFM EEWDVGEVML - 2640
RNLYTEIVYT PISTPDGTLV KKFKGNNSGQ PSTVVDNTLM VILAVNYSLK KGGIPSELRD - 2700
SIIRFFVNGD DLLLSVHPEY EYILDTMADN FRELGLKYTF DSRTREKGDL WFMSHQGHRR - 2760
EGIWIPKLEP ERIVSILEWD RSKEPCHRLE AICAAMIESW GYDKLTHEIR KFYAWMIEQA - 2820
PFSSLAQEGK APYIAETALR KLYLDKEPAQ EDLTQYLQAI FEDYEDGVEA CVYHQAGETL - 2880
DADLTEEQKQ AEKEKKEREK AEKERERQKQ LAFKKGKDVA QEEGKRDKEV NAGTSGTFSV - 2940
PRLKSLTSKM RVPRYEKRVA LNLDHLILYT PEQTDLSNTR STRKQFDTWF EGVMADYELT - 3000
EDKMQIILNG LRVWCIENGT SPNINGMWVM MDGDDQVEFP IKPLIDHAKP TFRQIMAHFS - 3060
DVAEAYIEKR NQDRPYMPRY GLQRNLTDMS LARYAFDFYE MTSRTPIRAR EAHIQMKAAA - 3120
LRGANNNLFG LDGNVGTTVE NTERHTTEDV NRNMHNLLGV QGL



Functional narrative    

Function: Capsid protein is involved in aphid transmission, cell- to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
Function: Nuclear inclusion protein B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Function: Helper component proteinase is required for aphid transmission and also has proteolytic activity. 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).
Function: Cytoplasmic inclusion protein has helicase activity. It may be involved in replication (By similarity).
Function: Both 6K peptides are indispensable for virus replication (By similarity).
Function: Nuclear inclusion protein A has RNA-binding and proteolytic activities.
CATALYTIC ACTIVITY: 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.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: 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.


Subcellular Location: Capsid protein: Virion (Potential). Event=Ribosomal frameshifting; Named isoforms=2; Comment=Knockout of PIPO ORF is lethal for the virus. Because of a common N-terminus, some results depicted for the genome polyprotein might belong to the PIPO isoform; Name=Genome polyprotein; IsoId=Q02597-1; Sequence=Displayed; Note=Produced by conventional translation; Name=PIPO; Synonyms=Pretty interesting potyviridae ORF; IsoId=Q02597-2; Sequence=VSP_034776, VSP_034777; Note=Produced by ribosomal frameshifting;
DOMAIN: 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.
PTM: 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).
PTM: The viral RNA of potyviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten 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).
SIMILARITY: Belongs to the potyviruses polyprotein family.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
SIMILARITY: Contains 1 peptidase C4 domain.
SIMILARITY: Contains 1 peptidase C6 domain.
SIMILARITY: Contains 1 peptidase S30 domain.
SIMILARITY: Contains 1 RdRp catalytic domain.
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Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Comments


Previous entry DP00560 has been split into polyprotein (DP00560) and cleavage product (DP00560_C007).


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