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UniProtKB/Swiss-Prot entry P31999

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name POLG_LMV0
Primary accession number P31999
Secondary accession number P90263
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on June 6, 2002 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name Genome polyprotein
Synonyms None
Contains P1 proteinase
     (N-terminal protein)
Helper component proteinase
     (HC-pro)
     (EC 3.4.22.45)
Protein P3
6 kDa protein 1
     (6K1)
Cytoplasmic inclusion protein
     (CI)
     (EC 3.6.1.-)
6 kDa protein 2
     (6K2)
Viral genome-linked protein
     (VPg)
Nuclear inclusion protein A
     (NI-a)
     (NIa)
     (EC 3.4.22.44)
     (NIa-pro)
     (49 kDa proteinase)
     (49 kDa-Pro)
Nuclear inclusion protein B
     (NI-b)
     (NIb)
     (EC 2.7.7.48)
     (RNA-directed RNA polymerase)
Coat protein
     (CP)
Gene name None
From
Lettuce mosaic virus (strain 0 / isolate French) (LMV) [TaxID: 117131] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Potyviridae; Potyvirus.
Virus hosts Cicer arietinum (Chickpea) (Garbanzo) [TaxID: 3827]
Lactuca [TaxID: 4235]
Pisum sativum (Garden pea) [TaxID: 3888]
Senecio vulgaris (Common groundsel) [TaxID: 76276]
Sonchus [TaxID: 50190]
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0168-1702(96)01411-6; PubMed=9085548 [NCBI, ExPASy, EBI, Israel, Japan]
Revers F., Yang S.J., Walter J., Souche S., Lot H., Le Gall O., Candresse T., Dunez J.;
"Comparison of the complete nucleotide sequences of two isolates of lettuce mosaic virus differing in their biological properties.";
Virus Res. 47:167-177(1997).
[2]
 SEQUENCE REVISION TO 1750 AND 1771.
Le Gall O.;
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2776-3255.
DOI=10.1007/BF01319245; PubMed=2001176 [NCBI, ExPASy, EBI, Israel, Japan]
Dinant S., Lot H., Albouy J., Kuziak C., Meyer M., Astier-Manifacier S.;
"Nucleotide sequence of the 3' terminal region of lettuce mosaic potyvirus RNA shows a Gln/Val dipeptide at the cleavage site between the polymerase and the coat protein.";
Arch. Virol. 116:235-252(1991).
[4]
 REVIEW.
DOI=10.1016/S0168-1702(01)00220-9; PubMed=11226583 [NCBI, ExPASy, EBI, Israel, Japan]
Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
"Potyvirus proteins: a wealth of functions.";
Virus Res. 74:157-175(2001).
Comments
  • FUNCTION: Coat 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.
  • 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: Coat protein: Virion (Potential).
  • 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 covalently linked to the genomic RNA (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 [view classification].
  • SIMILARITY: Contains 1 peptidase C6 domain [view classification].
  • SIMILARITY: Contains 1 peptidase S30 domain [view classification].
  • SIMILARITY: Contains 1 RdRp catalytic domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X97704; CAA66280.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65652; CAA46602.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S70859; S70859.
3D structure databases
HSSP P04517; 1LVM. [HSSP ENTRY / PDB]
ModBase P31999.
Protein family/group databases
MEROPS C06.001; -.
Ontologies
GO
GO:0019028; Cellular component: viral capsid (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008026; Molecular function: ATP-dependent helicase activity (inferred from electronic annotation from InterPro).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0003968; Molecular function: RNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0018144; Biological process: RNA-protein covalent cross-linking (inferred from electronic annotation from UniProtKB-KW).
GO:0006410; Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0019079; Biological process: viral genome replication (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR014001; DEAD-like_N.
IPR001650; DNA/RNA_helicase_C.
IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR002540; Pept_S30_P1_potyvir.
IPR001730; Peptidase_C4.
IPR001456; Peptidase_C6.
IPR001592; Poty_coat.
IPR013648; PP_Potyviridae.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.
Pfam PF00270; DEAD; 1.
PF00271; Helicase_C; 1.
PF00863; Peptidase_C4; 1.
PF00851; Peptidase_C6; 1.
PF01577; Peptidase_S30; 1.
PF00767; Poty_coat; 1.
PF08440; Poty_PP; 1.
PF00680; RdRP_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00966; NIAPOTYPTASE.
SMART SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.
PROSITE PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P31999.
ProtoNet P31999.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Helicase; Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-directed RNA polymerase; Suppressor of RNA silencing; Thiol protease; Transferase; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1    437  437     P1 proteinase (Potential). PRO_0000040269
CHAIN   438    895  458     Helper component proteinase (Potential). PRO_0000040270
CHAIN   896   1273  378     Protein P3 (By similarity). PRO_0000040271
CHAIN   1274   1325  52     6 kDa protein 1 (By similarity). PRO_0000040272
CHAIN   1326   1968  643     Cytoplasmic inclusion protein (By similarity). PRO_0000040273
CHAIN   1969   2021  53     6 kDa protein 2 (By similarity). PRO_0000040274
CHAIN   2022   2214  193     Viral genome-linked protein (By similarity). PRO_0000040275
CHAIN   2215   2457  243     Nuclear inclusion protein A (By similarity). PRO_0000040276
CHAIN   2458   2977  520     Nuclear inclusion protein B (By similarity). PRO_0000040277
CHAIN   2978   3255  278     Coat protein (By similarity). PRO_0000040278
DOMAIN   1397   1549  153     Helicase ATP-binding. 
DOMAIN   1568   1727  160     Helicase C-terminal. 
DOMAIN   2699   2823  125     RdRp catalytic. 
NP_BIND   1410   1417  8     ATP (Potential). 
MOTIF   489    492  4     Involved in interaction with stylet and aphid transmission (By similarity). 
MOTIF   747    749  3     Involved in virions binding and aphid transmission (By similarity). 
MOTIF   1499   1502  4     DECH box. 
MOTIF   2062   2069  8     Nuclear localization signal (Potential). 
COMPBIAS   1266   1271  6     Poly-Glu. 
COMPBIAS   2965   2972  8     Poly-Asp. 
ACT_SITE   345    345        For P1 proteinase activity (By similarity). 
ACT_SITE   354    354        For P1 proteinase activity (Potential). 
ACT_SITE   388    388        For P1 proteinase activity (By similarity). 
ACT_SITE   781    781        For helper component proteinase activity (By similarity). 
ACT_SITE   854    854        For helper component proteinase activity (By similarity). 
ACT_SITE   2260   2260        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2295   2295        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2365   2365        For nuclear inclusion protein A activity (By similarity). 
SITE   437    438  2     Cleavage; by P1 proteinase (Potential). 
SITE   895    896  2     Cleavage; by HC-pro (Potential). 
SITE   1273   1274  2     Cleavage; by NIa-pro (By similarity). 
SITE   1325   1326  2     Cleavage; by NIa-pro (By similarity). 
SITE   1968   1969  2     Cleavage; by NIa-pro (By similarity). 
SITE   2021   2022  2     Cleavage; by NIa-pro (By similarity). 
SITE   2214   2215  2     Cleavage; by NIa-pro (By similarity). 
SITE   2457   2458  2     Cleavage; by NIa-pro (By similarity). 
SITE   2977   2978  2     Cleavage; by NIa-pro (By similarity). 
MOD_RES   2084   2084        O-(5'-phospho-RNA)-tyrosine (By similarity). 
Sequence information
Length: 3255 AA [This is the length of the unprocessed precursor] Molecular weight: 367571 Da [This is the MW of the unprocessed precursor] CRC64: 763F676F95876A12 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATLDNCTQV HHMFAYNREH GTNYTRNHFR RYLAAQRIGF YYDWDDDVYE CPTCEAIYHS 

        70         80         90        100        110        120 
LDDIKNWHEC DPPAFDLNDF ITDARLKSAP VPDLGPVIIE IPKAEEKQEL NFFAATPAPE 

       130        140        150        160        170        180 
VSQWKCRGLQ FGSFTELETS EPVASAPEPK CEEPARTIAK PEESVEQETR GDGKRLLQAQ 

       190        200        210        220        230        240 
MEVDKAEQDL AFACLNASLK PRLEGRTTAT IARRRDGCLV YKTKPSWSQR RRAKKTLKVD 

       250        260        270        280        290        300 
TLACENPYIP AIVDKISIAG GSSASVMHEQ QKPKTLHTTP SRKVATHYKR TVMNQQTLMA 

       310        320        330        340        350        360 
FINQVGTILL NAEKEFEVVG CRKQKVTGKG TRHNGVRLVK LKTAHEEGHR RRVDIRIPNG 

       370        380        390        400        410        420 
LRPIVMRISA RGGWHRTWTD SELSPGSSGY VLNSSKIIGK FGLRRHSIFV VRGRVDGEVI 

       430        440        450        460        470        480 
DSQSKVTHSI THRMVQYSDV ARNFWNGYST CFMHNTPKDI LHTCTSDFDV KECGTVAALL 

       490        500        510        520        530        540 
TQTLFQFGKI TCEKCAIEYK NLTRDELATR VNKEIDGTII SIQTQHPRFV HVLNFLRLIK 

       550        560        570        580        590        600 
QVLNAKNGNF GAFQETERII GDRMDAPFSH VNKLNAIVIK GNQATSDEMA QASNHVLEIA 

       610        620        630        640        650        660 
RYLKNRTENI QKGSLKSFRN KISGKAHLNP SLMCDNQLDK NGGFEWGQRS YHAKRFFDGY 

       670        680        690        700        710        720 
FETIDPSDGY SKYTIRRNPN GHRKLAIGNL IVSTNFESHR RSMIGESIED PGLTNQCVSK 

       730        740        750        760        770        780 
EGDTFIYPCC CVTDEYGKPT LSEIKMPTKH HLVLGNAGDP KYVDLPKEAE GKMFVTKDGY 

       790        800        810        820        830        840 
CYINIFLAML VDVPEDQAKD FTKMAREIAV KQLGEWPSMM DVATACNILA TFHPDTRRSE 

       850        860        870        880        890        900 
LPRILVDHAT KTFHVIDSYG SITTGFHILK ANTVTQLVKF AHESLESEMQ HYRVGGEPDK 

       910        920        930        940        950        960 
APRKPAGSVP TLGISDLRDL GVELENEEHS IRPNLQRLIK AIYRPRMMRS LLTEEPYLLI 

       970        980        990       1000       1010       1020 
LSIVSPGVLM ALYNSGSLER TMHEFLQTDQ RLSATAQILK HLAKKVSLAK TLTIQNAILE 

      1030       1040       1050       1060       1070       1080 
GGAGSLNEIL DAPAGRSLSY RLAKQTVEVM MARSDMDKEL VDVGFSVLRD QKNELIEKSY 

      1090       1100       1110       1120       1130       1140 
LMDLEDSWHA LPLCGKLSAM RASRRWRDTS TPEVIPTGAA DLKGRYSISV GSVSKSAILH 

      1150       1160       1170       1180       1190       1200 
LKGICSGAVK RVRDKWVGVQ VQGVKWLAKS VHYMIPELTN ILNVGTLLLT LISLGVAFRN 

      1210       1220       1230       1240       1250       1260 
LTGQFKEMKH KETLAKEEEL RKRIRTYNST YYEIHGKHAD AKQITKFITH HDPKLLEVVE 

      1270       1280       1290       1300       1310       1320 
FYEGPEEEEV EHQAKREDQA NLERIIAFTA LVMMMFDSER SDCVYRSLSK LKSLVSTCED 

      1330       1340       1350       1360       1370       1380 
DVRHQSVDEI IDLFDEKKET IDFEIEGKEL YSSRVVDSTF SKWWDNQLVR GNTMAHYRTE 

      1390       1400       1410       1420       1430       1440 
GHFMTFTRET AASVAAEIAH NEYRDILLQG GVGSGKSTGL PFHLHRKGGV LLIEPTRPLA 

      1450       1460       1470       1480       1490       1500 
QNVYKQLGSS PFHLSPNLRM RGSCKFGSSQ VTVATSGYAL HFIANNAQSL KAYDFIIFDE 

      1510       1520       1530       1540       1550       1560 
CHVLDASAMA FRCLLQEFEY QGKIIKVSAT PPGRKLDFKP MHMVDIATEN ELSIQQFVQG 

      1570       1580       1590       1600       1610       1620 
QGTGVNCDAT KKGDNILVYV SSYNEVDMLS KMLNDKGYKV TKVDGRTMKL GSVEVETVGT 

      1630       1640       1650       1660       1670       1680 
PQRKHFVVAT NIIENGVTLD VDVVVDFGQK VVPILDSEHR MIRYTKKSIT YGERIQRVGR 

      1690       1700       1710       1720       1730       1740 
VGRNKAGSAI RIGSTEMGTE EIPASIATEA AFLCFTYGLP VMTSNVSTSV LGNCTVRQAR 

      1750       1760       1770       1780       1790       1800 
TMQKFELSPF FMVDLVHHDG TIHPAINSLL KQFKLKESDI KLSTLAIPNA VTTFWKSARE 

      1810       1820       1830       1840       1850       1860 
YNSLGARTTI DDAAKIPFMI KDVPEHLQEK LWETIQQYKG DAGFGRCTSA NACKIAYTLS 

      1870       1880       1890       1900       1910       1920 
VSPFMIPATI NKIDALMAEE RQKMEYFQTV TANTCTISNF SISSIGDMIR SRYSTNHSRE 

      1930       1940       1950       1960       1970       1980 
NLQKLQAVRD TIINFECQAG TGDGGSFDME TAQKLAEEYG CIDVIYHQSK EALSKRLGLK 

      1990       2000       2010       2020       2030       2040 
GRWNQSLICK DLLVFCGVAI GGTWMMFQSF KDGMADAVRH QGKGKRQRQK LRYRQARDNK 

      2050       2060       2070       2080       2090       2100 
VGIEVYGDDA TMEHYFGAAY TEKGKKSGKT KGMGTKNRRF VNMYGYNPED FSFIRFLDPL 

      2110       2120       2130       2140       2150       2160 
TGKTMDEQVF SDISLVQDAF SKERLKLLSE GEIESEHMRN GIRAYLVKNL TTAALEIDMT 

      2170       2180       2190       2200       2210       2220 
PHNSCQLGAK TNNIAGYVDR EYELRQTGEA RVVAPALIPK DNPITDEDIP VKHESKTLFR 

      2230       2240       2250       2260       2270       2280 
GLRDYNPIAA AICLLTNESD GMKETMYGIG FGNTIITNQH LFRRNNGVLR VQSRHGEYVL 

      2290       2300       2310       2320       2330       2340 
PNTTQLKVLP CEGRDIMVII LTPDFPPFPQ KLKFRPPIKG EKICLVGSLF QDKSITSTVS 

      2350       2360       2370       2380       2390       2400 
ETSVTTPVDN SFLWKHWITT KDGHCGLPLV SSNDGYIVGI HSATSSRQTQ NYHAAMPEDF 

      2410       2420       2430       2440       2450       2460 
HQTHLIDPAS KSWVKHWKYN PDNMVWGGIN LINSTPREPF KINKLVTDLF GDAVQFQSKQ 

      2470       2480       2490       2500       2510       2520 
DEWFASQLKG NLKAVGKSTS QLVTKHTVKG KCMMFELYLQ THEEEKEFFK PLMGAYQKSR 

      2530       2540       2550       2560       2570       2580 
LNREAFTKDI MKYSTPITVG IVDCDTFLKA EEGVIKRLER LGFSGCEYVT DEEAIFQALN 

      2590       2600       2610       2620       2630       2640 
MKAAVGALYS GKKRDYFEGY GPEEKENILR ESCKRLYTGK FGVWNGSLKS ELRPMEKVMA 

      2650       2660       2670       2680       2690       2700 
NKTRVFTAAP LDTLLAGKVC VDDFNNYFYS KNIEAPWTVG MTKFYGGWNE LLTKLPDGWV 

      2710       2720       2730       2740       2750       2760 
YCDADGSQFD SSLSPFLINS VLRIRLKFME DWDLGEQMLK NLYTEIVYTA ILTPDSTIVK 

      2770       2780       2790       2800       2810       2820 
KFKGNNSGQP STVVDNTLMV VLAMTYTLHK LGFEDEEQDS MCKYFVNGDD LIIAIKPEHE 

      2830       2840       2850       2860       2870       2880 
SLLDQFQHCF KSLGLNYDFN SRTRKKEELW FMSHCGIKKD GIFIPKLEPE RIVSILEWDR 

      2890       2900       2910       2920       2930       2940 
SDQPVHRLEA ICAAMIESWG YDKLTHEIRK FYKWCLEQAP YADLAKAGKA PYIAECALKR 

      2950       2960       2970       2980       2990       3000 
LYTSKEASEA ELEKYMEAIR SLVNDEDDDD MDEVYHQVDA KLDAGQGSKT DDKQKNSADP 

      3010       3020       3030       3040       3050       3060 
KDNIITEKGS GSGQMKKDDD INAGLHGKHT IPRTKAITQK MKLPMIRGKV ALNLDHLLEY 

      3070       3080       3090       3100       3110       3120 
EPNQRDISNT RATQKQYESW YDGVKNDYDV DDSGMQLILN GLMVWCIENG TSPNINGTWV 

      3130       3140       3150       3160       3170       3180 
MMDGEEQVEY ALKPIIEHAK PTFRQIMAHF SDAAEAYIEM RNKKKPYMPR YGRLRGLNDM 

      3190       3200       3210       3220       3230       3240 
GLARYAFDFY ETTSATPNRA REAHNQMKAA ALVGTQNRLF GMDGGGSTQE ENTERHTAAD 

      3250 
VNQNMHTLLG VRGLH
P31999 in FASTA format

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View entry in raw text format (no links)
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