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UniProtKB/Swiss-Prot entry P29152


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

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Entry information
Entry name POLG_PSBMV
Primary accession number P29152
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 78)
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
Pea seed-borne mosaic virus (strain DPD1) [TaxID: 31736] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Potyviridae; Potyvirus.
Virus host Pisum sativum (Garden pea) [TaxID: 3888]
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1940858 [NCBI, ExPASy, EBI, Israel, Japan]
Johansen E., Rasmussen O.F., Heide M., Borkhardt B.;
"The complete nucleotide sequence of pea seed-borne mosaic virus RNA.";
J. Gen. Virol. 72:2625-2632(1991).
[2]
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
D10930; BAA01726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ1331; GNVSPV.
RefSeq NP_056765.1; -.
3D structure databases
HSSP P04517; 1LVM. [HSSP ENTRY / PDB]
ModBase P29152.
Protein family/group databases
MEROPS C04.010; -.
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 P29152.
ProtoNet P29152.
Genome annotation databases
GeneID 1494045; -.
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    397  397     P1 proteinase (Potential). PRO_0000040375
CHAIN   398    856  459     Helper component proteinase (Potential). PRO_0000040376
CHAIN   857   1214  358     Protein P3 (By similarity). PRO_0000040377
CHAIN   1215   1266  52     6 kDa protein 1 (By similarity). PRO_0000040378
CHAIN   1267   1902  636     Cytoplasmic inclusion protein (By similarity). PRO_0000040379
CHAIN   1903   1955  53     6 kDa protein 2 (By similarity). PRO_0000040380
CHAIN   1956   2149  194     Viral genome-linked protein (By similarity). PRO_0000040381
CHAIN   2150   2395  246     Nuclear inclusion protein A (By similarity). PRO_0000040382
CHAIN   2396   2915  520     Nuclear inclusion protein B (By similarity). PRO_0000040383
CHAIN   2916   3206  291     Coat protein (By similarity). PRO_0000040384
DOMAIN   1338   1490  153     Helicase ATP-binding. 
DOMAIN   1494   1668  175     Helicase C-terminal. 
DOMAIN   2637   2761  125     RdRp catalytic. 
NP_BIND   1351   1358  8     ATP (Potential). 
MOTIF   450    453  4     Involved in interaction with stylet and aphid transmission (By similarity). 
MOTIF   708    710  3     Involved in virions binding and aphid transmission (By similarity). 
MOTIF   1440   1443  4     DECH box. 
MOTIF   1994   2001  8     Nuclear localization signal (Potential). 
ACT_SITE   348    348        For P1 proteinase activity (By similarity). 
ACT_SITE   742    742        For helper component proteinase activity (By similarity). 
ACT_SITE   815    815        For helper component proteinase activity (By similarity). 
ACT_SITE   2195   2195        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2230   2230        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2300   2300        For nuclear inclusion protein A activity (By similarity). 
SITE   397    398  2     Cleavage; by P1 proteinase (Potential). 
SITE   856    857  2     Cleavage; by HC-pro (Potential). 
SITE   1214   1215  2     Cleavage; by NIa-pro (By similarity). 
SITE   1266   1267  2     Cleavage; by NIa-pro (By similarity). 
SITE   1902   1903  2     Cleavage; by NIa-pro (By similarity). 
SITE   1955   1956  2     Cleavage; by NIa-pro (By similarity). 
SITE   2149   2150  2     Cleavage; by NIa-pro (By similarity). 
SITE   2395   2396  2     Cleavage; by NIa-pro (By similarity). 
SITE   2915   2916  2     Cleavage; by NIa-pro (By similarity). 
MOD_RES   2016   2016        O-(5'-phospho-RNA)-tyrosine (By similarity). 
Sequence information
Length: 3206 AA [This is the length of the unprocessed precursor] Molecular weight: 364276 Da [This is the MW of the unprocessed precursor] CRC64: 42A3D921BE9A0CBF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTLVCQAVA APVWSNGART RRIRDADGEY RCTQCDMGFD SMTMARPVNH CCDGIMIDEY 

        70         80         90        100        110        120 
NLYDDDPIMH LVDSKTPIKR GSQETEGDGM AAEAIKVTGA EPVNCFMVGT IKCKINENSI 

       130        140        150        160        170        180 
VAKGVMAAIP RQLTQDEVFM RKARLQAAVA KSTIEREEKE RQFAFSKLEE KLRARREKLK 

       190        200        210        220        230        240 
DGIVIKTRKG LEWREATPNQ QRGKLQSTSF DASGGKTLTP HTIYCKTKSS KFSNGGVKCA 

       250        260        270        280        290        300 
TSKKMRTVRK PQSLKMKTES IDVLIEQVMT IAGKHAKQVT LIDKQKTNRV WIRRVNGVRL 

       310        320        330        340        350        360 
LQVETKHHKG IISQKDASLN NLTKRVARHF ARKTAYIHPS DSITHGHSGV VFLRANISGS 

       370        380        390        400        410        420 
KSYSIDDLFV VRGKRNGKLM ESRNKVAWRK MFQIDHFSIV GIKIWNAFDA EYVKLRDESV 

       430        440        450        460        470        480 
SDHDCVGGIT PEECGILAAQ ILRVFYPCWR ITCTKCISNW LSKPTSEQIE HIYERGNLAI 

       490        500        510        520        530        540 
QDLNKRIPSA HHVTQMVELL RQRIKNTTFD MGNNTKVHEL IGHRQDGVFR HLNRLNNSIL 

       550        560        570        580        590        600 
AANGSSTIEW ESMNESLLEL ARWHNKRTES IASGGISSFR NKISAKAQIN FALMCDNQLD 

       610        620        630        640        650        660 
TNGNFVWGER GYHAKRFFSE FFTKIDPKDG YSHHTVRATP TGVRHLAIGN LIIPGDLQKL 

       670        680        690        700        710        720 
REKLEGVSIT AVGISEKCVS RRNGDFVYPC SCVTSENGKP VLSDVILPTR NHLVIGNTGD 

       730        740        750        760        770        780 
PKLVDLPKTE TGRMWIAKEG YCYINIFFAM LVNVSEKDAK DFTKFVRDEI MPQLGKWPTM 

       790        800        810        820        830        840 
MDVATACYKL AIIYPDVRDA QLPRILVDHS EQIFHVIDSY GSMTTGYHIL KAGTVSQLIS 

       850        860        870        880        890        900 
FAHGALLGEM KMYRVGGTQK MEINMCCCQR KNLLIKQLIR AIYRPKLLTE IIETEPFVLM 

       910        920        930        940        950        960 
LAIVSPSILK AMFRSGTFNQ AIKFYMHRSK PTAQTLAFLE ALSERVSRSR VLSEQFNIID 

       970        980        990       1000       1010       1020 
GALKELKSLA NMSMRTQHTY PIVQNQLDIM IERVSADAEL LRDGFVVSKG RVQALIEKNY 

      1030       1040       1050       1060       1070       1080 
QDDLRNSFTD LPYVQQLQQT MSFSRVKHGF GELCESKDLS FSKEAWMGHL SSFSAGGKQI 

      1090       1100       1110       1120       1130       1140 
IRLARTKSQQ MLASGGRRVT LAARNITMRM VTATFSEIMK FVNMLLVLSM IFKLWKQANT 

      1150       1160       1170       1180       1190       1200 
LLEEREKDKW EKFDRSQNEL RRQLRYTLWR FEAQEGRQVT REEFFDYLKY NEGIENRHEL 

      1210       1220       1230       1240       1250       1260 
INELIANQPL FSIQAKKHGE IRFEQTVALM ALLAMMFGSD RSDAVFSTLS KVRTIFTTMA 

      1270       1280       1290       1300       1310       1320 
QEVRCQSIDD IHDVFDEKKA TIDFELATDQ PAQVQMDKTF CEWWQNQMEQ NRTVPHYRTG 

      1330       1340       1350       1360       1370       1380 
GKFIEFTRSN AASVANEIAH TPDFSEYLIR GAVGSGKSTG LPCYLSAKGR VLLLEPTRPL 

      1390       1400       1410       1420       1430       1440 
TENVCAQLRG SPFHKSPSMS MRNGHTFGST PIHVMTTGYA LHFFCNNVER IREYDFVIFD 

      1450       1460       1470       1480       1490       1500 
ECHVIDSSAM SFYCALKEYS YQGKILKVSA TPPGREVEFK TQFPVTIATE DSLSFDQFVQ 

      1510       1520       1530       1540       1550       1560 
AQGSGANCDI LKKGHNILVY VSSYNEVDRL SKLLVDRGFK VTKVDGRTMK LGGVEINTSG 

      1570       1580       1590       1600       1610       1620 
TAEKPHFIVA TNIIENGVTL DIDVVVDFGV KVVAELDADA RTMRYNKQAI SYGERIQRLG 

      1630       1640       1650       1660       1670       1680 
RVGRLKDGHA LRIGHTEKGI TEIPVAIAVE SAFQCFAYGL PVMTSNVSTS IIGNCTVKQA 

      1690       1700       1710       1720       1730       1740 
RTMMNFELSP FFTVELVKYN GTMHPEIHKI LVPYKLRDSS MQLCKEAIPN SGVSRWHTAH 

      1750       1760       1770       1780       1790       1800 
EYISHGIVLE TLKSDVRIPF YLKGVPEKVY EKIWNAVCVF KSDSGFGRMS TASACNVAYT 

      1810       1820       1830       1840       1850       1860 
LKTDPLSITR TIAHIDALLI EEQEKKSQFD LMSSHVTNSS SISLAGLVNR LRSKWMVDHS 

      1870       1880       1890       1900       1910       1920 
GENIVKLQNA RSQLLEFRGM DINLDDVESF RKFGCAETVR CQSKSEVSKT LQLKGKWNKP 

      1930       1940       1950       1960       1970       1980 
LITSDFFVVC MVSIGCVVLM YQIFMAKWNE PVKLEGKSKA KTLRFRQARD NNAKYEVFAD 

      1990       2000       2010       2020       2030       2040 
EDTKRHYFGE AYTKKGKKSG KARGMGVKTK KFVNVYGFDP CEYSLVRFVD PLTGLTYDRH 

      2050       2060       2070       2080       2090       2100 
PMEHMMDVQE TIGDDRREAM WNDELDKQLF VTRPTIEAYY IKDKTTPALK IDLNPHNPMR 

      2110       2120       2130       2140       2150       2160 
VCDKAETIAG FPEREFELRQ SGSATLVPYS EVPVQNEKQE FDEEHVRTEA ASLHFGLRDY 

      2170       2180       2190       2200       2210       2220 
NPIAQAVCRI TNTGVDYDRS IFGIGFGQFL ITNAHCFKLN EGETRIVSRH GQFTIEKTHS 

      2230       2240       2250       2260       2270       2280 
LPIHQVKDKD MVIVRLPKDF PPFPQRLQFR APQEREKICL VGSNFQEKSI QSVITESCMT 

      2290       2300       2310       2320       2330       2340 
FKHNGGKYWK HWITTKEGHC GLPAVALKDG HIVGIHNLGG ENTNINYFTP FDADILDKYL 

      2350       2360       2370       2380       2390       2400 
LNAEALQWTK GWKYNKNKVC WGGLELLDDN EPEESGLFRM VKLLKSLEED GVRTQSRDDA 

      2410       2420       2430       2440       2450       2460 
WLEKEIKGSL KVVARCPGQL VTKHVVKGPC AMFQLYLELH EDAKSFFTPR MGSYGKSRLS 

      2470       2480       2490       2500       2510       2520 
KGAFIKDIMK YSSNTVVGNV DCDVFENAID NVEKILWKAG MMQCEYVTDA EAIFQSLNMN 

      2530       2540       2550       2560       2570       2580 
AAVGAMYQGK KKDYFEDFTA ADRELIVKQS CERLFLGKKG VWNGSLKAEL RPIEKVHENK 

      2590       2600       2610       2620       2630       2640 
TRTFTAAPLD TLLGGKVCVD DFNNFFYSCH LRGPWTVGIT KFYAGWNEFL SKLPDGWLYC 

      2650       2660       2670       2680       2690       2700 
DADGSRFDSS LTPYLINAVL ELRLRFMEEW DAGEQMLKNL YTEIIYTPIA TPDGSVIKKT 

      2710       2720       2730       2740       2750       2760 
KGNNSGQPST VVDNTLMVIL AMQYSLQLLG VDFETQDEVV RYFANGDDLL IAVRPDCEFV 

      2770       2780       2790       2800       2810       2820 
LKGLEIHFSN LGLNYNFSAR HHDKKDVWFM STRGILRDGI LIPKLEEERI VAILEWDRSR 

      2830       2840       2850       2860       2870       2880 
EFSHRLDAIC AAMIEAWGYD ELLQHIRKFY YWLLEQEPYR SIAQEGKAPY IAETALRHLY 

      2890       2900       2910       2920       2930       2940 
TNAMATQSEL EKYTEAINQH YNDEGGDGSI KVRLQAGDET KDDERRRKEE EDRKKREESI 

      2950       2960       2970       2980       2990       3000 
DASQFGSNRD NKKNKNKESD TPNKLIVKSD RDVDAGSSGT ITVPRLEKIS AKIRMPKHKG 

      3010       3020       3030       3040       3050       3060 
GVAISLQHLV DYNPAQVDIS NTRATQSQFD NWWRAVSQEY GVGDNEMQVL ASGLMVWCIE 

      3070       3080       3090       3100       3110       3120 
NGTSPNINGM WTMMDGEEQV EYPLKPVMDN ARPTFRQIMA HFSDVAEAYI EKRNSTEVYI 

      3130       3140       3150       3160       3170       3180 
PRYALQRNLR DPSLARYGFD FYEITAKTPV RAREAHFQMK AAAIRGKSNS LFGLDGNVGT 

      3190       3200 
QEENTERHTA EDVNQNMHNL LGMRAM 

P29152 in FASTA format

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