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UniProtKB/Swiss-Prot entry Q02963

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

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Entry information
Entry name POLG_PVYHU
Primary accession number Q02963
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (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
Potato virus Y (strain Hungarian) (PVY) [TaxID: 31739] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Potyviridae; Potyvirus.
Virus hosts Capsicum (peppers) [TaxID: 4071]
Nicotiana [TaxID: 4085]
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]
Solanum tuberosum (Potato) [TaxID: 4113]
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1016/0378-1119(93)90118-M; PubMed=8428653 [NCBI, ExPASy, EBI, Israel, Japan]
Thole V., Dalmay T., Burgyan J., Balazs E.;
"Cloning and sequencing of potato virus Y (Hungarian isolate) genomic RNA.";
Gene 123:149-156(1993).
[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
M95491; AAB59762.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0545; JN0545.
3D structure databases
HSSP P04517; 1LVM. [HSSP ENTRY / PDB]
ModBase Q02963.
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).
ProtoNet Q02963.
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    284  284     P1 proteinase (Potential). PRO_0000040397
CHAIN   285    740  456     Helper component proteinase (Potential). PRO_0000040398
CHAIN   741   1105  365     Protein P3 (By similarity). PRO_0000040399
CHAIN   1106   1157  52     6 kDa protein 1 (By similarity). PRO_0000040400
CHAIN   1158   1791  634     Cytoplasmic inclusion protein (By similarity). PRO_0000040401
CHAIN   1792   1843  52     6 kDa protein 2 (By similarity). PRO_0000040402
CHAIN   1844   2031  188     Viral genome-linked protein (By similarity). PRO_0000040403
CHAIN   2032   2275  244     Nuclear inclusion protein A (By similarity). PRO_0000040404
CHAIN   2276   2794  519     Nuclear inclusion protein B (By similarity). PRO_0000040405
CHAIN   2795   3061  267     Coat protein (By similarity). PRO_0000040406
DOMAIN   1229   1381  153     Helicase ATP-binding. 
DOMAIN   1400   1559  160     Helicase C-terminal. 
DOMAIN   2517   2641  125     RdRp catalytic. 
NP_BIND   1242   1249  8     ATP (Potential). 
MOTIF   334    337  4     Involved in interaction with stylet and aphid transmission (By similarity). 
MOTIF   592    594  3     Involved in virions binding and aphid transmission (By similarity). 
MOTIF   1331   1334  4     DECH box. 
MOTIF   1884   1892  9     Nuclear localization signal (Potential). 
ACT_SITE   192    192        For P1 proteinase activity (By similarity). 
ACT_SITE   201    201        For P1 proteinase activity (Potential). 
ACT_SITE   235    235        For P1 proteinase activity (By similarity). 
ACT_SITE   626    626        For helper component proteinase activity (By similarity). 
ACT_SITE   699    699        For helper component proteinase activity (By similarity). 
ACT_SITE   2077   2077        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2112   2112        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2182   2182        For nuclear inclusion protein A activity (By similarity). 
SITE   284    285  2     Cleavage; by P1 proteinase (Potential). 
SITE   740    741  2     Cleavage; by HC-pro (Potential). 
SITE   1105   1106  2     Cleavage; by NIa-pro (By similarity). 
SITE   1157   1158  2     Cleavage; by NIa-pro (By similarity). 
SITE   1791   1792  2     Cleavage; by NIa-pro (By similarity). 
SITE   1843   1844  2     Cleavage; by NIa-pro (By similarity). 
SITE   2031   2032  2     Cleavage; by NIa-pro (By similarity). 
SITE   2275   2276  2     Cleavage; by NIa-pro (By similarity). 
SITE   2794   2795  2     Cleavage; by NIa-pro (By similarity). 
MOD_RES   1907   1907        O-(5'-phospho-RNA)-tyrosine (By similarity). 
Sequence information
Length: 3061 AA [This is the length of the unprocessed precursor] Molecular weight: 347330 Da [This is the MW of the unprocessed precursor] CRC64: 737FFBA215B56F99 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATYTSTIQI GSIECKLPYS PAPFGLVAGK REVSTTTDPF ASLEMQLSAR LRRQEFATIR 

        70         80         90        100        110        120 
TSKNGTCMYR YKTDAQIARI QKKREERERE EYNFQMAASS VVSKITIAGG EPPSKLESQV 

       130        140        150        160        170        180 
RKGVIHTTPR MRTAKTYRTP KLTEGQMNHL IKQVKQIMST KGGSVQLISK KSTHVHYKEV 

       190        200        210        220        230        240 
LGSHRAVVCT AHMRGLRKRV DFRCDKWTVV RLQHLARTDK WTNQVRATDL RKGDSGVILS 

       250        260        270        280        290        300 
NTNLKGHFGR SSEGLFIVRG SHEGKIYDAR SKVTQGVMDS MVQFSSAESF WEGLDGNWAQ 

       310        320        330        340        350        360 
MRYPTDHTCV AGIPVEDCGR VAAIMTHSIL PCYKITCPTC AQQYANLPAS DLLKILHKHA 

       370        380        390        400        410        420 
SDGLNRLGAD KDRFVHVKKF LTILEHLTEP VDLSLEIFNE VFKSIGEKQQ SPFKNLNILN 

       430        440        450        460        470        480 
NFFLKGKENT AREWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD 

       490        500        510        520        530        540 
NQLDKNANFL WGQREYHAKR FFSNYFEEID PAKGYSAYEN RLHPNGTRKL AIGNLIVPLD 

       550        560        570        580        590        600 
LAEFRRKMKG DYKRQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAVESTFY PPTKKHLVIG 

       610        620        630        640        650        660 
NSGDQKYVDL PKGNSEMLYI ARQGFCYINI FLAMLINISE EDAKDFTKKV RDMCVPKLGT 

       670        680        690        700        710        720 
WPTMMDLATT CAQMKIFYPD VHDAELPRIL VDHETQTCHV VDSFGSQTTG YHILKASSVS 

       730        740        750        760        770        780 
QLILFANDEL ESDIKHYRVG GIPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPK 

       790        800        810        820        830        840 
VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVKLWI NEKQSIAMIA SLLSALALRV 

       850        860        870        880        890        900 
SAAETLVAQR IIIDTAATDL LDATCDGFNL HLTYPTALMV LQVVKNRNEC DDTLFKAGFP 

       910        920        930        940        950        960 
SYNTSVVQIM EKNYLNLLND AWKDLTWREK LSATWYSYRA KRSITRYIKP TGRADLKGLY 

       970        980        990       1000       1010       1020 
NISPQAFLGR GAQVVKGTAS GLSERFNNYF NTKCVNISSF FIRRIFRRLP TFVTFVNSLL 

      1030       1040       1050       1060       1070       1080 
VISMLTSVVA VCQAIILDQR KYRREIELMQ IEKNEIVCME LYASLQRKLE RDFTWDEYIE 

      1090       1100       1110       1120       1130       1140 
YLKSVNPQIV QFAQAQMEEY DVRHQRSTPG VKNLEQVVAF MALVIMVFDA ERSDCVFKTL 

      1150       1160       1170       1180       1190       1200 
NKFKGVLSSL DHEVRHQSLD DVIKNFDERN ETIDFELSED TIRTSSVLDT KFSDWWDRQI 

      1210       1220       1230       1240       1250       1260 
QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST GLPVHLSVAG 

      1270       1280       1290       1300       1310       1320 
SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSIFGS SPISVMTSGF ALHYFANNRS 

      1330       1340       1350       1360       1370       1380 
QLAQFNFVIF DECHVLDPSA MAFRSLLSVY HQACKVLKVS ATPVGREVEF TTQQPVKLIV 

      1390       1400       1410       1420       1430       1440 
EDTLSFQSFV DAQGSKTNAD VVQFGSNVLV YVSSYNEVDT LAKLLTDKNM MVTKVDGRTM 

      1450       1460       1470       1480       1490       1500 
KHGCLEIVTR GTSARPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKVS 

      1510       1520       1530       1540       1550       1560 
VSYGERIQRL GRVGRFKKGV ALRIGHTEKG IIENPSMIAT EAALACFAYN LPVMTGGVST 

      1570       1580       1590       1600       1610       1620 
SLIGNCTVRQ VKTMQQFELS PFFIQNFVAH DGSMHPVIHD ILKKYKLRDC MTPLCDQSIP 

      1630       1640       1650       1660       1670       1680 
YRASSTWLSV SEYERLGVAL EIPKQVKIAF HIKEIPPKLH EMLWETVVKY KDVCLFPSIR 

      1690       1700       1710       1720       1730       1740 
ASSISKIAYT LRTDLFAIPR TLILVERLLE EERVKQSQFR SLIDEGCSSM FSIVNLTNTL 

      1750       1760       1770       1780       1790       1800 
RARYAKDYTA ENIQKLEKVR SQLKEFSNLD GSACEENLIK RYESLQFVHH QAATSLAKDL 

      1810       1820       1830       1840       1850       1860 
KLKGTWKKSL VAKDLIIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR IQALKFRHAR 

      1870       1880       1890       1900       1910       1920 
DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS RRFVNMYGFD PTEYSFIQFV 

      1930       1940       1950       1960       1970       1980 
DPLTGAQIEE NVYADIRDIQ ERFSDVRKKM VEDDEIELQA LGSNTTIHAY FRKDWSDKAL 

      1990       2000       2010       2020       2030       2040 
KIDLMPHNPL KICDKSNGIA KFPERELELR QTGPAIEVDV KDIPKQEVEH EAKSLMRGLR 

      2050       2060       2070       2080       2090       2100 
DFNPIAQTVC RVKVSAEYGT SEMYGFGFGA YIIVNHHLFK SFNGSMEVRS MHGTFRVKNL 

      2110       2120       2130       2140       2150       2160 
HSLSVLPIKG RDIIIIKMPK DFPVFPQKLH FRAPVQNERI CLVGTNFQEK HASSIITETS 

      2170       2180       2190       2200       2210       2220 
TTYNVPGSTF WKHWIETNDG HCGLPVVSTA DGCLVGIHSL ANNVQTTNYY SAFDEDFESK 

      2230       2240       2250       2260       2270       2280 
YLRTNEHNEW TKSWVYNPDT VLWGPLKLKE STPKGLFKTT KLVQDLIDHD VVVEQAKHSA 

      2290       2300       2310       2320       2330       2340 
WMYEALTGNL QAVATMKSQL VTKHVVKGEC RHFKEFLTVD SEAEAFFRPL MDAYGKSLLN 

      2350       2360       2370       2380       2390       2400 
REAYIKDIMK YSKPIDVGIV DCDAFEEAIN RVIIYLQVHG FQKCNYITDE QEIFKALNMK 

      2410       2420       2430       2440       2450       2460 
AAVGAMYGGK KKDYFEHFTE ADKEEIVMQS CPRLYKGSLG IWNGSLKAEL RCKEKILANK 

      2470       2480       2490       2500       2510       2520 
TRTFTAAPLD TLLGGKVCVD DFNNQFYSKN IECCWTVGMT KFYGGWDRLL RRLPENWVYC 

      2530       2540       2550       2560       2570       2580 
DADGSQFDSS LTPYLINAVL IIRSTYMEDW DLGLQMLRNL YTEIIYTPIS TPDGTIVKKF 

      2590       2600       2610       2620       2630       2640 
RGNNSGQPST VVDNSLMVVL AMHYALIKEC VEFEEIDSTC VFFVNGDDLL IAVNPEKESI 

      2650       2660       2670       2680       2690       2700 
LDRMSQHFSD LGLNYDFSSR TRRKEELWFM SHRGLLIEGM YVPKLEEERI VSILQWDRAD 

      2710       2720       2730       2740       2750       2760 
LPEHRLEAIC AAMIESWGYS ELTHQIRRFY SWLLQQQPFS TIAQEGKAPY IASMALKKLY 

      2770       2780       2790       2800       2810       2820 
MNRTVDEEEL KAFTEMMVAL DDELECDTYE VHHQGNDTID AGGSTKKDAK QEQGSIQPNL 

      2830       2840       2850       2860       2870       2880 
NKEKEKDVNV GTSGTHTVPR IKAITSKMRM PKSKGAAVLN LKHLLEYAPQ QIDISNTRAT 

      2890       2900       2910       2920       2930       2940 
QSQFDTWYEA VQLAYDIGET EMPTVMNGLM VWCIENGTSP NINGVWVMMD GDEQVEYPLK 

      2950       2960       2970       2980       2990       3000 
PIVENAKPTL RQIMAHFSDV AEAYIEMRNK KEPYMPRYGL VRNLRDGSLA RYAFDFYEVT 

      3010       3020       3030       3040       3050       3060 
SRTPVRAREA HIQMKAAALK SAQSRLFGLD GGISTQEENT ERHTTEDVSP SMHTLLGVKN 


M
Q02963 in FASTA format

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