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UniProtKB/Swiss-Prot entry P21231


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

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Entry information
Entry name POLG_SBMVN
Primary accession number P21231
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on June 6, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 76)
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
Soybean mosaic virus (strain N) (SMV) [TaxID: 12223] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Potyviridae; Potyvirus.
Virus host Glycine max (Soybean) [TaxID: 3847]
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Eggenberger A.L., Beachy R.N., Hill J.H.;
"Two genes of soybean mosaic virus are involved in the interaction with the Rsv1 resistance allele of soybean.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2764-3066, AND PROTEIN SEQUENCE OF 2845-2859.
PubMed=2661723 [NCBI, ExPASy, EBI, Israel, Japan]
Eggenberger A.L., Stark D.M., Beachy R.N.;
"The nucleotide sequence of a soybean mosaic virus coat protein-coding region and its expression in Escherichia coli, Agrobacterium tumefaciens and tobacco callus.";
J. Gen. Virol. 70:1853-1860(1989).
[3]
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 (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 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.
  • 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).
  • 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
D00507; BAA00398.2; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR PS0081; PS0081.
RefSeq NP_072165.1; -.
3D structure databases
HSSP P04517; 1LVM. [HSSP ENTRY / PDB]
ModBase P21231.
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 P21231.
Genome annotation databases
GeneID 918483; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Direct protein sequencing; 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    308  308     P1 proteinase (Potential). PRO_0000040438
CHAIN   309    765  457     Helper component proteinase (Potential). PRO_0000040439
CHAIN   766   1112  347     Protein P3 (By similarity). PRO_0000040440
CHAIN   1113   1164  52     6 kDa protein 1 (By similarity). PRO_0000040441
CHAIN   1165   1798  634     Cytoplasmic inclusion protein (By similarity). PRO_0000040442
CHAIN   1799   1851  53     6 kDa protein 2 (By similarity). PRO_0000040443
CHAIN   1852   2041  190     Viral genome-linked protein (By similarity). PRO_0000040444
CHAIN   2042   2284  243     Nuclear inclusion protein A (By similarity). PRO_0000040445
CHAIN   2285   2801  517     Nuclear inclusion protein B (By similarity). PRO_0000040446
CHAIN   2802   3066  265     Coat protein (By similarity). PRO_0000040447
DOMAIN   1236   1388  153     Helicase ATP-binding. 
DOMAIN   1407   1566  160     Helicase C-terminal. 
DOMAIN   2526   2650  125     RdRp catalytic. 
NP_BIND   1249   1256  8     ATP (Potential). 
MOTIF   361    364  4     Involved in interaction with stylet and aphid transmission (By similarity). 
MOTIF   617    619  3     Involved in virions binding and aphid transmission (By similarity). 
MOTIF   1338   1341  4     DECH box. 
MOTIF   1891   1900  10     Nuclear localization signal (Potential). 
ACT_SITE   651    651        For helper component proteinase activity (By similarity). 
ACT_SITE   724    724        For helper component proteinase activity (By similarity). 
ACT_SITE   2087   2087        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2122   2122        For nuclear inclusion protein A activity (By similarity). 
ACT_SITE   2192   2192        For nuclear inclusion protein A activity (By similarity). 
SITE   308    309  2     Cleavage; by P1 proteinase (Potential). 
SITE   765    766  2     Cleavage; by HC-pro (Potential). 
SITE   1112   1113  2     Cleavage; by NIa-pro (By similarity). 
SITE   1164   1165  2     Cleavage; by NIa-pro (By similarity). 
SITE   1798   1799  2     Cleavage; by NIa-pro (By similarity). 
SITE   1851   1852  2     Cleavage; by NIa-pro (By similarity). 
SITE   2041   2042  2     Cleavage; by NIa-pro (By similarity). 
SITE   2284   2285  2     Cleavage; by NIa-pro (By similarity). 
SITE   2801   2802  2     Cleavage; by NIa-pro (By similarity). 
MOD_RES   1915   1915        O-(5'-phospho-RNA)-tyrosine (By similarity). 
CONFLICT   2764   2764        A -> L (in Ref. 2; AA sequence). 
Sequence information
Length: 3066 AA [This is the length of the unprocessed precursor] Molecular weight: 349846 Da [This is the MW of the unprocessed precursor] CRC64: 394149153DD5328F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATIMIGSMA ISVPNTHVSC ASNSVMPVQA VQMAKQVPSA RGVLYTLKRE GSTQVHKHEE 

        70         80         90        100        110        120 
ALRKFQEAFD QDVGIQRRLL VNKHSSIQST KKNGLTLRRL TLEQARAKEA AIARRKQEEE 

       130        140        150        160        170        180 
DFLNGKYEQQ FYAGVSATKS MKFEGGSVGF RTKYWRPTPK KTKERRATSQ CRKPTYVLEE 

       190        200        210        220        230        240 
VLSIASKSGK LVEFITGKGK RVKVCYVRKH GAILPKFSLP HEEGKYIHQE LQYASTYEFL 

       250        260        270        280        290        300 
PYICMFAKYK SINADDITYG DSGLLFDERS SLTTNHTKLP YFVVRGRRNG KLVNALEVVE 

       310        320        330        340        350        360 
NMEDIQHYSQ NPEAQFFRGW KKVFDKMPPH VENHECTTDF TNEQCGELAA AISQSIFPVK 

       370        380        390        400        410        420 
KLSCKQCRQH IKHLSWEEYK QFLLAHMGCH GPEWETFQEI DGMRYVKRVI ETSTAENASL 

       430        440        450        460        470        480 
QTSLEIVRLT QNYKSTHMLQ IQDINKALMK GPSVTQSELE QASKQLLAMT QWWKNHMTLT 

       490        500        510        520        530        540 
DEDALKVFRN KRSSKALLNP SLLCDNQLDK NGNFVWGERG RHSKRFFANY FEEVVPSEGY 

       550        560        570        580        590        600 
SKYVIRKNPN GQRELAIGSL IVPLDFERAR MALQGKSVTR EPITMSCISR QDGNFVYPCC 

       610        620        630        640        650        660 
CVTHDDGKAF YSELRSPTKR HLVIGTSGDP KYIDLPATDA DRMYIAKEGF CYLNIFLAML 

       670        680        690        700        710        720 
VNVNEDEAKD FTKMVRDVIV PRLGKWPTML DVATAAYMLT VFHPETRNAE LPRILVDHAC 

       730        740        750        760        770        780 
QTMHVIDSFG SLTVGYHVLK AGTVNQLIQF ASNDLQSEMK FYRVGGEVQQ RMKCETALIT 

       790        800        810        820        830        840 
SIFKPKRMIQ ILENDPYILL MGLVSPSILI HMYRMKHFEK GVELWISKEH SVAKIFIILE 

       850        860        870        880        890        900 
QLTKRVAAND VLLEQLEMIS ETSERFMSIL EDCPQAPHSY KTAKDLLTMY IERKASNNQL 

       910        920        930        940        950        960 
VENGFVDMND KLYMAYEKIY SDRLKQEWRA LSWLEKFSIT WQLKRFAPHT EKCLTKKVVE 

       970        980        990       1000       1010       1020 
ESSASSGNFA SVCFMNAQSH LRNVRNTLFQ KCDQVWTASV RAFVKLIIST LHRCYSDIVY 

      1030       1040       1050       1060       1070       1080 
LVNICIIFSL LVQMTSVLQG IVNTVRRDKA LLSGWKRKED EEAVIHLYEM CEKMEGGHPS 

      1090       1100       1110       1120       1130       1140 
IEKFLDHVKG VRPDLLPVAV SMTGQSEDVS AQAKTATQLQ LEKIVAFMAL LTMCIDNERS 

      1150       1160       1170       1180       1190       1200 
DAVFKVLSKL KAFFSTMGED VKVQSLDEIQ SIDEDKKLTI DFDLETNKES SSVSFDVKFE 

      1210       1220       1230       1240       1250       1260 
AWWNRQLEQN RVIPHYRSTG EFLEFTRETA AKIANLVATS SHTEFLIRGA VGSGKSTGLP 

      1270       1280       1290       1300       1310       1320 
HHLSKKGKVL LLEPTRPLAE NVSKQLSFEP FYHNVTLRMR GMSKFGSSNI VVMTSGFAFH 

      1330       1340       1350       1360       1370       1380 
YYVNNPQQLS DFDFIIIDEC HVQDSPTIAF NCALKEFEFS GKLIKVSATP PGRECEFTTQ 

      1390       1400       1410       1420       1430       1440 
HPVKLKVEDH LSFQNFVQAQ GTGSNADMIQ HGNNLLVYVA SYNEVDQLSR LLTEKHYKVT 

      1450       1460       1470       1480       1490       1500 
KVDGRTMQMG NVEIATTGTE GKPHFIVATN IIENGVTLDI DCVIDFGLKV VATLDTDNRC 

      1510       1520       1530       1540       1550       1560 
VRYNKQSVSY GERIQRLGRV GRCKPGFALR IGHTGKGVEE VPEFIATEAA FLSFAYGLPV 

      1570       1580       1590       1600       1610       1620 
TTQSVSTNIL SRCTVKQARV ALNFELTPFF TTNFIKYDGS MHPEIHRLLK SYKLRESEML 

      1630       1640       1650       1660       1670       1680 
LTKIAIPYQF VGQWVTVKEY ERQGIHLNCP EKVKIPFYVH GIPDKLYEML WDTVCKYKND 

      1690       1700       1710       1720       1730       1740 
AGFGSVKSVN ATKISYTLST DPTAIPRTLA ILDHLLSEEM TKKSHFDTIG SAVTGYSFSL 

      1750       1760       1770       1780       1790       1800 
AGIADGFRKR YLKDYTQHNI AVLQQAKAQL LEFDCNKVDI NNLHNVEGIG ILNAVQLQSK 

      1810       1820       1830       1840       1850       1860 
HEVSKFLQLK GKWDGKKFMN DAVVAIFTLV GGGWMLWDYF TRVIREPVST QGKKRQIQKL 

      1870       1880       1890       1900       1910       1920 
KFRDAFDRKI GREVYADDYT MEHTFGEAYT KKGKQKGSTR TKGMGRKSRN FIHLYGVEPE 

      1930       1940       1950       1960       1970       1980 
NYSMIRFVDP LTGHTMDEHP RVDIRMVQQE FEEIRKDMIG EGELDRQRVY HNPGLQAYFI 

      1990       2000       2010       2020       2030       2040 
GKNTEEALKV DLTPHRPTLL CQNSNAIAGF PEREDELRQT GLPQVVSKSD VPRAKERVEM 

      2050       2060       2070       2080       2090       2100 
ESKSVYKGLR DYSGISTLIC QLTNSSDGHK ETMFGVGYGS FIITNGHLFR RNNGMLTVKT 

      2110       2120       2130       2140       2150       2160 
WHGEFVIHNT TQLKIHFIQG KDVILIRMPK DFPPFGKRNL FRQPKREERV CMVGTNFQEK 

      2170       2180       2190       2200       2210       2220 
SLRATVSESS MILPEGKGSF WIHWITTQDG FCGLPLVSVN DGHIVGIHGL TSNDSEKNFF 

      2230       2240       2250       2260       2270       2280 
VPLTDGFEKE YLENADNLSW DKHWFWEPSK IAWGSLNLVE EQPKEEFKIS KLVSDLFGNT 

      2290       2300       2310       2320       2330       2340 
VTVQGRKERW VLDAMEGNLA ACGQADSALV TKHVVKGKCP YFAQYLSVNQ EAKSFFEPLM 

      2350       2360       2370       2380       2390       2400 
GAYQPSRLNK DAFKRDFFKY NKPVVLNEVD FQSFERAVAG VKLMMMEFDF KECVYVTDPD 

      2410       2420       2430       2440       2450       2460 
EIYDSLNMKA AVGAQYKGKK QDYFSGMDSF DKERLLYLSC ERLFYGEKGV WNGSLKAELR 

      2470       2480       2490       2500       2510       2520 
PIEKVQANKT RTFTAAPIDT LLGAKVCVDD FNNQFYSLNL TCPWTVGMTK FYRGWDKLMR 

      2530       2540       2550       2560       2570       2580 
SLPDGWVYCH ADGSQFDSSL TPLLLNAVLD VRSFFMEDWW VGREMLENLY AEIVYTPILA 

      2590       2600       2610       2620       2630       2640 
PDGTIFKKFR GNNSGQPSTV VDNTLMVVIA MYYSCCKQGW SEEDIQERLV FFANGDDIIL 

      2650       2660       2670       2680       2690       2700 
AVSDKDTWLY DTLSTSFAEL GLNYNFEERT KKREELWFMS HKAVLVDGIY IPKLEPERIV 

      2710       2720       2730       2740       2750       2760 
SILEWDRSKE LMHRTEAICA SMIEAWGYTE LLQEIRKFYL WLLNKDEFKE LASSGKAPYI 

      2770       2780       2790       2800       2810       2820 
AETALRKLYT DVNAQTSELQ RYLEVLDFNH ADDCCESVSL QSGKEKEGDM DADKDPKKST 

      2830       2840       2850       2860       2870       2880 
SSSKGAGTSS KDVNVGSKGK VVPRLQKITR KMNLPMVEGK IILSLDHLLE YKPNQVDLFN 

      2890       2900       2910       2920       2930       2940 
TRATRTQFEA WYNAVKDEYE LDDEQMGVVM NGFMVWCIDN GTSPDANGVW VMMDGEEQIE 

      2950       2960       2970       2980       2990       3000 
YPLKPIVENA KPTLRQIMHH FSDAAEAYIE MRNSESPYMP RYGLLRNLRD RELARYAFDF 

      3010       3020       3030       3040       3050       3060 
YEVTSKTPNR AREAIAQMKA AALSGVNNKL FGLDGNISTN SENTERHTAR DVNQNMHTLL 


GMGPPQ 

P21231 in FASTA format

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