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Protein

Non-structural polyprotein

Gene
N/A
Organism
Semliki forest virus (SFV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

P123 is short-lived polyproteins, accumulating during early stage of infection. It localizes the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, it starts viral genome replication into antigenome. After these early events, P123 is cleaved sequentially into nsP1, nsP2 and nsP3. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex.
nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell.
nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Also inhibits cellular transcription by inducing rapid degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response.
nsP3 is essential for minus strand and subgenomic 26S mRNA synthesis.
nsP4 is an RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA codes for structural proteins.

Catalytic activityi

S-adenosyl-L-methionine + GTP = m7GTP.
m7GTP + [nsP1 protein] = m7GMP-[nsP1 protein] + diphosphate.
m7GMP-[nsP1 protein] + (5')pp-Pur-mRNA = m7G(5')ppp-Pur-mRNA + [nsP1 protein].
(5')ppp-mRNA + H2O = (5')pp-mRNA + phosphate.
A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

Kineticsi

  1. KM=2.99 mM for triphosphatase (at pH 8.0)1 Publication
  2. KM=90 mM for NTPase (at pH 7.5)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei1015For cysteine protease nsP2 activityPROSITE-ProRule annotation1
    Active sitei1085For cysteine protease nsP2 activityPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi723 – 730ATPSequence analysis8

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
    Biological processEukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host RNA polymerase II by virus, mRNA capping, mRNA processing, Viral RNA replication
    LigandATP-binding, GTP-binding, Nucleotide-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    SABIO-RKiP08411.

    Protein family/group databases

    MEROPSiC09.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-structural polyprotein
    Alternative name(s):
    Polyprotein nsP1234
    Short name:
    P1234
    Cleaved into the following 5 chains:
    Alternative name(s):
    Non-structural protein 1
    Alternative name(s):
    Non-structural protein 2
    Short name:
    nsP2
    Non-structural protein 3
    Short name:
    nsP3
    Alternative name(s):
    Non-structural protein 4
    Short name:
    nsP4
    OrganismiSemliki forest virus (SFV)
    Taxonomic identifieri11033 [NCBI]
    Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
    Virus hostiAedes [TaxID: 7158]
    Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog) [TaxID: 9368]
    Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
    Halcyon [TaxID: 170865]
    Homo sapiens (Human) [TaxID: 9606]
    Quelea [TaxID: 158617]
    Rhipicephalus [TaxID: 34630]
    Proteomesi
    • UP000100607 Componenti: Genome
    • UP000166518 Componenti: Genome
    • UP000174511 Componenti: Genome
    • UP000000570 Componenti: Genome
    • UP000136172 Componenti: Genome

    Subcellular locationi

    Non-structural polyprotein :
    mRNA-capping enzyme nsP1 :
    Protease nsP2 :
    Non-structural protein 3 :

    GO - Cellular componenti

    Keywords - Cellular componenti

    Host cell membrane, Host cell projection, Host cytoplasm, Host endosome, Host lysosome, Host membrane, Host nucleus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi19L → E: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi38H → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi64D → A: 60% increase of guanine-7-methyl transferase activity in vitro. Complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi81 – 83CVC → AVA: 60% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication3
    Mutagenesisi90D → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi93R → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi135C → A: 90% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi142C → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi153D → A: No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi169K → A: 50% loss of guanine-7-methyl transferase activity and no effect on guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi180D → A: No effect on guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi203E → A: No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi214C → A: 90% loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi249Y → A: 97% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi317K → A: 95% loss of guanine-7-methyl transferase activity and 98% loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi418 – 420CCC → AAA: Complete loss of palmitoylation. Complete loss of pathogenicity in mice. 2 Publications3
    Mutagenesisi729K → N: Complete loss of NTPase and helicase activity. 1 Publication1
    Mutagenesisi1015C → A: Complete loss of polyprotein processing. 1 Publication1
    Mutagenesisi1186R → D: Complete loss of nuclear localization for nsP2. 1 Publication1
    Mutagenesisi1680T → A: Complete loss of threonine phosphorylation. 1 Publication1
    Mutagenesisi1681T → A: Complete loss of threonine phosphorylation. 1 Publication1
    Mutagenesisi1824D → A: No effect on polyprotein processing. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003084031 – 2432Non-structural polyproteinAdd BLAST2432
    ChainiPRO_00002277701 – 1818P123Add BLAST1818
    ChainiPRO_00000412281 – 537mRNA-capping enzyme nsP1Add BLAST537
    ChainiPRO_0000041229538 – 1336Protease nsP2Add BLAST799
    ChainiPRO_00000412301337 – 1818Non-structural protein 3Add BLAST482
    ChainiPRO_00000412311819 – 2431RNA-directed RNA polymerase nsP4Add BLAST613

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Lipidationi418S-palmitoyl cysteine; by host2 Publications1
    Lipidationi420S-palmitoyl cysteine; by host2 Publications1
    Modified residuei1680Phosphothreonine; by host1 Publication1
    Modified residuei1681Phosphothreonine; by host1 Publication1

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. The polyprotein is synthesized as P1234 by stop codon readthrough. This polyprotein is processed differently depending on the stage of infection. In early stages, P1234 is first cleaved in trans, through its nsP2 protease activity, releasing P123 and nsP4. P123 and nsP4 start to replicate the viral genome into its antigenome. After these early events, nsP1 is cleaved in cis by nsP2 protease, releasing P23 polyprotein. Cleavage of nsP1 exposes an 'activator' at the N-terminus of P23 which induces its cleavage into nsP2 and nsP3 by the viral protease. This sequence of delayed processing would allow correct assembly and membrane association of the RNA-polymerase complex. In the late stage of infection, the presence of free nsP2 in the cytoplasm cleaves P1234 quickly into P12 and P34, then into the four nsP.1 Publication
    nsP1 is palmitoylated by host.2 Publications
    nsP3 is phosphorylated by host on serines and threonines.1 Publication
    nsP4 is ubiquitinated; targets the protein for rapid degradation via the ubiquitin system.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei537 – 538Cleavage; by nsP22
    Sitei1336 – 1337Cleavage; by nsP22
    Sitei1818 – 1819Cleavage; by nsP22

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP08411.

    PTM databases

    iPTMnetiP08411.
    SwissPalmiP08411.

    Expressioni

    Inductioni

    Viral replication produces dsRNA in the late phsae of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A. This inactivates completely cellular translation initiation, resulting in a dramatic shutoff of proteins synthesis. Translation of viral non-structural polyprotein and all cellular proteins are stopped in infected cell between 2 and 4 hours post infection. Only the 26S mRNA is still translated into viral structural proteins, presumably through a unique mechanism of enhancer element which counteract the translation inhibition mediated by EIF2A. By doing this, the virus uses the cellular defense for its own advantage: shutoff of cellular translation allows to produce big amounts of structural proteins needed for the virus to bud out of the doomed cell.2 Publications

    Interactioni

    Subunit structurei

    P123 interacts with nsP4; nsP1, nsP2, nsP3 and nsP4 interact with each other, and with uncharacterized host factors.

    Protein-protein interaction databases

    ELMiP08411.

    Structurei

    Secondary structure

    12432
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi246 – 259Combined sources14
    Beta strandi1786 – 1789Combined sources4
    Helixi1794 – 1799Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FW5NMR-A245-264[»]
    5DRVX-ray2.75B1785-1792[»]
    5FW5X-ray1.92C1785-1809[»]
    ProteinModelPortaliP08411.
    SMRiP08411.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08411.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini29 – 260Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
    Domaini692 – 844(+)RNA virus helicase ATP-bindingAdd BLAST153
    Domaini845 – 993(+)RNA virus helicase C-terminalAdd BLAST149
    Domaini1006 – 1329Peptidase C9PROSITE-ProRule annotationAdd BLAST324
    Domaini1337 – 1495MacroPROSITE-ProRule annotationAdd BLAST159
    Domaini2182 – 2297RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni245 – 264nsP1 membrane-bindingAdd BLAST20
    Regioni1007 – 1026Nucleolus localization signalAdd BLAST20

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi1184 – 1188Nuclear localization signal5

    Phylogenomic databases

    OrthoDBiVOG09000007.

    Family and domain databases

    InterProiView protein in InterPro
    IPR027351. (+)RNA_virus_helicase_core_dom.
    IPR002588. Alphavirus-like_MT_dom.
    IPR002620. Alphavirus_nsp2pro.
    IPR002589. Macro_dom.
    IPR027417. P-loop_NTPase.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR001788. Tymovirus_RNA-dep_RNA_pol.
    PfamiView protein in Pfam
    PF01661. Macro. 1 hit.
    PF01707. Peptidase_C9. 1 hit.
    PF00978. RdRP_2. 1 hit.
    PF01443. Viral_helicase1. 1 hit.
    PF01660. Vmethyltransf. 1 hit.
    SMARTiView protein in SMART
    SM00506. A1pp. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiView protein in PROSITE
    PS51743. ALPHAVIRUS_MT. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51520. NSP2PRO. 1 hit.
    PS51657. PSRV_HELICASE. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08411-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAKVHVDIE ADSPFIKSLQ KAFPSFEVES LQVTPNDHAN ARAFSHLATK
    60 70 80 90 100
    LIEQETDKDT LILDIGSAPS RRMMSTHKYH CVCPMRSAED PERLVCYAKK
    110 120 130 140 150
    LAAASGKVLD REIAGKITDL QTVMATPDAE SPTFCLHTDV TCRTAAEVAV
    160 170 180 190 200
    YQDVYAVHAP TSLYHQAMKG VRTAYWIGFD TTPFMFDALA GAYPTYATNW
    210 220 230 240 250
    ADEQVLQARN IGLCAASLTE GRLGKLSILR KKQLKPCDTV MFSVGSTLYT
    260 270 280 290 300
    ESRKLLRSWH LPSVFHLKGK QSFTCRCDTI VSCEGYVVKK ITMCPGLYGK
    310 320 330 340 350
    TVGYAVTYHA EGFLVCKTTD TVKGERVSFP VCTYVPSTIC DQMTGILATD
    360 370 380 390 400
    VTPEDAQKLL VGLNQRIVVN GRTQRNTNTM KNYLLPIVAV AFSKWAREYK
    410 420 430 440 450
    ADLDDEKPLG VRERSLTCCC LWAFKTRKMH TMYKKPDTQT IVKVPSEFNS
    460 470 480 490 500
    FVIPSLWSTG LAIPVRSRIK MLLAKKTKRE LIPVLDASSA RDAEQEEKER
    510 520 530 540 550
    LEAELTREAL PPLVPIAPAE TGVVDVDVEE LEYHAGAGVV ETPRSALKVT
    560 570 580 590 600
    AQPNDVLLGN YVVLSPQTVL KSSKLAPVHP LAEQVKIITH NGRAGRYQVD
    610 620 630 640 650
    GYDGRVLLPC GSAIPVPEFQ ALSESATMVY NEREFVNRKL YHIAVHGPSL
    660 670 680 690 700
    NTDEENYEKV RAERTDAEYV FDVDKKCCVK REEASGLVLV GELTNPPFHE
    710 720 730 740 750
    FAYEGLKIRP SAPYKTTVVG VFGVPGSGKS AIIKSLVTKH DLVTSGKKEN
    760 770 780 790 800
    CQEIVNDVKK HRGLDIQAKT VDSILLNGCR RAVDILYVDE AFACHSGTLL
    810 820 830 840 850
    ALIALVKPRS KVVLCGDPKQ CGFFNMMQLK VNFNHNICTE VCHKSISRRC
    860 870 880 890 900
    TRPVTAIVST LHYGGKMRTT NPCNKPIIID TTGQTKPKPG DIVLTCFRGW
    910 920 930 940 950
    VKQLQLDYRG HEVMTAAASQ GLTRKGVYAV RQKVNENPLY APASEHVNVL
    960 970 980 990 1000
    LTRTEDRLVW KTLAGDPWIK VLSNIPQGNF TATLEEWQEE HDKIMKVIEG
    1010 1020 1030 1040 1050
    PAAPVDAFQN KANVCWAKSL VPVLDTAGIR LTAEEWSTII TAFKEDRAYS
    1060 1070 1080 1090 1100
    PVVALNEICT KYYGVDLDSG LFSAPKVSLY YENNHWDNRP GGRMYGFNAA
    1110 1120 1130 1140 1150
    TAARLEARHT FLKGQWHTGK QAVIAERKIQ PLSVLDNVIP INRRLPHALV
    1160 1170 1180 1190 1200
    AEYKTVKGSR VEWLVNKVRG YHVLLVSEYN LALPRRRVTW LSPLNVTGAD
    1210 1220 1230 1240 1250
    RCYDLSLGLP ADAGRFDLVF VNIHTEFRIH HYQQCVDHAM KLQMLGGDAL
    1260 1270 1280 1290 1300
    RLLKPGGSLL MRAYGYADKI SEAVVSSLSR KFSSARVLRP DCVTSNTEVF
    1310 1320 1330 1340 1350
    LLFSNFDNGK RPSTLHQMNT KLSAVYAGEA MHTAGCAPSY RVKRADIATC
    1360 1370 1380 1390 1400
    TEAAVVNAAN ARGTVGDGVC RAVAKKWPSA FKGAATPVGT IKTVMCGSYP
    1410 1420 1430 1440 1450
    VIHAVAPNFS ATTEAEGDRE LAAVYRAVAA EVNRLSLSSV AIPLLSTGVF
    1460 1470 1480 1490 1500
    SGGRDRLQQS LNHLFTAMDA TDADVTIYCR DKSWEKKIQE AIDMRTAVEL
    1510 1520 1530 1540 1550
    LNDDVELTTD LVRVHPDSSL VGRKGYSTTD GSLYSYFEGT KFNQAAIDMA
    1560 1570 1580 1590 1600
    EILTLWPRLQ EANEQICLYA LGETMDNIRS KCPVNDSDSS TPPRTVPCLC
    1610 1620 1630 1640 1650
    RYAMTAERIA RLRSHQVKSM VVCSSFPLPK YHVDGVQKVK CEKGLLFDPT
    1660 1670 1680 1690 1700
    VPSVVSPRKY AASTTDHSDR SLRGFDLDWT TDSSSTASDT MSLPSLQSCD
    1710 1720 1730 1740 1750
    IDSIYEPMAP IVVTADVHPE PAGIADLAAD VHPEPADHVD LENPIPPPRP
    1760 1770 1780 1790 1800
    KRAAYLASRA AERPVPAPRK PTPAPRTAFR NKLPLTFGDF DEHEVDALAS
    1810 1820 1830 1840 1850
    GITFGDFDDV LRLGRAGAYI FSSDTGSGHL QQKSVRQHNL QCAQLDAVEE
    1860 1870 1880 1890 1900
    EKMYPPKLDT EREKLLLLKM QMHPSEANKS RYQSRKVENM KATVVDRLTS
    1910 1920 1930 1940 1950
    GARLYTGADV GRIPTYAVRY PRPVYSPTVI ERFSSPDVAI AACNEYLSRN
    1960 1970 1980 1990 2000
    YPTVASYQIT DEYDAYLDMV DGSDSCLDRA TFCPAKLRCY PKHHAYHQPT
    2010 2020 2030 2040 2050
    VRSAVPSPFQ NTLQNVLAAA TKRNCNVTQM RELPTMDSAV FNVECFKRYA
    2060 2070 2080 2090 2100
    CSGEYWEEYA KQPIRITTEN ITTYVTKLKG PKAAALFAKT HNLVPLQEVP
    2110 2120 2130 2140 2150
    MDRFTVDMKR DVKVTPGTKH TEERPKVQVI QAAEPLATAY LCGIHRELVR
    2160 2170 2180 2190 2200
    RLNAVLRPNV HTLFDMSAED FDAIIASHFH PGDPVLETDI ASFDKSQDDS
    2210 2220 2230 2240 2250
    LALTGLMILE DLGVDQYLLD LIEAAFGEIS SCHLPTGTRF KFGAMMKSGM
    2260 2270 2280 2290 2300
    FLTLFINTVL NITIASRVLE QRLTDSACAA FIGDDNIVHG VISDKLMAER
    2310 2320 2330 2340 2350
    CASWVNMEVK IIDAVMGEKP PYFCGGFIVF DSVTQTACRV SDPLKRLFKL
    2360 2370 2380 2390 2400
    GKPLTAEDKQ DEDRRRALSD EVSKWFRTGL GAELEVALTS RYEVEGCKSI
    2410 2420 2430
    LIAMATLARD IKAFKKLRGP VIHLYGGPRL VR
    Length:2,432
    Mass (Da):269,512
    Last modified:March 21, 2006 - v2
    Checksum:iBE7104A1EC3EF6EE
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti6H → Y in strain: Isolate L10. 1
    Natural varianti95 – 96VC → DS in strain: Isolate Garoff/Takkinen. 2
    Natural varianti119D → N in strain: Isolate Ts14. 1
    Natural varianti311E → K in strain: Isolate L10. 1
    Natural varianti529E → D in strain: Isolate Ts10. 1
    Natural varianti596R → G in strain: Isolate Garoff/Takkinen. 1
    Natural varianti764 – 771LDIQAKTV → KGTSRENS in strain: Isolate Garoff/Takkinen. 8
    Natural varianti764 – 771LDIQAKTV → NWTSRKNS in strain: Isolate L10. 8
    Natural varianti817D → N in strain: Isolate L10. 1
    Natural varianti826M → T in strain: Isolate L10. 1
    Natural varianti843H → N in strain: Isolate L10. 1
    Natural varianti845S → N in strain: Isolate Ts1. 1
    Natural varianti859S → C in strain: Isolate L10. 1
    Natural varianti869T → S in strain: Isolate Ts13. 1
    Natural varianti901V → A in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1114G → R in strain: Isolate Ts11. 1
    Natural varianti1199A → T in strain: Isolate Ts6. 1
    Natural varianti1258 – 1259SL → I in strain: Isolate Garoff/Takkinen and Isolate L10. 2
    Natural varianti1384A → E in strain: Isolate L10 clone SFV4. 1
    Natural varianti1565Q → R in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1579R → G in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1644G → V in strain: Isolate Garoff/Takkinen, Isolate L10 and Isolate L10 clone SFV4. 1
    Natural varianti1849E → Q in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1921P → R in strain: Isolate L10. 1
    Natural varianti1938V → A in strain: Isolate L10. 1
    Natural varianti2060A → V in strain: Isolate Ts13. 1
    Natural varianti2088A → D in strain: Isolate L10. 1
    Natural varianti2405A → T in strain: Isolate Garoff/Takkinen. 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X04129 Genomic RNA. Translation: CAA27741.1.
    AJ251359 Genomic RNA. Translation: CAB62256.1.
    AY112987 Genomic RNA. Translation: AAM64226.1.
    DQ189079 Genomic RNA. Translation: ABA29023.1.
    DQ189080 Genomic RNA. Translation: ABA29024.1.
    DQ189081 Genomic RNA. Translation: ABA29025.1.
    DQ189082 Genomic RNA. Translation: ABA29026.1.
    DQ189083 Genomic RNA. Translation: ABA29028.1.
    DQ189084 Genomic RNA. Translation: ABA29029.1.
    DQ189085 Genomic RNA. Translation: ABA29031.1.
    DQ189086 Genomic RNA. Translation: ABA29032.1.
    PIRiA23592. MNWVSF.
    RefSeqiNP_463457.1. NC_003215.1.

    Genome annotation databases

    GeneIDi922350.
    KEGGivg:922350.

    Keywords - Coding sequence diversityi

    RNA suppression of termination

    Similar proteinsi

    Entry informationi

    Entry nameiPOLN_SFV
    AccessioniPrimary (citable) accession number: P08411
    Secondary accession number(s): Q3LRQ3
    , Q3LRQ4, Q3LRQ6, Q3LRQ7, Q3LRQ9, Q3LRR0, Q3LRR1, Q3LRR2, Q8JMP6, Q9QBM1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: March 21, 2006
    Last modified: October 25, 2017
    This is version 150 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Caution

    There is no stop codon readthrough before nsp4.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references