UniProtKB - P27282 (POLN_EEVVT)
Polyprotein P1234
Functioni
Miscellaneous
Catalytic activityi
- [nsP1 protein]-L-histidine + N7-methyl-GTP = [nsP1 protein]-Nτ-(N7-methylguanosine 5'-phospho)-L-histidine + diphosphate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H+ + phosphateBy similarityEC:3.1.3.33By similarity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphateBy similarityEC:3.6.1.15By similarity
- EC:3.6.4.13By similarity
- EC:2.7.7.48PROSITE-ProRule annotation
- 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H+ + L-aspartyl-[protein]1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose + H+ + L-glutamyl-[protein]2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- EC:2.7.7.19By similarity
- EC:3.1.3.84By similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Protein has several cofactor binding sites:- Mg2+By similarity, Mn2+By similarityNote: For nsP4 adenylyltransferase activity; Mn2+ supports catalysis at 60% of the levels observed with Mg2+.By similarity
- Mg2+By similarityNote: For nsP4 RNA-directed RNA polymerase activity.By similarity
- Mg2+1 PublicationNote: For nsP1 guanylylation.1 Publication
- Mg2+Note: For nsP2 RNA triphosphatase activity.By similarity
- Mg2+Note: For nsP2 NTPase activity.By similarity
Activity regulationi
Kineticsi
- KM=110 µM for a 12 residues substrate for nsp2 protease activity1 Publication
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 37 | Involved in the phosphoramide link with 7-methyl-GMP1 Publication | 1 | |
Active sitei | 1012 | For cysteine protease nsP2 activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 1081 | For cysteine protease nsP2 activityPROSITE-ProRule annotation1 Publication | 1 | |
Binding sitei | 1339 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1353 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1361 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1441 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1442 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1443 | ADP-riboseBy similarity | 1 | |
Metal bindingi | 1596 | ZincBy similarity | 1 | |
Metal bindingi | 1598 | ZincBy similarity | 1 | |
Metal bindingi | 1621 | ZincBy similarity | 1 | |
Metal bindingi | 1639 | ZincBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 721 – 728 | NTPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ADP-ribosyl-[dinitrogen reductase] hydrolase activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
- cysteine-type peptidase activity Source: UniProtKB-KW
- GTP binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- mRNA methyltransferase activity Source: InterPro
- polynucleotide 5'-phosphatase activity Source: UniProtKB-EC
- polynucleotide adenylyltransferase activity Source: UniProtKB-EC
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
GO - Biological processi
- 7-methylguanosine mRNA capping Source: UniProtKB
- suppression by virus of host RNA polymerase II activity Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral RNA genome replication Source: InterPro
Keywordsi
Protein family/group databases
MEROPSi | C09.002 |
Names & Taxonomyi
Protein namesi | Recommended name: Polyprotein P1234Short name: P1234 Alternative name(s): Non-structural polyprotein Cleaved into the following 7 chains: mRNA-capping enzyme nsP1 (EC:2.1.1.-1 Publication, EC:2.7.7.-1 Publication) Alternative name(s): Non-structural protein 1 Protease nsP2 (EC:3.1.3.33By similarity, EC:3.4.22.-By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity) Alternative name(s): Non-structural protein 2 Short name: nsP2 RNA-directed RNA polymerase nsP4 (EC:2.7.7.19By similarity, EC:2.7.7.48PROSITE-ProRule annotation) Alternative name(s): Non-structural protein 4 Short name: nsP4 |
Organismi | Venezuelan equine encephalitis virus (strain Trinidad donkey) (VEEV) |
Taxonomic identifieri | 11038 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Martellivirales › Togaviridae › Alphavirus › |
Virus hosti | Bos taurus (Bovine) [TaxID: 9913] Didelphis marsupialis (Southern opossum) [TaxID: 9268] Equus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793] Equus caballus (Horse) [TaxID: 9796] Homo sapiens (Human) [TaxID: 9606] Melanoconion [TaxID: 53535] Philander opossum (Gray four-eyed opossum) [TaxID: 9272] Proechimys [TaxID: 10162] Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415] |
Proteomesi |
|
Subcellular locationi
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.Curated
- Host cytoplasmic vesicle membrane By similarity; Lipid-anchor By similarity
- Host cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
- host filopodium By similarity Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then a fraction of nsP1 localizes to the inner surface of the plasma membrane and its filopodial extensions. Only the palmitoylated nsP1 localizes to the host filopodia (By similarity). NsP1 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity
- Host nucleus 1 Publication
- Host cytoplasm 1 Publication Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then approximately half of nsP2 is found in the nucleus (By similarity). Shuttles between cytoplasm and nucleus (PubMed:17652399). NsP2 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity1 Publication
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3' is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (Probable).By similarityCurated
- Host cytoplasmic vesicle membrane ; Peripheral membrane protein By similarity Note: NsP4 is part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.By similarity
GO - Cellular componenti
- host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- host cell filopodium Source: UniProtKB-SubCell
- host cell nucleus Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB-SubCell
- membrane Source: UniProtKB-KW
Keywords - Cellular componenti
Host cell membrane, Host cell projection, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 37 | H → A: Complete loss of nsP1 guanylylation; increased methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 45 | H → A: Almost no effect on nsP1 guanylylation; 50% loss of methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 63 | D → A: Complete loss of nsP1 guanylylation; 80% loss of methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 118 | E → A: Almost no effect on formation of nsP1 guanylylation. 1 Publication | 1 | |
Mutagenesisi | 285 | Y → A: 85% loss of formation of nsP1 guanylylation; 70% loss of methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 354 | D → A: Increased formation of nsP1 guanylylation; slightly increased methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 365 | R → A: Increased formation of nsP1 guanylylation; slightly increased methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 369 | N → A: 50% loss of formation of nsP1 guanylylation; 50% loss of methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 375 | N → A: 50% loss of formation of nsP1 guanylylation; 40% loss of methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 538 | V → A: Increased viral replication and cytopathogenicity. 1 Publication | 1 | |
Mutagenesisi | 540 | T → A: Increased viral replication and cytopathogenicity. 1 Publication | 1 | |
Mutagenesisi | 1006 | Q → A: Increased viral replication and cytopathogenicity. 1 Publication | 1 | |
Mutagenesisi | 1010 | N → A: 24 fold reduced Kcat/Km for nsP2 protease activity. 1 Publication | 1 | |
Mutagenesisi | 1010 | N → A: NsP2 is in a self-inhibited state. 1 Publication | 1 | |
Mutagenesisi | 1015 | K → A: 9 fold reduced Kcat/Km for nsP2 protease activity. 1 Publication | 1 | |
Mutagenesisi | 1056 | V → A: No effect on nuclear export of nsP2. 1 Publication | 1 | |
Mutagenesisi | 1061 | L → A: Inhibits the nuclear export of nsP2; when associated with Ala-1063. 1 Publication | 1 | |
Mutagenesisi | 1063 | L → A: Inhibits the nuclear export of nsP2; when associated with Ala-1061. 1 Publication | 1 | |
Mutagenesisi | 1181 | K → D: Decreased protease nsP2 nuclear localization. 1 Publication | 1 | |
Mutagenesisi | 1197 | R → A or K: 16 fold reduced Kcat/Km for nsP2 protease activity. 1 Publication | 1 | |
Mutagenesisi | 1248 | P → S: No effect on host shutoff induction by nsP2 at 6h p.i. 1 Publication | 1 | |
Mutagenesisi | 1274 | Q → L: 50% loss of host shutoff induction by nsP2 at 6h p.i. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000308391 | 1 – 2493 | Polyprotein P1234Add BLAST | 2493 | |
ChainiPRO_0000228770 | 1 – 1886 | Polyprotein P123'Add BLAST | 1886 | |
ChainiPRO_0000228771 | 1 – 1879 | Polyprotein P123Add BLAST | 1879 | |
ChainiPRO_0000041208 | 1 – 535 | mRNA-capping enzyme nsP1Add BLAST | 535 | |
ChainiPRO_0000041209 | 536 – 1329 | Protease nsP2Add BLAST | 794 | |
ChainiPRO_0000228772 | 1330 – 1886 | Non-structural protein 3'Add BLAST | 557 | |
ChainiPRO_0000041210 | 1330 – 1879 | Non-structural protein 3Add BLAST | 550 | |
ChainiPRO_0000041211 | 1887 – 2493 | RNA-directed RNA polymerase nsP4Add BLAST | 607 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 419 | S-palmitoyl cysteine; by hostBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 535 – 536 | Cleavage; by protease nsP2By similarity | 2 | |
Sitei | 1329 – 1330 | Cleavage; by protease nsP2By similarity | 2 | |
Sitei | 1886 – 1887 | Cleavage; by protease nsP2By similarity | 2 |
Keywords - PTMi
Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
PRIDEi | P27282 |
Interactioni
Subunit structurei
Interacts with non-structural protein 3 (By similarity).
Interacts with RNA-directed RNA polymerase nsP4 (By similarity).
Interacts with protease nsP2 (By similarity). interacts with itself (By similarity).
By similarityInteracts with mRNA-capping enzyme nsP1 (By similarity).
Interacts with host DDX1 (PubMed:27105836).
Interacts with host DDX3 (PubMed:27105836).
Interacts (via C-terminus) with host FXR1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:27509095).
Interacts (via C-terminus) with host FXR2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:27509095).
Interacts (via C-terminus) with host FMR1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FMR1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:27509095).
By similarity2 PublicationsInteracts with mRNA-capping enzyme nsP1 (By similarity).
Interacts with protease nsP2 (By similarity). interacts with itself (By similarity).
By similarityInteracts with RNA-directed RNA polymerase nsP4 (By similarity).
Interacts with mRNA-capping enzyme nsP1 (By similarity).
Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus (PubMed:17652399).
By similarity1 PublicationStructurei
Secondary structure
3D structure databases
SMRi | P27282 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P27282 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 28 – 259 | Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST | 232 | |
Domaini | 690 – 841 | (+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST | 152 | |
Domaini | 842 – 990 | (+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST | 149 | |
Domaini | 1003 – 1322 | Peptidase C9PROSITE-ProRule annotation1 PublicationAdd BLAST | 320 | |
Domaini | 1330 – 1489 | MacroPROSITE-ProRule annotation1 PublicationAdd BLAST | 160 | |
Repeati | 1818 – 1839 | 11 PublicationAdd BLAST | 22 | |
Repeati | 1852 – 1873 | 21 PublicationAdd BLAST | 22 | |
Domaini | 2250 – 2365 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 116 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 244 – 263 | NsP1 membrane-bindingBy similarityAdd BLAST | 20 | |
Regioni | 1004 – 1023 | Nucleolus localization signalBy similarityAdd BLAST | 20 | |
Regioni | 1818 – 1873 | 2 X 21 AA approximate repeats, binding to host FXR family members1 PublicationAdd BLAST | 56 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1056 – 1065 | Nuclear export signal1 Publication | 10 | |
Motifi | 1179 – 1183 | Nuclear localization signal1 Publication | 5 |
Domaini
Keywords - Domaini
RepeatFamily and domain databases
Gene3Di | 3.40.220.10, 1 hit |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR002588, Alphavirus-like_MT_dom IPR002620, Alphavirus_nsp2pro IPR043502, DNA/RNA_pol_sf IPR002589, Macro_dom IPR043472, Macro_dom-like IPR027417, P-loop_NTPase IPR007094, RNA-dir_pol_PSvirus IPR001788, Tymovirus_RNA-dep_RNA_pol |
Pfami | View 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 |
SMARTi | View protein in SMART SM00506, A1pp, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit SSF52949, SSF52949, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MEKVHVDIEE DSPFLRALQR SFPQFEVEAK QVTDNDHANA RAFSHLASKL
60 70 80 90 100
IETEVDPSDT ILDIGSAPAR RMYSKHKYHC ICPMRCAEDP DRLYKYATKL
110 120 130 140 150
KKNCKEITDK ELDKKMKELA AVMSDPDLET ETMCLHDDES CRYEGQVAVY
160 170 180 190 200
QDVYAVDGPT SLYHQANKGV RVAYWIGFDT TPFMFKNLAG AYPSYSTNWA
210 220 230 240 250
DETVLTARNI GLCSSDVMER SRRGMSILRK KYLKPSNNVL FSVGSTIYHE
260 270 280 290 300
KRDLLRSWHL PSVFHLRGKQ NYTCRCETIV SCDGYVVKRI AISPGLYGKP
310 320 330 340 350
SGYAATMHRE GFLCCKVTDT LNGERVSFPV CTYVPATLCD QMTGILATDV
360 370 380 390 400
SADDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FARWAKEYKE
410 420 430 440 450
DQEDERPLGL RDRQLVMGCC WAFRRHKITS IYKRPDTQTI IKVNSDFHSF
460 470 480 490 500
VLPRIGSNTL EIGLRTRIRK MLEEHKEPSP LITAEDVQEA KCAADEAKEV
510 520 530 540 550
REAEELRAAL PPLAADVEEP TLEADVDLML QEAGAGSVET PRGLIKVTSY
560 570 580 590 600
AGEDKIGSYA VLSPQAVLKS EKLSCIHPLA EQVIVITHSG RKGRYAVEPY
610 620 630 640 650
HGKVVVPEGH AIPVQDFQAL SESATIVYNE REFVNRYLHH IATHGGALNT
660 670 680 690 700
DEEYYKTVKP SEHDGEYLYD IDRKQCVKKE LVTGLGLTGE LVDPPFHEFA
710 720 730 740 750
YESLRTRPAA PYQVPTIGVY GVPGSGKSGI IKSAVTKKDL VVSAKKENCA
760 770 780 790 800
EIIRDVKKMK GLDVNARTVD SVLLNGCKHP VETLYIDEAF ACHAGTLRAL
810 820 830 840 850
IAIIRPKKAV LCGDPKQCGF FNMMCLKVHF NHEICTQVFH KSISRRCTKS
860 870 880 890 900
VTSVVSTLFY DKKMRTTNPK ETKIVIDTTG STKPKQDDLI LTCFRGWVKQ
910 920 930 940 950
LQIDYKGNEI MTAAASQGLT RKGVYAVRYK VNENPLYAPT SEHVNVLLTR
960 970 980 990 1000
TEDRIVWKTL AGDPWIKTLT AKYPGNFTAT IEEWQAEHDA IMRHILERPD
1010 1020 1030 1040 1050
PTDVFQNKAN VCWAKALVPV LKTAGIDMTT EQWNTVDYFE TDKAHSAEIV
1060 1070 1080 1090 1100
LNQLCVRFFG LDLDSGLFSA PTVPLSIRNN HWDNSPSPNM YGLNKEVVRQ
1110 1120 1130 1140 1150
LSRRYPQLPR AVATGRVYDM NTGTLRNYDP RINLVPVNRR LPHALVLHHN
1160 1170 1180 1190 1200
EHPQSDFSSF VSKLKGRTVL VVGEKLSVPG KMVDWLSDRP EATFRARLDL
1210 1220 1230 1240 1250
GIPGDVPKYD IIFVNVRTPY KYHHYQQCED HAIKLSMLTK KACLHLNPGG
1260 1270 1280 1290 1300
TCVSIGYGYA DRASESIIGA IARQFKFSRV CKPKSSLEET EVLFVFIGYD
1310 1320 1330 1340 1350
RKARTHNPYK LSSTLTNIYT GSRLHEAGCA PSYHVVRGDI ATATEGVIIN
1360 1370 1380 1390 1400
AANSKGQPGG GVCGALYKKF PESFDLQPIE VGKARLVKGA AKHIIHAVGP
1410 1420 1430 1440 1450
NFNKVSEVEG DKQLAEAYES IAKIVNDNNY KSVAIPLLST GIFSGNKDRL
1460 1470 1480 1490 1500
TQSLNHLLTA LDTTDADVAI YCRDKKWEMT LKEAVARREA VEEICISDDS
1510 1520 1530 1540 1550
SVTEPDAELV RVHPKSSLAG RKGYSTSDGK TFSYLEGTKF HQAAKDIAEI
1560 1570 1580 1590 1600
NAMWPVATEA NEQVCMYILG ESMSSIRSKC PVEESEASTP PSTLPCLCIH
1610 1620 1630 1640 1650
AMTPERVQRL KASRPEQITV CSSFPLPKYR ITGVQKIQCS QPILFSPKVP
1660 1670 1680 1690 1700
AYIHPRKYLV ETPPVDETPE PSAENQSTEG TPEQPPLITE DETRTRTPEP
1710 1720 1730 1740 1750
IIIEEEEEDS ISLLSDGPTH QVLQVEADIH GPPSVSSSSW SIPHASDFDV
1760 1770 1780 1790 1800
DSLSILDTLE GASVTSGATS AETNSYFAKS MEFLARPVPA PRTVFRNPPH
1810 1820 1830 1840 1850
PAPRTRTPSL APSRACSRTS LVSTPPGVNR VITREELEAL TPSRTPSRSV
1860 1870 1880 1890 1900
SRTSLVSNPP GVNRVITREE FEAFVAQQQX RFDAGAYIFS SDTGQGHLQQ
1910 1920 1930 1940 1950
KSVRQTVLSE VVLERTELEI SYAPRLDQEK EELLRKKLQL NPTPANRSRY
1960 1970 1980 1990 2000
QSRKVENMKA ITARRILQGL GHYLKAEGKV ECYRTLHPVP LYSSSVNRAF
2010 2020 2030 2040 2050
SSPKVAVEAC NAMLKENFPT VASYCIIPEY DAYLDMVDGA SCCLDTASFC
2060 2070 2080 2090 2100
PAKLRSFPKK HSYLEPTIRS AVPSAIQNTL QNVLAAATKR NCNVTQMREL
2110 2120 2130 2140 2150
PVLDSAAFNV ECFKKYACNN EYWETFKENP IRLTEENVVN YITKLKGPKA
2160 2170 2180 2190 2200
AALFAKTHNL NMLQDIPMDR FVMDLKRDVK VTPGTKHTEE RPKVQVIQAA
2210 2220 2230 2240 2250
DPLATAYLCG IHRELVRRLN AVLLPNIHTL FDMSAEDFDA IIAEHFQPGD
2260 2270 2280 2290 2300
CVLETDIASF DKSEDDAMAL TALMILEDLG VDAELLTLIE AAFGEISSIH
2310 2320 2330 2340 2350
LPTKTKFKFG AMMKSGMFLT LFVNTVINIV IASRVLRERL TGSPCAAFIG
2360 2370 2380 2390 2400
DDNIVKGVKS DKLMADRCAT WLNMEVKIID AVVGEKAPYF CGGFILCDSV
2410 2420 2430 2440 2450
TGTACRVADP LKRLFKLGKP LAADDEHDDD RRRALHEEST RWNRVGILSE
2460 2470 2480 2490
LCKAVESRYE TVGTSIIVMA MTTLASSVKS FSYLRGAPIT LYG
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 21 | S → T in AAB02518 (PubMed:2524126).Curated | 1 | |
Sequence conflicti | 497 | A → R in AAB02518 (PubMed:2524126).Curated | 1 | |
Sequence conflicti | 1589 | T → S in AAB02518 (PubMed:2524126).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 222 | R → C in strain: 71-180 and COAN5506. | 1 | |
Natural varianti | 551 | A → D in strain: TC-83. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J04332 Genomic RNA Translation: AAB02518.1 L01442 Genomic RNA Translation: AAC19321.2 L01443 Genomic RNA Translation: AAB02516.1 AF069903 Genomic RNA Translation: AAC24033.1 AY741139 Genomic RNA Translation: AAU89533.1 KR260736 Genomic RNA Translation: ALE15112.1 Different initiation. |
PIRi | A31467, MNWVTD |
Keywords - Coding sequence diversityi
RNA suppression of terminationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J04332 Genomic RNA Translation: AAB02518.1 L01442 Genomic RNA Translation: AAC19321.2 L01443 Genomic RNA Translation: AAB02516.1 AF069903 Genomic RNA Translation: AAC24033.1 AY741139 Genomic RNA Translation: AAU89533.1 KR260736 Genomic RNA Translation: ALE15112.1 Different initiation. |
PIRi | A31467, MNWVTD |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2HWK | X-ray | 2.45 | A | 1003-1322 | [»] | |
5EZQ | X-ray | 1.66 | A | 992-1327 | [»] | |
5EZS | X-ray | 2.16 | A | 992-1327 | [»] | |
6BCM | X-ray | 2.10 | A | 1003-1338 | [»] | |
SMRi | P27282 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | C09.002 |
Proteomic databases
PRIDEi | P27282 |
Miscellaneous databases
EvolutionaryTracei | P27282 |
Family and domain databases
Gene3Di | 3.40.220.10, 1 hit |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR002588, Alphavirus-like_MT_dom IPR002620, Alphavirus_nsp2pro IPR043502, DNA/RNA_pol_sf IPR002589, Macro_dom IPR043472, Macro_dom-like IPR027417, P-loop_NTPase IPR007094, RNA-dir_pol_PSvirus IPR001788, Tymovirus_RNA-dep_RNA_pol |
Pfami | View 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 |
SMARTi | View protein in SMART SM00506, A1pp, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit SSF52949, SSF52949, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLN_EEVVT | |
Accessioni | P27282Primary (citable) accession number: P27282 Secondary accession number(s): A0A0M3T9D8 Q66594 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | April 10, 2019 | |
Last modified: | December 2, 2020 | |
This is version 155 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references