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Protein

Non-structural polyprotein

Gene
N/A
Organism
Venezuelan equine encephalitis virus (strain P676) (VEEV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

P123 and P123' are short-lived polyproteins, accumulating during early stage of infection. P123 is directly translated from the genome, whereas P123' is a product of the cleavage of P1234. They localize the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, they start viral genome replication into antigenome. After these early events, P123 and P123' are cleaved sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex (By similarity).By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity
nsP3 and nsP3' are essential for minus strand and subgenomic 26S mRNA synthesis.By similarity
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. nsP4 is a short-lived protein regulated by several ways: the opal codon readthrough and degradation by ubiquitin pathway (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + GTP = m7GTP.
m7GTP + (5')pp-Pur-mRNA = diphosphate + m7G(5')ppp-Pur-mRNA.
(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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1012For cysteine protease nsP2 activityPROSITE-ProRule annotation1
Active sitei1081For cysteine protease nsP2 activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi721 – 728ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

Keywords - Biological processi

Eukaryotic 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

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural polyprotein
Alternative name(s):
Polyprotein nsP1234
Short name:
P1234
Cleaved into the following 7 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
Non-structural protein 3'
Short name:
nsP3'
Alternative name(s):
Non-structural protein 4
Short name:
nsP4
OrganismiVenezuelan equine encephalitis virus (strain P676) (VEEV)
Taxonomic identifieri36385 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusVEEV complex
Virus hostiBos 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
  • UP000008658 Componenti: Genome

Subcellular locationi

Non-structural polyprotein :
P123 :
P123' :
mRNA-capping enzyme nsP1 :
Protease nsP2 :
Non-structural protein 3 :
Non-structural protein 3' :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003083901 – 2492Non-structural polyproteinAdd BLAST2492
ChainiPRO_00002287671 – 1885P123'Add BLAST1885
ChainiPRO_00002287681 – 1879P123Add BLAST1879
ChainiPRO_00000412041 – 535mRNA-capping enzyme nsP1Add BLAST535
ChainiPRO_0000041205536 – 1329Protease nsP2Add BLAST794
ChainiPRO_00002287691330 – 1885Non-structural protein 3'Add BLAST556
ChainiPRO_00000412061330 – 1879Non-structural protein 3Add BLAST550
ChainiPRO_00000412071886 – 2492RNA-directed RNA polymerase nsP4Add BLAST607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi419S-palmitoyl cysteine; by hostBy similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The polyprotein is synthesized as P123, or P1234 by stop codon readthrough. These polyproteins are 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/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 the P23/P23' polyprotein. Cleavage of nsP1 exposes an 'activator' at the N-terminus of P23/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 (By similarity).By similarity
nsP1 is palmitoylated by host.By similarity
nsP4 is ubiquitinated; targets the protein for rapid degradation via the ubiquitin system.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei535 – 536Cleavage; by nsP2By similarity2
Sitei1329 – 1330Cleavage; by nsP2By similarity2
Sitei1885 – 1886Cleavage; by nsP2By similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP36328.

Expressioni

Inductioni

Viral replication produces dsRNA in the late phase 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.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

12492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1332 – 1338Combined sources7
Helixi1340 – 1342Combined sources3
Beta strandi1345 – 1352Combined sources8
Helixi1361 – 1363Combined sources3
Helixi1365 – 1369Combined sources5
Helixi1371 – 1373Combined sources3
Beta strandi1384 – 1387Combined sources4
Beta strandi1394 – 1398Combined sources5
Turni1402 – 1404Combined sources3
Helixi1407 – 1427Combined sources21
Beta strandi1431 – 1436Combined sources6
Helixi1450 – 1461Combined sources12
Beta strandi1467 – 1473Combined sources7
Helixi1475 – 1487Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GQEX-ray2.30A/B1330-1489[»]
3GQOX-ray2.60A/B/C/D1330-1489[»]
ProteinModelPortaliP36328.
SMRiP36328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36328.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 259Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
Domaini690 – 841(+)RNA virus helicase ATP-bindingAdd BLAST152
Domaini842 – 990(+)RNA virus helicase C-terminalAdd BLAST149
Domaini1003 – 1322Peptidase C9PROSITE-ProRule annotationAdd BLAST320
Domaini1330 – 1489MacroPROSITE-ProRule annotationAdd BLAST160
Domaini2249 – 2364RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 263nsP1 membrane-bindingBy similarityAdd BLAST20
Regioni1004 – 1023Nucleolus localization signalBy similarityAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1179 – 1183Nuclear localization signalBy similarity5

Sequence similaritiesi

Contains 1 alphavirus-like MT (methyltransferase) domain.PROSITE-ProRule annotation
Contains 1 Macro domain.PROSITE-ProRule annotation
Contains 1 peptidase C9 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027351. (+)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.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
PF01707. Peptidase_C9. 1 hit.
PF00978. RdRP_2. 1 hit.
PF01443. Viral_helicase1. 1 hit.
PF01660. Vmethyltransf. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51743. ALPHAVIRUS_MT. 1 hit.
PS51154. MACRO. 1 hit.
PS51520. NSP2PRO. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36328-1 [UniParc]FASTAAdd to basket

« Hide

        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 LITAEDIQEA KCAADEAKEV
510 520 530 540 550
REAEELRAAL PPLAADFEEP 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 DKRMRTTNPK ETKIVIDTTG STKPKQDDLI LTCFRGWVKQ
910 920 930 940 950
LQIDYKGNEI MTAAASQGLT RKGVYAVRYK VNENPLYAPT SEHVNVLLTR
960 970 980 990 1000
TEDRIVWKTL AGDPWIKILT 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 KKVDWLSDQP EATFRARLDL
1210 1220 1230 1240 1250
GIPGDVPKYD IVFINVRTPY KYHHYQQCED HAIKLSMLTK KACLHLNPGG
1260 1270 1280 1290 1300
TCVSIGYGYA DRASESIIGA IARQFKFSRV CKPKSSHEET 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 ETPPVEETPE SPAENQSTEG TPEQPALVNV DATRTRMPEP
1710 1720 1730 1740 1750
IIIEEEEEDS ISLLSDGPTH QVLQVEADIH GSPSVSSSSW SIPHASDFDV
1760 1770 1780 1790 1800
DSLSILDTLD GASVTSGAVS AETNSYFARS MEFRARPVPA PRTVFRNPPH
1810 1820 1830 1840 1850
PAPRTRTPPL AHSRASSRTS LVSTPPGVNR VITREELEAL TPSRAPSRSA
1860 1870 1880 1890 1900
SRTSLVSNPP GVNRVITREE FEAFVAQQQR FDAGAYIFSS DTGQGHLQQK
1910 1920 1930 1940 1950
SVRQTVLSEV VLERTELEIS YAPRLDQEKE ELLRKKLQLN PTPANRSRYQ
1960 1970 1980 1990 2000
SRRVENMKAI TARRILQGLG HYLKAEGKVE CYRTLHPVPL YSSSVNRAFS
2010 2020 2030 2040 2050
SPKVAVEACN AMLKENFPTV ASYCIIPEYD AYLDMVDGAS CCLDTASFCP
2060 2070 2080 2090 2100
AKLRSFPKKH SYLEPTIRSA VPSAIQNTLQ NVLAAATKRN CNVTQMRELP
2110 2120 2130 2140 2150
VLDSAAFNVE CFKKYACNNE YWETFKENPI RLTEENVVNY ITKLKGPKAA
2160 2170 2180 2190 2200
ALFAKTHNLN MLQDIPMDRF VMDLKRDVKV TPGTKHTEER PKVQVIQAAD
2210 2220 2230 2240 2250
PLATADLCGI HRELVRRLNA VLLPNIHTLF DMSAEDFDAI IAEHFQPGDC
2260 2270 2280 2290 2300
VLETDIASFD KSEDDAMALT ALMILEDLGV DAELLTLIEA AFGEISSIHL
2310 2320 2330 2340 2350
PTKTKFKFGA MMKSGMFLTL FVNTVINIVI ASRVLRERLT GSPCAAFIGD
2360 2370 2380 2390 2400
DNIVKGVKSD KLMADRCATW LNMEVKIIDA VVGEKAPYFC GGFILCDSVT
2410 2420 2430 2440 2450
GTACRVADPL KRLFKLGKPL AVDDEHDDDR RRALHEESTR WNRVGILPEL
2460 2470 2480 2490
CKAVESRYET VGTSIIVMAM TTLASSVKSF SYLRGAPITL YG
Length:2,492
Mass (Da):277,839
Last modified:June 1, 1994 - v1
Checksum:iE55D056CD7AED6EE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti875V → E in strain: 3908, 6119, 254934, PMCHo5 and V198. 1
Natural varianti968I → T in strain: 3908, 6119, 254934, PMCHo5 and V198. 1
Natural varianti1390 – 1391AA → VT in strain: 3908, 6119, 254934, PMCHo5 and V198. 2
Natural varianti1767 – 1769GAV → EAA in strain: PMCHo5 and V198. 3
Natural varianti1767G → E in strain: 3908, 6119 and 254934. 1
Natural varianti1809P → S in strain: V198. 1
Natural varianti2093V → I in strain: 254934. 1
Natural varianti2206D → Y in strain: 3908, 6119, 254934, PMCHo5 and V198. 1
Natural varianti2422V → A in strain: V198. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04653 Genomic RNA. Translation: AAC19318.1. Sequence problems.
L04653 Genomic RNA. Translation: AAC19320.1.
U55347 Genomic RNA. Translation: AAM28637.1.
AF375051 Genomic RNA. Translation: AAK66989.1.
U55350 Genomic RNA. Translation: AAM28638.1.
AY986475 Genomic RNA. Translation: AAY16369.1.
AY973944 Genomic RNA. Translation: AAY16003.1.
U55345 Genomic RNA. Translation: AAM28636.1.
U55342 Genomic RNA. Translation: AAL61965.1.
PIRiA44213.
RefSeqiNP_040822.1. NC_001449.1.
NP_040823.1. NC_001449.1.

Genome annotation databases

GeneIDi2652923.
2652925.
KEGGivg:2652923.

Keywords - Coding sequence diversityi

RNA suppression of termination

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04653 Genomic RNA. Translation: AAC19318.1. Sequence problems.
L04653 Genomic RNA. Translation: AAC19320.1.
U55347 Genomic RNA. Translation: AAM28637.1.
AF375051 Genomic RNA. Translation: AAK66989.1.
U55350 Genomic RNA. Translation: AAM28638.1.
AY986475 Genomic RNA. Translation: AAY16369.1.
AY973944 Genomic RNA. Translation: AAY16003.1.
U55345 Genomic RNA. Translation: AAM28636.1.
U55342 Genomic RNA. Translation: AAL61965.1.
PIRiA44213.
RefSeqiNP_040822.1. NC_001449.1.
NP_040823.1. NC_001449.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GQEX-ray2.30A/B1330-1489[»]
3GQOX-ray2.60A/B/C/D1330-1489[»]
ProteinModelPortaliP36328.
SMRiP36328.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP36328.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652923.
2652925.
KEGGivg:2652923.

Miscellaneous databases

EvolutionaryTraceiP36328.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027351. (+)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.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
PF01707. Peptidase_C9. 1 hit.
PF00978. RdRP_2. 1 hit.
PF01443. Viral_helicase1. 1 hit.
PF01660. Vmethyltransf. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51743. ALPHAVIRUS_MT. 1 hit.
PS51154. MACRO. 1 hit.
PS51520. NSP2PRO. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLN_EEVVP
AccessioniPrimary (citable) accession number: P36328
Secondary accession number(s): Q52QW0
, Q8JJT2, Q8QKW7, Q8UYL4, Q911J8, Q91KW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The genome codes for P123, but readthrough of a terminator codon UGA occurs between the codons for Gln-1879 and Arg-1880. This readthrough produces P1234, cleaved quickly by nsP2 into P123' and nsP4. Further processing of p123' gives nsP1, nsP2 and nsP3' which is 7 amino acids longer than nsP3 since the cleavage site is after the readthrough. This unusual molecular mechanism ensures that few nsP4 are produced compared to other non-structural proteins. Mutant viruses with no alternative termination site grow significantly slower than wild-type virus (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.