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Protein

Non-structural polyprotein

Gene
N/A
Organism
Chikungunya virus (strain S27-African prototype) (CHIKV)
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 (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 (By similarity). 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 similarity1 Publication
nsP3 is 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 (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 sitei1013For cysteine protease nsP2 activityPROSITE-ProRule annotation1
Active sitei1083For 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

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
OrganismiChikungunya virus (strain S27-African prototype) (CHIKV)
Taxonomic identifieri371094 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes furcifer (Mosquito) [TaxID: 299627]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Cercopithecus [TaxID: 9533]
Homo sapiens (Human) [TaxID: 9606]
Macaca (macaques) [TaxID: 9539]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Papio (baboons) [TaxID: 9554]
Presbytis [TaxID: 9573]
Proteomesi
  • UP000000569 Componenti: Genome

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003083951 – 2474Non-structural polyproteinAdd BLAST2474
ChainiPRO_00002277601 – 1863P123By similarityAdd BLAST1863
ChainiPRO_00002277611 – 535mRNA-capping enzyme nsP1By similarityAdd BLAST535
ChainiPRO_0000227762536 – 1333Protease nsP2By similarityAdd BLAST798
ChainiPRO_00002277631334 – 1863Non-structural protein 3By similarityAdd BLAST530
ChainiPRO_00002277641864 – 2474RNA-directed RNA polymerase nsP4By similarityAdd BLAST611

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi417S-palmitoyl cysteine; by hostBy similarity1
Lipidationi419S-palmitoyl cysteine; by hostBy similarity1

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 (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
Sitei1333 – 1334Cleavage; by nsP2By similarity2
Sitei1863 – 1864Cleavage; by nsP2By similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ8JUX6.

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.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

12474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1013 – 1024Combined sources12
Helixi1031 – 1037Combined sources7
Helixi1039 – 1042Combined sources4
Helixi1049 – 1061Combined sources13
Helixi1065 – 1067Combined sources3
Beta strandi1075 – 1079Combined sources5
Beta strandi1088 – 1094Combined sources7
Helixi1097 – 1106Combined sources10
Helixi1108 – 1110Combined sources3
Beta strandi1119 – 1121Combined sources3
Turni1122 – 1125Combined sources4
Beta strandi1126 – 1129Combined sources4
Helixi1160 – 1163Combined sources4
Beta strandi1169 – 1177Combined sources9
Beta strandi1184 – 1191Combined sources8
Beta strandi1198 – 1201Combined sources4
Helixi1203 – 1205Combined sources3
Helixi1209 – 1211Combined sources3
Beta strandi1214 – 1220Combined sources7
Helixi1229 – 1246Combined sources18
Helixi1247 – 1250Combined sources4
Beta strandi1251 – 1261Combined sources11
Helixi1267 – 1277Combined sources11
Beta strandi1280 – 1286Combined sources7
Beta strandi1297 – 1304Combined sources8
Helixi1314 – 1323Combined sources10
Beta strandi1337 – 1342Combined sources6
Helixi1344 – 1346Combined sources3
Beta strandi1352 – 1355Combined sources4
Helixi1365 – 1373Combined sources9
Helixi1375 – 1378Combined sources4
Beta strandi1388 – 1393Combined sources6
Beta strandi1396 – 1401Combined sources6
Turni1406 – 1408Combined sources3
Helixi1411 – 1432Combined sources22
Beta strandi1435 – 1440Combined sources6
Helixi1445 – 1447Combined sources3
Helixi1454 – 1465Combined sources12
Beta strandi1470 – 1477Combined sources8
Helixi1479 – 1490Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GPGX-ray1.65A/B/C/D1334-1493[»]
3GPOX-ray1.90A/B/C/D1334-1493[»]
3GPQX-ray2.00A/B/C/D1334-1493[»]
3TRKX-ray2.40A1006-1326[»]
4TU0X-ray2.30A/B/C/D1334-1493[»]
5I22NMR-B1728-1744[»]
ProteinModelPortaliQ8JUX6.
SMRiQ8JUX6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8JUX6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 259Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
Domaini690 – 842(+)RNA virus helicase ATP-bindingAdd BLAST153
Domaini843 – 991(+)RNA virus helicase C-terminalAdd BLAST149
Domaini1004 – 1327Peptidase C9PROSITE-ProRule annotationAdd BLAST324
Domaini1334 – 1493MacroPROSITE-ProRule annotationAdd BLAST160
Domaini2228 – 2343RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 263nsP1 membrane-bindingBy similarityAdd BLAST20
Regioni1005 – 1024Nucleolus localization signalBy similarityAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1182 – 1186Nuclear 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.

Q8JUX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPVYVDIDA DSAFLKALQR AYPMFEVEPR QVTPNDHANA RAFSHLAIKL
60 70 80 90 100
IEQEIDPDST ILDIGSAPAR RMMSDRKYHC VCPMRSAEDP ERLANYARKL
110 120 130 140 150
ASAAGKVLDR NISGKIGDLQ AVMAVPDTET PTFCLHTDVS CRQRADVAIY
160 170 180 190 200
QDVYAVHAPT SLYHQAIKGV RLAYWVGFDT TPFMYNAMAG AYPSYSTNWA
210 220 230 240 250
DEQVLKAKNI GLCSTDLTEG RRGKLSIMRG KKLEPCDRVL FSVGSTLYPE
260 270 280 290 300
SRKLLKSWHL PSVFHLKGKL SFTCRCDTVV SCEGYVVKRI TMSPGLYGKT
310 320 330 340 350
TGYAVTHHAD GFLMCKTTDT VDGERVSFSV CTYVPATICD QMTGILATEV
360 370 380 390 400
TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYMIPVVAQA FSKWAKECRK
410 420 430 440 450
DMEDEKLLGV RERTLTCCCL WAFKKQKTHT VYKRPDTQSI QKVQAEFDSF
460 470 480 490 500
VVPSLWSSGL SIPLRTRIKW LLSKVPKTDL TPYSGDAQEA RDAEKEAEEE
510 520 530 540 550
REAELTLEAL PPLQAAQEDV QVEIDVEQLE DRAGAGIIET PRGAIKVTAQ
560 570 580 590 600
PTDHVVGEYL VLSPQTVLRS QKLSLIHALA EQVKTCTHSG RAGRYAVEAY
610 620 630 640 650
DGRVLVPSGY AISPEDFQSL SESATMVYNE REFVNRKLHH IAMHGPALNT
660 670 680 690 700
DEESYELVRA ERTEHEYVYD VDQRRCCKKE EAAGLVLVGD LTNPPYHEFA
710 720 730 740 750
YEGLKIRPAC PYKIAVIGVF GVPGSGKSAI IKNLVTRQDL VTSGKKENCQ
760 770 780 790 800
EITTDVMRQR GLEISARTVD SLLLNGCNRP VDVLYVDEAF ACHSGTLLAL
810 820 830 840 850
IALVRPRQKV VLCGDPKQCG FFNMMQMKVN YNHNICTQVY HKSISRRCTL
860 870 880 890 900
PVTAIVSSLH YEGKMRTTNE YNKPIVVDTT GSTKPDPGDL VLTCFRGWVK
910 920 930 940 950
QLQIDYRGHE VMTAAASQGL TRKGVYAVRQ KVNENPLYAS TSEHVNVLLT
960 970 980 990 1000
RTEGKLVWKT LSGDPWIKTL QNPPKGNFKA TIKEWEVEHA SIMAGICSHQ
1010 1020 1030 1040 1050
MTFDTFQNKA NVCWAKSLVP ILETAGIKLN DRQWSQIIQA FKEDKAYSPE
1060 1070 1080 1090 1100
VALNEICTRM YGVDLDSGLF SKPLVSVYYA DNHWDNRPGG KMFGFNPEAA
1110 1120 1130 1140 1150
SILERKYPFT KGKWNINKQI CVTTRRIEDF NPTTNIIPAN RRLPHSLVAE
1160 1170 1180 1190 1200
HRPVKGERME WLVNKINGHH VLLVSGCSLA LPTKRVTWVA PLGVRGADYT
1210 1220 1230 1240 1250
YNLELGLPAT LGRYDLVVIN IHTPFRIHHY QQCVDHAMKL QMLGGDSLRL
1260 1270 1280 1290 1300
LKPGGSLLIR AYGYADRTSE RVICVLGRKF RSSRALKPPC VTSNTEMFFL
1310 1320 1330 1340 1350
FSNFDNGRRN FTTHVMNNQL NAAFVGQATR AGCAPSYRVK RMDIAKNDEE
1360 1370 1380 1390 1400
CVVNAANPRG LPGDGVCKAV YKKWPESFKN SATPVGTAKT VMCGTYPVIH
1410 1420 1430 1440 1450
AVGPNFSNYS ESEGDRELAA AYREVAKEVT RLGVNSVAIP LLSTGVYSGG
1460 1470 1480 1490 1500
KDRLTQSLNH LFTAMDSTDA DVVIYCRDKE WEKKISEAIQ MRTQVELLDE
1510 1520 1530 1540 1550
HISIDCDVVR VHPDSSLAGR KGYSTTEGAL YSYLEGTRFH QTAVDMAEIY
1560 1570 1580 1590 1600
TMWPKQTEAN EQVCLYALGE SIESIRQKCP VDDADASSPP KTVPCLCRYA
1610 1620 1630 1640 1650
MTPERVTRLR MNHVTSIIVC SSFPLPKYKI EGVQKVKCSK VMLFDHNVPS
1660 1670 1680 1690 1700
RVSPREYRPS QESVQEASTT TSLTHSQFDL SVDGKILPVP SDLDADAPAL
1710 1720 1730 1740 1750
EPALDDGAIH TLPSATGNLA AVSDWVMSTV PVAPPRRRRG RNLTVTCDER
1760 1770 1780 1790 1800
EGNITPMASV RFFRAELCPV VQETAETRDT AMSLQAPPST ATELSHPPIS
1810 1820 1830 1840 1850
FGAPSETFPI TFGDFNEGEI ESLSSELLTF GDFLPGEVDD LTDSDWSTCS
1860 1870 1880 1890 1900
DTDDELRLDR AGGYIFSSDT GPGHLQQKSV RQSVLPVNTL EEVHEEKCYP
1910 1920 1930 1940 1950
PKLDEAKEQL LLKKLQESAS MANRSRYQSR KVENMKATII QRLKRGCRLY
1960 1970 1980 1990 2000
LMSETPKVPT YRTTYPAPVY SPPINVRLSN PESAVAACNE FLARNYPTVS
2010 2020 2030 2040 2050
SYQITDEYDA YLDMVDGSES CLDRATFNPS KLRSYPKQHA YHAPSIRSAV
2060 2070 2080 2090 2100
PSPFQNTLQN VLAAATKRNC NVTQMRELPT LDSAVFNVEC FKKFACNQEY
2110 2120 2130 2140 2150
WEEFAASPIR ITTENLTTYV TKLKGPKAAA LFAKTHNLLP LQEVPMDRFT
2160 2170 2180 2190 2200
VDMKRDVKVT PGTKHTEERP KVQVIQAAEP LATAYLCGIH RELVRRLNAV
2210 2220 2230 2240 2250
LLPNVHTLFD MSAEDFDAII AAHFKPGDTV LETDIASFDK SQDDSLALTA
2260 2270 2280 2290 2300
LMLLEDLGVD HSLLDLIEAA FGEISSCHLP TGTRFKFGAM MKSGMFLTLF
2310 2320 2330 2340 2350
VNTLLNITIA SRVLEDRLTK SACAAFIGDD NIIHGVVSDE LMAARCATWM
2360 2370 2380 2390 2400
NMEVKIIDAV VSQKAPYFCG GFILHDIVTG TACRVADPLK RLFKLGKPLA
2410 2420 2430 2440 2450
AGDEQDEDRR RALADEVVRW QRTGLIDELE KAVYSRYEVQ GISVVVMSMA
2460 2470
TFASSRSNFE KLRGPVVTLY GGPK
Length:2,474
Mass (Da):275,652
Last modified:October 1, 2002 - v1
Checksum:i97D250B9EB5A3BB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF369024 Genomic RNA. Translation: AAN05101.1.
RefSeqiNP_690588.1. NC_004162.2.

Genome annotation databases

GeneIDi956309.
KEGGivg:956309.

Keywords - Coding sequence diversityi

RNA suppression of termination

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF369024 Genomic RNA. Translation: AAN05101.1.
RefSeqiNP_690588.1. NC_004162.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GPGX-ray1.65A/B/C/D1334-1493[»]
3GPOX-ray1.90A/B/C/D1334-1493[»]
3GPQX-ray2.00A/B/C/D1334-1493[»]
3TRKX-ray2.40A1006-1326[»]
4TU0X-ray2.30A/B/C/D1334-1493[»]
5I22NMR-B1728-1744[»]
ProteinModelPortaliQ8JUX6.
SMRiQ8JUX6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC09.001.

Proteomic databases

PRIDEiQ8JUX6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956309.
KEGGivg:956309.

Miscellaneous databases

EvolutionaryTraceiQ8JUX6.

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_CHIKS
AccessioniPrimary (citable) accession number: Q8JUX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [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
  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.