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Q8QZ73

- POLN_MAYAB

UniProt

Q8QZ73 - POLN_MAYAB

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Protein

Non-structural polyprotein

Gene
N/A
Organism
Mayaro virus (strain Brazil) (MAYV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei536 – 5372Cleavage; by nsP2By similarity
Active sitei1014 – 10141For cysteine protease nsP2 activityPROSITE-ProRule annotation
Active sitei1084 – 10841For cysteine protease nsP2 activityPROSITE-ProRule annotation
Sitei1334 – 13352Cleavage; by nsP2By similarity
Sitei1825 – 18262Cleavage; by nsP2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi722 – 7298ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type peptidase activity Source: UniProtKB-KW
  3. GTP binding Source: UniProtKB-KW
  4. helicase activity Source: UniProtKB-KW
  5. mRNA methyltransferase activity Source: InterPro
  6. polynucleotide 5'-phosphatase activity Source: UniProtKB-EC
  7. RNA binding Source: UniProtKB-KW
  8. RNA-directed RNA polymerase activity Source: UniProtKB-KW

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB-KW
  2. suppression by virus of host RNA polymerase II activity Source: UniProtKB-KW
  3. transcription, DNA-templated Source: InterPro
  4. viral RNA genome replication Source: InterPro
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
OrganismiMayaro virus (strain Brazil) (MAYV)
Taxonomic identifieri374990 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Haemagogus [TaxID: 7180]
Homo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007774: Genome

Subcellular locationi

Chain Non-structural polyprotein : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Located on the cytoplasmic surface of modified endosomes and lysosomes, also called cytopathic vacuoles type I (CPVI). These vacuoles contain numerous small circular invaginations (spherules) which may be the sites of RNA synthesis.
Chain P123 : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Chain P123' : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Chain mRNA-capping enzyme nsP1 : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host cell projectionhost 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 (By similarity).By similarity
Chain Protease nsP2 : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host nucleus By similarity
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).By similarity
Chain Non-structural protein 3 : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host cytoplasm By similarity
Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' seems to aggregate in cytoplasm (By similarity).By similarity
Chain Non-structural protein 3' : Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Host cytoplasm By similarity
Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' seems to aggregate in cytoplasm (By similarity).By similarity

GO - Cellular componenti

  1. host cell endosome Source: UniProtKB-KW
  2. host cell lysosome Source: UniProtKB-KW
  3. host cell nucleus Source: UniProtKB-KW
  4. host cell plasma membrane Source: UniProtKB-KW
  5. host cell projection Source: UniProtKB-KW
  6. membrane Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24362436Non-structural polyproteinPRO_0000308393Add
BLAST
Chaini1 – 18251825P123'PRO_0000229927Add
BLAST
Chaini1 – 18191819P123PRO_0000229926Add
BLAST
Chaini1 – 536536mRNA-capping enzyme nsP1PRO_0000229928Add
BLAST
Chaini537 – 1334798Protease nsP2PRO_0000229929Add
BLAST
Chaini1335 – 1825491Non-structural protein 3'PRO_0000229931Add
BLAST
Chaini1335 – 1819485Non-structural protein 3PRO_0000229930Add
BLAST
Chaini1826 – 2436611RNA-directed RNA polymerase nsP4PRO_0000229932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi417 – 4171S-palmitoyl cysteine; by hostBy similarity
Lipidationi419 – 4191S-palmitoyl cysteine; by hostBy similarity

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

Keywords - PTMi

Lipoprotein, Palmitate, Ubl conjugation

Proteomic databases

PRIDEiQ8QZ73.

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.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8QZ73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini691 – 843153(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini844 – 992149(+)RNA virus helicase C-terminalAdd
BLAST
Domaini1005 – 1327323Peptidase C9PROSITE-ProRule annotationAdd
BLAST
Domaini1335 – 1493159MacroPROSITE-ProRule annotationAdd
BLAST
Domaini2190 – 2305116RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 26320nsP1 membrane-bindingBy similarityAdd
BLAST
Regioni1006 – 102520Nucleolus localization signalBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1182 – 11865Nuclear localization signalBy similarity

Sequence similaritiesi

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.
IPR002620. Alphavirus_nsp2pro.
IPR002589. Macro_dom.
IPR027417. P-loop_NTPase.
IPR007094. RNA-dir_pol_PSvirus.
IPR029063. SAM-dependent_MTases-like.
IPR002588. Tymovirus_MeTrfase.
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.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51154. 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.

Q8QZ73-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSKVFVDIEA ESPFLKSLQR AFPAFEVEAQ QVTPNDHANA RAFSHLATKL
60 70 80 90 100
IEQETEKDTL ILDIGSAPAR RMMSEHTYHC VCPMRSAEDP ERLLYYARKL
110 120 130 140 150
AKASGEVVDR NIAAKIDDLQ SVMATPDNES RTFCLHTDQT CRTQAEVAVY
160 170 180 190 200
QDVYAVHAPT SLYFQAMKGV RTAYWIGFDT TPFMFDTMAG AYPTYATNWA
210 220 230 240 250
DEQVLKARNI GLCSASLTEG HLGKLSIMRK KKMTPSDQIM FSVGSTLYIE
260 270 280 290 300
SRRLLKSWHL PSVFHLKGRQ SYTCRCDTIV SCEGYVVKKI TMSPGVFGKT
310 320 330 340 350
SGYAVTHHAE GFLVCKTTDT IAGERVSFPI CTYVPSTICD QMTGILATEV
360 370 380 390 400
TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVSQA FSKWAKEYRL
410 420 430 440 450
DQEDEKNMGM RERTLTCCCL WAFKTHKNHT MYKKPDTQTI VKVPSEFNSF
460 470 480 490 500
VIPSLWSAGL SIGIRHRIRL LLQSRRVEPL VPSMDVGEAR AAEREAAEAK
510 520 530 540 550
EAEDTLAALP PLIPTAPVLD DIPEVDVEEL EFRAGAGVVE TPRNALKVTP
560 570 580 590 600
QDRDTMVGSY LVLSPQTVLK SVKLQALHPL AESVKIITHK GRAGRYQVDA
610 620 630 640 650
YDGRVLLPTG AAIPVPDFQA LSESATMVYN EREFINRKLY HIAVHGAALN
660 670 680 690 700
TDEEGYEKVR AESTDAEYVY DVDRKQCVKR EEAEGLVMIG DLINPPFHEF
710 720 730 740 750
AYEGLKRRPA APYKTTVVGV FGVPGSGKSG IIKSLVTRGD LVASGKKENC
760 770 780 790 800
QEIMLDVKRY RDLDMTAKTV DSVLLNGVKQ TVDVLYVDEA FACHAGTLLA
810 820 830 840 850
LIATVRPRKK VVLCGDPKQC GFFNLMQLQV NFNHNICTEV DHKSISRRCT
860 870 880 890 900
LPITAIVSTL HYEGRMRTTN PYNKPVIIDT TGQTKPNRED IVLTCFRGWV
910 920 930 940 950
KQLQLDYRGH EVMTAAASQG LTRKGVYAVR MKVNENPLYA QSSEHVNVLL
960 970 980 990 1000
TRTEGRLVWK TLSGDPWIKT LSNIPKGNFT ATLEDWQREH DTIMRAITQE
1010 1020 1030 1040 1050
AAPLDVFQNK AKVCWAKCLV PVLETAGIKL SATDWSAIIL AFKEDRAYSP
1060 1070 1080 1090 1100
EVALNEICTK IYGVDLDSGL FSAPRVSLHY TTNHWDNSPG GRMYGFSVEA
1110 1120 1130 1140 1150
ANRLEQQHPF YRGRWASGQV LVAERKTQPI DVTCNLIPFN RRLPHTLVTE
1160 1170 1180 1190 1200
YHPIKGERVE WLVNKIPGYH VLLVSEYNLI LPRRKVTWIA PPTVTGADLT
1210 1220 1230 1240 1250
YDLDLGLPPN AGRYDLVFVN MHTPYRLHHY QQCVDHAMKL QMLGGDALYL
1260 1270 1280 1290 1300
LKPGGSLLLS TYAYADRTSE AVVTALARRF SSFRAVTVRC VTSNTEVFLL
1310 1320 1330 1340 1350
FTNFDNGRRT VTLHQTNGKL SSIYAGTVLQ AAGCAPAYAV KRADIATAIE
1360 1370 1380 1390 1400
DAVVNAANHR GQVGDGVCRA VARKWPQAFR NAATPVGTAK TVKCDETYII
1410 1420 1430 1440 1450
HAVGPNFNNT SEAEGDRDLA AAYRAVAAEI NRLSISSVAI PLLSTGIFSA
1460 1470 1480 1490 1500
GKDRVHQSLS HLLAAMDTTE ARVTIYCRDK TWEQKIKTVL QNRSATELVS
1510 1520 1530 1540 1550
DELQFEVNLT RVHPDSSLVG RPGYSTTDGT LYSYMEGTKF HQAALDMAEI
1560 1570 1580 1590 1600
TTLWPRVQDA NEHICLYALG ETMDNIRARC PVEDSDSSTP PKTVPCLCRY
1610 1620 1630 1640 1650
AMTPERVTRL RMHHTKDFVV CSSFQLPKYR IPGVQRVKCE KVMLFDAAPP
1660 1670 1680 1690 1700
ASVSPVQYLT NQSETTISLS SFSITSDSSS LSTFPDLESA EELDHDSQSV
1710 1720 1730 1740 1750
RPALNEPDDH QPTPTAELAT HPVPPPRPNR ARRLAAARVQ VQVEVHQPPS
1760 1770 1780 1790 1800
NQPTKPIPAP RTSLRPVPAP RRYVPRPVVE LPWPLETIDV EFGAPTEEES
1810 1820 1830 1840 1850
DITFGDFSAS EWETISNSSL GRAGAYIFSS DVGPGHLQQK SVRQHDLEVP
1860 1870 1880 1890 1900
IMDRVIEEKV YPPKLDEAKE KQLLLKLQMH ATDANRSRYQ SRKVENMKAT
1910 1920 1930 1940 1950
IIDRLKQGSA YYVSAAADKA VTYHVRYAKP RYSVPVMQRL SSATIAVATC
1960 1970 1980 1990 2000
NEFLARNYPT VASYQITDEY DAYLDMVDGS ESCLDRANFC PAKLRCYPKH
2010 2020 2030 2040 2050
HAYHMPQIRS AVPSPFQNTL QNVLAAATKR NCNVTQMREL PTLDSAVYNV
2060 2070 2080 2090 2100
ECFRKYACNN EYWEEFAKKP IRITTENLTT YVTKLKGGKA AALFAKTHNL
2110 2120 2130 2140 2150
VPLQEVPMDR FIMDMKRDVK VTPGTKHTEE RPKVQVIQAA EPLATAYLCG
2160 2170 2180 2190 2200
IHRELVRRLN AVLLPNIHTL FDMSAEDFDA IISEHFKPGD HVLETDIASF
2210 2220 2230 2240 2250
DKSQDDSLAL TGLMILEDLG VDNQLLDLIE AAFGQITSCH LPTGTRFKFG
2260 2270 2280 2290 2300
AMMKSGMFLT LFINTVLNIT IASRVLEARL TNSACAAFIG DDNVVHGVVS
2310 2320 2330 2340 2350
DKLMADRCAT WVNMEVKIID AVMCIKPPYF CGGFLVYDHV TRTACRIADP
2360 2370 2380 2390 2400
LKRLFKLGKP LPADDCQDED RRRALYDEVK KWSRSGLGSE IEVALASRYR
2410 2420 2430
LEGSYNLLLA MSTFAHSMKN FSALRGPVIH LYGGPK
Length:2,436
Mass (Da):271,885
Last modified:April 4, 2006 - v2
Checksum:iBFF43A0DC04D3C59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237947 Genomic RNA. Translation: AAL79763.1.
AF237947 Genomic RNA. Translation: AAL79765.1. Sequence problems.
RefSeqiNP_579968.1. NC_003417.1.
NP_579969.1. NC_003417.1.

Genome annotation databases

GeneIDi935140.
935142.

Keywords - Coding sequence diversityi

RNA suppression of termination

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237947 Genomic RNA. Translation: AAL79763.1 .
AF237947 Genomic RNA. Translation: AAL79765.1 . Sequence problems.
RefSeqi NP_579968.1. NC_003417.1.
NP_579969.1. NC_003417.1.

3D structure databases

ProteinModelPortali Q8QZ73.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q8QZ73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 935140.
935142.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
IPR002620. Alphavirus_nsp2pro.
IPR002589. Macro_dom.
IPR027417. P-loop_NTPase.
IPR007094. RNA-dir_pol_PSvirus.
IPR029063. SAM-dependent_MTases-like.
IPR002588. Tymovirus_MeTrfase.
IPR001788. Tymovirus_RNA-dep_RNA_pol.
[Graphical view ]
Pfami PF01661. Macro. 1 hit.
PF01707. Peptidase_C9. 1 hit.
PF00978. RdRP_2. 1 hit.
PF01443. Viral_helicase1. 1 hit.
PF01660. Vmethyltransf. 1 hit.
[Graphical view ]
SMARTi SM00506. A1pp. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEi PS51154. MACRO. 1 hit.
PS51520. NSP2PRO. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Netto M.C.M.G., Shirako Y., Strauss E.G., Carvalho M.G.C., Strauss J.H.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLN_MAYAB
AccessioniPrimary (citable) accession number: Q8QZ73
Secondary accession number(s): Q8QHM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: October 29, 2014
This is version 90 of the entry and version 2 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 Ser-1819 and Leu-1820. This readthrough produces P1234, cleaved quickly by nsP2 into P123' and nsP4. Further processing of p123' gives nsP1, nsP2 and nsP3' which is 6 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.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3