Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8QZ73

- POLN_MAYAB

UniProt

Q8QZ73 - POLN_MAYAB

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 membrane Source: UniProtKB-SubCell
    2. host cell filopodium Source: UniProtKB-SubCell
    3. host cell lysosomal membrane Source: UniProtKB-SubCell
    4. host cell nucleus Source: UniProtKB-SubCell
    5. host cell plasma membrane Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB-KW

    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

    « Hide

    MSKVFVDIEA ESPFLKSLQR AFPAFEVEAQ QVTPNDHANA RAFSHLATKL     50
    IEQETEKDTL ILDIGSAPAR RMMSEHTYHC VCPMRSAEDP ERLLYYARKL 100
    AKASGEVVDR NIAAKIDDLQ SVMATPDNES RTFCLHTDQT CRTQAEVAVY 150
    QDVYAVHAPT SLYFQAMKGV RTAYWIGFDT TPFMFDTMAG AYPTYATNWA 200
    DEQVLKARNI GLCSASLTEG HLGKLSIMRK KKMTPSDQIM FSVGSTLYIE 250
    SRRLLKSWHL PSVFHLKGRQ SYTCRCDTIV SCEGYVVKKI TMSPGVFGKT 300
    SGYAVTHHAE GFLVCKTTDT IAGERVSFPI CTYVPSTICD QMTGILATEV 350
    TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVSQA FSKWAKEYRL 400
    DQEDEKNMGM RERTLTCCCL WAFKTHKNHT MYKKPDTQTI VKVPSEFNSF 450
    VIPSLWSAGL SIGIRHRIRL LLQSRRVEPL VPSMDVGEAR AAEREAAEAK 500
    EAEDTLAALP PLIPTAPVLD DIPEVDVEEL EFRAGAGVVE TPRNALKVTP 550
    QDRDTMVGSY LVLSPQTVLK SVKLQALHPL AESVKIITHK GRAGRYQVDA 600
    YDGRVLLPTG AAIPVPDFQA LSESATMVYN EREFINRKLY HIAVHGAALN 650
    TDEEGYEKVR AESTDAEYVY DVDRKQCVKR EEAEGLVMIG DLINPPFHEF 700
    AYEGLKRRPA APYKTTVVGV FGVPGSGKSG IIKSLVTRGD LVASGKKENC 750
    QEIMLDVKRY RDLDMTAKTV DSVLLNGVKQ TVDVLYVDEA FACHAGTLLA 800
    LIATVRPRKK VVLCGDPKQC GFFNLMQLQV NFNHNICTEV DHKSISRRCT 850
    LPITAIVSTL HYEGRMRTTN PYNKPVIIDT TGQTKPNRED IVLTCFRGWV 900
    KQLQLDYRGH EVMTAAASQG LTRKGVYAVR MKVNENPLYA QSSEHVNVLL 950
    TRTEGRLVWK TLSGDPWIKT LSNIPKGNFT ATLEDWQREH DTIMRAITQE 1000
    AAPLDVFQNK AKVCWAKCLV PVLETAGIKL SATDWSAIIL AFKEDRAYSP 1050
    EVALNEICTK IYGVDLDSGL FSAPRVSLHY TTNHWDNSPG GRMYGFSVEA 1100
    ANRLEQQHPF YRGRWASGQV LVAERKTQPI DVTCNLIPFN RRLPHTLVTE 1150
    YHPIKGERVE WLVNKIPGYH VLLVSEYNLI LPRRKVTWIA PPTVTGADLT 1200
    YDLDLGLPPN AGRYDLVFVN MHTPYRLHHY QQCVDHAMKL QMLGGDALYL 1250
    LKPGGSLLLS TYAYADRTSE AVVTALARRF SSFRAVTVRC VTSNTEVFLL 1300
    FTNFDNGRRT VTLHQTNGKL SSIYAGTVLQ AAGCAPAYAV KRADIATAIE 1350
    DAVVNAANHR GQVGDGVCRA VARKWPQAFR NAATPVGTAK TVKCDETYII 1400
    HAVGPNFNNT SEAEGDRDLA AAYRAVAAEI NRLSISSVAI PLLSTGIFSA 1450
    GKDRVHQSLS HLLAAMDTTE ARVTIYCRDK TWEQKIKTVL QNRSATELVS 1500
    DELQFEVNLT RVHPDSSLVG RPGYSTTDGT LYSYMEGTKF HQAALDMAEI 1550
    TTLWPRVQDA NEHICLYALG ETMDNIRARC PVEDSDSSTP PKTVPCLCRY 1600
    AMTPERVTRL RMHHTKDFVV CSSFQLPKYR IPGVQRVKCE KVMLFDAAPP 1650
    ASVSPVQYLT NQSETTISLS SFSITSDSSS LSTFPDLESA EELDHDSQSV 1700
    RPALNEPDDH QPTPTAELAT HPVPPPRPNR ARRLAAARVQ VQVEVHQPPS 1750
    NQPTKPIPAP RTSLRPVPAP RRYVPRPVVE LPWPLETIDV EFGAPTEEES 1800
    DITFGDFSAS EWETISNSSL GRAGAYIFSS DVGPGHLQQK SVRQHDLEVP 1850
    IMDRVIEEKV YPPKLDEAKE KQLLLKLQMH ATDANRSRYQ SRKVENMKAT 1900
    IIDRLKQGSA YYVSAAADKA VTYHVRYAKP RYSVPVMQRL SSATIAVATC 1950
    NEFLARNYPT VASYQITDEY DAYLDMVDGS ESCLDRANFC PAKLRCYPKH 2000
    HAYHMPQIRS AVPSPFQNTL QNVLAAATKR NCNVTQMREL PTLDSAVYNV 2050
    ECFRKYACNN EYWEEFAKKP IRITTENLTT YVTKLKGGKA AALFAKTHNL 2100
    VPLQEVPMDR FIMDMKRDVK VTPGTKHTEE RPKVQVIQAA EPLATAYLCG 2150
    IHRELVRRLN AVLLPNIHTL FDMSAEDFDA IISEHFKPGD HVLETDIASF 2200
    DKSQDDSLAL TGLMILEDLG VDNQLLDLIE AAFGQITSCH LPTGTRFKFG 2250
    AMMKSGMFLT LFINTVLNIT IASRVLEARL TNSACAAFIG DDNVVHGVVS 2300
    DKLMADRCAT WVNMEVKIID AVMCIKPPYF CGGFLVYDHV TRTACRIADP 2350
    LKRLFKLGKP LPADDCQDED RRRALYDEVK KWSRSGLGSE IEVALASRYR 2400
    LEGSYNLLLA MSTFAHSMKN FSALRGPVIH LYGGPK 2436
    Length:2,436
    Mass (Da):271,885
    Last modified:April 4, 2006 - v2
    Checksum:iBFF43A0DC04D3C59
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 1, 2014
    This is version 89 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