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Protein

Non-structural polyprotein

Gene
N/A
Organism
Semliki forest virus (SFV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.
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.
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.
nsP3 is essential for minus strand and subgenomic 26S mRNA synthesis.
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.

Caution

There is no stop codon readthrough before nsp4.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.99 mM for triphosphatase (at pH 8.0)1 Publication
  2. KM=90 mM for NTPase (at pH 7.5)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1015For cysteine protease nsP2 activityPROSITE-ProRule annotation1
    Active sitei1085For cysteine protease nsP2 activityPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi723 – 730ATPSequence analysis8

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
    Biological processEukaryotic 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
    LigandATP-binding, GTP-binding, Nucleotide-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P08411

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    C09.001

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSemliki forest virus (SFV)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11033 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes [TaxID: 7158]
    Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog) [TaxID: 9368]
    Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
    Halcyon [TaxID: 170865]
    Homo sapiens (Human) [TaxID: 9606]
    Quelea [TaxID: 158617]
    Rhipicephalus [TaxID: 34630]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000100607 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
    • UP000166518 Componenti: Genome
    • UP000174511 Componenti: Genome
    • UP000000570 Componenti: Genome
    • UP000136172 Componenti: Genome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

    GO - Cellular componenti

    Keywords - Cellular componenti

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

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi19L → E: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi38H → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi64D → A: 60% increase of guanine-7-methyl transferase activity in vitro. Complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi81 – 83CVC → AVA: 60% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication3
    Mutagenesisi90D → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi93R → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi135C → A: 90% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi142C → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi153D → A: No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi169K → A: 50% loss of guanine-7-methyl transferase activity and no effect on guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi180D → A: No effect on guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi203E → A: No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi214C → A: 90% loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi249Y → A: 97% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi317K → A: 95% loss of guanine-7-methyl transferase activity and 98% loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi418 – 420CCC → AAA: Complete loss of palmitoylation. Complete loss of pathogenicity in mice. 2 Publications3
    Mutagenesisi729K → N: Complete loss of NTPase and helicase activity. 1 Publication1
    Mutagenesisi1015C → A: Complete loss of polyprotein processing. 1 Publication1
    Mutagenesisi1186R → D: Complete loss of nuclear localization for nsP2. 1 Publication1
    Mutagenesisi1680T → A: Complete loss of threonine phosphorylation. 1 Publication1
    Mutagenesisi1681T → A: Complete loss of threonine phosphorylation. 1 Publication1
    Mutagenesisi1824D → A: No effect on polyprotein processing. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003084031 – 2432Non-structural polyproteinAdd BLAST2432
    ChainiPRO_00002277701 – 1818P123Add BLAST1818
    ChainiPRO_00000412281 – 537mRNA-capping enzyme nsP1Add BLAST537
    ChainiPRO_0000041229538 – 1336Protease nsP2Add BLAST799
    ChainiPRO_00000412301337 – 1818Non-structural protein 3Add BLAST482
    ChainiPRO_00000412311819 – 2431RNA-directed RNA polymerase nsP4Add BLAST613

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi418S-palmitoyl cysteine; by host2 Publications1
    Lipidationi420S-palmitoyl cysteine; by host2 Publications1
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1680Phosphothreonine; by host1 Publication1
    Modified residuei1681Phosphothreonine; by host1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.1 Publication
    nsP1 is palmitoylated by host.2 Publications
    nsP3 is phosphorylated by host on serines and threonines.1 Publication
    nsP4 is ubiquitinated; targets the protein for rapid degradation via the ubiquitin system.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei537 – 538Cleavage; by nsP22
    Sitei1336 – 1337Cleavage; by nsP22
    Sitei1818 – 1819Cleavage; by nsP22

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P08411

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P08411

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P08411

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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.2 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

    Protein-protein interaction databases

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    P08411

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    12432
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P08411

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P08411

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P08411

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini29 – 260Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
    Domaini692 – 844(+)RNA virus helicase ATP-bindingAdd BLAST153
    Domaini845 – 993(+)RNA virus helicase C-terminalAdd BLAST149
    Domaini1006 – 1329Peptidase C9PROSITE-ProRule annotationAdd BLAST324
    Domaini1337 – 1495MacroPROSITE-ProRule annotationAdd BLAST159
    Domaini2182 – 2297RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni245 – 264nsP1 membrane-bindingAdd BLAST20
    Regioni1007 – 1026Nucleolus localization signalAdd BLAST20

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1184 – 1188Nuclear localization signal5

    Phylogenomic databases

    Database of Orthologous Groups

    More...
    OrthoDBi
    VOG09000007

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR027351 (+)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

    Pfam protein domain database

    More...
    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

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00506 A1pp, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540 SSF52540, 1 hit

    PROSITE; a protein domain and family database

    More...
    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

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P08411-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAAKVHVDIE ADSPFIKSLQ KAFPSFEVES LQVTPNDHAN ARAFSHLATK
    60 70 80 90 100
    LIEQETDKDT LILDIGSAPS RRMMSTHKYH CVCPMRSAED PERLVCYAKK
    110 120 130 140 150
    LAAASGKVLD REIAGKITDL QTVMATPDAE SPTFCLHTDV TCRTAAEVAV
    160 170 180 190 200
    YQDVYAVHAP TSLYHQAMKG VRTAYWIGFD TTPFMFDALA GAYPTYATNW
    210 220 230 240 250
    ADEQVLQARN IGLCAASLTE GRLGKLSILR KKQLKPCDTV MFSVGSTLYT
    260 270 280 290 300
    ESRKLLRSWH LPSVFHLKGK QSFTCRCDTI VSCEGYVVKK ITMCPGLYGK
    310 320 330 340 350
    TVGYAVTYHA EGFLVCKTTD TVKGERVSFP VCTYVPSTIC DQMTGILATD
    360 370 380 390 400
    VTPEDAQKLL VGLNQRIVVN GRTQRNTNTM KNYLLPIVAV AFSKWAREYK
    410 420 430 440 450
    ADLDDEKPLG VRERSLTCCC LWAFKTRKMH TMYKKPDTQT IVKVPSEFNS
    460 470 480 490 500
    FVIPSLWSTG LAIPVRSRIK MLLAKKTKRE LIPVLDASSA RDAEQEEKER
    510 520 530 540 550
    LEAELTREAL PPLVPIAPAE TGVVDVDVEE LEYHAGAGVV ETPRSALKVT
    560 570 580 590 600
    AQPNDVLLGN YVVLSPQTVL KSSKLAPVHP LAEQVKIITH NGRAGRYQVD
    610 620 630 640 650
    GYDGRVLLPC GSAIPVPEFQ ALSESATMVY NEREFVNRKL YHIAVHGPSL
    660 670 680 690 700
    NTDEENYEKV RAERTDAEYV FDVDKKCCVK REEASGLVLV GELTNPPFHE
    710 720 730 740 750
    FAYEGLKIRP SAPYKTTVVG VFGVPGSGKS AIIKSLVTKH DLVTSGKKEN
    760 770 780 790 800
    CQEIVNDVKK HRGLDIQAKT VDSILLNGCR RAVDILYVDE AFACHSGTLL
    810 820 830 840 850
    ALIALVKPRS KVVLCGDPKQ CGFFNMMQLK VNFNHNICTE VCHKSISRRC
    860 870 880 890 900
    TRPVTAIVST LHYGGKMRTT NPCNKPIIID TTGQTKPKPG DIVLTCFRGW
    910 920 930 940 950
    VKQLQLDYRG HEVMTAAASQ GLTRKGVYAV RQKVNENPLY APASEHVNVL
    960 970 980 990 1000
    LTRTEDRLVW KTLAGDPWIK VLSNIPQGNF TATLEEWQEE HDKIMKVIEG
    1010 1020 1030 1040 1050
    PAAPVDAFQN KANVCWAKSL VPVLDTAGIR LTAEEWSTII TAFKEDRAYS
    1060 1070 1080 1090 1100
    PVVALNEICT KYYGVDLDSG LFSAPKVSLY YENNHWDNRP GGRMYGFNAA
    1110 1120 1130 1140 1150
    TAARLEARHT FLKGQWHTGK QAVIAERKIQ PLSVLDNVIP INRRLPHALV
    1160 1170 1180 1190 1200
    AEYKTVKGSR VEWLVNKVRG YHVLLVSEYN LALPRRRVTW LSPLNVTGAD
    1210 1220 1230 1240 1250
    RCYDLSLGLP ADAGRFDLVF VNIHTEFRIH HYQQCVDHAM KLQMLGGDAL
    1260 1270 1280 1290 1300
    RLLKPGGSLL MRAYGYADKI SEAVVSSLSR KFSSARVLRP DCVTSNTEVF
    1310 1320 1330 1340 1350
    LLFSNFDNGK RPSTLHQMNT KLSAVYAGEA MHTAGCAPSY RVKRADIATC
    1360 1370 1380 1390 1400
    TEAAVVNAAN ARGTVGDGVC RAVAKKWPSA FKGAATPVGT IKTVMCGSYP
    1410 1420 1430 1440 1450
    VIHAVAPNFS ATTEAEGDRE LAAVYRAVAA EVNRLSLSSV AIPLLSTGVF
    1460 1470 1480 1490 1500
    SGGRDRLQQS LNHLFTAMDA TDADVTIYCR DKSWEKKIQE AIDMRTAVEL
    1510 1520 1530 1540 1550
    LNDDVELTTD LVRVHPDSSL VGRKGYSTTD GSLYSYFEGT KFNQAAIDMA
    1560 1570 1580 1590 1600
    EILTLWPRLQ EANEQICLYA LGETMDNIRS KCPVNDSDSS TPPRTVPCLC
    1610 1620 1630 1640 1650
    RYAMTAERIA RLRSHQVKSM VVCSSFPLPK YHVDGVQKVK CEKGLLFDPT
    1660 1670 1680 1690 1700
    VPSVVSPRKY AASTTDHSDR SLRGFDLDWT TDSSSTASDT MSLPSLQSCD
    1710 1720 1730 1740 1750
    IDSIYEPMAP IVVTADVHPE PAGIADLAAD VHPEPADHVD LENPIPPPRP
    1760 1770 1780 1790 1800
    KRAAYLASRA AERPVPAPRK PTPAPRTAFR NKLPLTFGDF DEHEVDALAS
    1810 1820 1830 1840 1850
    GITFGDFDDV LRLGRAGAYI FSSDTGSGHL QQKSVRQHNL QCAQLDAVEE
    1860 1870 1880 1890 1900
    EKMYPPKLDT EREKLLLLKM QMHPSEANKS RYQSRKVENM KATVVDRLTS
    1910 1920 1930 1940 1950
    GARLYTGADV GRIPTYAVRY PRPVYSPTVI ERFSSPDVAI AACNEYLSRN
    1960 1970 1980 1990 2000
    YPTVASYQIT DEYDAYLDMV DGSDSCLDRA TFCPAKLRCY PKHHAYHQPT
    2010 2020 2030 2040 2050
    VRSAVPSPFQ NTLQNVLAAA TKRNCNVTQM RELPTMDSAV FNVECFKRYA
    2060 2070 2080 2090 2100
    CSGEYWEEYA KQPIRITTEN ITTYVTKLKG PKAAALFAKT HNLVPLQEVP
    2110 2120 2130 2140 2150
    MDRFTVDMKR DVKVTPGTKH TEERPKVQVI QAAEPLATAY LCGIHRELVR
    2160 2170 2180 2190 2200
    RLNAVLRPNV HTLFDMSAED FDAIIASHFH PGDPVLETDI ASFDKSQDDS
    2210 2220 2230 2240 2250
    LALTGLMILE DLGVDQYLLD LIEAAFGEIS SCHLPTGTRF KFGAMMKSGM
    2260 2270 2280 2290 2300
    FLTLFINTVL NITIASRVLE QRLTDSACAA FIGDDNIVHG VISDKLMAER
    2310 2320 2330 2340 2350
    CASWVNMEVK IIDAVMGEKP PYFCGGFIVF DSVTQTACRV SDPLKRLFKL
    2360 2370 2380 2390 2400
    GKPLTAEDKQ DEDRRRALSD EVSKWFRTGL GAELEVALTS RYEVEGCKSI
    2410 2420 2430
    LIAMATLARD IKAFKKLRGP VIHLYGGPRL VR
    Length:2,432
    Mass (Da):269,512
    Last modified:March 21, 2006 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBE7104A1EC3EF6EE
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti6H → Y in strain: Isolate L10. 1
    Natural varianti95 – 96VC → DS in strain: Isolate Garoff/Takkinen. 2
    Natural varianti119D → N in strain: Isolate Ts14. 1
    Natural varianti311E → K in strain: Isolate L10. 1
    Natural varianti529E → D in strain: Isolate Ts10. 1
    Natural varianti596R → G in strain: Isolate Garoff/Takkinen. 1
    Natural varianti764 – 771LDIQAKTV → KGTSRENS in strain: Isolate Garoff/Takkinen. 8
    Natural varianti764 – 771LDIQAKTV → NWTSRKNS in strain: Isolate L10. 8
    Natural varianti817D → N in strain: Isolate L10. 1
    Natural varianti826M → T in strain: Isolate L10. 1
    Natural varianti843H → N in strain: Isolate L10. 1
    Natural varianti845S → N in strain: Isolate Ts1. 1
    Natural varianti859S → C in strain: Isolate L10. 1
    Natural varianti869T → S in strain: Isolate Ts13. 1
    Natural varianti901V → A in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1114G → R in strain: Isolate Ts11. 1
    Natural varianti1199A → T in strain: Isolate Ts6. 1
    Natural varianti1258 – 1259SL → I in strain: Isolate Garoff/Takkinen and Isolate L10. 2
    Natural varianti1384A → E in strain: Isolate L10 clone SFV4. 1
    Natural varianti1565Q → R in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1579R → G in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1644G → V in strain: Isolate Garoff/Takkinen, Isolate L10 and Isolate L10 clone SFV4. 1
    Natural varianti1849E → Q in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1921P → R in strain: Isolate L10. 1
    Natural varianti1938V → A in strain: Isolate L10. 1
    Natural varianti2060A → V in strain: Isolate Ts13. 1
    Natural varianti2088A → D in strain: Isolate L10. 1
    Natural varianti2405A → T in strain: Isolate Garoff/Takkinen. 1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X04129 Genomic RNA Translation: CAA27741.1
    AJ251359 Genomic RNA Translation: CAB62256.1
    AY112987 Genomic RNA Translation: AAM64226.1
    DQ189079 Genomic RNA Translation: ABA29023.1
    DQ189080 Genomic RNA Translation: ABA29024.1
    DQ189081 Genomic RNA Translation: ABA29025.1
    DQ189082 Genomic RNA Translation: ABA29026.1
    DQ189083 Genomic RNA Translation: ABA29028.1
    DQ189084 Genomic RNA Translation: ABA29029.1
    DQ189085 Genomic RNA Translation: ABA29031.1
    DQ189086 Genomic RNA Translation: ABA29032.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A23592 MNWVSF

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_463457.1, NC_003215.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    922350

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vg:922350

    Keywords - Coding sequence diversityi

    RNA suppression of termination

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X04129 Genomic RNA Translation: CAA27741.1
    AJ251359 Genomic RNA Translation: CAB62256.1
    AY112987 Genomic RNA Translation: AAM64226.1
    DQ189079 Genomic RNA Translation: ABA29023.1
    DQ189080 Genomic RNA Translation: ABA29024.1
    DQ189081 Genomic RNA Translation: ABA29025.1
    DQ189082 Genomic RNA Translation: ABA29026.1
    DQ189083 Genomic RNA Translation: ABA29028.1
    DQ189084 Genomic RNA Translation: ABA29029.1
    DQ189085 Genomic RNA Translation: ABA29031.1
    DQ189086 Genomic RNA Translation: ABA29032.1
    PIRiA23592 MNWVSF
    RefSeqiNP_463457.1, NC_003215.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FW5NMR-A245-264[»]
    5DRVX-ray2.75B1785-1792[»]
    5FW5X-ray1.92C1785-1809[»]
    ProteinModelPortaliP08411
    SMRiP08411
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    ELMiP08411

    Protein family/group databases

    MEROPSiC09.001

    PTM databases

    iPTMnetiP08411
    SwissPalmiP08411

    Proteomic databases

    PRIDEiP08411

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi922350
    KEGGivg:922350

    Phylogenomic databases

    OrthoDBiVOG09000007

    Enzyme and pathway databases

    SABIO-RKiP08411

    Miscellaneous databases

    EvolutionaryTraceiP08411

    Family and domain databases

    InterProiView protein in InterPro
    IPR027351 (+)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
    PfamiView 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
    SMARTiView protein in SMART
    SM00506 A1pp, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    PROSITEiView 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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLN_SFV
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08411
    Secondary accession number(s): Q3LRQ3
    , Q3LRQ4, Q3LRQ6, Q3LRQ7, Q3LRQ9, Q3LRR0, Q3LRR1, Q3LRR2, Q8JMP6, Q9QBM1
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: March 21, 2006
    Last modified: December 5, 2018
    This is version 152 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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