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Protein

Non-structural polyprotein

Gene
N/A
Organism
Mayaro virus (strain Brazil) (MAYV)
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 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

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.

<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

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 sitei1014For cysteine protease nsP2 activityPROSITE-ProRule annotation1
Active sitei1084For 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 bindingi722 – 729ATPSequence 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

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 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
<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>OrganismiMayaro virus (strain Brazil) (MAYV)
<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 identifieri374990 [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 aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Haemagogus [TaxID: 7180]
Homo sapiens (Human) [TaxID: 9606]
<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
  • UP000007774 <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

<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 :
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 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_00003083931 – 2436Non-structural polyproteinAdd BLAST2436
ChainiPRO_00002299271 – 1825P123'Add BLAST1825
ChainiPRO_00002299261 – 1819P123Add BLAST1819
ChainiPRO_00002299281 – 536mRNA-capping enzyme nsP1Add BLAST536
ChainiPRO_0000229929537 – 1334Protease nsP2Add BLAST798
ChainiPRO_00002299311335 – 1825Non-structural protein 3'Add BLAST491
ChainiPRO_00002299301335 – 1819Non-structural protein 3Add BLAST485
ChainiPRO_00002299321826 – 2436RNA-directed RNA polymerase nsP4Add BLAST611

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>Lipidationi417S-palmitoyl cysteine; by hostBy similarity1
Lipidationi419S-palmitoyl cysteine; by hostBy similarity1

<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 P123, or P1234 by stop codon readthrough. These polyproteins are processed differently depending on the stage of infection. In early stages, P1234 is first cleaved in trans, through its nsP2 protease activity, releasing P123' and nsP4. P123/P123' and nsP4 start to replicate the viral genome into its antigenome. After these early events, nsP1 is cleaved in cis by nsP2 protease, releasing the P23/P23' polyprotein. Cleavage of nsP1 exposes an "activator" at the N-terminus of P23/P23' which induces its cleavage into nsP2 and nsP3 by the viral protease. This sequence of delayed processing would allow correct assembly and membrane association of the RNA-polymerase complex. In the late stage of infection, the presence of free nsP2 in the cytoplasm cleaves P1234 quickly into P12 and P34, then into the four nsP (By similarity).By similarity
nsP1 is palmitoylated by host.By similarity
nsP4 is ubiquitinated; targets the protein for rapid degradation via the ubiquitin system.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei536 – 537Cleavage; by nsP2By similarity2
Sitei1334 – 1335Cleavage; by nsP2By similarity2
Sitei1825 – 1826Cleavage; by nsP2By similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8QZ73

<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 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.

<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.By similarity

<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

12436
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q8QZ73

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

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SMRi
Q8QZ73

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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>Domaini28 – 259Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
Domaini691 – 843(+)RNA virus helicase ATP-bindingAdd BLAST153
Domaini844 – 992(+)RNA virus helicase C-terminalAdd BLAST149
Domaini1005 – 1327Peptidase C9PROSITE-ProRule annotationAdd BLAST323
Domaini1335 – 1493MacroPROSITE-ProRule annotationAdd BLAST159
Domaini2190 – 2305RdRp 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>Regioni244 – 263nsP1 membrane-bindingBy similarityAdd BLAST20
Regioni1006 – 1025Nucleolus localization signalBy similarityAdd 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>Motifi1182 – 1186Nuclear localization signalBy similarity5

Phylogenomic databases

Database of Orthologous Groups

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OrthoDBi
VOG09000007

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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
IPR029063 SAM-dependent_MTases
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

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SMARTi
View protein in SMART
SM00506 A1pp, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit
SSF53335 SSF53335, 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.

Q8QZ73-1 [UniParc]FASTAAdd to basket
« Hide
        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
<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:iBFF43A0DC04D3C59
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF237947 Genomic RNA Translation: AAL79763.1
AF237947 Genomic RNA Translation: AAL79765.1 Sequence problems.

NCBI Reference Sequences

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RefSeqi
NP_579968.1, NC_003417.1
NP_579969.1, NC_003417.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
935140
935142

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:935140
vg:935142

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
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IQ5NMR-A1335-1493[»]
ProteinModelPortaliQ8QZ73
SMRiQ8QZ73
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC09.001

Proteomic databases

PRIDEiQ8QZ73

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi935140
935142
KEGGivg:935140
vg:935142

Phylogenomic databases

OrthoDBiVOG09000007

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
IPR029063 SAM-dependent_MTases
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
SSF53335 SSF53335, 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

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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_MAYAB
<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: Q8QZ73
Secondary accession number(s): Q8QHM4
<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: April 4, 2006
Last sequence update: April 4, 2006
Last modified: December 5, 2018
This is version 106 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

Documents

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