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P13900

- POLG_SVDVU

UniProt

P13900 - POLG_SVDVU

Protein

Genome polyprotein

Gene
N/A
Organism
Swine vesicular disease virus (strain UKG/27/72) (SVDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host CXADR to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks By similarity.By similarity
    Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.By similarity
    Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.By similarity
    Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks By similarity.By similarity
    Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step By similarity.By similarity
    Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores By similarity.By similarity
    Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication By similarity.By similarity
    Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 By similarity.By similarity
    Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity By similarity.By similarity
    Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface By similarity.By similarity
    Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication By similarity.By similarity
    Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity By similarity.By similarity
    Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity.By similarity
    RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated By similarity.PROSITE-ProRule annotation

    Catalytic activityi

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
    Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
    NTP + H2O = NDP + phosphate.

    Enzyme regulationi

    RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei69 – 702Cleavage; by autolysisSequence Analysis
    Sitei330 – 3312Cleavage; by Protease 3CSequence Analysis
    Active sitei872 – 8721For Protease 2A activityBy similarity
    Active sitei890 – 8901For Protease 2A activityBy similarity
    Active sitei961 – 9611For Protease 2A activityBy similarity
    Sitei1001 – 10022Cleavage; by Protease 3CSequence Analysis
    Sitei1429 – 14302Cleavage; by Protease 3CSequence Analysis
    Sitei1518 – 15192Cleavage; by Protease 3CSequence Analysis
    Sitei1540 – 15412Cleavage; by Protease 3CSequence Analysis
    Active sitei1580 – 15801For Protease 3C activitySequence Analysis
    Active sitei1611 – 16111For Protease 3C activitySequence Analysis
    Active sitei1687 – 16871For Protease 3C activityBy similarity
    Sitei1723 – 17242Cleavage; by Protease 3CSequence Analysis
    Active sitei2052 – 20521For RdRp activityBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. ion channel activity Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW
    5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    6. RNA helicase activity Source: InterPro
    7. structural molecule activity Source: InterPro

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW
    2. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB
    4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    6. protein oligomerization Source: UniProtKB-KW
    7. RNA-protein covalent cross-linking Source: UniProtKB-KW
    8. suppression by virus of host gene expression Source: UniProtKB-KW
    9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    11. suppression by virus of host translation initiation factor activity Source: UniProtKB
    12. transcription, DNA-templated Source: InterPro
    13. viral RNA genome replication Source: InterPro
    14. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

    Keywords - Biological processi

    Activation of host autophagy by virus, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Protein family/group databases

    MEROPSiC03.020.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 17 chains:
    Alternative name(s):
    VP4-VP2
    Alternative name(s):
    P1A
    Virion protein 4
    Alternative name(s):
    P1B
    Virion protein 2
    Alternative name(s):
    P1C
    Virion protein 3
    Alternative name(s):
    P1D
    Virion protein 1
    Protease 2A (EC:3.4.22.29)
    Short name:
    P2A
    Alternative name(s):
    Picornain 2A
    Protein 2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Alternative name(s):
    Protein 3B
    Short name:
    P3B
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    3D polymerase
    Short name:
    3Dpol
    Protein 3D
    Short name:
    3D
    OrganismiSwine vesicular disease virus (strain UKG/27/72) (SVDV)
    Taxonomic identifieri12077 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
    Virus hostiSus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000007234: Genome

    Subcellular locationi

    Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
    Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 3CD : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain RNA-directed RNA polymerase : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

    GO - Cellular componenti

    1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. integral to membrane of host cell Source: UniProtKB-KW
    3. membrane Source: UniProtKB-KW
    4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 21852184Genome polyproteinBy similarityPRO_0000426686Add
    BLAST
    Chaini2 – 848847P1By similarityPRO_0000426687Add
    BLAST
    Chaini2 – 330329Capsid protein VP0Sequence AnalysisPRO_0000426688Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426689Add
    BLAST
    Chaini70 – 330261Capsid protein VP2Sequence AnalysisPRO_0000426690Add
    BLAST
    Chaini331 – 566236Capsid protein VP3Sequence AnalysisPRO_0000426691Add
    BLAST
    Chaini566 – 848283Capsid protein VP1Sequence AnalysisPRO_0000426692Add
    BLAST
    Chaini849 – 1429581P2By similarityPRO_0000426693Add
    BLAST
    Chaini849 – 1001153Protease 2ASequence AnalysisPRO_0000426694Add
    BLAST
    Chaini1002 – 110099Protein 2BSequence AnalysisPRO_0000040162Add
    BLAST
    Chaini1101 – 1429329Protein 2CSequence AnalysisPRO_0000040163Add
    BLAST
    Chaini1430 – 2185756P3By similarityPRO_0000426695Add
    BLAST
    Chaini1430 – 1540111Protein 3ABSequence AnalysisPRO_0000426696Add
    BLAST
    Chaini1430 – 151889Protein 3ASequence AnalysisPRO_0000040164Add
    BLAST
    Chaini1519 – 154022Viral protein genome-linkedSequence AnalysisPRO_0000426697Add
    BLAST
    Chaini1541 – 2185645Protein 3CDSequence AnalysisPRO_0000426698Add
    BLAST
    Chaini1541 – 1722182Protease 3CSequence AnalysisPRO_0000426699Add
    BLAST
    Chaini1723 – 2185463RNA-directed RNA polymeraseBy similarityPRO_0000426700Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1521 – 15211O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.By similarity
    VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity
    Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
    Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion By similarity.By similarity
    Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
    Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion By similarity.By similarity
    Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Interactioni

    Subunit structurei

    Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Interact with host CXADR. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid By similarity. Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 By similarity. Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis By similarity. Protein 3AB: interacts with protein 3CD By similarity. Viral protein genome-linked: interacts with RNA-directed RNA polymerase By similarity. Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD By similarity.By similarity

    Structurei

    Secondary structure

    1
    2185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 353
    Helixi36 – 383
    Helixi51 – 544
    Beta strandi63 – 653
    Beta strandi83 – 875
    Beta strandi90 – 967
    Turni113 – 1153
    Turni127 – 1293
    Beta strandi138 – 1403
    Beta strandi147 – 1515
    Helixi153 – 1553
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi188 – 19811
    Beta strandi203 – 2053
    Helixi212 – 2154
    Beta strandi225 – 2273
    Helixi239 – 2413
    Turni242 – 2443
    Helixi248 – 2536
    Beta strandi254 – 2607
    Turni261 – 2633
    Beta strandi265 – 2717
    Beta strandi276 – 2783
    Turni282 – 2843
    Beta strandi288 – 29912
    Beta strandi308 – 32417
    Turni338 – 3414
    Beta strandi353 – 3553
    Helixi373 – 3775
    Helixi391 – 3933
    Helixi395 – 3984
    Beta strandi400 – 4034
    Beta strandi406 – 4094
    Beta strandi411 – 4177
    Turni419 – 4213
    Turni423 – 4275
    Helixi429 – 4346
    Beta strandi437 – 4415
    Beta strandi444 – 4507
    Beta strandi459 – 4657
    Beta strandi467 – 4693
    Helixi475 – 4784
    Beta strandi481 – 4877
    Beta strandi493 – 4986
    Beta strandi503 – 5053
    Beta strandi519 – 5268
    Beta strandi536 – 54611
    Beta strandi551 – 5555
    Beta strandi597 – 6004
    Helixi602 – 6043
    Helixi612 – 6143
    Helixi628 – 6303
    Helixi632 – 6365
    Beta strandi640 – 65112
    Beta strandi657 – 6615
    Helixi668 – 6747
    Beta strandi677 – 69418
    Beta strandi708 – 7147
    Helixi727 – 7304
    Beta strandi732 – 7343
    Beta strandi736 – 7405
    Beta strandi747 – 7504
    Beta strandi755 – 7617
    Beta strandi765 – 7684
    Helixi777 – 7793
    Beta strandi785 – 7928
    Beta strandi799 – 81719
    Beta strandi828 – 8303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OOPX-ray3.00A569-851[»]
    B70-330[»]
    C331-568[»]
    D1-69[»]
    ProteinModelPortaliP13900.
    SMRiP13900. Positions 2-69, 79-568, 581-1001, 1541-2185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13900.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14951494CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1512 – 2185674CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1496 – 151116Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1205 – 1361157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1541 – 1706166Peptidase C3Add
    BLAST
    Domaini1950 – 2066117RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni566 – 58217Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1430 – 145324DisorderedBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated
    Contains 1 peptidase C3 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR014838. P3A.
    IPR000081. Peptidase_C3.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR003138. Pico_P1A.
    IPR002527. Pico_P2B.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF08727. P3A. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF02226. Pico_P1A. 1 hit.
    PF00947. Pico_P2A. 1 hit.
    PF01552. Pico_P2B. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 3 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    ProDomiPD001306. Peptidase_C3. 1 hit.
    PD649346. Pico_P2B. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 2 hits.
    SSF52540. SSF52540. 1 hit.
    SSF89043. SSF89043. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13900-1 [UniParc]FASTAAdd to Basket

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    MGAQVSTQKT GAHETSLSAA GNSVIHYTNI NYYKDAASNS ANRQDFTQDP     50
    GKFTEPVKDI MVKSMPALNS PSAEECGYSD RVRSITLGNS TITTQECANV 100
    VVGYGVWPTY LKDEEATAED QPTQPDVATC RFYTLESVMW QQSSPGWWWK 150
    FPDALSNMGL FGQNMQYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE 200
    MGCATLANKP DPKSLSKGEI ANMFESQNST GETAVQANVI NAGMGVGVGN 250
    LTIFPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MVIPFAPLSY 300
    STGATTYVPI TVTVAPMCAE YNGLRLAGKQ GLPTLSTPGS NQFLTSDDFQ 350
    SPSAMPQFDV TPEMDIPGQV NNLMEIAEVD SVVPVNNTEG KVMSIEAYQI 400
    PVQSNPTNGS QVFGFPLTPG ANSVLNRTLL GEILNYYAHW SGSIKLTFMF 450
    CGSAMATGKF LLAYSPPGAG APTTRKEAML GTHVIWDVGL QSSCVLCIPW 500
    ISQTHYRYVV MDEYTAGGYI TCWYQTNIVV PADAQSDCKI LCFVSACNDF 550
    SVRMLKDTPF IKQDNFFQGP PGEVMGRAIA RVADTIGSGP VNSESIPALT 600
    AAETGHTSQV VPSDTMQTRH VKNYHSRSES TVENFLCRSA CVFYTTYKNH 650
    DSDGDNFAYW VINTRQVAQL RRKLEMFTYA RFDLELTFVI TSTQEQPTVR 700
    GQDAPVLTHQ IMYVPPGGPV PTKVNSYSWQ TSTNPSVFWT EGSAPPRMSI 750
    PFIGIGNAYS MFYDGWARFD KQGTYGISTL NNMGTLYMRH VNDGGPGPIV 800
    STVRIYFKPK HVKTWVPRPP RLCQYQKAGN VNFEPTGVTE GRTDITTMKT 850
    TGAFGQQSGA VYVGNYRVVN RHLATRADWQ NCVWEDYNRD LLVSTTTAHG 900
    CDTIARCDCT AGVYFCASRN KHYPVTFEGP GLVEVQESEY YPKKYQSHVL 950
    LAAGFAEPGD CGGILRCQHG VIGIVTVGGE GVVGFADVRD LLWLEDDAME 1000
    QGVRDYVEQL GNCFGSGFTN QICEQVTLLK ESLIGQDSIL EKSLKALVKI 1050
    VSALVIVVRN HDDLITVTAT LALIGCTTSP WRWLKQKVSQ YYGIPMAERQ 1100
    NSGWLKKFTE MTNACKGMEW IAIKIQKFIE WLKVKILPEV KEKHEFLNRL 1150
    KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR 1200
    VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL 1250
    NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV 1300
    PPMAALEEKG ILFTSPFVLA STNAGSVNAP TVSDSRALVR RFHFDMNIEV 1350
    VSMYSQNGKI NMPMAVKTCD EECCPVNFKK CCPLVCGKAI QFIDRRTQVR 1400
    YSLDMLVTEM FREYNHRHSV GATLEALFQG PPVYREIKIS VAPETPPPPA 1450
    VADLLKSVDS EAVREYCKEK GWLIPEVDST LQIEKHVNRA FICLQALTTF 1500
    VSVAGIIYII YKLFAGFQGA YTGMPNQKPR VPTLRQAKVQ GPAFEFAVAM 1550
    MKRNASTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQVVGVLDAK 1600
    ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AREEVEVNEA VLAINTSKFP 1650
    NMYIPVGRVT DYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI 1700
    HVGGNGHQGF SAALLRHYFN EEQGEIEFIE SSKDAGFPVI NTPSKTKLEP 1750
    SVFHHVFEGN KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMMEA 1800
    VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK 1850
    RDILSKKTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK VAKGKSRLIE 1900
    ASSLNDSVAM RQTFGNLYKT FHLNPGIVTG SAVGCDPDVF WSKIPVMLDG 1950
    HLIAFDYSGY DASLSPVWFT CLKLLLEKLG YTNKETNYID YLCNSHHLYR 2000
    DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY 2050
    GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR 2100
    YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE 2150
    HEYEEFIRKI RSVRVGRCLS LPAFSTLRRK WLDSF 2185
    Length:2,185
    Mass (Da):243,365
    Last modified:January 23, 2007 - v3
    Checksum:iC9B103052934E1B8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54521 Genomic RNA. Translation: CAA38377.1.
    PIRiS11670. GNNYSV.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54521 Genomic RNA. Translation: CAA38377.1 .
    PIRi S11670. GNNYSV.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OOP X-ray 3.00 A 569-851 [» ]
    B 70-330 [» ]
    C 331-568 [» ]
    D 1-69 [» ]
    ProteinModelPortali P13900.
    SMRi P13900. Positions 2-69, 79-568, 581-1001, 1541-2185.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.020.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P13900.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR014838. P3A.
    IPR000081. Peptidase_C3.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR003138. Pico_P1A.
    IPR002527. Pico_P2B.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF08727. P3A. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF02226. Pico_P1A. 1 hit.
    PF00947. Pico_P2A. 1 hit.
    PF01552. Pico_P2B. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 3 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    ProDomi PD001306. Peptidase_C3. 1 hit.
    PD649346. Pico_P2B. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 2 hits.
    SSF52540. SSF52540. 1 hit.
    SSF89043. SSF89043. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence of a pathogenic swine vesicular disease virus."
      Seechurn P., Knowles N.J., McCauley J.W.
      Virus Res. 16:255-274(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "The coxsackie-adenovirus receptor (CAR) is used by reference strains and clinical isolates representing all six serotypes of coxsackievirus group B and by swine vesicular disease virus."
      Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A., Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N., Gauntt C.J., Liu P.P.
      Virology 271:99-108(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST CXADR.
    3. "Crystal structure of Swine vesicular disease virus and implications for host adaptation."
      Fry E.E., Knowles N.J., Newman J.W., Wilsden G., Rao Z., King A.M., Stuart D.I.
      J. Virol. 77:5475-5486(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 71-851.

    Entry informationi

    Entry nameiPOLG_SVDVU
    AccessioniPrimary (citable) accession number: P13900
    Secondary accession number(s): Q84794
    , Q84795, Q84796, Q84797, Q84798, Q84799, Q84800, Q84801, Q84802, Q84803, Q84804
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3