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P13900

- POLG_SVDVU

UniProt

P13900 - POLG_SVDVU

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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

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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 14951494CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1496 – 151116Sequence AnalysisAdd
BLAST
Topological domaini1512 – 2185674CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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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        10         20         30         40         50
MGAQVSTQKT GAHETSLSAA GNSVIHYTNI NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
GKFTEPVKDI MVKSMPALNS PSAEECGYSD RVRSITLGNS TITTQECANV
110 120 130 140 150
VVGYGVWPTY LKDEEATAED QPTQPDVATC RFYTLESVMW QQSSPGWWWK
160 170 180 190 200
FPDALSNMGL FGQNMQYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGCATLANKP DPKSLSKGEI ANMFESQNST GETAVQANVI NAGMGVGVGN
260 270 280 290 300
LTIFPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MVIPFAPLSY
310 320 330 340 350
STGATTYVPI TVTVAPMCAE YNGLRLAGKQ GLPTLSTPGS NQFLTSDDFQ
360 370 380 390 400
SPSAMPQFDV TPEMDIPGQV NNLMEIAEVD SVVPVNNTEG KVMSIEAYQI
410 420 430 440 450
PVQSNPTNGS QVFGFPLTPG ANSVLNRTLL GEILNYYAHW SGSIKLTFMF
460 470 480 490 500
CGSAMATGKF LLAYSPPGAG APTTRKEAML GTHVIWDVGL QSSCVLCIPW
510 520 530 540 550
ISQTHYRYVV MDEYTAGGYI TCWYQTNIVV PADAQSDCKI LCFVSACNDF
560 570 580 590 600
SVRMLKDTPF IKQDNFFQGP PGEVMGRAIA RVADTIGSGP VNSESIPALT
610 620 630 640 650
AAETGHTSQV VPSDTMQTRH VKNYHSRSES TVENFLCRSA CVFYTTYKNH
660 670 680 690 700
DSDGDNFAYW VINTRQVAQL RRKLEMFTYA RFDLELTFVI TSTQEQPTVR
710 720 730 740 750
GQDAPVLTHQ IMYVPPGGPV PTKVNSYSWQ TSTNPSVFWT EGSAPPRMSI
760 770 780 790 800
PFIGIGNAYS MFYDGWARFD KQGTYGISTL NNMGTLYMRH VNDGGPGPIV
810 820 830 840 850
STVRIYFKPK HVKTWVPRPP RLCQYQKAGN VNFEPTGVTE GRTDITTMKT
860 870 880 890 900
TGAFGQQSGA VYVGNYRVVN RHLATRADWQ NCVWEDYNRD LLVSTTTAHG
910 920 930 940 950
CDTIARCDCT AGVYFCASRN KHYPVTFEGP GLVEVQESEY YPKKYQSHVL
960 970 980 990 1000
LAAGFAEPGD CGGILRCQHG VIGIVTVGGE GVVGFADVRD LLWLEDDAME
1010 1020 1030 1040 1050
QGVRDYVEQL GNCFGSGFTN QICEQVTLLK ESLIGQDSIL EKSLKALVKI
1060 1070 1080 1090 1100
VSALVIVVRN HDDLITVTAT LALIGCTTSP WRWLKQKVSQ YYGIPMAERQ
1110 1120 1130 1140 1150
NSGWLKKFTE MTNACKGMEW IAIKIQKFIE WLKVKILPEV KEKHEFLNRL
1160 1170 1180 1190 1200
KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR
1210 1220 1230 1240 1250
VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL
1260 1270 1280 1290 1300
NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV
1310 1320 1330 1340 1350
PPMAALEEKG ILFTSPFVLA STNAGSVNAP TVSDSRALVR RFHFDMNIEV
1360 1370 1380 1390 1400
VSMYSQNGKI NMPMAVKTCD EECCPVNFKK CCPLVCGKAI QFIDRRTQVR
1410 1420 1430 1440 1450
YSLDMLVTEM FREYNHRHSV GATLEALFQG PPVYREIKIS VAPETPPPPA
1460 1470 1480 1490 1500
VADLLKSVDS EAVREYCKEK GWLIPEVDST LQIEKHVNRA FICLQALTTF
1510 1520 1530 1540 1550
VSVAGIIYII YKLFAGFQGA YTGMPNQKPR VPTLRQAKVQ GPAFEFAVAM
1560 1570 1580 1590 1600
MKRNASTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQVVGVLDAK
1610 1620 1630 1640 1650
ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AREEVEVNEA VLAINTSKFP
1660 1670 1680 1690 1700
NMYIPVGRVT DYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI
1710 1720 1730 1740 1750
HVGGNGHQGF SAALLRHYFN EEQGEIEFIE SSKDAGFPVI NTPSKTKLEP
1760 1770 1780 1790 1800
SVFHHVFEGN KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMMEA
1810 1820 1830 1840 1850
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK
1860 1870 1880 1890 1900
RDILSKKTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK VAKGKSRLIE
1910 1920 1930 1940 1950
ASSLNDSVAM RQTFGNLYKT FHLNPGIVTG SAVGCDPDVF WSKIPVMLDG
1960 1970 1980 1990 2000
HLIAFDYSGY DASLSPVWFT CLKLLLEKLG YTNKETNYID YLCNSHHLYR
2010 2020 2030 2040 2050
DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY
2060 2070 2080 2090 2100
GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR
2110 2120 2130 2140 2150
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE
2160 2170 2180
HEYEEFIRKI RSVRVGRCLS LPAFSTLRRK WLDSF
Length:2,185
Mass (Da):243,365
Last modified:January 23, 2007 - v3
Checksum:iC9B103052934E1B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X54521 Genomic RNA. Translation: CAA38377.1 .
PIRi S11670. GNNYSV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 151 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