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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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 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.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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 autolysis Reviewed prediction
Sitei330 – 3312Cleavage; by Protease 3C Reviewed prediction
Active sitei872 – 8721For Protease 2A activity By similarity
Active sitei890 – 8901For Protease 2A activity By similarity
Active sitei961 – 9611For Protease 2A activity By similarity
Sitei1001 – 10022Cleavage; by Protease 3C Reviewed prediction
Sitei1429 – 14302Cleavage; by Protease 3C Reviewed prediction
Sitei1518 – 15192Cleavage; by Protease 3C Reviewed prediction
Sitei1540 – 15412Cleavage; by Protease 3C Reviewed prediction
Active sitei1580 – 15801For Protease 3C activity Reviewed prediction
Active sitei1611 – 16111For Protease 3C activity Reviewed prediction
Active sitei1687 – 16871For Protease 3C activity By similarity
Sitei1723 – 17242Cleavage; by Protease 3C Reviewed prediction
Active sitei2052 – 20521For RdRp activity By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. RNA-protein covalent cross-linking Source: UniProtKB-KW
  3. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  4. induction by virus of host autophagy Source: UniProtKB
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  7. protein oligomerization Source: UniProtKB-KW
  8. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  10. suppression by virus of host translation Source: UniProtKB-KW
  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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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 – 14951494Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1496 – 151116 Reviewed prediction
Add
BLAST
Topological domaini1512 – 2185674Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
  2. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane 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 host By similarity
Chaini2 – 21852184Genome polyprotein By similarity
PRO_0000426686Add
BLAST
Chaini2 – 848847P1 By similarity
PRO_0000426687Add
BLAST
Chaini2 – 330329Capsid protein VP0 Reviewed prediction
PRO_0000426688Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed prediction
PRO_0000426689Add
BLAST
Chaini70 – 330261Capsid protein VP2 Reviewed prediction
PRO_0000426690Add
BLAST
Chaini331 – 566236Capsid protein VP3 Reviewed prediction
PRO_0000426691Add
BLAST
Chaini566 – 848283Capsid protein VP1 Reviewed prediction
PRO_0000426692Add
BLAST
Chaini849 – 1429581P2 By similarity
PRO_0000426693Add
BLAST
Chaini849 – 1001153Protease 2A Reviewed prediction
PRO_0000426694Add
BLAST
Chaini1002 – 110099Protein 2B Reviewed prediction
PRO_0000040162Add
BLAST
Chaini1101 – 1429329Protein 2C Reviewed prediction
PRO_0000040163Add
BLAST
Chaini1430 – 2185756P3 By similarity
PRO_0000426695Add
BLAST
Chaini1430 – 1540111Protein 3AB Reviewed prediction
PRO_0000426696Add
BLAST
Chaini1430 – 151889Protein 3A Reviewed prediction
PRO_0000040164Add
BLAST
Chaini1519 – 154022Viral protein genome-linked Reviewed prediction
PRO_0000426697Add
BLAST
Chaini1541 – 2185645Protein 3CD Reviewed prediction
PRO_0000426698Add
BLAST
Chaini1541 – 1722182Protease 3C Reviewed prediction
PRO_0000426699Add
BLAST
Chaini1723 – 2185463RNA-directed RNA polymerase By similarity
PRO_0000426700Add
BLAST

Amino acid modifications

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

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.1 Publication

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP13900.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1205 – 1361157SF3 helicase
Add
BLAST
Domaini1541 – 1706166Peptidase C3
Add
BLAST
Domaini1950 – 2066117RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni566 – 58217Amphipatic alpha-helix Reviewed prediction
Add
BLAST
Regioni1430 – 145324Disordered By similarity
Add
BLAST

Sequence similaritiesi

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: July 9, 2014
This is version 148 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

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