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P03313

- POLG_CXB3N

UniProt

P03313 - POLG_CXB3N

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Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus B3 (strain Nancy)
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 CD55 and 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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity.1 Publication
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.1 Publication

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
Sitei332 – 3332Cleavage; 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. 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 mRNA export from nucleus Source: UniProtKB-KW
  9. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  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

MEROPSiC03.011.

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
OrganismiCoxsackievirus B3 (strain Nancy)
Taxonomic identifieri103903 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007760: 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 predictionAdd
BLAST
Intramembranei1496 – 151116 Reviewed predictionAdd
BLAST
Topological domaini1512 – 2185674Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. host cell nucleus Source: CACAO
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane Source: UniProtKB-KW
  5. 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 host By similarity
Chaini2 – 21852184Genome polyprotein By similarityPRO_0000426266Add
BLAST
Chaini2 – 848847P1 By similarityPRO_0000426267Add
BLAST
Chaini2 – 332331Capsid protein VP0 Reviewed predictionPRO_0000426268Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed predictionPRO_0000426269Add
BLAST
Chaini70 – 332263Capsid protein VP2 Reviewed predictionPRO_0000426270Add
BLAST
Chaini333 – 568236Capsid protein VP3 Reviewed predictionPRO_0000426271Add
BLAST
Chaini568 – 848281Capsid protein VP1 Reviewed predictionPRO_0000426272Add
BLAST
Chaini849 – 1429581P2 By similarityPRO_0000426273Add
BLAST
Chaini849 – 1001153Protease 2A Reviewed predictionPRO_0000426274Add
BLAST
Chaini1002 – 110099Protein 2B Reviewed predictionPRO_0000039587Add
BLAST
Chaini1101 – 1429329Protein 2C Reviewed predictionPRO_0000039588Add
BLAST
Chaini1430 – 2185756P3 By similarityPRO_0000426275Add
BLAST
Chaini1430 – 1540111Protein 3AB Reviewed predictionPRO_0000426276Add
BLAST
Chaini1430 – 151889Protein 3A Reviewed predictionPRO_0000039589Add
BLAST
Chaini1519 – 154022Viral protein genome-linked Reviewed predictionPRO_0000426277Add
BLAST
Chaini1541 – 2185645Protein 3CD Reviewed predictionPRO_0000426278Add
BLAST
Chaini1541 – 1722182Protease 3C Reviewed predictionPRO_0000426279Add
BLAST
Chaini1723 – 2185463RNA-directed RNA polymerase By similarityPRO_0000426280Add
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 CD55 and 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.2 Publications

Structurei

Secondary structure

1
2185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1528 – 15303
Helixi1542 – 155413
Beta strandi1555 – 15606
Beta strandi1563 – 157210
Beta strandi1574 – 15785
Helixi1579 – 15813
Beta strandi1585 – 15895
Beta strandi1592 – 160312
Beta strandi1609 – 16179
Helixi1627 – 16293
Beta strandi1637 – 16448
Beta strandi1646 – 16494
Beta strandi1652 – 166716
Beta strandi1670 – 168011
Beta strandi1690 – 16934
Beta strandi1696 – 170510
Beta strandi1708 – 17136
Helixi1716 – 17194
Beta strandi1725 – 17317
Helixi1732 – 17354
Turni1752 – 17565
Helixi1777 – 17826
Helixi1795 – 180915
Helixi1820 – 18256
Helixi1843 – 18453
Helixi1850 – 18523
Turni1856 – 18583
Helixi1862 – 187110
Beta strandi1877 – 18815
Helixi1888 – 18925
Beta strandi1898 – 19014
Helixi1904 – 192320
Turni1927 – 19304
Helixi1937 – 19404
Turni1941 – 19433
Helixi1944 – 19474
Beta strandi1950 – 19534
Beta strandi1956 – 19594
Helixi1960 – 19634
Helixi1966 – 197813
Turni1983 – 19864
Helixi1987 – 19937
Beta strandi1994 – 19996
Beta strandi2002 – 20098
Helixi2017 – 203620
Helixi2042 – 20443
Beta strandi2046 – 20505
Beta strandi2053 – 20608
Helixi2064 – 20729
Turni2073 – 20753
Beta strandi2078 – 20803
Helixi2081 – 20833
Turni2092 – 20943
Beta strandi2100 – 21045
Beta strandi2106 – 21083
Beta strandi2111 – 21155
Helixi2118 – 21258
Beta strandi2127 – 21293
Helixi2131 – 21333
Helixi2134 – 214512
Helixi2146 – 21483
Helixi2150 – 216011
Helixi2164 – 21685
Helixi2174 – 218411

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VB0X-ray2.40A1541-1723[»]
2ZTXX-ray1.72A1541-1723[»]
2ZTYX-ray1.72A1541-1723[»]
2ZTZX-ray2.00A/B1541-1723[»]
2ZU1X-ray1.38A/B1541-1723[»]
2ZU3X-ray1.75A1541-1723[»]
3CDUX-ray2.10A1724-2185[»]
3CDWX-ray2.50A1724-2185[»]
H1519-1540[»]
ProteinModelPortaliP03313.
SMRiP03313. Positions 2-69, 77-570, 583-1001, 1541-2185.

Miscellaneous databases

EvolutionaryTraceiP03313.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1205 – 1361157SF3 helicaseAdd
BLAST
Domaini1541 – 1706166Peptidase C3Add
BLAST
Domaini1950 – 2066117RdRp catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni568 – 58417Amphipatic alpha-helix Reviewed predictionAdd
BLAST
Regioni1430 – 145324Disordered By similarityAdd
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.

P03313-1 [UniParc]FASTAAdd to Basket

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MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP     50
GKFTEPVKDI MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV 100
VVGYGVWPDY LKDSEATAED QPTQPDVATC RFYTLDSVQW QKTSPGWWWK 150
LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ CNASKFHQGC LLVVCVPEAE 200
MGCATLDNTP SSAELLGGDT AKEFADKPVA SGSNKLVQRV VYNAGMGVGV 250
GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL 300
DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD 350
FQSPSAMPQY DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY 400
QIPVRSNEGS GTQVFGFPLQ PGYSSVFSRT LLGEILNYYT HWSGSIKLTF 450
MFCGSAMATG KFLLAYSPPG AGAPTKRVDA MLGTHVIWDV GLQSSCVLCI 500
PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC YIMCFVSACN 550
DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA 600
LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK 650
NSGAKRYAEW VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ 700
NQDAQILTHQ IMYVPPGGPV PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI 750
PFLSIGNAYS NFYDGWSEFS RNGVYGINTL NNMGTLYARH VNAGSTGPIK 800
STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT TRQSITTMTN 850
TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG 900
CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL 950
LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME 1000
QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI 1050
ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ 1100
NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV REKHEFLNRL 1150
KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR 1200
VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL 1250
NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV 1300
PPMAALEEKG ILFTSPFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV 1350
ISMYSQNGKI NMPMSVKTCD DECCPVNFKK CCPLVCGKAI QFIDRRTQVR 1400
YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS VAPETPPPPA 1450
IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF 1500
VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM 1550
MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK 1600
ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP 1650
NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI 1700
HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI NTPSKTKLEP 1750
SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA 1800
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK 1850
RDILSKKTKD LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE 1900
ASSLNDSVAM RQTFGNLYKT FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG 1950
HLIAFDYSGY DASLSPVWFA CLKMLLEKLG YTHKETNYID YLCNSHHLYR 2000
DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY 2050
GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNATFLKR 2100
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE 2150
HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF 2185
Length:2,185
Mass (Da):243,453
Last modified:January 23, 2007 - v4
Checksum:i1B5ECE3DA47338FF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161R → G in AAA74400. 1 Publication
Sequence conflicti177 – 1771V → D in AAA74400. 1 Publication
Sequence conflicti469 – 4691P → L in AAA74400. 1 Publication
Sequence conflicti487 – 4871I → V in AAA74400. 1 Publication
Sequence conflicti510 – 5101F → Y in AAA74400. 1 Publication
Sequence conflicti516 – 5161Y → C in AAA74400. 1 Publication
Sequence conflicti566 – 5661Q → E in AAA74400. 1 Publication
Sequence conflicti593 – 5931T → N in AAA74400. 1 Publication
Sequence conflicti650 – 6501K → E in AAA74400. 1 Publication
Sequence conflicti854 – 86512FGQQS…VYVGN → IWTTIRGSVCGD in AAA74400. 1 PublicationAdd
BLAST
Sequence conflicti873 – 8731L → S in AAA74400. 1 Publication
Sequence conflicti1097 – 10971A → P in AAA74400. 1 Publication
Sequence conflicti1280 – 12801Q → H in AAA74400. 1 Publication
Sequence conflicti1437 – 14371I → F in AAA74400. 1 Publication
Sequence conflicti1503 – 15031V → M in AAA74400. 1 Publication
Sequence conflicti1616 – 16161K → E in AAA74400. 1 Publication
Sequence conflicti1624 – 16241R → G in AAA74400. 1 Publication
Sequence conflicti1627 – 16271R → G in AAA74400. 1 Publication
Sequence conflicti1630 – 16301L → V in AAA74400. 1 Publication
Sequence conflicti1718 – 17181Y → N in AAA74400. 1 Publication
Sequence conflicti1734 – 17341D → V in AAA74400. 1 Publication
Sequence conflicti1758 – 17581E → V1 Publication
Sequence conflicti1758 – 17581E → V1 Publication
Sequence conflicti1824 – 18241V → R1 Publication
Sequence conflicti1824 – 18241V → R1 Publication
Sequence conflicti1867 – 18671C → R1 Publication
Sequence conflicti1867 – 18671C → R1 Publication
Sequence conflicti1880 – 18801Y → H1 Publication
Sequence conflicti1880 – 18801Y → H1 Publication
Sequence conflicti2001 – 20011D → N1 Publication
Sequence conflicti2001 – 20011D → N1 Publication
Sequence conflicti2095 – 20951A → V1 Publication
Sequence conflicti2095 – 20951A → V1 Publication
Sequence conflicti2115 – 21151V → A1 Publication
Sequence conflicti2115 – 21151V → A1 Publication
Sequence conflicti2175 – 21751S → T1 Publication
Sequence conflicti2175 – 21751S → T1 Publication
Sequence conflicti2178 – 21781R → G1 Publication
Sequence conflicti2178 – 21781R → G1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M33854 Genomic RNA. Translation: AAA42931.1.
K02709 Genomic RNA. Translation: AAA42932.1.
M16572 Genomic RNA. Translation: AAA74400.1.
PIRiA26354. GNNYB3.
A34664. GNNYBT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M33854 Genomic RNA. Translation: AAA42931.1 .
K02709 Genomic RNA. Translation: AAA42932.1 .
M16572 Genomic RNA. Translation: AAA74400.1 .
PIRi A26354. GNNYB3.
A34664. GNNYBT.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VB0 X-ray 2.40 A 1541-1723 [» ]
2ZTX X-ray 1.72 A 1541-1723 [» ]
2ZTY X-ray 1.72 A 1541-1723 [» ]
2ZTZ X-ray 2.00 A/B 1541-1723 [» ]
2ZU1 X-ray 1.38 A/B 1541-1723 [» ]
2ZU3 X-ray 1.75 A 1541-1723 [» ]
3CDU X-ray 2.10 A 1724-2185 [» ]
3CDW X-ray 2.50 A 1724-2185 [» ]
H 1519-1540 [» ]
ProteinModelPortali P03313.
SMRi P03313. Positions 2-69, 77-570, 583-1001, 1541-2185.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2396505.

Protein family/group databases

MEROPSi C03.011.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03313.

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. "Complete nucleotide sequence of infectious Coxsackievirus B3 cDNA: two initial 5' uridine residues are regained during plus-strand RNA synthesis."
    Klump W.M., Bergmann I., Mueller B.C., Ameis D., Kandolf R.
    J. Virol. 64:1573-1583(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Replicase gene of coxsackievirus B3."
    Staalhandske P.O.K., Lindberg A.M., Pettersson U.
    J. Virol. 51:742-746(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1724-2185.
  4. "Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment."
    Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F., Barry R.D.
    J. Virol. 69:3873-3877(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST CD55.
  5. "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.
  6. "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment."
    Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L., Melchers W.J., van Kuppeveld F.J.
    J. Virol. 80:11852-11860(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEIN 3A.

Entry informationi

Entry nameiPOLG_CXB3N
AccessioniPrimary (citable) accession number: P03313
Secondary accession number(s): Q66322
, Q66323, Q66324, Q66325, Q66326, Q66327, Q66328, Q83744
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 155 of the entry and version 4 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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