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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).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
Sitei332 – 3332Cleavage; 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
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 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. 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 hostBy similarity
Chaini2 – 21852184Genome polyproteinBy similarityPRO_0000426266Add
BLAST
Chaini2 – 848847P1By similarityPRO_0000426267Add
BLAST
Chaini2 – 332331Capsid protein VP0Sequence AnalysisPRO_0000426268Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426269Add
BLAST
Chaini70 – 332263Capsid protein VP2Sequence AnalysisPRO_0000426270Add
BLAST
Chaini333 – 568236Capsid protein VP3Sequence AnalysisPRO_0000426271Add
BLAST
Chaini568 – 848281Capsid protein VP1Sequence AnalysisPRO_0000426272Add
BLAST
Chaini849 – 1429581P2By similarityPRO_0000426273Add
BLAST
Chaini849 – 1001153Protease 2ASequence AnalysisPRO_0000426274Add
BLAST
Chaini1002 – 110099Protein 2BSequence AnalysisPRO_0000039587Add
BLAST
Chaini1101 – 1429329Protein 2CSequence AnalysisPRO_0000039588Add
BLAST
Chaini1430 – 2185756P3By similarityPRO_0000426275Add
BLAST
Chaini1430 – 1540111Protein 3ABSequence AnalysisPRO_0000426276Add
BLAST
Chaini1430 – 151889Protein 3ASequence AnalysisPRO_0000039589Add
BLAST
Chaini1519 – 154022Viral protein genome-linkedSequence AnalysisPRO_0000426277Add
BLAST
Chaini1541 – 2185645Protein 3CDSequence AnalysisPRO_0000426278Add
BLAST
Chaini1541 – 1722182Protease 3CSequence AnalysisPRO_0000426279Add
BLAST
Chaini1723 – 2185463RNA-directed RNA polymeraseBy similarityPRO_0000426280Add
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 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).By similarity

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03313.

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
Regioni568 – 58417Amphipatic 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.

P03313-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
GKFTEPVKDI MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV
110 120 130 140 150
VVGYGVWPDY LKDSEATAED QPTQPDVATC RFYTLDSVQW QKTSPGWWWK
160 170 180 190 200
LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGCATLDNTP SSAELLGGDT AKEFADKPVA SGSNKLVQRV VYNAGMGVGV
260 270 280 290 300
GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
310 320 330 340 350
DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD
360 370 380 390 400
FQSPSAMPQY DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY
410 420 430 440 450
QIPVRSNEGS GTQVFGFPLQ PGYSSVFSRT LLGEILNYYT HWSGSIKLTF
460 470 480 490 500
MFCGSAMATG KFLLAYSPPG AGAPTKRVDA MLGTHVIWDV GLQSSCVLCI
510 520 530 540 550
PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC YIMCFVSACN
560 570 580 590 600
DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
610 620 630 640 650
LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK
660 670 680 690 700
NSGAKRYAEW VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ
710 720 730 740 750
NQDAQILTHQ IMYVPPGGPV PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI
760 770 780 790 800
PFLSIGNAYS NFYDGWSEFS RNGVYGINTL NNMGTLYARH VNAGSTGPIK
810 820 830 840 850
STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT TRQSITTMTN
860 870 880 890 900
TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG
910 920 930 940 950
CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL
960 970 980 990 1000
LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME
1010 1020 1030 1040 1050
QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI
1060 1070 1080 1090 1100
ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ
1110 1120 1130 1140 1150
NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV REKHEFLNRL
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 STNAGSINAP TVSDSRALAR RFHFDMNIEV
1360 1370 1380 1390 1400
ISMYSQNGKI NMPMSVKTCD DECCPVNFKK CCPLVCGKAI QFIDRRTQVR
1410 1420 1430 1440 1450
YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS VAPETPPPPA
1460 1470 1480 1490 1500
IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF
1510 1520 1530 1540 1550
VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM
1560 1570 1580 1590 1600
MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK
1610 1620 1630 1640 1650
ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP
1660 1670 1680 1690 1700
NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI
1710 1720 1730 1740 1750
HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI NTPSKTKLEP
1760 1770 1780 1790 1800
SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA
1810 1820 1830 1840 1850
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK
1860 1870 1880 1890 1900
RDILSKKTKD LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE
1910 1920 1930 1940 1950
ASSLNDSVAM RQTFGNLYKT FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG
1960 1970 1980 1990 2000
HLIAFDYSGY DASLSPVWFA CLKMLLEKLG YTHKETNYID YLCNSHHLYR
2010 2020 2030 2040 2050
DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY
2060 2070 2080 2090 2100
GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNATFLKR
2110 2120 2130 2140 2150
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE
2160 2170 2180
HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF
Length:2,185
Mass (Da):243,453
Last modified:January 23, 2007 - v4
Checksum:i1B5ECE3DA47338FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161R → G in AAA74400. (PubMed:3027968)Curated
Sequence conflicti177 – 1771V → D in AAA74400. (PubMed:3027968)Curated
Sequence conflicti469 – 4691P → L in AAA74400. (PubMed:3027968)Curated
Sequence conflicti487 – 4871I → V in AAA74400. (PubMed:3027968)Curated
Sequence conflicti510 – 5101F → Y in AAA74400. (PubMed:3027968)Curated
Sequence conflicti516 – 5161Y → C in AAA74400. (PubMed:3027968)Curated
Sequence conflicti566 – 5661Q → E in AAA74400. (PubMed:3027968)Curated
Sequence conflicti593 – 5931T → N in AAA74400. (PubMed:3027968)Curated
Sequence conflicti650 – 6501K → E in AAA74400. (PubMed:3027968)Curated
Sequence conflicti854 – 86512FGQQS…VYVGN → IWTTIRGSVCGD in AAA74400. (PubMed:3027968)CuratedAdd
BLAST
Sequence conflicti873 – 8731L → S in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1097 – 10971A → P in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1280 – 12801Q → H in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1437 – 14371I → F in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1503 – 15031V → M in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1616 – 16161K → E in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1624 – 16241R → G in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1627 – 16271R → G in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1630 – 16301L → V in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1718 – 17181Y → N in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1734 – 17341D → V in AAA74400. (PubMed:3027968)Curated
Sequence conflicti1758 – 17581E → V(PubMed:3027968)Curated
Sequence conflicti1758 – 17581E → V(PubMed:6088796)Curated
Sequence conflicti1824 – 18241V → R(PubMed:3027968)Curated
Sequence conflicti1824 – 18241V → R(PubMed:6088796)Curated
Sequence conflicti1867 – 18671C → R(PubMed:3027968)Curated
Sequence conflicti1867 – 18671C → R(PubMed:6088796)Curated
Sequence conflicti1880 – 18801Y → H(PubMed:3027968)Curated
Sequence conflicti1880 – 18801Y → H(PubMed:6088796)Curated
Sequence conflicti2001 – 20011D → N(PubMed:3027968)Curated
Sequence conflicti2001 – 20011D → N(PubMed:6088796)Curated
Sequence conflicti2095 – 20951A → V(PubMed:3027968)Curated
Sequence conflicti2095 – 20951A → V(PubMed:6088796)Curated
Sequence conflicti2115 – 21151V → A(PubMed:3027968)Curated
Sequence conflicti2115 – 21151V → A(PubMed:6088796)Curated
Sequence conflicti2175 – 21751S → T(PubMed:3027968)Curated
Sequence conflicti2175 – 21751S → T(PubMed:6088796)Curated
Sequence conflicti2178 – 21781R → G(PubMed:3027968)Curated
Sequence conflicti2178 – 21781R → G(PubMed:6088796)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BindingDBi P03313.
ChEMBLi CHEMBL2396505.

Protein family/group databases

MEROPSi C03.020.

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: November 26, 2014
This is version 158 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