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P21404

- POLG_CXA9

UniProt

P21404 - POLG_CXA9

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Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus A9 (strain Griggs)
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 integrin ITGAV/ITGB6 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).By similarity
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).By similarity
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated (By similarity).PROSITE-ProRule annotation

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei69 – 702Cleavage; by autolysisSequence Analysis
Sitei330 – 3312Cleavage; by Protease 3CSequence Analysis
Active sitei888 – 8881For Protease 2A activityBy similarity
Active sitei906 – 9061For Protease 2A activityBy similarity
Active sitei977 – 9771For Protease 2A activityBy similarity
Sitei1017 – 10182Cleavage; by Protease 3CSequence Analysis
Sitei1445 – 14462Cleavage; by Protease 3CSequence Analysis
Sitei1534 – 15352Cleavage; by Protease 3CSequence Analysis
Sitei1556 – 15572Cleavage; by Protease 3CSequence Analysis
Active sitei1596 – 15961For Protease 3C activitySequence Analysis
Active sitei1627 – 16271For Protease 3C activitySequence Analysis
Active sitei1703 – 17031For Protease 3C activityBy similarity
Sitei1739 – 17402Cleavage; by Protease 3CSequence Analysis
Active sitei2068 – 20681For 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

MEROPSiC03.011.

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 A9 (strain Griggs)
Taxonomic identifieri12068 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000000288: 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 – 15111510CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1512 – 152716Sequence AnalysisAdd
BLAST
Topological domaini1528 – 2201674CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 22012200Genome polyproteinBy similarityPRO_0000426164Add
BLAST
Chaini2 – 849848P1By similarityPRO_0000426165Add
BLAST
Chaini2 – 330329Capsid protein VP0Sequence AnalysisPRO_0000426166Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426167Add
BLAST
Chaini70 – 330261Capsid protein VP2Sequence AnalysisPRO_0000426168Add
BLAST
Chaini331 – 566236Capsid protein VP3Sequence AnalysisPRO_0000426169Add
BLAST
Chaini566 – 849284Capsid protein VP1Sequence AnalysisPRO_0000426170Add
BLAST
Chaini850 – 1445596P2By similarityPRO_0000426171Add
BLAST
Chaini850 – 1017168Protease 2ASequence AnalysisPRO_0000426172Add
BLAST
Chaini1018 – 111699Protein 2BSequence AnalysisPRO_0000039508Add
BLAST
Chaini1117 – 1445329Protein 2CSequence AnalysisPRO_0000039509Add
BLAST
Chaini1446 – 2201756P3By similarityPRO_0000426173Add
BLAST
Chaini1446 – 1556111Protein 3ABSequence AnalysisPRO_0000426174Add
BLAST
Chaini1446 – 153489Protein 3ASequence AnalysisPRO_0000039510Add
BLAST
Chaini1535 – 155622Viral protein genome-linkedSequence AnalysisPRO_0000426175Add
BLAST
Chaini1557 – 2201645Protein 3CDSequence AnalysisPRO_0000426176Add
BLAST
Chaini1557 – 1738182Protease 3CSequence AnalysisPRO_0000426177Add
BLAST
Chaini1739 – 2201463RNA-directed RNA polymeraseBy similarityPRO_0000426178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1537 – 15371O-(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 integrin ITGAV/ITGB6 heterodimer. 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
2201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi26 – 294Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Helixi51 – 544Combined sources
Beta strandi57 – 593Combined sources
Beta strandi63 – 653Combined sources
Beta strandi83 – 875Combined sources
Beta strandi90 – 967Combined sources
Turni113 – 1153Combined sources
Helixi126 – 1283Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi147 – 1515Combined sources
Helixi153 – 1553Combined sources
Helixi159 – 1679Combined sources
Beta strandi168 – 18013Combined sources
Beta strandi188 – 19710Combined sources
Beta strandi203 – 2053Combined sources
Helixi212 – 2143Combined sources
Beta strandi225 – 2273Combined sources
Helixi239 – 2413Combined sources
Turni242 – 2454Combined sources
Helixi248 – 2536Combined sources
Beta strandi254 – 2607Combined sources
Turni261 – 2633Combined sources
Beta strandi265 – 2717Combined sources
Beta strandi276 – 2805Combined sources
Turni282 – 2843Combined sources
Beta strandi288 – 29912Combined sources
Beta strandi308 – 32417Combined sources
Turni338 – 3414Combined sources
Beta strandi353 – 3553Combined sources
Helixi374 – 3774Combined sources
Helixi394 – 3985Combined sources
Beta strandi400 – 4045Combined sources
Beta strandi411 – 4166Combined sources
Turni419 – 4213Combined sources
Turni423 – 4275Combined sources
Helixi429 – 4346Combined sources
Beta strandi437 – 4426Combined sources
Beta strandi444 – 4507Combined sources
Beta strandi459 – 4657Combined sources
Helixi475 – 4784Combined sources
Beta strandi481 – 4877Combined sources
Beta strandi493 – 4986Combined sources
Beta strandi503 – 5053Combined sources
Beta strandi507 – 5104Combined sources
Beta strandi519 – 5268Combined sources
Beta strandi536 – 54611Combined sources
Beta strandi551 – 5555Combined sources
Helixi602 – 6043Combined sources
Helixi612 – 6154Combined sources
Helixi628 – 6303Combined sources
Helixi632 – 6365Combined sources
Beta strandi640 – 65011Combined sources
Helixi654 – 6574Combined sources
Beta strandi658 – 6625Combined sources
Beta strandi665 – 6684Combined sources
Helixi669 – 6757Combined sources
Beta strandi678 – 69518Combined sources
Beta strandi709 – 7157Combined sources
Helixi728 – 7314Combined sources
Beta strandi733 – 7353Combined sources
Beta strandi737 – 7415Combined sources
Beta strandi748 – 7514Combined sources
Beta strandi756 – 7627Combined sources
Beta strandi766 – 7694Combined sources
Turni770 – 7723Combined sources
Beta strandi773 – 7775Combined sources
Helixi778 – 7814Combined sources
Beta strandi786 – 7938Combined sources
Beta strandi800 – 81819Combined sources
Beta strandi843 – 8453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4MX-ray2.901569-867[»]
270-330[»]
3331-568[»]
42-69[»]
3J2Jelectron microscopy9.54A631-852[»]
B331-568[»]
C79-330[»]
ProteinModelPortaliP21404.
SMRiP21404. Positions 2-69, 79-852, 868-1017, 1557-2201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21404.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1221 – 1377157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1557 – 1722166Peptidase C3Add
BLAST
Domaini1966 – 2082117RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni566 – 58217Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1446 – 146924DisorderedBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi858 – 8603Cell attachment site

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 2 peptidase C3 domains.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.

P21404-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGAQVSTQKT GAHETSLSAA GNSIIHYTNI NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
SKFTEPVKDV MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV
110 120 130 140 150
VVGYGRWPTY LRDDEATAED QPTQPDVATC RFYTLDSIKW EKGSVGWWWK
160 170 180 190 200
FPEALSDMGL FGQNMQYHYL GRAGYTIHLQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGGAVVGQAF SATAMANGDK AYEFTSATQS DQTKVQTAIH NAGMGVGVGN
260 270 280 290 300
LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHYNFTL MVIPFVKLDY
310 320 330 340 350
ADTASTYVPI TVTVAPMCAE YNGLRLAQAQ GLPTMNTPGS TQFLTSDDFQ
360 370 380 390 400
SPCALPQFDV TPSMNIPGEV KNLMEIAEVD SVVPVNNVQD TTDQMEMFRI
410 420 430 440 450
PVTINAPLQQ QVFGLRLQPG LDSVFKHTLL GEILNYYAHW SGSMKLTFVF
460 470 480 490 500
CGSAMATGKF LIAYSPPGAN PPKTRKDAML GTHIIWDIGL QSSCVLCVPW
510 520 530 540 550
ISQTHYRLVQ QDEYTSAGYV TCWYQTGMIV PPGTPNSSSI MCFASACNDF
560 570 580 590 600
SVRMLRDTPF ISQDNKLQGD VEEAIERARC TVADTMRTGP SNSASVPALT
610 620 630 640 650
AVETGHTSQV TPSDTMQTRH VKNYHSRSES TVENFLGRSA CVYMEEYKTT
660 670 680 690 700
DKHVNKKFVA WPINTKQMVQ MRRKLEMFTY LRFDMEVTFV ITSRQDPGTT
710 720 730 740 750
LAQDMPVLTR QIMYVPPGGP IPAKVDDYAW QTSTNPSIFW TEGNAPARMS
760 770 780 790 800
IPFISIGNAY SNFYDGWSNF DQRGSYGYNT LNNLGHIYVR HVSGSSPHPI
810 820 830 840 850
TSTIRVYFKP KHTRAWVPRP PRLCQYKKAF SVDFTPTPIT DTRKDINTVT
860 870 880 890 900
TVAQSRRRGD MSTLNTHGAF GQQSGAVYVG NYRVINRHLA THTDWQNCVW
910 920 930 940 950
EDYNRDLLVS TTTAHGCDVI ARCQCTTGVY FCASKNKHYP VSFEGPGLVE
960 970 980 990 1000
VQESEYYPKR YQSHVLLAAG FSEPGDCGGI LRCEHGVIGI VTMGGEGVVG
1010 1020 1030 1040 1050
FADVRDLLWL EDDAMEQGVK DYVEQLGNAF GSGFTNQICE QVNLLKESLV
1060 1070 1080 1090 1100
GQDSILEKSL KALVKIISAL VIVVRNHDDL ITVTAILALI GCTSSPWRWL
1110 1120 1130 1140 1150
KQKVSQYYGI PMAERQNDSW LKKFTEMTNA CKRMEWIAIK IQKFIEWLKV
1160 1170 1180 1190 1200
KILPEVREKH EFLNRLKQLP LLESQIATIE QSAPSQSDQE QLFSNVQYFA
1210 1220 1230 1240 1250
HYCRKYAPLY AAEAKRVFSL EKKMSNYIQF KSKCRIEPVC LLLHGSPGAG
1260 1270 1280 1290 1300
KSVATNLIGR SLAEKLNSSV YSLPPDPDHF DGYKQQAVVI MDDLCQNPDG
1310 1320 1330 1340 1350
KDVSLFCQMV SSVDFVPPMA ALEEKGILFT SPFVLASTNA GSINAPTVSD
1360 1370 1380 1390 1400
SRALARRFHF DMNIEVISMY SQNGKINMPM SVKTCDEECC PVNFKKCCPL
1410 1420 1430 1440 1450
VCGKAIQFID RRTQVRYSLD MLVTEMFREY NHRHSVGATL EALFQGPPIY
1460 1470 1480 1490 1500
REIKISVAPE TPPPPVIADL LKSVDSEDVR EYCKEKGWLI PEVNSTLQIE
1510 1520 1530 1540 1550
KYVSRAFICL QAITTFVSVA GIIYIIYKLF AGFQGAYTGI PNQKPKVPTL
1560 1570 1580 1590 1600
RQAKVQGPAF EFAVAMMKRN SSTVKTEYGE FTMLGIYDRW AVLPRHAKPG
1610 1620 1630 1640 1650
PTILMNDQEV GVMDAKELVD KDGTNLELTL LKLNRNEKFR DIRGFLAKEE
1660 1670 1680 1690 1700
MEVNEAVLAI NTSKFPNMYI PVGQVTDYGF LNLGGTPTKR MLMYNFPTRA
1710 1720 1730 1740 1750
GQCGGVLMST GKVLGIHVGG NGHQGFSAAL LKHYFNDEQG EIEFIESSKD
1760 1770 1780 1790 1800
AGFPIINTPS KTKLEPSVFH QVFEGVKEPA VLRNGDPRLK ANFEEAIFSK
1810 1820 1830 1840 1850
YIGNVNTHVD EYMLEAVDHY AGQLATLDIS TEPMKLEDAV YGTEGLEALD
1860 1870 1880 1890 1900
LTTSAGYPYV ALGIKKRDIL SKKTRDLTKL KECMDKYGLN LPMITYVKDQ
1910 1920 1930 1940 1950
LRSAEKVAKG KSRLIEASSL NDSVAMRQTF GNLYKTFHLN PGIVTGSAVG
1960 1970 1980 1990 2000
CDPDLFWSKI PVMLNGHLIA FDYSGYDASL SPVWFACLKL LLEKLGYSHK
2010 2020 2030 2040 2050
ETNYIDYLCN SHHLYRDKHY FVRGGMPSGC SGTSIFNSMI NNIIIRTLML
2060 2070 2080 2090 2100
KVYKGIDLDQ FRMIAYGDDV IASYPWPIDA SLLAEAGKDY GLIMTPADKG
2110 2120 2130 2140 2150
ECFNEVTWTN VTFLKRYFRA DEQYPFLVHP VMPMKDIHES IRWTKDPKNT
2160 2170 2180 2190 2200
QDHVRSLCLL AWHNGEHEYE EFIRKIRSVP VGRCLTLPAF STLRRKWLDS

F
Length:2,201
Mass (Da):246,535
Last modified:January 23, 2007 - v4
Checksum:iCCEA86F9E80F385F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00627 Genomic RNA. Translation: BAA00518.1.
PIRiJQ0523. GNNYA9.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00627 Genomic RNA. Translation: BAA00518.1 .
PIRi JQ0523. GNNYA9.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D4M X-ray 2.90 1 569-867 [» ]
2 70-330 [» ]
3 331-568 [» ]
4 2-69 [» ]
3J2J electron microscopy 9.54 A 631-852 [» ]
B 331-568 [» ]
C 79-330 [» ]
ProteinModelPortali P21404.
SMRi P21404. Positions 2-69, 79-852, 868-1017, 1557-2201.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.011.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P21404.

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 nucleotide sequence of coxsackievirus A9; implications for receptor binding and enterovirus classification."
    Chang K.H., Auvinen P., Hyypiae T., Stanway G.
    J. Gen. Virol. 70:3269-3280(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9."
    Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.
    J. Virol. 78:6967-6973(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ITGAV/ITGB6 INTEGRIN.
  3. "The crystal structure of coxsackievirus A9: new insights into the uncoating mechanisms of enteroviruses."
    Hendry E., Hatanaka H., Fry E., Smyth M., Tate J., Stanway G., Santti J., Maaronen M., Hyypia T., Stuart D.
    Structure 7:1527-1538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-870.

Entry informationi

Entry nameiPOLG_CXA9
AccessioniPrimary (citable) accession number: P21404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 145 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