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Q9QL88

- POLG_CXB6S

UniProt

Q9QL88 - POLG_CXB6S

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Protein
Genome polyprotein
Gene
N/A
Organism
Coxsackievirus B6 (strain Schmitt)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei69 – 702Cleavage; by autolysis Reviewed prediction
Sitei330 – 3312Cleavage; by Protease 3C Reviewed prediction
Active sitei871 – 8711For Protease 2A activity By similarity
Active sitei889 – 8891For Protease 2A activity By similarity
Active sitei960 – 9601For Protease 2A activity By similarity
Sitei1000 – 10012Cleavage; by Protease 3C Reviewed prediction
Sitei1428 – 14292Cleavage; by Protease 3C Reviewed prediction
Sitei1517 – 15182Cleavage; by Protease 3C Reviewed prediction
Sitei1539 – 15402Cleavage; by Protease 3C Reviewed prediction
Active sitei1579 – 15791For Protease 3C activity Reviewed prediction
Active sitei1610 – 16101For Protease 3C activity Reviewed prediction
Active sitei1686 – 16861For Protease 3C activity By similarity
Sitei1722 – 17232Cleavage; by Protease 3C Reviewed prediction
Active sitei2051 – 20511For RdRp activity By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. RNA-protein covalent cross-linking Source: UniProtKB-KW
  3. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  4. induction by virus of host autophagy Source: UniProtKB
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  7. protein oligomerization Source: UniProtKB-KW
  8. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  10. suppression by virus of host translation Source: UniProtKB-KW
  11. suppression by virus of host translation initiation factor activity Source: UniProtKB
  12. transcription, DNA-templated Source: InterPro
  13. viral RNA genome replication Source: InterPro
  14. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.011.

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 B6 (strain Schmitt)
Taxonomic identifieri231474 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007762: 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 – 14941493Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1495 – 151016 Reviewed prediction
Add
BLAST
Topological domaini1511 – 2184674Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 21842183Genome polyprotein By similarity
PRO_0000426341Add
BLAST
Chaini2 – 847846P1 By similarity
PRO_0000426342Add
BLAST
Chaini2 – 330329Capsid protein VP0 Reviewed prediction
PRO_0000426343Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed prediction
PRO_0000426344Add
BLAST
Chaini70 – 330261Capsid protein VP2 Reviewed prediction
PRO_0000426345Add
BLAST
Chaini331 – 566236Capsid protein VP3 Reviewed prediction
PRO_0000426346Add
BLAST
Chaini566 – 847282Capsid protein VP1 Reviewed prediction
PRO_0000426347Add
BLAST
Chaini848 – 1428581P2 By similarity
PRO_0000426348Add
BLAST
Chaini848 – 1000153Protease 2A Reviewed prediction
PRO_0000426349Add
BLAST
Chaini1001 – 109999Protein 2B Reviewed prediction
PRO_0000039642Add
BLAST
Chaini1100 – 1428329Protein 2C Reviewed prediction
PRO_0000039643Add
BLAST
Chaini1429 – 2184756P3 By similarity
PRO_0000426350Add
BLAST
Chaini1429 – 1539111Protein 3AB Reviewed prediction
PRO_0000426351Add
BLAST
Chaini1429 – 151789Protein 3A Reviewed prediction
PRO_0000039644Add
BLAST
Chaini1518 – 153922Viral protein genome-linked Reviewed prediction
PRO_0000426352Add
BLAST
Chaini1540 – 2184645Protein 3CD Reviewed prediction
PRO_0000426353Add
BLAST
Chaini1540 – 1721182Protease 3C Reviewed prediction
PRO_0000426354Add
BLAST
Chaini1722 – 2184463RNA-directed RNA polymerase By similarity
PRO_0000426355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1520 – 15201O-(5'-phospho-RNA)-tyrosine By similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion By similarity.
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins By similarity.
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion By similarity.
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication By similarity.

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Interact with host CXADR. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid By similarity. Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid By similarity. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 By similarity. Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis By similarity. Protein 3AB: interacts with protein 3CD By similarity. Viral protein genome-linked: interacts with RNA-directed RNA polymerase By similarity. Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD By similarity.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9QL88.
SMRiQ9QL88. Positions 2-69, 77-568, 581-1000, 1540-2184.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1204 – 1360157SF3 helicase
Add
BLAST
Domaini1540 – 1705166Peptidase C3
Add
BLAST
Domaini1949 – 2065117RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni566 – 58217Amphipatic alpha-helix Reviewed prediction
Add
BLAST
Regioni1429 – 145224Disordered By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QL88-1 [UniParc]FASTAAdd to Basket

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MGAQVSTQKT GAHETALNAQ GNSVIHYTNI NYYKDAASNS ANRQDFTQDP     50
SKFTEPVKDV MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV 100
VVAYGVWPDY LHDDEATAED QPTQPDVATC RFYTLDSVSW QSSSAGWWWK 150
FPDALSNMGL FGQNMQYHYL GRSGYTIHVQ CNASKFHQGC LLVVCVPEAE 200
MGCSNLNNAP LAADLSAGEV ARQFTVEPAN GQNQVQTAVH NAAMGVAVGN 250
LTIFPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MIIPFAKLAY 300
SDGASTFVPI TVTIAPMNAE YNGLRLAGHQ GLPVMTTPGS TQFLTSDDFQ 350
SPCAMPQFDV TPEMNIPGQV NNLMEIAEVD SVVPVNNTET NVNGMDAYRI 400
PVQSNMDTGG QVFGFPLQPG ASSVFQRTLL GEILNYYTHW SGSIKLTFMF 450
CGSAMATGKF LLAYSPPGAG APKSRKDAML GTHVIWDVGL QSSCVLCIPW 500
ISQTHYRFVV ADEYTAGGFI TCWYQTNVIV PLGAQSNCSI LCFVSACNDF 550
SVRMLRDTKF ISQTAFYQSP VEGAIERAIA RVADTMPSGP TNSEAVPALT 600
AVETGHTSQV VPSDNMQTRH VKNYHSRSET SVENFLCRSA CVYFTTYKNQ 650
TGATNRFASW VITTRQVAQL RRKLEMFTYL RFDIELTFVI TSAQDQSTIS 700
QDAPVQTHQI MYVPPGGPVP TKVDDYAWQT STNPSVFWTE GNAPPRMSVP 750
FMSIGNAYST FYDGWSDFSN KGIYGLNTLN NMGTLYIRHV NGPNPVPITS 800
TVRIYFKPKH VKAWVPRPPR LCQYKTSRQV NFTVTGVTES RANITTMNTT 850
GAFGQQSGAA YVGNYRVVNR HLATHADWQN CVWEDYNRDL LVSTTTAHGC 900
DVIARCQCNT GVYFCASRNK HYPVTFEGPG LVEVQESEYY PKRYQSHVLL 950
AAGFSEPGDC GGILRCEHGV IGLVTMGGEG VVGFADVRDL LWLEDDAMEQ 1000
GVRDYVEQLG NAFGSGFTNQ ICEQVNLLKE SLVGQDSILE KSLKALVKII 1050
SALVIVVRNH DDLITVTATL ALIGCTTSPW RWLKQKVSQY YGIPMAERQS 1100
NGWLKKFTEM TNACKGMEWI AIKIQKFIEW LKARILPEVK EKHEFLNRLK 1150
QLPLLESQIA TIEQSAPSQS DQEQLFSNVQ YFAHYCRKYA PLYAAEAKRV 1200
FSLEKKMSNY IQFKSKCRIE PVCLLLHGSP GAGKSVATSL IGRSLAEKLN 1250
SSVYSLPPDP DHFDGYKQQA VVIMDDLCQN PDGKDVSLFC QMVSSVDFVP 1300
PMAALEEKGI LFTSPFVLAS TNAGSINAPT VSDSRALARR FHFDMNIEVI 1350
SMYSQNGKIN MPMSVKTCDE ECCPVNFKKC CPLVCGKAIQ FIDRRTQVRY 1400
SLDMLVTEMF REYNHRHSVG ATLEALFQGP PVYREIKISV APETPPPPAI 1450
ADLLKSVDSE AVREYCKEKG WLVPEINSTL QIEKHVSRAF ICLQALTTFV 1500
SVAGIIYIIY KLFAGFQGAY TGMPNQKPKV PTLRQAKVQG PAFEFAVAMM 1550
KRNSSTVKTE YGEFTMLGVY DRWAVLPRHA KPGPTILMND QEVGVLDAKE 1600
LVDKDGTNLE LTLLKLNRNE KFRDIRGFLA KEEVEVNEAV LAINTSKFPN 1650
MYIPVGQVTD YGFLNLGGTP TKRMLMYNFP TRAGQCGGVL MSTGKVLGIH 1700
VGGNGHQGFS AALLKHYFND EQGEIEFIES SKDAGFPIIN TPSKTKLEPS 1750
VFHQVFEGNK EPAVLRNGDP RLKANFEEAI FSKYIGNVNT HVDEYMLEAV 1800
DHYAGQLATL DINTEPMKLE DAVYGTEGLE ALDLTTSAGY PYVALGIKKR 1850
DILSKKSKDL TKLKECMDKY GLNLPMVTYV KDELRSAEKV AKGKSRLIEA 1900
SSLNDSVAMR QTFGNLYKTF HLNPGIVTGS AVGCDPDLFW SKIPVMLDGH 1950
LIAFDYSGYD ASLSPVWFAC LKLLLEKLGY THKETNYIDY LCNSHHLYRD 2000
KHYFVRGGMP SGCSGTSIFN SMINNIIIRT LMLKVYKGID LDQFRMIAYG 2050
DDVIASYPWP IDASLLAEAG KGYGLIMTPA DKGECFNEVT WTNVTFLKRY 2100
FRADEQYPFL VHPVMPMKDI HESIRWTKDP KNTQDHVRSL CLLAWHNGEH 2150
EYEEFIRKVR SVPVGRCLTL PAFSTLRRKW LDSF 2184
Length:2,184
Mass (Da):243,256
Last modified:January 23, 2007 - v4
Checksum:iD739B8F9E9B033C8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251I → L in AAD02132. 1 Publication
Sequence conflicti447 – 4471T → P in AAD02132. 1 Publication
Sequence conflicti562 – 5621S → R in AAF21972. 1 Publication
Sequence conflicti654 – 6541T → K in AAD02132. 1 Publication
Sequence conflicti986 – 9861D → N in AAF12719. 1 Publication
Sequence conflicti1110 – 11101M → V in AAD02132. 1 Publication
Sequence conflicti2126 – 21261W → R in AAD02132. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF105342 Genomic RNA. Translation: AAF12719.1.
AF039205 Genomic RNA. Translation: AAD02132.1.
AF114384 Genomic RNA. Translation: AAF21972.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF105342 Genomic RNA. Translation: AAF12719.1 .
AF039205 Genomic RNA. Translation: AAD02132.1 .
AF114384 Genomic RNA. Translation: AAF21972.1 .

3D structure databases

ProteinModelPortali Q9QL88.
SMRi Q9QL88. Positions 2-69, 77-568, 581-1000, 1540-2184.
ModBasei Search...

Protein family/group databases

MEROPSi C03.011.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 ]
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Publicationsi

  1. "The complete consensus sequence of coxsackievirus B6 and generation of infectious clones by long RT-PCR."
    Martino T.A., Tellier R., Petric M., Irwin D.M., Afshar A., Liu P.P.
    Virus Res. 64:77-86(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Cloning and sequencing of an infectious cDNA of Coxsackievirus B6 (CVB6)."
    Zell R.H.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Strategy for sequence analysis of complete enterovirus genomes. The prototype strain of coxsackievirus B6."
    Lindberg A.M., Polacek C., Johansson S., Lundgren A., Andersson A., Van Ranst M.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  4. "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.

Entry informationi

Entry nameiPOLG_CXB6S
AccessioniPrimary (citable) accession number: Q9QL88
Secondary accession number(s): Q9QAH1, Q9YXE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 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

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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