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B2ZUN0

- B2ZUN0_9ENTO

UniProt

B2ZUN0 - B2ZUN0_9ENTO

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Protein
Submitted name:

Polyprotein

Gene
N/A
Organism
Enterovirus A71
Status
Unreviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

NTP + H2O = NDP + phosphate.SAAS annotations
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).SAAS annotations
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.SAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi328 – 3281Potassium 1Imported
Metal bindingi328 – 3281Sodium 1Imported
Metal bindingi328 – 3281Sodium 2Imported
Metal bindingi331 – 3311Potassium 1; via carbonyl oxygenImported
Metal bindingi331 – 3311Sodium 1; via carbonyl oxygenImported
Metal bindingi343 – 3431Potassium 1; via carbonyl oxygenImported
Metal bindingi343 – 3431Sodium 1; via carbonyl oxygenImported
Metal bindingi344 – 3441Sodium 1Imported
Metal bindingi344 – 3441Sodium 2Imported
Metal bindingi345 – 3451Sodium 2; via amide nitrogenImported
Metal bindingi593 – 5931Potassium 2Imported
Binding sitei593 – 5931AMP; via carbonyl oxygenImported
Metal bindingi594 – 5941Potassium 2; via carbonyl oxygenImported
Metal bindingi596 – 5961Potassium 2Imported
Metal bindingi636 – 6361Potassium 2; via carbonyl oxygenImported

GO - Molecular functioni

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

GO - Biological processi

  1. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  2. protein oligomerization Source: UniProtKB-KW
  3. RNA-protein covalent cross-linking Source: InterPro
  4. transcription, DNA-templated Source: InterPro
  5. viral entry into host cell Source: UniProtKB-KW
  6. viral RNA genome replication Source: InterPro
  7. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

HelicaseSAAS annotations, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymeraseSAAS annotations, Thiol proteaseSAAS annotations, Transferase, Viral ion channelSAAS annotations

Keywords - Biological processi

Host-virus interaction, Ion transport, Transport, Viral attachment to host cellSAAS annotations, Viral RNA replicationSAAS annotations, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-bindingImported, Nucleotide-binding, PotassiumImported, RNA-bindingSAAS annotations, SodiumImported

Names & Taxonomyi

Protein namesi
Submitted name:
PolyproteinImported
OrganismiEnterovirus A71Imported
Taxonomic identifieri39054 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus A

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Capsid proteinSAAS annotations, Host cytoplasmSAAS annotations, Host cytoplasmic vesicleSAAS annotations, Host membraneSAAS annotations, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6969VP4 (1A)ImportedPRO_5000373532Add
BLAST
Chaini70 – 323254VP2ImportedPRO_5000373533Add
BLAST
Chaini324 – 565242VP3ImportedPRO_5000373534Add
BLAST
Chaini566 – 862297VP1ImportedPRO_5000373535Add
BLAST
Chaini863 – 10121502AImportedPRO_5000373536Add
BLAST
Chaini1013 – 1111992BImportedPRO_5000373537Add
BLAST
Chaini1112 – 14403292CImportedPRO_5000373538Add
BLAST
Chaini1441 – 1526863AImportedPRO_5000373539Add
BLAST
Chaini1527 – 1548223BImportedPRO_5000373540Add
BLAST
Chaini1549 – 17311833CImportedPRO_5000373541Add
BLAST
Chaini1732 – 21934623DImportedPRO_5000373542Add
BLAST

Keywords - PTMi

PhosphoproteinSAAS annotations

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J22electron microscopy6.30A638-862[»]
B82-318[»]
C324-562[»]
3J23electron microscopy9.20A638-862[»]
B82-318[»]
C324-562[»]
3VBFX-ray2.60A566-862[»]
B79-323[»]
C324-565[»]
D12-69[»]
3VBHX-ray2.30A566-862[»]
B79-323[»]
C324-565[»]
D12-69[»]
3VBOX-ray2.88A566-862[»]
B82-318[»]
C324-562[»]
3VBRX-ray3.80A638-862[»]
B82-318[»]
C324-562[»]
3VBSX-ray3.00A566-862[»]
B79-323[»]
C324-565[»]
D12-69[»]
3VBUX-ray4.00A638-862[»]
B82-318[»]
C324-562[»]
4CDQX-ray2.65A566-862[»]
B70-323[»]
C324-565[»]
D1-69[»]
4CDUX-ray2.80A566-862[»]
B70-323[»]
C324-565[»]
D1-69[»]
4CDWX-ray2.80A566-862[»]
B70-323[»]
C324-565[»]
D1-69[»]
4CDXX-ray2.80A566-862[»]
B70-323[»]
C324-565[»]
D1-69[»]
4CEWX-ray2.75A566-862[»]
B70-323[»]
C324-565[»]
D1-69[»]
4CEYX-ray2.75A566-862[»]
B70-323[»]
C324-565[»]
D1-69[»]
4IKAX-ray2.70D1527-1548[»]

Family & Domainsi

Sequence similaritiesi

Contains RdRp catalytic domain.SAAS annotations
Contains SF3 helicase domain.SAAS annotations
Contains SFhelicase domain.SAAS annotations

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
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.

B2ZUN0-1 [UniParc]FASTAAdd to Basket

« Hide

MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP     50
DKFANPVKDI FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI 100
IVGYGEWPSY CSDSDATAVD KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK 150
FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ CNASKFHQGA LLVAVLPEYV 200
IGTVAGGTGT EDTHPPYKQT QPGADGFELQ HPYVLDAGIP ISQLTVCPHQ 250
WINLRTNNCA TIIVPYINAL PFDSALNHCN FGLLVVPISP LDYDQGATPV 300
IPITITLAPM CSEFAGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN 350
FHPTPCIHIP GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA 400
GKGELCAVFR ADPGRNGPWQ STLLGQLCGY YTQWSGSLEV TFMFTGSFMA 450
TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW DFGLQSSVTL VIPWISNTHY 500
RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL AAAQKNFTMK 550
LCKDASDILQ TGTIQGDRVA DVIESSIGDS VSRALTHALP APTGQNTQVS 600
SHRLDTGKVP ALQAAEIGAS SNASDESMIE TRCVLNSHST AETTLDSFFS 650
RAGLVGEIDL PLKGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF 700
TFVACTPTGE VVPQLLQYMF VPPGAPKPDS RESLAWQTAT NPSVFVKLSD 750
PPAQVSVPFM SPASAYQWFY DGYPTFGEHK QEKDLEYGAC PNNMMGTFSV 800
RTVGTSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA NPNYAGNSIK 850
PTGASRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR 900
DLLVSSTTAQ GCDTIARCDC QTGVYYCNSM RKHYPVSFSK PSLIYVEASE 950
YYPARYQSHL MLAQGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR 1000
DLLWLDEEAM EQGVSDYIKG LGDAFGTGFT DAVSREVEAL KNYLIGSEGA 1050
VEKILKNLIK LISALVIVIR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA 1100
SILGIPIAQK QSASWLKKFN DMANAAKGLE WVSNKISKFI DWLKEKIVPA 1150
AREKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEVMFGN VSYLAHFCRK 1200
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT 1250
GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL 1300
FCQMVSTVDF IPPMASLEEK GVSFTSKFVI ASTNASNIIV PTVSDSDAIR 1350
RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL CSENNTANFK RCSPLVCGKA 1400
IQLRDRKSKV RYSVDTVVSE LIREYSNRSA IGNTIEALFQ GPPKFRPIRI 1450
SLEEKPAPDA ISDLLASVDS EEVRQYCRDQ GWIIPEAPTN VERHLNRAVL 1500
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQVLKKP ALRTATVQGP 1550
SLDFALSLLR RNIRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWIEHK 1600
LVNVLDAVEL VDEQGVNLEL TLITLDTNEK FRDITKFIPE NISTASDATL 1650
VINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT 1700
SVGKVVGIHI GGNGRQGFCA GLKRSYFASE QGEIQWVKPN KETGRLNING 1750
PTRTKLEPSV FHDIFEGNKE PAVLHSKDPR LEVDFEQALF SKYVGNTLHE 1800
PDEYIKEAAL HYANQLKQLE INTSQMSMEE ACYGTENLEA IDLHTSAGYP 1850
YSALGIKKRD ILDPTTRDVS RMKFYMDKYG LDLPYSTYVK DELRSIDKIK 1900
KGKSRLIEAS SLNDSVYLRM AFGHLYEAFH ANPGTITGSA VGCNPDTFWS 1950
KLPILLPGSL FAFDYSGYDA SLSPVWFRAL ELVLREIGYS EEAISLIEGI 2000
NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRAL LIKTFKGIDL 2050
DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAD KSPCFNEVNW 2100
GNATFLKRGF LPDEQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC 2150
LLAWHNGKQE YEKFVSTIRS VPVGRALAIP NYENLRRNWL ELF 2193
Length:2,193
Mass (Da):242,822
Last modified:July 1, 2008 - v1
Checksum:iB676993C284B76B9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU703812 Genomic RNA. Translation: ACD63039.1.
EU703814 Genomic RNA. Translation: ACD63041.1.
JX678875 Genomic RNA. Translation: AGH30716.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU703812 Genomic RNA. Translation: ACD63039.1 .
EU703814 Genomic RNA. Translation: ACD63041.1 .
JX678875 Genomic RNA. Translation: AGH30716.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J22 electron microscopy 6.30 A 638-862 [» ]
B 82-318 [» ]
C 324-562 [» ]
3J23 electron microscopy 9.20 A 638-862 [» ]
B 82-318 [» ]
C 324-562 [» ]
3VBF X-ray 2.60 A 566-862 [» ]
B 79-323 [» ]
C 324-565 [» ]
D 12-69 [» ]
3VBH X-ray 2.30 A 566-862 [» ]
B 79-323 [» ]
C 324-565 [» ]
D 12-69 [» ]
3VBO X-ray 2.88 A 566-862 [» ]
B 82-318 [» ]
C 324-562 [» ]
3VBR X-ray 3.80 A 638-862 [» ]
B 82-318 [» ]
C 324-562 [» ]
3VBS X-ray 3.00 A 566-862 [» ]
B 79-323 [» ]
C 324-565 [» ]
D 12-69 [» ]
3VBU X-ray 4.00 A 638-862 [» ]
B 82-318 [» ]
C 324-562 [» ]
4CDQ X-ray 2.65 A 566-862 [» ]
B 70-323 [» ]
C 324-565 [» ]
D 1-69 [» ]
4CDU X-ray 2.80 A 566-862 [» ]
B 70-323 [» ]
C 324-565 [» ]
D 1-69 [» ]
4CDW X-ray 2.80 A 566-862 [» ]
B 70-323 [» ]
C 324-565 [» ]
D 1-69 [» ]
4CDX X-ray 2.80 A 566-862 [» ]
B 70-323 [» ]
C 324-565 [» ]
D 1-69 [» ]
4CEW X-ray 2.75 A 566-862 [» ]
B 70-323 [» ]
C 324-565 [» ]
D 1-69 [» ]
4CEY X-ray 2.75 A 566-862 [» ]
B 70-323 [» ]
C 324-565 [» ]
D 1-69 [» ]
4IKA X-ray 2.70 D 1527-1548 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
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. "An emerging recombinant human enterovirus 71 responsible for the 2008 outbreak of hand foot and mouth disease in Fuyang city of China."
    Zhang Y., Zhu Z., Yang W., Ren J., Tan X., Wang Y., Mao N., Xu S., Zhu S., Cui A., Zhang Y., Yan D., Li Q., Dong X., Zhang J., Zhao Y., Wan J., Feng Z.
    , Sun J., Wang S., Li D., Xu W.
    Virol. J. 7:94-94(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: EV71/Fuyang.Anhui.P.R.C/17.08/1Imported and EV71/Fuyang.Anhui.P.R.C/17.08/3Imported.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 566-862; 79-323; 324-565 AND 12-69 IN COMPLEX WITH AMP AND POTASSIUM.
  3. "Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: implication for a trans mechanism of VPg uridylylation."
    Chen C., Wang Y., Shan C., Sun Y., Xu P., Zhou H., Yang C., Shi P.Y., Rao Z., Zhang B., Lou Z.
    J. Virol. 87:5755-5768(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1527-1548.
  4. "Complete genome analysis of the c4 subgenotype strains of enterovirus 71: predominant recombination c4 viruses persistently circulating in china for 14 years."
    Zhang Y., Tan X., Cui A., Mao N., Xu S., Zhu Z., Zhou J., Shi J., Zhao Y., Wang X., Huang X., Zhu S., Zhang Y., Tang W., Ling H., Xu W.
    PLoS ONE 8:E56341-E56341(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FY17.08-4/AH/CHN/2008Imported.
  5. "The enterovirus 71 A-particle forms a gateway to allow genome release: a cryoEM study of picornavirus uncoating."
    Shingler K.L., Yoder J.L., Carnegie M.S., Ashley R.E., Makhov A.M., Conway J.F., Hafenstein S.
    PLoS Pathog. 9:e1003240-e1003240(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.30 ANGSTROMS) OF 638-862; 82-318 AND 324-562.
  6. "More-powerful virus inhibitors from structure-based analysis of HEV71 capsid-binding molecules."
    De Colibus L., Wang X., Spyrou J.A., Kelly J., Ren J., Grimes J., Puerstinger G., Stonehouse N., Walter T.S., Hu Z., Wang J., Li X., Peng W., Rowlands D.J., Fry E.E., Rao Z., Stuart D.I.
    Nat. Struct. Mol. Biol. 21:282-288(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 566-862; 70-323; 324-565 AND 1-69 IN COMPLEX WITH SODIUM.

Entry informationi

Entry nameiB2ZUN0_9ENTO
AccessioniPrimary (citable) accession number: B2ZUN0
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: September 3, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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