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B2ZUN0 (B2ZUN0_9ENTO) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
OrganismEnterovirus A71 EMBL ACD63039.1
Taxonomic identifier39054 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus A

Protein attributes

Sequence length2193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

NTP + H2O = NDP + phosphate. SAAS SAAS014759

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). SAAS SAAS014759

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 SAAS014759

Subcellular location

Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity SAAS SAAS014759.

Sequence similarities

Contains RdRp catalytic domain. SAAS SAAS014759

Contains SF3 helicase domain. SAAS SAAS014759

Contains SFhelicase domain. SAAS SAAS014759

Ontologies

Keywords
   Biological processHost-virus interaction
Ion transport
Transport
Viral attachment to host cell SAAS SAAS014759
Viral RNA replication SAAS SAAS014759
Virus entry into host cell
   Cellular componentCapsid protein SAAS SAAS014759
Host cytoplasm SAAS SAAS014759
Host cytoplasmic vesicle SAAS SAAS014759
Host membrane SAAS SAAS014759
Membrane
Virion
   LigandATP-binding
Chloride PDB 3VBF PDB 3VBH PDB 4CDU
Metal-binding PDB 3VBF PDB 3VBH PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX PDB 4CDQ PDB 3VBO
Nucleotide-binding
Potassium PDB 3VBF PDB 3VBH
RNA-binding SAAS SAAS014759
Sodium PDB 3VBF PDB 3VBH PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX PDB 4CDQ PDB 3VBO
   Molecular functionHelicase SAAS SAAS014759
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase SAAS SAAS014759
Thiol protease SAAS SAAS014759
Transferase
Viral ion channel SAAS SAAS014759
   PTMPhosphoprotein SAAS SAAS014759
   Technical term3D-structure PDB 3VBF PDB 3VBH PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX PDB 4CDQ PDB 3VBO PDB 3VBU PDB 3VBS PDB 3VBR PDB 4CEW PDB 3J23 PDB 4IKA PDB 3J22
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: InterPro

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6969VP4 (1A) EMBL ACD63039.1
PRO_5000373532
Chain70 – 323254VP2 EMBL ACD63039.1
PRO_5000373533
Chain324 – 565242VP3 EMBL ACD63039.1
PRO_5000373534
Chain566 – 862297VP1 EMBL ACD63039.1
PRO_5000373535
Chain863 – 10121502A EMBL ACD63039.1
PRO_5000373536
Chain1013 – 1111992B EMBL ACD63039.1
PRO_5000373537
Chain1112 – 14403292C EMBL ACD63039.1
PRO_5000373538
Chain1441 – 1526863A EMBL ACD63039.1
PRO_5000373539
Chain1527 – 1548223B EMBL ACD63039.1
PRO_5000373540
Chain1549 – 17311833C EMBL ACD63039.1
PRO_5000373541
Chain1732 – 21934623D EMBL ACD63039.1
PRO_5000373542

Sites

Metal binding3281Potassium 1 PDB 3VBF PDB 3VBH
Metal binding3281Sodium 1 PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX
Metal binding3281Sodium 2 PDB 4CDX
Metal binding3311Potassium 1; via carbonyl oxygen PDB 3VBF PDB 3VBH
Metal binding3311Sodium 1; via carbonyl oxygen PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX
Metal binding3431Potassium 1; via carbonyl oxygen PDB 3VBF PDB 3VBH
Metal binding3431Sodium 1; via carbonyl oxygen PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX
Metal binding3441Sodium 1 PDB 4CEY PDB 4CDU PDB 4CDW PDB 4CDX
Metal binding3441Sodium 2 PDB 4CDX
Metal binding3451Sodium 2; via amide nitrogen PDB 4CDX
Metal binding5931Potassium 2 PDB 3VBF PDB 3VBH
Metal binding5941Potassium 2; via carbonyl oxygen PDB 3VBF PDB 3VBH
Metal binding5961Potassium 2 PDB 3VBF PDB 3VBH
Metal binding6361Potassium 2; via carbonyl oxygen PDB 3VBF PDB 3VBH
Binding site1591Chloride 1; via amide nitrogen PDB 4CDU
Binding site4141Chloride 2; via amide nitrogen PDB 3VBF PDB 3VBH
Binding site5931AMP; via carbonyl oxygen PDB 3VBF

Sequences

Sequence LengthMass (Da)Tools
B2ZUN0 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: B676993C284B76B9

FASTA2,193242,822
        10         20         30         40         50         60 
MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP DKFANPVKDI 

        70         80         90        100        110        120 
FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI IVGYGEWPSY CSDSDATAVD 

       130        140        150        160        170        180 
KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ 

       190        200        210        220        230        240 
CNASKFHQGA LLVAVLPEYV IGTVAGGTGT EDTHPPYKQT QPGADGFELQ HPYVLDAGIP 

       250        260        270        280        290        300 
ISQLTVCPHQ WINLRTNNCA TIIVPYINAL PFDSALNHCN FGLLVVPISP LDYDQGATPV 

       310        320        330        340        350        360 
IPITITLAPM CSEFAGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN FHPTPCIHIP 

       370        380        390        400        410        420 
GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA GKGELCAVFR ADPGRNGPWQ 

       430        440        450        460        470        480 
STLLGQLCGY YTQWSGSLEV TFMFTGSFMA TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW 

       490        500        510        520        530        540 
DFGLQSSVTL VIPWISNTHY RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL 

       550        560        570        580        590        600 
AAAQKNFTMK LCKDASDILQ TGTIQGDRVA DVIESSIGDS VSRALTHALP APTGQNTQVS 

       610        620        630        640        650        660 
SHRLDTGKVP ALQAAEIGAS SNASDESMIE TRCVLNSHST AETTLDSFFS RAGLVGEIDL 

       670        680        690        700        710        720 
PLKGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF TFVACTPTGE VVPQLLQYMF 

       730        740        750        760        770        780 
VPPGAPKPDS RESLAWQTAT NPSVFVKLSD PPAQVSVPFM SPASAYQWFY DGYPTFGEHK 

       790        800        810        820        830        840 
QEKDLEYGAC PNNMMGTFSV RTVGTSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA 

       850        860        870        880        890        900 
NPNYAGNSIK PTGASRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR 

       910        920        930        940        950        960 
DLLVSSTTAQ GCDTIARCDC QTGVYYCNSM RKHYPVSFSK PSLIYVEASE YYPARYQSHL 

       970        980        990       1000       1010       1020 
MLAQGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR DLLWLDEEAM EQGVSDYIKG 

      1030       1040       1050       1060       1070       1080 
LGDAFGTGFT DAVSREVEAL KNYLIGSEGA VEKILKNLIK LISALVIVIR SDYDMVTLTA 

      1090       1100       1110       1120       1130       1140 
TLALIGCHGS PWAWIKAKTA SILGIPIAQK QSASWLKKFN DMANAAKGLE WVSNKISKFI 

      1150       1160       1170       1180       1190       1200 
DWLKEKIVPA AREKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEVMFGN VSYLAHFCRK 

      1210       1220       1230       1240       1250       1260 
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK 

      1270       1280       1290       1300       1310       1320 
YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL FCQMVSTVDF IPPMASLEEK 

      1330       1340       1350       1360       1370       1380 
GVSFTSKFVI ASTNASNIIV PTVSDSDAIR RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL 

      1390       1400       1410       1420       1430       1440 
CSENNTANFK RCSPLVCGKA IQLRDRKSKV RYSVDTVVSE LIREYSNRSA IGNTIEALFQ 

      1450       1460       1470       1480       1490       1500 
GPPKFRPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCRDQ GWIIPEAPTN VERHLNRAVL 

      1510       1520       1530       1540       1550       1560 
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQVLKKP ALRTATVQGP SLDFALSLLR 

      1570       1580       1590       1600       1610       1620 
RNIRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWIEHK LVNVLDAVEL VDEQGVNLEL 

      1630       1640       1650       1660       1670       1680 
TLITLDTNEK FRDITKFIPE NISTASDATL VINTEHMPSM FVPVGDVVQY GFLNLSGKPT 

      1690       1700       1710       1720       1730       1740 
HRTMMYNFPT KAGQCGGVVT SVGKVVGIHI GGNGRQGFCA GLKRSYFASE QGEIQWVKPN 

      1750       1760       1770       1780       1790       1800 
KETGRLNING PTRTKLEPSV FHDIFEGNKE PAVLHSKDPR LEVDFEQALF SKYVGNTLHE 

      1810       1820       1830       1840       1850       1860 
PDEYIKEAAL HYANQLKQLE INTSQMSMEE ACYGTENLEA IDLHTSAGYP YSALGIKKRD 

      1870       1880       1890       1900       1910       1920 
ILDPTTRDVS RMKFYMDKYG LDLPYSTYVK DELRSIDKIK KGKSRLIEAS SLNDSVYLRM 

      1930       1940       1950       1960       1970       1980 
AFGHLYEAFH ANPGTITGSA VGCNPDTFWS KLPILLPGSL FAFDYSGYDA SLSPVWFRAL 

      1990       2000       2010       2020       2030       2040 
ELVLREIGYS EEAISLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRAL 

      2050       2060       2070       2080       2090       2100 
LIKTFKGIDL DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAD KSPCFNEVNW 

      2110       2120       2130       2140       2150       2160 
GNATFLKRGF LPDEQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKQE 

      2170       2180       2190 
YEKFVSTIRS VPVGRALAIP NYENLRRNWL ELF 

« Hide

References

[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. expand/collapse author list , 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/17.08/1 EMBL ACD63039.1 and EV71/Fuyang.Anhui.P.R.C/17.08/3 EMBL ACD63041.1.
[2]"A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71."
Wang X., Peng W., Ren J., Hu Z., Xu J., Lou Z., Li X., Yin W., Shen X., Porta C., Walter T.S., Evans G., Axford D., Owen R., Rowlands D.J., Wang J., Stuart D.I., Fry E.E., Rao Z.
Nat. Struct. Mol. Biol. 19:424-429(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 566-862; 79-323; 324-565 AND 12-69 IN COMPLEX WITH AMP; CHLORIDE 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/2008 EMBL AGH30716.1.
[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. 0:0-0(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 CHLORIDE AND SODIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU703812 Genomic RNA. Translation: ACD63039.1.
EU703814 Genomic RNA. Translation: ACD63041.1.
JX678875 Genomic RNA. Translation: AGH30716.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProIPR003593. 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.
[Graphical view]
PfamPF08727. 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]
ProDomPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB2ZUN0_9ENTO
AccessionPrimary (citable) accession number: B2ZUN0
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)