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B2ZUN0

- B2ZUN0_9ENTO

UniProt

B2ZUN0 - B2ZUN0_9ENTO

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Protein

Genome polyprotein

Gene
N/A
Organism
Enterovirus A71
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei593 – 5931AMP; 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. 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. 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 annotation, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymeraseSAAS annotation, Thiol proteaseSAAS annotation, Transferase, Viral ion channelSAAS annotation

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-bindingSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyproteinSAAS annotation
OrganismiEnterovirus A71Imported
Taxonomic identifieri39054 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus A

Subcellular locationi

Host cytoplasm SAAS annotation
Host cytoplasmic vesicle membrane SAAS annotation; Peripheral membrane protein SAAS annotation; Cytoplasmic side SAAS annotation

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 annotation, Host cytoplasmSAAS annotation, Host cytoplasmic vesicleSAAS annotation, Host membraneSAAS annotation, 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 annotation

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[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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

        10         20         30         40         50
MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP
60 70 80 90 100
DKFANPVKDI FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI
110 120 130 140 150
IVGYGEWPSY CSDSDATAVD KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK
160 170 180 190 200
FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ CNASKFHQGA LLVAVLPEYV
210 220 230 240 250
IGTVAGGTGT EDTHPPYKQT QPGADGFELQ HPYVLDAGIP ISQLTVCPHQ
260 270 280 290 300
WINLRTNNCA TIIVPYINAL PFDSALNHCN FGLLVVPISP LDYDQGATPV
310 320 330 340 350
IPITITLAPM CSEFAGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN
360 370 380 390 400
FHPTPCIHIP GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA
410 420 430 440 450
GKGELCAVFR ADPGRNGPWQ STLLGQLCGY YTQWSGSLEV TFMFTGSFMA
460 470 480 490 500
TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW DFGLQSSVTL VIPWISNTHY
510 520 530 540 550
RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL AAAQKNFTMK
560 570 580 590 600
LCKDASDILQ TGTIQGDRVA DVIESSIGDS VSRALTHALP APTGQNTQVS
610 620 630 640 650
SHRLDTGKVP ALQAAEIGAS SNASDESMIE TRCVLNSHST AETTLDSFFS
660 670 680 690 700
RAGLVGEIDL PLKGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF
710 720 730 740 750
TFVACTPTGE VVPQLLQYMF VPPGAPKPDS RESLAWQTAT NPSVFVKLSD
760 770 780 790 800
PPAQVSVPFM SPASAYQWFY DGYPTFGEHK QEKDLEYGAC PNNMMGTFSV
810 820 830 840 850
RTVGTSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA NPNYAGNSIK
860 870 880 890 900
PTGASRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR
910 920 930 940 950
DLLVSSTTAQ GCDTIARCDC QTGVYYCNSM RKHYPVSFSK PSLIYVEASE
960 970 980 990 1000
YYPARYQSHL MLAQGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR
1010 1020 1030 1040 1050
DLLWLDEEAM EQGVSDYIKG LGDAFGTGFT DAVSREVEAL KNYLIGSEGA
1060 1070 1080 1090 1100
VEKILKNLIK LISALVIVIR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA
1110 1120 1130 1140 1150
SILGIPIAQK QSASWLKKFN DMANAAKGLE WVSNKISKFI DWLKEKIVPA
1160 1170 1180 1190 1200
AREKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEVMFGN VSYLAHFCRK
1210 1220 1230 1240 1250
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT
1260 1270 1280 1290 1300
GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL
1310 1320 1330 1340 1350
FCQMVSTVDF IPPMASLEEK GVSFTSKFVI ASTNASNIIV PTVSDSDAIR
1360 1370 1380 1390 1400
RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL CSENNTANFK RCSPLVCGKA
1410 1420 1430 1440 1450
IQLRDRKSKV RYSVDTVVSE LIREYSNRSA IGNTIEALFQ GPPKFRPIRI
1460 1470 1480 1490 1500
SLEEKPAPDA ISDLLASVDS EEVRQYCRDQ GWIIPEAPTN VERHLNRAVL
1510 1520 1530 1540 1550
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQVLKKP ALRTATVQGP
1560 1570 1580 1590 1600
SLDFALSLLR RNIRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWIEHK
1610 1620 1630 1640 1650
LVNVLDAVEL VDEQGVNLEL TLITLDTNEK FRDITKFIPE NISTASDATL
1660 1670 1680 1690 1700
VINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT
1710 1720 1730 1740 1750
SVGKVVGIHI GGNGRQGFCA GLKRSYFASE QGEIQWVKPN KETGRLNING
1760 1770 1780 1790 1800
PTRTKLEPSV FHDIFEGNKE PAVLHSKDPR LEVDFEQALF SKYVGNTLHE
1810 1820 1830 1840 1850
PDEYIKEAAL HYANQLKQLE INTSQMSMEE ACYGTENLEA IDLHTSAGYP
1860 1870 1880 1890 1900
YSALGIKKRD ILDPTTRDVS RMKFYMDKYG LDLPYSTYVK DELRSIDKIK
1910 1920 1930 1940 1950
KGKSRLIEAS SLNDSVYLRM AFGHLYEAFH ANPGTITGSA VGCNPDTFWS
1960 1970 1980 1990 2000
KLPILLPGSL FAFDYSGYDA SLSPVWFRAL ELVLREIGYS EEAISLIEGI
2010 2020 2030 2040 2050
NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRAL LIKTFKGIDL
2060 2070 2080 2090 2100
DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAD KSPCFNEVNW
2110 2120 2130 2140 2150
GNATFLKRGF LPDEQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC
2160 2170 2180 2190
LLAWHNGKQE YEKFVSTIRS VPVGRALAIP NYENLRRNWL ELF
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.
  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.

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: October 29, 2014
This is version 53 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