Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5UEA2

- Q5UEA2_9ENTO

UniProt

Q5UEA2 - Q5UEA2_9ENTO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus B3
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 sitei1768 – 17681Sulfate 2
Binding sitei1820 – 18201Acetate; via amide nitrogenImported
Binding sitei1897 – 18971Sulfate 1
Binding sitei1897 – 18971Sulfate 4
Binding sitei1911 – 19111Sulfate 3
Binding sitei1959 – 19591Sulfate 4; via amide nitrogen
Binding sitei1990 – 19901Sulfate 6
Binding sitei2000 – 20001Sulfate 2
Binding sitei2099 – 20991Sulfate 1

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

Protein family/group databases

MEROPSiN08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyproteinSAAS annotation
OrganismiCoxsackievirus B3Imported
Taxonomic identifieri12072 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B

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

Keywords - PTMi

PhosphoproteinSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DDKX-ray2.25A1724-2185[»]
3ZYDX-ray1.70A1541-1723[»]
3ZYEX-ray1.85A1541-1723[»]
3ZZ3X-ray1.89A/B1541-1723[»]
3ZZ4X-ray2.10A/B1541-1723[»]
3ZZ5X-ray2.20A1541-1723[»]
3ZZ6X-ray2.05A1541-1723[»]
3ZZ7X-ray1.80A1541-1723[»]
3ZZ8X-ray1.85A1541-1723[»]
3ZZ9X-ray1.90A1541-1723[»]
3ZZAX-ray1.80A1541-1723[»]
3ZZBX-ray2.10A1541-1723[»]
3ZZCX-ray2.10A1541-1723[»]
3ZZDX-ray2.10A1541-1723[»]
4K4XX-ray2.37A/E/I/M1724-2185[»]
4K4YX-ray2.72A/E/I/M1724-2185[»]
4K4ZX-ray2.17A/E/I/M1724-2185[»]
ProteinModelPortaliQ5UEA2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5UEA2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1950 – 19523Sulfate 5 binding

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.
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.

Q5UEA2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAQVSTQKT GAHETGLNAS GNSIIHYTNV NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
GKFTEPVKDI MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV
110 120 130 140 150
VVGYGVWPDY LKDSEATAED QPTQPDVATC RFYTLDSVQW QKTSPGWWWK
160 170 180 190 200
LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGCATLDNTP SSAELLGGDS AKEFADKPVA SGSNKLVQRV VYNAGMGVGV
260 270 280 290 300
GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
310 320 330 340 350
DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD
360 370 380 390 400
FQSPSAMPQY DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY
410 420 430 440 450
QIPVRSNEGS GTQVFGFPLQ PGYSSVFSRT LLGEILNYYT HWSGSIKLTF
460 470 480 490 500
MFCGSAMATG KFLLAYSPPG AGAPTKRVDA MLGTHVVWDV GLQSSCVLCI
510 520 530 540 550
PWISQTHYRY VASDEYTAGG FITCWYQTNI VVPADAQSSC YIMCFVSACN
560 570 580 590 600
DFSVRLLKDT PFISQENFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
610 620 630 640 650
LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYE
660 670 680 690 700
NSGAKRYAEW VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ
710 720 730 740 750
NQDAQILTHQ IMYVPPGGPV PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI
760 770 780 790 800
PFLSIGNAYS NFYDGWSEFS RNGVYGINTL NNMGTLYARH VNAGSTGPIK
810 820 830 840 850
STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFRPSGVTT TRQSITTMTN
860 870 880 890 900
TGAFGQQSGA AYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG
910 920 930 940 950
CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL
960 970 980 990 1000
LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME
1010 1020 1030 1040 1050
QGVKDYVEQL GNAFGSGFTN RICEQVNLLK ESLVGQDSIL EKSLKALVKI
1060 1070 1080 1090 1100
ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPLAERQ
1110 1120 1130 1140 1150
NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV REKHEFLNRL
1160 1170 1180 1190 1200
KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR
1210 1220 1230 1240 1250
VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL
1260 1270 1280 1290 1300
NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV
1310 1320 1330 1340 1350
PPMAALEEKG ILFTSPFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV
1360 1370 1380 1390 1400
ISMYSQNGKI NMPMSVKTCD DECCPVNFKK CCPLVCGKAI QFIDRRTQVR
1410 1420 1430 1440 1450
YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS VAPETPPPPA
1460 1470 1480 1490 1500
IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF
1510 1520 1530 1540 1550
VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM
1560 1570 1580 1590 1600
MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK
1610 1620 1630 1640 1650
ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP
1660 1670 1680 1690 1700
NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI
1710 1720 1730 1740 1750
HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI NTPSKTKLEP
1760 1770 1780 1790 1800
SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA
1810 1820 1830 1840 1850
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK
1860 1870 1880 1890 1900
RDILSKKTKD LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE
1910 1920 1930 1940 1950
ASSLNDSVAM RQTFGNLYKT FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG
1960 1970 1980 1990 2000
HLIAFDYSGY DASLSPVWFA CLKMLLEKLG YTHKETNYID YLCNSHHLYR
2010 2020 2030 2040 2050
DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY
2060 2070 2080 2090 2100
GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNVTFLKR
2110 2120 2130 2140 2150
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE
2160 2170 2180
HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF
Length:2,185
Mass (Da):243,368
Last modified:December 7, 2004 - v1
Checksum:i86068AAD2A4DF167
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY752945 Genomic RNA. Translation: AAV34212.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY752945 Genomic RNA. Translation: AAV34212.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DDK X-ray 2.25 A 1724-2185 [» ]
3ZYD X-ray 1.70 A 1541-1723 [» ]
3ZYE X-ray 1.85 A 1541-1723 [» ]
3ZZ3 X-ray 1.89 A/B 1541-1723 [» ]
3ZZ4 X-ray 2.10 A/B 1541-1723 [» ]
3ZZ5 X-ray 2.20 A 1541-1723 [» ]
3ZZ6 X-ray 2.05 A 1541-1723 [» ]
3ZZ7 X-ray 1.80 A 1541-1723 [» ]
3ZZ8 X-ray 1.85 A 1541-1723 [» ]
3ZZ9 X-ray 1.90 A 1541-1723 [» ]
3ZZA X-ray 1.80 A 1541-1723 [» ]
3ZZB X-ray 2.10 A 1541-1723 [» ]
3ZZC X-ray 2.10 A 1541-1723 [» ]
3ZZD X-ray 2.10 A 1541-1723 [» ]
4K4X X-ray 2.37 A/E/I/M 1724-2185 [» ]
4K4Y X-ray 2.72 A/E/I/M 1724-2185 [» ]
4K4Z X-ray 2.17 A/E/I/M 1724-2185 [» ]
ProteinModelPortali Q5UEA2.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi N08.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q5UEA2.

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. "An infectious cDNA copy of the genome of a non-cardiovirulent coxsackievirus B3 strain: its complete sequence analysis and comparison to the genomes of cardiovirulent coxsackieviruses."
    Chapman N.M., Tu Z., Tracy S., Gauntt C.J.
    Arch. Virol. 135:115-130(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 0Imported.
  2. Chapman N.M., Tu Z., Tracy S., Gauntt C.J.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 0Imported.
  3. "Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases."
    Campagnola G., Weygandt M., Scoggin K., Peersen O.
    J. Virol. 82:9458-9464(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1724-2185.
  4. "Peptidic Ab-Nonsaturated Ethyl Esters as Inhibitors of the 3C Protease of Coxsackie Virus B3: Crystal Structures, Antiviral Activities, and Resistance Mutations."
    Tan J., Anand K., Mesters J.R., Hilgenfeld R.
    Submitted (AUG-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1541-1723.
  5. "Peptidic Alpha, Beta-Unsaturated Ethyl Esters as Inhibitors of the 3C Protease of Coxsackie Virus B3: Crystal Structures, Antiviral Activities, and Resistance Mutations."
    Tan J., Anand K., Mesters J.R., Hilgenfeld R.
    Submitted (AUG-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1541-1723.
  6. "Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts."
    Gong P., Kortus M.G., Nix J.C., Davis R.E., Peersen O.B.
    PLoS ONE 8:e60272-e60272(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1724-2185.

Entry informationi

Entry nameiQ5UEA2_9ENTO
AccessioniPrimary (citable) accession number: Q5UEA2
Entry historyi
Integrated into UniProtKB/TrEMBL: December 7, 2004
Last sequence update: December 7, 2004
Last modified: October 29, 2014
This is version 87 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