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Q9QCE4

- Q9QCE4_9PICO

UniProt

Q9QCE4 - Q9QCE4_9PICO

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Protein
Submitted name: Polyprotein
Gene
N/A
Organism
Foot-and-mouth disease virus - type C
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
Binding sitei2025 – 20251Diphosphate 2Imported
Binding sitei2036 – 20361Diphosphate 1Imported
Metal bindingi2095 – 20951MagnesiumImported
Binding sitei2100 – 21001Diphosphate 2; via amide nitrogenImported
Metal bindingi2196 – 21961MagnesiumImported
Metal bindingi2241 – 22411Magnesium; via carbonyl oxygenImported
Binding sitei2244 – 22441Diphosphate 1Imported

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. metal ion binding Source: UniProtKB-KW
  8. structural molecule activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  2. protein oligomerization Source: UniProtKB-KW
  3. transcription, DNA-templated Source: InterPro
  4. viral RNA genome replication Source: InterPro
  5. viral entry into host cell Source: UniProtKB-KW
  6. viral protein processing 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, MagnesiumImported, Metal-bindingImported, Nucleotide-binding, RNA-bindingSAAS annotations

Protein family/group databases

MEROPSiC03.008.

Names & Taxonomyi

Protein namesi
Submitted name:
PolyproteinImported
OrganismiFoot-and-mouth disease virus - type CImported
Taxonomic identifieri12116 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeAphthovirus

Subcellular locationi

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. icosahedral viral capsid Source: InterPro
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane 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 – 201201leader proteaseImported
PRO_5000064857Add
BLAST
Chaini202 – 28685VP4 proteinImported
PRO_5000064858Add
BLAST
Chaini287 – 504218VP2 proteinImported
PRO_5000064859Add
BLAST
Chaini505 – 723219VP3 proteinImported
PRO_5000064860Add
BLAST
Chaini724 – 932209VP1 proteinImported
PRO_5000064861Add
BLAST
Chaini933 – 948162A proteaseImported
PRO_5000064862Add
BLAST
Chaini949 – 11361882B proteinImported
PRO_5000064863Add
BLAST
Chaini1136 – 14202852C proteinImported
PRO_5000064864Add
BLAST
Chaini1421 – 15731533A proteinImported
PRO_5000064865Add
BLAST
Chaini1574 – 159623VPg1 proteinImported
PRO_5000064866Add
BLAST
Chaini1597 – 162024VPg2 proteinImported
PRO_5000064867Add
BLAST
Chaini1621 – 164424VPg3 proteinImported
PRO_5000064868Add
BLAST
Chaini1645 – 18572133C proteaseImported
PRO_5000064869Add
BLAST
Chaini1858 – 23274703D polymeraseImported
PRO_5000064870Add
BLAST

Keywords - PTMi

PhosphoproteinSAAS annotations

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U09X-ray1.91A1858-2327[»]
1WNEX-ray3.00A1858-2327[»]
2D7SX-ray3.00A1858-2327[»]
B1574-1596[»]
2E9RX-ray2.81X1858-2327[»]
2E9TX-ray2.60A/D1858-2327[»]
2E9ZX-ray3.00A1858-2327[»]
2EC0X-ray2.75A/D1858-2327[»]
3NKYX-ray2.28A1858-2327[»]
3NL0X-ray2.60A1858-2327[»]
3NMAX-ray2.60A1858-2327[»]
4IQXX-ray2.50A1858-2327[»]
ProteinModelPortaliQ9QCE4.
SMRiQ9QCE4. Positions 29-201, 216-930, 1651-1851, 1858-2327.

Miscellaneous databases

EvolutionaryTraceiQ9QCE4.

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.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004080. FMDV_VP1_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR008739. Peptidase_C28.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF05408. Peptidase_C28. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QCE4-1 [UniParc]FASTAAdd to Basket

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MNTTDCFIAV VNAIKEVRAL FLPRTAGKME FTLHDGEKKV FYSRPNNHDN     50
CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLDLREGGPP 100
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGREHAV 150
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNE GWKASVQRKL 200
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM 350
ALFDWVPSQN FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN 400
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG 450
VNRYDQYKQH RPWTLVVMVV APLTTNTVGA QQIKVYANIA PTNVHVAGEL 500
PSKEGIFPVA CSAGYGHLVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD 550
VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 600
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW 650
DTGLNSKFTF SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD 700
ALVVSASAGK DFELRLPVDA RQQTTTTGES ADPVTTTVEN YGGETQVQRR 750
HHTDVAFVLD RFVKVTVSDN QHTLDVMQAH KDNIVGALLR AATYYFSDLE 800
IAVTHTGKLT WVPNGAPVSA LNNTTNPTAY HKGPVTRLAL PYTAPHRVLA 850
TAYTGTTTYT ASARGDLAHL KTTHARHLPT SFNFGAVKAE TITELLVRMK 900
RAELYCPRPI LPIQPTDDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF 950
FFSDVRSNFS KLVETINQMQ EDMSTRHGPD FNRLVSAFEE LASGVKAIRT 1000
GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF 1050
VVKKISDSLS SLFHVPAPAF SFGAPILLAG LVKVASSFFR STPEDLERAE 1100
KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE KYVTMTDLVP 1150
GILEKQRDLN DPSKYKDAKE WLDNTRQVCL KSGNVHIANL CKVVAPAPSK 1200
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF 1250
DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFN 1300
SKVIIATTNL YSGFTPKTMV CPDALNRRFH FDIDVSAKDG YKTNNKLDII 1350
KALEDTHTNP VAMFQYDCAL LNGMAVEMKR LQQDMFKPQP PLQNVYQLVQ 1400
EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV 1450
HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH 1500
KRQKMVDDAV NEYIEKANIT TDDQTLDEAE KNPLETSGAS TVGFRERTLP 1550
GQKARDDVNS EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPRQEGPYA 1600
GPMERQKPLK VKARAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT 1650
DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM 1700
LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDV 1750
ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA 1800
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI 1850
DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD 1900
PRLNEGVVLD EVIFSKHKGD TKMSAEDKAL FRRCAADYAS RLHSVLGTAN 1950
APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV 2000
EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR 2050
MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA 2100
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE 2150
GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA 2200
SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD 2250
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF 2300
EPFQGLFEIP SYRSLYLRWV NAVCGDA 2327
Length:2,327
Mass (Da):258,245
Last modified:May 1, 2000 - v1
Checksum:i8AE69D7939F08BB1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ133358 Genomic RNA. Translation: CAB60265.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ133358 Genomic RNA. Translation: CAB60265.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U09 X-ray 1.91 A 1858-2327 [» ]
1WNE X-ray 3.00 A 1858-2327 [» ]
2D7S X-ray 3.00 A 1858-2327 [» ]
B 1574-1596 [» ]
2E9R X-ray 2.81 X 1858-2327 [» ]
2E9T X-ray 2.60 A/D 1858-2327 [» ]
2E9Z X-ray 3.00 A 1858-2327 [» ]
2EC0 X-ray 2.75 A/D 1858-2327 [» ]
3NKY X-ray 2.28 A 1858-2327 [» ]
3NL0 X-ray 2.60 A 1858-2327 [» ]
3NMA X-ray 2.60 A 1858-2327 [» ]
4IQX X-ray 2.50 A 1858-2327 [» ]
ProteinModelPortali Q9QCE4.
SMRi Q9QCE4. Positions 29-201, 216-930, 1651-1851, 1858-2327.
ModBasei Search...

Protein family/group databases

MEROPSi C03.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9QCE4.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProi IPR015031. Capsid_VP4_Picornavir.
IPR004080. FMDV_VP1_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR008739. Peptidase_C28.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF05408. Peptidase_C28. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
[Graphical view ]
PRINTSi PR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genomic nucleotide sequence of a foot-and-mouth disease virus clone and its persistent derivatives. Implications for the evolution of viral quasispecies during a persistent infection."
    Toja M., Escarmis C., Domingo E.
    Virus Res. 64:161-171(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CImported.
  2. "Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA."
    Ferrer-Orta C., Arias A., Perez-Luque R., Escarmis C., Domingo E., Verdaguer N.
    J. Biol. Chem. 279:47212-47221(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1858-2327.
  3. "The structure of a protein primer-polymerase complex in the initiation of genome replication."
    Ferrer-Orta C., Arias A., Agudo R., Perez-Luque R., Escarmis C., Domingo E., Verdaguer N.
    EMBO J. 25:880-888(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1858-2327 AND 1574-1596.
  4. "Sequential structures provide insights into the fidelity of RNA replication."
    Ferrer-Orta C., Arias A., Perez-Luque R., Escarmis C., Domingo E., Verdaguer N.
    Proc. Natl. Acad. Sci. U.S.A. 104:9463-9468(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1858-2327 IN COMPLEX WITH DIPHOSPHATE AND MAGNESIUM.
  5. "A multi-step process of viral adaptation to a mutagenic nucleoside analogue by modulation of transition types leads to extinction-escape."
    Agudo R., Ferrer-Orta C., Arias A., de la Higuera I., Perales C., Perez-Luque R., Verdaguer N., Domingo E.
    PLoS Pathog. 6:e1001072-e1001072(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 1858-2327.

Entry informationi

Entry nameiQ9QCE4_9PICO
AccessioniPrimary (citable) accession number: Q9QCE4
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 96 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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