Polyprotein - Foot-and-mouth disease virus

Sequence or UniProt identifier

>tr|Q9QCE4|Q9QCE4_9PICO Polyprotein OS=Foot-and-mouth disease virus - type C PE=1 SV=1 MNTTDCFIAVVNAIKEVRALFLPRTAGKMEFTLHDGEKKVFYSRPNNHDNCWLNTILQLF RYVDEPFFDWVYNSPENLTLEAIKQLEELTGLDLREGGPPALVIWNIKHLLHTGIGTASR PSEVCMVDGTDMCLADFHAGIFMKGREHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVF VPYDQEPLNEGWKASVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLG DNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRI LTTRNGHTTSTTQSSVGVTFGYATAEDSTSGPNTSGLETRVHQAERFFKMALFDWVPSQN FGHMHKVVLPHEPKGVYGGLVKSYAYMRNGWDVEVTAVGNQFNGGCLLVALVPEMGDISD REKYQLTLYPHQFINPRTNMTAHITVPYVGVNRYDQYKQHRPWTLVVMVVAPLTTNTVGA QQIKVYANIAPTNVHVAGELPSKEGIFPVACSAGYGHLVTTDPKTADPAYGKVYNPPRTA LPGRFTNYLDVAEACPTFLMFENVPYVSTRTDGQRLLAKFDVSLAAKHMSNTYLAGLAQY YTQYTGTINLHFMFTGPTDAKARYMVAYVPPGMDAPDNPEEAAHCIHAEWDTGLNSKFTF SIPYISAADYAYTASHEAETTCVQGWVCVYQITHGKADADALVVSASAGKDFELRLPVDA RQQTTTTGESADPVTTTVENYGGETQVQRRHHTDVAFVLDRFVKVTVSDNQHTLDVMQAH KDNIVGALLRAATYYFSDLEIAVTHTGKLTWVPNGAPVSALNNTTNPTAYHKGPVTRLAL PYTAPHRVLATAYTGTTTYTASARGDLAHLKTTHARHLPTSFNFGAVKAETITELLVRMK RAELYCPRPILPIQPTDDRHKQPLVAPAKQLLNFDLLKLAGDVESNPGPFFFSDVRSNFS KLVETINQMQEDMSTRHGPDFNRLVSAFEELASGVKAIRTGLDEAKPWYKLIKLLSRLSC MAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKISDSLSSLFHVPAPAFSFGAPILLAG LVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAWIASEE KYVTMTDLVPGILEKQRDLNDPSKYKDAKEWLDNTRQVCLKSGNVHIANLCKVVAPAPSK SRPEPVVVCLRGKSGQGKSFLANVLAQAISTHLTGRTDSVWYCPPDPDHFDGYNQQTVVV MDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFTPKTMV CPDALNRRFHFDIDVSAKDGYKTNNKLDIIKALEDTHTNPVAMFQYDCALLNGMAVEMKR LQQDMFKPQPPLQNVYQLVQEVIERVELHEKVSSHPIFKQISIPSQKSVLYFLIEKGQHE AAIEFFEGMVHDSIKEELRPLIQQTSFVKRAFKRLKENFEIVALCLTLLANIVIMIRETH KRQKMVDDAVNEYIEKANITTDDQTLDEAEKNPLETSGASTVGFRERTLPGQKARDDVNS EPAQPTEEQPQAEGPYAGPLERQRPLKVRAKLPRQEGPYAGPMERQKPLKVKARAPVVKE GPYEGPVKKPVALKVKAKNLIVTESGAPPTDLQKMVMGNTKPVELILDGKTVAICCATGV FGTAYLVPRHLFAEKYDKIMLDGRALTDSDYRVFEFEIKVKGQDMLSDAALMVLHRGNRV RDITKHFRDVARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGLFAYKA ATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLLKMKAHIDPEPHHEGLI VDTRDVEERVHVMRKTKLAPTVAHGVFNPEFGPAALSNKDPRLNEGVVLDEVIFSKHKGD TKMSAEDKALFRRCAADYASRLHSVLGTANAPLSIYEAIKGVDGLDAMEPDTAPGLPWAL QGKRRGALIDFENGTVGPEVEAALKLMEKREYKFACQTFLKDEIRPMEKVRAGKTRIVDV LPVEHILYTRMMIGRFCAQMHSNNGPQIGSAVGCNPDVDWQRFGTHFAQYRNVWDVDYSA FDANHCSDAMNIMFEEVFRTEFGFHPNAEWILKTLVNTEHAYENKRITVEGGMPSGCSAT SIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFKSLGQT ITPADKSDKGFVLGHSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRGTIQEK LISVAGLAVHSGPDEYRRLFEPFQGLFEIPSYRSLYLRWVNAVCGDA

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Protein names	Submitted name: Polyprotein EMBL CAB60265.1
Organism	Foot-and-mouth disease virus - type C EMBL CAB60265.1
Taxonomic identifier	12116 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Aphthovirus › Foot-and-mouth disease virus

Sequence length	2327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Function	Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease By similarity. SAAS SAAS000199 RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. SAAS SAAS001676
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). SAAS SAAS001205 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 SAAS001676
Subcellular location	Host cytoplasm By similarity SAAS SAAS001676.
Sequence similarities	Contains 1 RdRp catalytic domain. SAAS SAAS001205 Contains 1 SF3 helicase domain. SAAS SAAS001205

Keywords
Biological process	Host-virus interaction Ion transport Transport Viral RNA replication SAAS SAAS001205 Viral attachment to host cell SAAS SAAS001676 Virus entry into host cell
Cellular component	Host cytoplasm SAAS SAAS001676 Host cytoplasmic vesicle SAAS SAAS001676 Host membrane SAAS SAAS001205 Membrane Virion
Ligand	ATP-binding Nucleotide-binding RNA-binding SAAS SAAS001676
Molecular function	Capsid protein SAAS SAAS001205 Helicase SAAS SAAS014759 Hydrolase Ion channel Nucleotidyltransferase Protease RNA-directed RNA polymerase SAAS SAAS001205 Thiol protease SAAS SAAS001205 Transferase Viral ion channel SAAS SAAS001676
PTM	Phosphoprotein SAAS SAAS014759
Technical term	3D-structure PDB 4IQX PDB 1U09 PDB 1WNE PDB 2D7S PDB 3NMA PDB 3NKY PDB 3NL0
Gene Ontology (GO)
Biological_process	ion transport Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro viral protein processing Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW host cell membrane Inferred from electronic annotation. Source: UniProtKB-KW icosahedral viral capsid Inferred from electronic annotation. Source: InterPro membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP 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 structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

[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: C EMBL CAB60265.1.
[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]	"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.

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