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Q9QCE4 (Q9QCE4_9PICO) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 93. 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

Protein attributes

Sequence length2327 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
Magnesium PDB 2E9R PDB 2E9T PDB 2E9Z PDB 2EC0 PDB 1WNE PDB 3NMA PDB 3NKY PDB 3NL0
Metal-binding PDB 2E9R PDB 2E9T PDB 2E9Z PDB 2EC0 PDB 1WNE PDB 3NMA PDB 3NKY PDB 3NL0
Nucleotide-binding
RNA-binding SAAS SAAS014759
   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 2E9R PDB 4IQX PDB 2E9T PDB 2E9Z PDB 2EC0 PDB 1U09 PDB 1WNE PDB 2D7S PDB 3NMA PDB 3NKY PDB 3NL0
Gene Ontology (GO)
   Biological_processpore 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

viral protein processing

Inferred from electronic annotation. Source: InterPro

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

icosahedral viral capsid

Inferred from electronic annotation. Source: InterPro

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

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 – 201201leader protease EMBL CAB60265.1
PRO_5000064857
Chain202 – 28685VP4 protein EMBL CAB60265.1
PRO_5000064858
Chain287 – 504218VP2 protein EMBL CAB60265.1
PRO_5000064859
Chain505 – 723219VP3 protein EMBL CAB60265.1
PRO_5000064860
Chain724 – 932209VP1 protein EMBL CAB60265.1
PRO_5000064861
Chain933 – 948162A protease EMBL CAB60265.1
PRO_5000064862
Chain949 – 11361882B protein EMBL CAB60265.1
PRO_5000064863
Chain1136 – 14202852C protein EMBL CAB60265.1
PRO_5000064864
Chain1421 – 15731533A protein EMBL CAB60265.1
PRO_5000064865
Chain1574 – 159623VPg1 protein EMBL CAB60265.1
PRO_5000064866
Chain1597 – 162024VPg2 protein EMBL CAB60265.1
PRO_5000064867
Chain1621 – 164424VPg3 protein EMBL CAB60265.1
PRO_5000064868
Chain1645 – 18572133C protease EMBL CAB60265.1
PRO_5000064869
Chain1858 – 23274703D polymerase EMBL CAB60265.1
PRO_5000064870

Sites

Metal binding20951Magnesium PDB 2EC0
Metal binding21961Magnesium PDB 2EC0
Metal binding22411Magnesium; via carbonyl oxygen PDB 2EC0
Binding site20251Diphosphate 2 PDB 2E9T PDB 2EC0
Binding site20361Diphosphate 1 PDB 2E9Z
Binding site21001Diphosphate 2; via amide nitrogen PDB 2E9T PDB 2EC0
Binding site22441Diphosphate 1 PDB 2E9Z

Sequences

Sequence LengthMass (Da)Tools
Q9QCE4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8AE69D7939F08BB1

FASTA2,327258,245
        10         20         30         40         50         60 
MNTTDCFIAV VNAIKEVRAL FLPRTAGKME FTLHDGEKKV FYSRPNNHDN CWLNTILQLF 

        70         80         90        100        110        120 
RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLDLREGGPP ALVIWNIKHL LHTGIGTASR 

       130        140        150        160        170        180 
PSEVCMVDGT DMCLADFHAG IFMKGREHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF 

       190        200        210        220        230        240 
VPYDQEPLNE GWKASVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG 

       250        260        270        280        290        300 
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 

       310        320        330        340        350        360 
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM ALFDWVPSQN 

       370        380        390        400        410        420 
FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN QFNGGCLLVA LVPEMGDISD 

       430        440        450        460        470        480 
REKYQLTLYP HQFINPRTNM TAHITVPYVG VNRYDQYKQH RPWTLVVMVV APLTTNTVGA 

       490        500        510        520        530        540 
QQIKVYANIA PTNVHVAGEL PSKEGIFPVA CSAGYGHLVT TDPKTADPAY GKVYNPPRTA 

       550        560        570        580        590        600 
LPGRFTNYLD VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 

       610        620        630        640        650        660 
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW DTGLNSKFTF 

       670        680        690        700        710        720 
SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD ALVVSASAGK DFELRLPVDA 

       730        740        750        760        770        780 
RQQTTTTGES ADPVTTTVEN YGGETQVQRR HHTDVAFVLD RFVKVTVSDN QHTLDVMQAH 

       790        800        810        820        830        840 
KDNIVGALLR AATYYFSDLE IAVTHTGKLT WVPNGAPVSA LNNTTNPTAY HKGPVTRLAL 

       850        860        870        880        890        900 
PYTAPHRVLA TAYTGTTTYT ASARGDLAHL KTTHARHLPT SFNFGAVKAE TITELLVRMK 

       910        920        930        940        950        960 
RAELYCPRPI LPIQPTDDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF FFSDVRSNFS 

       970        980        990       1000       1010       1020 
KLVETINQMQ EDMSTRHGPD FNRLVSAFEE LASGVKAIRT GLDEAKPWYK LIKLLSRLSC 

      1030       1040       1050       1060       1070       1080 
MAAVAARSKD PVLVAIMLAD TGLEILDSTF VVKKISDSLS SLFHVPAPAF SFGAPILLAG 

      1090       1100       1110       1120       1130       1140 
LVKVASSFFR STPEDLERAE KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE 

      1150       1160       1170       1180       1190       1200 
KYVTMTDLVP GILEKQRDLN DPSKYKDAKE WLDNTRQVCL KSGNVHIANL CKVVAPAPSK 

      1210       1220       1230       1240       1250       1260 
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF DGYNQQTVVV 

      1270       1280       1290       1300       1310       1320 
MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFN SKVIIATTNL YSGFTPKTMV 

      1330       1340       1350       1360       1370       1380 
CPDALNRRFH FDIDVSAKDG YKTNNKLDII KALEDTHTNP VAMFQYDCAL LNGMAVEMKR 

      1390       1400       1410       1420       1430       1440 
LQQDMFKPQP PLQNVYQLVQ EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE 

      1450       1460       1470       1480       1490       1500 
AAIEFFEGMV HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH 

      1510       1520       1530       1540       1550       1560 
KRQKMVDDAV NEYIEKANIT TDDQTLDEAE KNPLETSGAS TVGFRERTLP GQKARDDVNS 

      1570       1580       1590       1600       1610       1620 
EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPRQEGPYA GPMERQKPLK VKARAPVVKE 

      1630       1640       1650       1660       1670       1680 
GPYEGPVKKP VALKVKAKNL IVTESGAPPT DLQKMVMGNT KPVELILDGK TVAICCATGV 

      1690       1700       1710       1720       1730       1740 
FGTAYLVPRH LFAEKYDKIM LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV 

      1750       1760       1770       1780       1790       1800 
RDITKHFRDV ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA 

      1810       1820       1830       1840       1850       1860 
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI DPEPHHEGLI 

      1870       1880       1890       1900       1910       1920 
VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD PRLNEGVVLD EVIFSKHKGD 

      1930       1940       1950       1960       1970       1980 
TKMSAEDKAL FRRCAADYAS RLHSVLGTAN APLSIYEAIK GVDGLDAMEP DTAPGLPWAL 

      1990       2000       2010       2020       2030       2040 
QGKRRGALID FENGTVGPEV EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV 

      2050       2060       2070       2080       2090       2100 
LPVEHILYTR MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA 

      2110       2120       2130       2140       2150       2160 
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE GGMPSGCSAT 

      2170       2180       2190       2200       2210       2220 
SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA SDYDLDFEAL KPHFKSLGQT 

      2230       2240       2250       2260       2270       2280 
ITPADKSDKG FVLGHSITDV TFLKRHFHMD YGTGFYKPVM ASKTLEAILS FARRGTIQEK 

      2290       2300       2310       2320 
LISVAGLAVH SGPDEYRRLF EPFQGLFEIP SYRSLYLRWV NAVCGDA 

« Hide

References

[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ133358 Genomic RNA. Translation: CAB60265.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9QCE4.
SMRQ9QCE4. Positions 29-201, 216-930, 1651-1851, 1858-2327.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D4.10.90.10. 1 hit.
InterProIPR015031. 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.
[Graphical view]
PfamPF05408. 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]
PRINTSPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9QCE4.

Entry information

Entry nameQ9QCE4_9PICO
AccessionPrimary (citable) accession number: Q9QCE4
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)