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P03311

- POLG_FMDVS

UniProt

P03311 - POLG_FMDVS

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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Spain/S8c1SantaPau/1970 serotype C) (FMDV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription (By similarity).By similarity
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta6, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity).By similarity
Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).By similarity
Protease 3C: 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 cooperatively to the protease (By similarity).By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

Catalytic activityi

Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
NTP + H2O = NDP + phosphate.
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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511For leader protease activityBy similarity
Active sitei148 – 1481For leader protease activityBy similarity
Active sitei163 – 1631For leader protease activityBy similarity
Sitei201 – 2022Cleavage; by leader proteaseSequence Analysis
Sitei286 – 2872CleavageSequence Analysis
Sitei504 – 5052Cleavage; by picornain 3CSequence Analysis
Sitei723 – 7242Cleavage; by picornain 3CSequence Analysis
Sitei930 – 9312Cleavage; by picornain 3CSequence Analysis
Sitei948 – 9492Cleavage; by ribosomal skipSequence Analysis
Sitei1102 – 11032Cleavage; by picornain 3CSequence Analysis
Sitei1420 – 14212Cleavage; by picornain 3CSequence Analysis
Sitei1573 – 15742Cleavage; by picornain 3CSequence Analysis
Sitei1596 – 15972Cleavage; by picornain 3CSequence Analysis
Sitei1620 – 16212Cleavage; by picornain 3CSequence Analysis
Sitei1644 – 16452Cleavage; by picornain 3CSequence Analysis
Active sitei1690 – 16901For picornain 3C activitySequence Analysis
Active sitei1717 – 17171For picornain 3C activitySequence Analysis
Active sitei1807 – 18071For picornain 3C activitySequence Analysis
Sitei1857 – 18582Cleavage; by picornain 3CSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1212 – 12198ATPPROSITE-ProRule annotation

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. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. induction by virus of host autophagy Source: UniProtKB
  3. modulation by virus of host chromatin organization Source: UniProtKB-KW
  4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  5. protein oligomerization Source: UniProtKB-KW
  6. RNA-protein covalent cross-linking Source: UniProtKB-KW
  7. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  8. suppression by virus of host translation initiation factor activity Source: UniProtKB
  9. transcription, DNA-templated Source: InterPro
  10. viral protein processing Source: InterPro
  11. viral RNA genome replication Source: InterPro
  12. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Clathrin- and caveolin-independent endocytosis of virus by host, Clathrin-mediated endocytosis of virus by host, Host-virus interaction, Ion transport, Modulation of host chromatin by virus, Transport, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 15 chains:
Leader protease (EC:3.4.22.46)
Short name:
Lpro
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
P52
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B-1
Short name:
P3B-1
Alternative name(s):
Genome-linked protein VPg1
Protein 3B-2
Short name:
P3B-2
Alternative name(s):
Genome-linked protein VPg2
Protein 3B-3
Short name:
P3B-3
Alternative name(s):
Genome-linked protein VPg3
Alternative name(s):
Protease 3C
Short name:
P3C
Protease P20B
Alternative name(s):
P56A
OrganismiFoot-and-mouth disease virus (isolate -/Spain/S8c1SantaPau/1970 serotype C) (FMDV)
Taxonomic identifieri12120 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeAphthovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Capra hircus (Goat) [TaxID: 9925]
Cervidae (deer) [TaxID: 9850]
Erinaceidae (hedgehogs) [TaxID: 9363]
Loxodonta africana (African elephant) [TaxID: 9785]
Ovis aries (Sheep) [TaxID: 9940]
Rattus norvegicus (Rat) [TaxID: 10116]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000012670: Genome

Subcellular locationi

Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  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 protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23272327Genome polyproteinBy similarityPRO_0000422517Add
BLAST
Chaini1 – 201201Leader proteaseBy similarityPRO_5000064843Add
BLAST
Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000422518Add
BLAST
Chaini202 – 28685Protein VP4Sequence AnalysisPRO_5000064844Add
BLAST
Chaini287 – 504218Protein VP2Sequence AnalysisPRO_5000064845Add
BLAST
Chaini505 – 723219Protein VP3Sequence AnalysisPRO_0000039886Add
BLAST
Chaini724 – 930207Protein VP1By similarityPRO_0000039887Add
BLAST
Chaini931 – 94818Protein 2ASequence AnalysisPRO_0000039888Add
BLAST
Chaini949 – 1102154Protein 2BSequence AnalysisPRO_0000310979Add
BLAST
Chaini1103 – 1420318Protein 2CSequence AnalysisPRO_5000064850Add
BLAST
Chaini1421 – 1573153Protein 3ASequence AnalysisPRO_5000064851Add
BLAST
Chaini1574 – 159623Protein 3B-1Sequence AnalysisPRO_5000064852Add
BLAST
Chaini1597 – 162024Protein 3B-2Sequence AnalysisPRO_5000064853Add
BLAST
Chaini1621 – 164424Protein 3B-3Sequence AnalysisPRO_5000064854Add
BLAST
Chaini1645 – 1857213Picornain 3CSequence AnalysisPRO_0000039889Add
BLAST
Chaini1858 – 2327470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
Disulfide bondi511 – 511Interchain; in VP3 dimerBy similarity
Modified residuei1576 – 15761O-(5'-phospho-RNA)-tyrosineBy similarity
Modified residuei1599 – 15991O-(5'-phospho-RNA)-tyrosineBy similarity
Modified residuei1623 – 16231O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase (By similarity).By similarity

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

VP1 interacts (via RGD) with integrins heterodimers alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8.By similarity

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QGCelectron microscopy30.001724-930[»]
5856-879[»]
ProteinModelPortaliP03311.
SMRiP03311. Positions 29-201, 216-930, 1651-1851, 1858-2327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03311.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14751475CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1497 – 2327831CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1476 – 149621Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28Add
BLAST
Domaini1184 – 1348165SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1647 – 1831185Peptidase C3Add
BLAST
Domaini2091 – 2209119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi864 – 8663Cell attachment siteBy similarity

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C28 domain.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Lab (identifier: P03311-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNTTDCFIAV VNAIKEVRAL FLPRTAGKME FTLHDGEKKV FYSRPNNHDN
60 70 80 90 100
CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGREHAV
160 170 180 190 200
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNE GWKASVQRKL
210 220 230 240 250
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE
260 270 280 290 300
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
310 320 330 340 350
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM
360 370 380 390 400
ALFDWVPSQN FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG
460 470 480 490 500
VNRYDQYKQH RPWTLVVMVV APLTTNTAGA QQIKVYANIA PTNVHVAGEL
510 520 530 540 550
PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD
560 570 580 590 600
VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
610 620 630 640 650
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW
660 670 680 690 700
DTGLNSKFTF SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD
710 720 730 740 750
ALVVSASAGK DFELRLPVDA RQQTTTTGES ADPVTTTVEN YGGETQVQRR
760 770 780 790 800
HHTDVAFVLD RFVKVTVSDN QHTLDVMQAH KDNIVGALLR AATYYFSDLE
810 820 830 840 850
IAVTHTGKLT WVPNGAPVSA LNNTTNPTAY HKGPVTRLAL PYTAPHRVLA
860 870 880 890 900
TAYTGTTTYT ASARGDLAHL TTTHARHLPT SFNFGAVKAE TITELLVRMK
910 920 930 940 950
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF
960 970 980 990 1000
FFSDVRSNFS KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT
1010 1020 1030 1040 1050
GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF
1060 1070 1080 1090 1100
VVKKISDSLS SLFHVPAPAF SFGAPILLAG LVKVASSFFR STPEDLERAE
1110 1120 1130 1140 1150
KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP
1160 1170 1180 1190 1200
GILEKQRDLN DPSKYKDAKE WLDNTRQVCL KSGNVHIANL CKVVAPAPSK
1210 1220 1230 1240 1250
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF
1260 1270 1280 1290 1300
DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS
1310 1320 1330 1340 1350
SKVIIATTNL YSGFTPKTMV CPDALNRRFH FDIDVSAKDG YKINNKLDII
1360 1370 1380 1390 1400
KALEDTHTNP VAMFQYDCAL LNGMAVEMKR LQQDMFKPQP PLQNVYQLVQ
1410 1420 1430 1440 1450
EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV
1460 1470 1480 1490 1500
HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH
1510 1520 1530 1540 1550
KRQKMVDDAV NEYIEKANIT TDDQTLDEAE KNPLETSGAS TVGFRERTLP
1560 1570 1580 1590 1600
GQKARDDVNS EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPRQEGPYA
1610 1620 1630 1640 1650
GPMERQKPLK VKARAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT
1660 1670 1680 1690 1700
DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM
1710 1720 1730 1740 1750
LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDV
1760 1770 1780 1790 1800
ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA
1810 1820 1830 1840 1850
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI
1860 1870 1880 1890 1900
DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD
1910 1920 1930 1940 1950
PRLNEGVVLD EVIFSKHKGD TKMSAEDKAL FRRCAADYAS RLHSVLGTAN
1960 1970 1980 1990 2000
APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV
2010 2020 2030 2040 2050
EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR
2060 2070 2080 2090 2100
MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA
2110 2120 2130 2140 2150
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE
2160 2170 2180 2190 2200
GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA
2210 2220 2230 2240 2250
SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD
2260 2270 2280 2290 2300
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF
2310 2320
EPFQGLFEIP SYRSLYLRWV NAVCGDA
Length:2,327
Mass (Da):258,126
Last modified:May 29, 2013 - v2
Checksum:i00D677DBA57026AD
GO
Isoform Lb (identifier: P03311-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:2,299
Mass (Da):255,064
Checksum:i8E0FE54A24F3A3A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti789 – 7924LRAA → SRH no nucleotide entry (PubMed:6311686)Curated
Sequence conflicti947 – 9471P → L no nucleotide entry (PubMed:6311686)Curated
Sequence conflicti1008 – 10081Missing no nucleotide entry (PubMed:6311686)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1804 – 18041A → V.
Natural varianti1916 – 19161K → R.
Natural varianti1958 – 19581A → V.
Natural varianti1975 – 19751G → S.
Natural varianti2000 – 20001V → A.
Natural varianti2080 – 20801W → R.
Natural varianti2083 – 20831F → S.
Natural varianti2087 – 20871F → L.
Natural varianti2140 – 21401H → Y.
Natural varianti2163 – 21631I → V.
Natural varianti2261 – 22611A → T.
Natural varianti2299 – 22991L → F.
Natural varianti2326 – 23261D → R.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_046532Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ133357 Genomic RNA. Translation: CAB60267.1.
M11027 Genomic RNA. Translation: AAA42654.1.
PIRiJC1328.
JC1330.
JC1331.
JC1334.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ133357 Genomic RNA. Translation: CAB60267.1 .
M11027 Genomic RNA. Translation: AAA42654.1 .
PIRi JC1328.
JC1330.
JC1331.
JC1334.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QGC electron microscopy 30.00 1 724-930 [» ]
5 856-879 [» ]
ProteinModelPortali P03311.
SMRi P03311. Positions 29-201, 216-930, 1651-1851, 1858-2327.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03311.

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.
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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 [GENOMIC RNA].
  2. "Molecular cloning of cDNA from foot-and-mouth disease virus C1-Santa Pau (C-S8). Sequence of protein-VP1-coding segment."
    Villanueva N., Davila M., Ortin J., Domingo E.
    Gene 23:185-194(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 678-1011.
  3. "Sequence of the viral replicase gene from foot-and-mouth disease virus C1-Santa Pau (C-S8)."
    Martinez-Salas E., Ortin J., Domingo E.
    Gene 35:55-61(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1799-2327.
  4. "Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop."
    Hewat E.A., Verdaguer N., Fita I., Blakemore W., Brookes S., King A., Newman J., Domingo E., Mateu M.G., Stuart D.I.
    EMBO J. 16:1492-1500(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (30.00 ANGSTROMS) OF 855-878.

Entry informationi

Entry nameiPOLG_FMDVS
AccessioniPrimary (citable) accession number: P03311
Secondary accession number(s): Q84781, Q84782, Q9QCE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 29, 2013
Last modified: October 29, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The capsid protein VP1 contains the main antigenic determinants of the virion; therefore, changes in its sequence must be responsible for the high antigenic variability of the virus.By similarity

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

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