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P03306

- POLG_FMDV1

UniProt

P03306 - POLG_FMDV1

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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (strain A10-61) (Aphthovirus A) (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
Sitei725 – 7262Cleavage; by picornain 3CSequence Analysis
Sitei935 – 9362Cleavage; by picornain 3CSequence Analysis
Sitei953 – 9542Cleavage; by ribosomal skipSequence Analysis
Sitei1107 – 11082Cleavage; by picornain 3CSequence Analysis
Sitei1425 – 14262Cleavage; by picornain 3CSequence Analysis
Sitei1578 – 15792Cleavage; by picornain 3CSequence Analysis
Sitei1601 – 16022Cleavage; by picornain 3CSequence Analysis
Sitei1625 – 16262Cleavage; by picornain 3CSequence Analysis
Sitei1649 – 16502Cleavage; by picornain 3CSequence Analysis
Active sitei1695 – 16951For picornain 3C activitySequence Analysis
Active sitei1722 – 17221For picornain 3C activitySequence Analysis
Active sitei1812 – 18121For picornain 3C activitySequence Analysis
Sitei1862 – 18632Cleavage; by picornain 3CSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1217 – 12248ATPPROSITE-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-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 (strain A10-61) (Aphthovirus A) (FMDV)
Taxonomic identifieri12112 [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]
ProteomesiUP000008764: 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 – 23322332Genome polyproteinPRO_0000039816Add
BLAST
Chaini1 – 201201Leader proteaseSequence AnalysisPRO_0000039817Add
BLAST
Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374073Add
BLAST
Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039820Add
BLAST
Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039821Add
BLAST
Chaini505 – 725221Protein VP3Sequence AnalysisPRO_0000039822Add
BLAST
Chaini726 – 935210Protein VP1Sequence AnalysisPRO_0000039823Add
BLAST
Chaini936 – 95318Protein 2ASequence AnalysisPRO_0000039824Add
BLAST
Chaini954 – 1107154Protein 2BSequence AnalysisPRO_0000310973Add
BLAST
Chaini1108 – 1425318Protein 2CSequence AnalysisPRO_0000310974Add
BLAST
Chaini1426 – 1578153Protein 3ASequence AnalysisPRO_0000310975Add
BLAST
Chaini1579 – 160123Protein 3B-1Sequence AnalysisPRO_0000039825Add
BLAST
Chaini1602 – 162524Protein 3B-2Sequence AnalysisPRO_0000039826Add
BLAST
Chaini1626 – 164924Protein 3B-3Sequence AnalysisPRO_0000039827Add
BLAST
Chaini1650 – 1862213Picornain 3CSequence AnalysisPRO_0000039828Add
BLAST
Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039829Add
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 residuei1581 – 15811O-(5'-phospho-RNA)-tyrosineBy similarity
Modified residuei1604 – 16041O-(5'-phospho-RNA)-tyrosineBy similarity
Modified residuei1628 – 16281O-(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

Secondary structure

1
2332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi229 – 2324
Helixi268 – 2747
Beta strandi301 – 3055
Beta strandi308 – 3147
Helixi332 – 3343
Helixi342 – 3443
Beta strandi348 – 3558
Beta strandi364 – 3707
Helixi376 – 3838
Beta strandi384 – 39714
Beta strandi404 – 41411
Helixi422 – 4287
Beta strandi429 – 4346
Turni436 – 4383
Beta strandi440 – 4467
Beta strandi450 – 4556
Turni457 – 4593
Beta strandi463 – 47412
Beta strandi477 – 4793
Beta strandi483 – 49917
Helixi548 – 5547
Turni562 – 5643
Beta strandi565 – 5695
Beta strandi572 – 5743
Beta strandi577 – 5837
Helixi588 – 5903
Helixi594 – 5996
Beta strandi602 – 6076
Beta strandi609 – 6157
Beta strandi622 – 6309
Beta strandi632 – 6365
Helixi641 – 6444
Beta strandi647 – 6537
Beta strandi659 – 6646
Beta strandi669 – 6713
Beta strandi673 – 6764
Beta strandi688 – 69811
Beta strandi703 – 7108
Beta strandi715 – 7195
Helixi730 – 7323
Helixi740 – 7434
Helixi753 – 7553
Helixi757 – 7615
Beta strandi763 – 7675
Beta strandi772 – 7754
Helixi778 – 7803
Helixi786 – 7927
Beta strandi794 – 80916
Beta strandi811 – 8144
Helixi820 – 8245
Beta strandi828 – 8314
Beta strandi838 – 8425
Beta strandi847 – 8537
Beta strandi890 – 8923
Beta strandi894 – 91118
Beta strandi921 – 9233
Beta strandi936 – 9383
Helixi1657 – 16648
Beta strandi1665 – 16728
Beta strandi1675 – 168713
Beta strandi1689 – 16935
Helixi1694 – 16974
Beta strandi1702 – 17065
Beta strandi1709 – 17113
Helixi1713 – 17153
Beta strandi1716 – 17194
Beta strandi1722 – 17254
Beta strandi1726 – 17283
Beta strandi1733 – 174210
Helixi1749 – 17513
Beta strandi1752 – 17554
Beta strandi1763 – 17708
Turni1771 – 17733
Beta strandi1774 – 178411
Beta strandi1800 – 18045
Beta strandi1815 – 18206
Beta strandi1823 – 183412
Beta strandi1837 – 18426
Helixi1845 – 18539

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZBAX-ray2.001726-937[»]
2287-504[»]
3505-725[»]
4202-286[»]
1ZBEX-ray3.001726-937[»]
2287-504[»]
3505-725[»]
4202-286[»]
2BHGX-ray1.90A/B1650-1855[»]
2J92X-ray2.20A/B1649-1855[»]
2WV4X-ray2.50A/B1650-1862[»]
C/D931-940[»]
2WV5X-ray2.70A/B/C/D1650-1862[»]
E/F/G/H936-940[»]
ProteinModelPortaliP03306.
SMRiP03306. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03306.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14801480CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1502 – 2332831CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1481 – 150121Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28Add
BLAST
Domaini1189 – 1353165SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1652 – 1836185Peptidase C3Add
BLAST
Domaini2096 – 2214119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi868 – 8703Cell attachment site

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

Note: Both isoforms are able to cleave the L/VP0 junction and the host translation initiation factor EIF4G1.

Isoform Lab (identifier: P03306-1) [UniParc]FASTAAdd to Basket

Also known as: P20a

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
MNTTNCFIAL VYLIREIKTL FRSRTKGKME FTLHNGEKKT FYSRPNNHDN
60 70 80 90 100
CWLNTILQLF RYVDEPFFDW VYNSPENLTL DAIKQLENFT GLELHEGGPP
110 120 130 140 150
ALVIWNIKHL LQTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGQEHAV
160 170 180 190 200
FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG DWKTQVQKKL
210 220 230 240 250
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMSTQLG DNTISGGSNE
260 270 280 290 300
GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI
310 320 330 340 350
LTTRNGHTTS TTQSSVGVTY GYSTEEDHVA GPNTSGLETR VVQAERFFKK
360 370 380 390 400
FLFDWTTDKP FGYLTKLELP TDHHGVFGHL VDSYAYMRNG WDVEVSAVGN
410 420 430 440 450
QFNGGCLLVA MVPEWKAFDT REKYQLTLFP HQFISPRTNM TAHITVPYLG
460 470 480 490 500
VNRYDQYKKH KPWTLVVMVL SPLTVSNTAA PQIKVYANIA PTYVHVAGEL
510 520 530 540 550
PSKEGIFPVA CADGYGGLVT TDPKTADPVY GKVYNPPKTN YPGRFTNLLD
560 570 580 590 600
VAEACPTFLR FDDGKPYVVT RADDTRLLAK FDVSLAAKHM SNTYLSGIAQ
610 620 630 640 650
YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPDT PEEAAHCIHA
660 670 680 690 700
EWDTGLNSKF TFSIPYVSAA DYAYTASDTA ETTNVQGWVC VYQITHGKAE
710 720 730 740 750
NDTLLVSASA GKDFELRLPI DPRTQTTTTG ESADPVTTTV ENYGGDTQVQ
760 770 780 790 800
RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ THKHGIVGAL LRAATYYFSD
810 820 830 840 850
LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL ALPYTAPHRV
860 870 880 890 900
LATVYDGTNK YSASDSRSGD LGSIAARVAT QLPASFNYGA IQAQAIHELL
910 920 930 940 950
VRMKRAELYC PRPLLAIKVT SQDRYKQKII APAKQLLNFD LLKLAGDVES
960 970 980 990 1000
NLGPFFFADV RSNFSKLVDT INQMQEDMST KHGPDFNRLV SAFEELATGV
1010 1020 1030 1040 1050
KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI
1060 1070 1080 1090 1100
LDSTFVVKKS SDSLSSLFHV PAPAFSFGAP VLLAGLVKVA SSFFRSTPED
1110 1120 1130 1140 1150
LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM
1160 1170 1180 1190 1200
TDLVPGILEK QRDLNDPGKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
1210 1220 1230 1240 1250
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP
1260 1270 1280 1290 1300
DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK
1310 1320 1330 1340 1350
GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINN
1360 1370 1380 1390 1400
KLDIIKALED THTNPVAMFQ YDCALLNGMA VEMKRLQQDM FKPQPPLQNV
1410 1420 1430 1440 1450
YQLVQEVIER VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF
1460 1470 1480 1490 1500
FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
1510 1520 1530 1540 1550
IRETRKRQKM VDDAVNEYIE RANITTDDKT LDEAEKNPLE TSGASTVGFR
1560 1570 1580 1590 1600
ERSLTGQKVR DDVSSEPAQP AEDQPQAEGP YSGPLERQKP LKVRAKLPQQ
1610 1620 1630 1640 1650
EGPYAGPMER QKPLKVKVKA PVVKEGPYEG PVKKPVALKV KARNLIVTES
1660 1670 1680 1690 1700
GAPPTDLQKM VMGNTKPVEL NLDGKTVAIC CATGVFGTAY LVPRHLFAEK
1710 1720 1730 1740 1750
YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALIVLH RGNCVRDITK
1760 1770 1780 1790 1800
HFRDTARMKK GTPVVGVVNN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
1810 1820 1830 1840 1850
FAYKAATRAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLQK
1860 1870 1880 1890 1900
MKAHVDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAYG VFNPEFGPAA
1910 1920 1930 1940 1950
LSNKDPRLNE GVVLDDVIFS KHKGDAKMTE EDKALFRRCA ADYASRLHSV
1960 1970 1980 1990 2000
LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT
2010 2020 2030 2040 2050
VGPEVEAALK LMEKREYKFA CQTFLKDEIR PMEKVRAGKT RIVDVLPVEH
2060 2070 2080 2090 2100
ILYTKMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
2110 2120 2130 2140 2150
VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK
2160 2170 2180 2190 2200
RITVEGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD
2210 2220 2230 2240 2250
DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGQ SITDVTFLKR
2260 2270 2280 2290 2300
HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE
2310 2320 2330
YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
Length:2,332
Mass (Da):259,319
Last modified:February 1, 2005 - v2
Checksum:iFE8A553569F1A6DD
GO
Isoform Lb (identifier: P03306-2) [UniParc]FASTAAdd to Basket

Also known as: P16

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

Show »
Length:2,304
Mass (Da):256,019
Checksum:i77C9C2F0CE91C454
GO

Sequence cautioni

The sequence CAA25127.1 differs from that shown. Reason: Frameshift at positions 1727 and 1739.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961S → C in CAA24361. (PubMed:6282711)Curated
Sequence conflicti632 – 6321P → L in CAA24361. (PubMed:6282711)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018979Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00429 Genomic RNA. Translation: CAA25127.1. Frameshift.
V01130 Genomic RNA. Translation: CAA24361.1.
PIRiA93508. GNNY2F.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00429 Genomic RNA. Translation: CAA25127.1 . Frameshift.
V01130 Genomic RNA. Translation: CAA24361.1 .
PIRi A93508. GNNY2F.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZBA X-ray 2.00 1 726-937 [» ]
2 287-504 [» ]
3 505-725 [» ]
4 202-286 [» ]
1ZBE X-ray 3.00 1 726-937 [» ]
2 287-504 [» ]
3 505-725 [» ]
4 202-286 [» ]
2BHG X-ray 1.90 A/B 1650-1855 [» ]
2J92 X-ray 2.20 A/B 1649-1855 [» ]
2WV4 X-ray 2.50 A/B 1650-1862 [» ]
C/D 931-940 [» ]
2WV5 X-ray 2.70 A/B/C/D 1650-1862 [» ]
E/F/G/H 936-940 [» ]
ProteinModelPortali P03306.
SMRi P03306. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03306.

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. "The complete nucleotide sequence of the RNA coding for the primary translation product of foot and mouth disease virus."
    Carroll A.R., Rowlands D.J., Clarke B.E.
    Nucleic Acids Res. 12:2461-2472(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "The nucleotide sequence of cDNA coding for the structural proteins of foot-and-mouth disease virus."
    Boothroyd J.C., Harris T.J.R., Rowlands D.J., Lowe P.A.
    Gene 17:153-161(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 115-1048.
  3. "All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs."
    Sangar D.V., Newton S.E., Rowlands D.J., Clarke B.E.
    Nucleic Acids Res. 15:3305-3315(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION.

Entry informationi

Entry nameiPOLG_FMDV1
AccessioniPrimary (citable) accession number: P03306
Secondary accession number(s): Q64768
, Q84750, Q84751, Q84752, Q84753, Q84754, Q84760, Q84761, Q84762, Q84763, Q84764, Q84765, Q84766, Q84767, Q84768, Q84769, Q89824
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 2005
Last modified: October 29, 2014
This is version 152 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

Dasty 3