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P03305

- POLG_FMDVO

UniProt

P03305 - POLG_FMDVO

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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (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 also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.
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 (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.
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 activity
Active sitei148 – 1481For leader protease activity
Active sitei163 – 1631For leader protease activity
Sitei201 – 2022Cleavage; by leader proteaseSequence Analysis
Sitei286 – 2872CleavageSequence Analysis
Sitei504 – 5052Cleavage; by picornain 3CSequence Analysis
Sitei724 – 7252Cleavage; 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- 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 Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)
Taxonomic identifieri73482 [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]
ProteomesiUP000008765: 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14801480CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1481 – 150121Sequence AnalysisAdd
BLAST
Topological domaini1502 – 2332831CytoplasmicSequence AnalysisAdd
BLAST

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_0000039872Add
BLAST
Chaini1 – 201201Leader proteasePRO_0000039873Add
BLAST
Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374076Add
BLAST
Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039876Add
BLAST
Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039877Add
BLAST
Chaini505 – 724220Protein VP3Sequence AnalysisPRO_0000039878Add
BLAST
Chaini725 – 935211Protein VP1PRO_0000039879Add
BLAST
Chaini936 – 95318Protein 2ASequence AnalysisPRO_0000039880Add
BLAST
Chaini954 – 1107154Protein 2BSequence AnalysisPRO_0000310976Add
BLAST
Chaini1108 – 1425318Protein 2CSequence AnalysisPRO_0000039881Add
BLAST
Chaini1426 – 1578153Protein 3ASequence AnalysisPRO_0000039882Add
BLAST
Chaini1579 – 160123Protein 3B-1Sequence AnalysisPRO_0000039883Add
BLAST
Chaini1602 – 162524Protein 3B-2Sequence AnalysisPRO_0000310977Add
BLAST
Chaini1626 – 164924Protein 3B-3Sequence AnalysisPRO_0000310978Add
BLAST
Chaini1650 – 1862213Picornain 3CSequence AnalysisPRO_0000039884Add
BLAST
Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
Disulfide bondi406 ↔ 858Interchain (between VP2 and VP1 chains)
Disulfide bondi511 – 511Interchain; in VP3 dimer
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.

Structurei

Secondary structure

1
2332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi38 – 403Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 6313Combined sources
Helixi66 – 683Combined sources
Helixi69 – 724Combined sources
Beta strandi73 – 764Combined sources
Helixi79 – 9012Combined sources
Helixi100 – 1078Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi129 – 1313Combined sources
Helixi134 – 1363Combined sources
Beta strandi137 – 1448Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi166 – 1694Combined sources
Helixi174 – 1763Combined sources
Beta strandi177 – 1826Combined sources
Turni195 – 1973Combined sources
Helixi229 – 2324Combined sources
Helixi268 – 2747Combined sources
Helixi297 – 2993Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi308 – 3147Combined sources
Helixi332 – 3343Combined sources
Helixi342 – 3443Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi364 – 3707Combined sources
Helixi376 – 3838Combined sources
Beta strandi384 – 39714Combined sources
Beta strandi404 – 41310Combined sources
Helixi421 – 4288Combined sources
Beta strandi429 – 4346Combined sources
Turni436 – 4383Combined sources
Beta strandi440 – 4467Combined sources
Beta strandi451 – 4555Combined sources
Turni457 – 4593Combined sources
Beta strandi463 – 47412Combined sources
Turni476 – 4783Combined sources
Beta strandi483 – 49917Combined sources
Helixi548 – 5547Combined sources
Turni562 – 5643Combined sources
Beta strandi565 – 5695Combined sources
Beta strandi577 – 5837Combined sources
Helixi588 – 5903Combined sources
Helixi594 – 5996Combined sources
Beta strandi602 – 6076Combined sources
Beta strandi609 – 6157Combined sources
Beta strandi622 – 6309Combined sources
Helixi640 – 6434Combined sources
Beta strandi646 – 6527Combined sources
Beta strandi658 – 6636Combined sources
Beta strandi668 – 6703Combined sources
Beta strandi672 – 6754Combined sources
Beta strandi687 – 69711Combined sources
Beta strandi702 – 7098Combined sources
Beta strandi714 – 7185Combined sources
Helixi739 – 7424Combined sources
Helixi752 – 7543Combined sources
Helixi756 – 7605Combined sources
Beta strandi762 – 7665Combined sources
Helixi777 – 7793Combined sources
Helixi785 – 7917Combined sources
Beta strandi793 – 80816Combined sources
Beta strandi810 – 8134Combined sources
Helixi819 – 8235Combined sources
Beta strandi827 – 8304Combined sources
Beta strandi837 – 8415Combined sources
Beta strandi846 – 8527Combined sources
Beta strandi891 – 8933Combined sources
Beta strandi895 – 91218Combined sources
Beta strandi921 – 9244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QMYX-ray1.90A/B/C29-195[»]
1QOLX-ray3.00A/B/C/D/E/F/G/H29-201[»]
1QQPX-ray1.901725-937[»]
2287-504[»]
3505-724[»]
4202-286[»]
2JQFNMR-R/S29-201[»]
2JQGNMR-R29-195[»]
DisProtiDP00573.
ProteinModelPortaliP03305.
SMRiP03305. Positions 29-201, 216-286, 291-934, 1656-1856, 1863-2332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03305.

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
Motifi869 – 8713Cell 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: P03305-1) [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
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN
60 70 80 90 100
CWLNAILQLF RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV
160 170 180 190 200
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQRKL
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 TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT
360 370 380 390 400
HLFDWVTSDS FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA MVPELYSIQK RELYQLTLFP HQFINPRTNM TAHITVPFVG
460 470 480 490 500
VNRYDQYKVH KPWTLVVMVV APLTVNTEGA PQIKVYANIA PTNVHVAGEF
510 520 530 540 550
PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ LPGRFTNLLD
560 570 580 590 600
VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ
610 620 630 640 650
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE
660 670 680 690 700
WDTGLNSKFT FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG
710 720 730 740 750
DALVVLASAG KDFELRLPVD ARAETTSAGE SADPVTTTVE NYGGETQIQR
760 770 780 790 800
RQHTDVSFIM DRFVKVTPQN QINILDLMQI PSHTLVGALL RASTYYFSDL
810 820 830 840 850
EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA LPYTAPHRVL
860 870 880 890 900
ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL
910 920 930 940 950
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES
960 970 980 990 1000
NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV
1010 1020 1030 1040 1050
KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI
1060 1070 1080 1090 1100
LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP VLLAGLVKVA SSFFRSTPED
1110 1120 1130 1140 1150
LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM
1160 1170 1180 1190 1200
TDLVPGILEK QRDLNDPSKY 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 SAKDGYKINS
1360 1370 1380 1390 1400
KLDIIKALED THANPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV
1410 1420 1430 1440 1450
YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF
1460 1470 1480 1490 1500
FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
1510 1520 1530 1540 1550
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR
1560 1570 1580 1590 1600
ERTLPGQKAC DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ
1610 1620 1630 1640 1650
EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV KAKNLIVTES
1660 1670 1680 1690 1700
GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK
1710 1720 1730 1740 1750
YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK
1760 1770 1780 1790 1800
HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
1810 1820 1830 1840 1850
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK
1860 1870 1880 1890 1900
MKAHIDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA
1910 1920 1930 1940 1950
LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV
1960 1970 1980 1990 2000
LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT
2010 2020 2030 2040 2050
VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT RIVDVLPVEH
2060 2070 2080 2090 2100
ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
2110 2120 2130 2140 2150
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK
2160 2170 2180 2190 2200
RITVGGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD
2210 2220 2230 2240 2250
DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGH SITDVTFLKR
2260 2270 2280 2290 2300
HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE
2310 2320 2330
YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
Length:2,332
Mass (Da):258,927
Last modified:July 21, 1986 - v1
Checksum:i4A83176F43447D68
GO
Isoform Lb (identifier: P03305-2) [UniParc]FASTAAdd to Basket

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

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Length:2,304
Mass (Da):255,803
Checksum:i5372D197CC761349
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti780 – 7801I → V in strain: Isolate O1BFS.
Natural varianti808 – 8081G → R in strain: Isolate O1BFS.
Natural varianti861 – 8611N → S in strain: Isolate O1BFS.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018982Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00871 Genomic RNA. Translation: CAA25416.1.
J02185 Genomic RNA. Translation: AAA42635.1.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with oligosaccharide receptor

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00871 Genomic RNA. Translation: CAA25416.1 .
J02185 Genomic RNA. Translation: AAA42635.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QMY X-ray 1.90 A/B/C 29-195 [» ]
1QOL X-ray 3.00 A/B/C/D/E/F/G/H 29-201 [» ]
1QQP X-ray 1.90 1 725-937 [» ]
2 287-504 [» ]
3 505-724 [» ]
4 202-286 [» ]
2JQF NMR - R/S 29-201 [» ]
2JQG NMR - R 29-195 [» ]
DisProti DP00573.
ProteinModelPortali P03305.
SMRi P03305. Positions 29-201, 216-286, 291-934, 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 P03305.

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. "Nucleotide sequence and genome organization of foot-and-mouth disease virus."
    Forss S., Strebel K., Beck E., Schaller H.
    Nucleic Acids Res. 12:6587-6601(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Comparison of the amino acid sequence of the major immunogen from three serotypes of foot and mouth disease virus."
    Makoff A.J., Paynter C.A., Rowlands D.J., Boothroyd J.C.
    Nucleic Acids Res. 10:8285-8295(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate O1BFS/Britain/1968.
  3. "Foot-and-mouth disease virus leader proteinase: specificity at the P2 and P3 positions and comparison with other papain-like enzymes."
    Kuehnel E., Cencic R., Foeger N., Skern T.
    Biochemistry 43:11482-11490(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "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.
  5. "The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities."
    Medina M., Domingo E., Brangwyn J.K., Belsham G.J.
    Virology 194:355-359(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE LEADER PROTEASE.
  6. "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
    Glaser W., Skern T.
    FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE LEADER PROTEASE, CLEAVAGE OF HOST EIF4G1.
    Strain: Isolate O1k.
  7. "Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'."
    Donnelly M.L.L., Luke G., Mehrotra A., Li X., Hughes L.E., Gani D., Ryan M.D.
    J. Gen. Virol. 82:1013-1025(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYPROTEIN PROCESSING.
  8. "Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro."
    Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T., Belsham G.J.
    J. Virol. 78:3271-3278(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE LEADER PROTEASE, CLEAVAGE OF HOST EIF4G3.
  9. "Factors required for the uridylylation of the foot-and-mouth disease virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in vitro."
    Nayak A., Goodfellow I.G., Belsham G.J.
    J. Virol. 79:7698-7706(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT RNA-LINKAGE OF 3B PROTEINS, URIDYLYLATION.
  10. "Heparan sulfate-binding foot-and-mouth disease virus enters cells via caveola-mediated endocytosis."
    O'Donnell V., Larocco M., Baxt B.
    J. Virol. 82:9075-9085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF CAPSID PROTEINS.
  11. "Cellular receptors for foot and mouth disease virus."
    Ruiz-Saenz J., Goez Y., Tabares W., Lopez-Herrera A.
    Intervirology 52:201-212(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "The three-dimensional structure of foot-and-mouth disease virus at 2.9-A resolution."
    Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F.
    Nature 337:709-716(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  13. "Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition."
    Guarne A., Tormo J., Kirchweger R., Pfistermueller D., Fita I., Skern T.
    EMBO J. 17:7469-7479(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-201 OF MUTANT ALA-51.
  14. "Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes."
    Guarne A., Hampoelz B., Glaser W., Carpena X., Tormo J., Fita I., Skern T.
    J. Mol. Biol. 302:1227-1240(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-195 OF MUTANT ALA-51/SER-133.

Entry informationi

Entry nameiPOLG_FMDVO
AccessioniPrimary (citable) accession number: P03305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 157 of the entry and version 1 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.

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