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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: 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. Increases translation driven by the viral internal ribosome entry site (IRES).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)DescriptionActionsGraphical viewLength
Active sitei51For leader protease activityBy similarity1
Active sitei148For leader protease activityBy similarity1
Active sitei163For leader protease activityBy similarity1
Active sitei1695For picornain 3C activitySequence analysis1
Active sitei1695For picornain 3C activity; Proton donor/acceptorSequence analysisCombined sources1
Active sitei1733For picornain 3C activityCombined sources1
Active sitei1812For picornain 3C activitySequence analysisCombined sources1
Sitei1831Important for catalytic activityCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1217 – 1224ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

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, Translation regulation, 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 virusesssRNA 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]
Proteomesi
  • UP000008764 Componenti: Chromosome

Subcellular locationi

Protein 2B :
Protein 2C :
Protein 3A :
RNA-directed RNA polymerase 3D-POL :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1480CytoplasmicSequence analysisAdd BLAST1480
Intramembranei1481 – 1501Sequence analysisAdd BLAST21
Topological domaini1502 – 2332CytoplasmicSequence analysisAdd BLAST831

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1791C → S: Almost complete loss of picornain 3C activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000398161 – 2332Genome polyproteinAdd BLAST2332
ChainiPRO_00000398171 – 201Leader proteaseSequence analysisAdd BLAST201
ChainiPRO_0000374073202 – 504Protein VP0Sequence analysisAdd BLAST303
ChainiPRO_0000039820202 – 286Protein VP4Sequence analysisAdd BLAST85
ChainiPRO_0000039821287 – 504Protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039822505 – 725Protein VP3Sequence analysisAdd BLAST221
ChainiPRO_0000039823726 – 935Protein VP1Sequence analysisAdd BLAST210
ChainiPRO_0000039824936 – 953Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000310973954 – 1107Protein 2BSequence analysisAdd BLAST154
ChainiPRO_00003109741108 – 1425Protein 2CSequence analysisAdd BLAST318
ChainiPRO_00003109751426 – 1578Protein 3ASequence analysisAdd BLAST153
ChainiPRO_00000398251579 – 1601Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_00000398261602 – 1625Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_00000398271626 – 1649Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00000398281650 – 1862Picornain 3CSequence analysisAdd BLAST213
ChainiPRO_00000398291863 – 2332RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi202N-myristoyl glycine; by hostBy similarity1
Disulfide bondi511Interchain; in VP3 dimerBy similarity
Modified residuei1581O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1604O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1628O-(5'-phospho-RNA)-tyrosineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei201 – 202Cleavage; by leader proteaseSequence analysis2
Sitei286 – 287CleavageSequence analysis2
Sitei504 – 505Cleavage; by picornain 3CSequence analysis2
Sitei725 – 726Cleavage; by picornain 3CSequence analysis2
Sitei935 – 936Cleavage; by picornain 3CSequence analysis2
Sitei953 – 954Cleavage; by ribosomal skipSequence analysis2
Sitei1107 – 1108Cleavage; by picornain 3CSequence analysis2
Sitei1425 – 1426Cleavage; by picornain 3CSequence analysis2
Sitei1578 – 1579Cleavage; by picornain 3CSequence analysis2
Sitei1601 – 1602Cleavage; by picornain 3CSequence analysis2
Sitei1625 – 1626Cleavage; by picornain 3CSequence analysis2
Sitei1649 – 1650Cleavage; by picornain 3CSequence analysis2
Sitei1862 – 1863Cleavage; by picornain 3CSequence analysis2

Keywords - PTMi

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

Interactioni

Subunit structurei

VP1 interacts with integrins heterodimers alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8 (By similarity). This virus has an RGSD motif in place of the otherwise conserved RGD integrin-binding motif and the potential to bind heparan sulfate as well (PubMed:15958669).By similarity1 Publication

Structurei

Secondary structure

12332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi229 – 232Combined sources4
Helixi268 – 274Combined sources7
Beta strandi301 – 305Combined sources5
Beta strandi308 – 314Combined sources7
Helixi332 – 334Combined sources3
Helixi342 – 344Combined sources3
Beta strandi348 – 355Combined sources8
Beta strandi364 – 370Combined sources7
Helixi376 – 383Combined sources8
Beta strandi384 – 397Combined sources14
Beta strandi404 – 414Combined sources11
Helixi422 – 428Combined sources7
Beta strandi429 – 434Combined sources6
Turni436 – 438Combined sources3
Beta strandi440 – 446Combined sources7
Beta strandi450 – 455Combined sources6
Turni457 – 459Combined sources3
Beta strandi463 – 474Combined sources12
Beta strandi477 – 479Combined sources3
Beta strandi483 – 499Combined sources17
Helixi548 – 554Combined sources7
Turni562 – 564Combined sources3
Beta strandi565 – 569Combined sources5
Beta strandi572 – 574Combined sources3
Beta strandi577 – 583Combined sources7
Helixi588 – 590Combined sources3
Helixi594 – 599Combined sources6
Beta strandi602 – 607Combined sources6
Beta strandi609 – 615Combined sources7
Beta strandi622 – 630Combined sources9
Beta strandi632 – 636Combined sources5
Helixi641 – 644Combined sources4
Beta strandi647 – 653Combined sources7
Beta strandi659 – 664Combined sources6
Beta strandi669 – 671Combined sources3
Beta strandi673 – 676Combined sources4
Beta strandi688 – 698Combined sources11
Beta strandi703 – 710Combined sources8
Beta strandi715 – 719Combined sources5
Helixi730 – 732Combined sources3
Helixi740 – 743Combined sources4
Helixi753 – 755Combined sources3
Helixi757 – 761Combined sources5
Beta strandi763 – 767Combined sources5
Beta strandi772 – 775Combined sources4
Helixi778 – 780Combined sources3
Helixi786 – 792Combined sources7
Beta strandi794 – 809Combined sources16
Beta strandi811 – 814Combined sources4
Helixi820 – 824Combined sources5
Beta strandi828 – 831Combined sources4
Beta strandi838 – 842Combined sources5
Beta strandi847 – 853Combined sources7
Beta strandi890 – 892Combined sources3
Beta strandi894 – 911Combined sources18
Beta strandi921 – 923Combined sources3
Beta strandi936 – 938Combined sources3
Helixi1657 – 1664Combined sources8
Beta strandi1665 – 1672Combined sources8
Beta strandi1675 – 1687Combined sources13
Beta strandi1689 – 1693Combined sources5
Helixi1694 – 1697Combined sources4
Beta strandi1702 – 1706Combined sources5
Beta strandi1709 – 1711Combined sources3
Helixi1713 – 1715Combined sources3
Beta strandi1716 – 1719Combined sources4
Beta strandi1722 – 1725Combined sources4
Beta strandi1726 – 1728Combined sources3
Beta strandi1733 – 1742Combined sources10
Helixi1749 – 1751Combined sources3
Beta strandi1752 – 1755Combined sources4
Beta strandi1763 – 1770Combined sources8
Turni1771 – 1773Combined sources3
Beta strandi1774 – 1784Combined sources11
Beta strandi1800 – 1804Combined sources5
Beta strandi1815 – 1820Combined sources6
Beta strandi1823 – 1834Combined sources12
Beta strandi1837 – 1842Combined sources6
Helixi1845 – 1853Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03306.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 201Peptidase C28Add BLAST201
Domaini1189 – 1353SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1652 – 1836Peptidase C3Add BLAST185
Domaini2096 – 2214RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi867 – 870Cell attachment site1 Publication4

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

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
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.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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. AlignAdd to basket

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 differs from that shown. Reason: Frameshift at positions 1727 and 1739.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti396S → C in CAA24361 (PubMed:6282711).Curated1
Sequence conflicti632P → L in CAA24361 (PubMed:6282711).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189791 – 28Missing in isoform Lb. CuratedAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X00429 Genomic RNA. Translation: CAA25127.1. Frameshift.
V01130 Genomic RNA. Translation: CAA24361.1.
PIRiA93508. GNNY2F.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03306.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
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.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.