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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: 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). Increases translation driven by the viral internal ribosome entry site (IRES) (PubMed:25268112).By similarity1 Publication
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 sitei1690For picornain 3C activity; Proton donor/acceptorSequence analysisBy similarity1
Active sitei1728For picornain 3C activityBy similarity1
Active sitei1807For picornain 3C activitySequence analysisBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1212 – 1219ATPPROSITE-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- 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, 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

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 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
  • UP000012670 Componenti: Genome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1475CytoplasmicSequence analysisAdd BLAST1475
Intramembranei1476 – 1496Sequence analysisAdd BLAST21
Topological domaini1497 – 2327CytoplasmicSequence analysisAdd BLAST831

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004225171 – 2327Genome polyproteinBy similarityAdd BLAST2327
ChainiPRO_50000648431 – 201Leader proteaseBy similarityAdd BLAST201
ChainiPRO_0000422518202 – 504Protein VP0Sequence analysisAdd BLAST303
ChainiPRO_5000064844202 – 286Protein VP4Sequence analysisAdd BLAST85
ChainiPRO_5000064845287 – 504Protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039886505 – 723Protein VP3Sequence analysisAdd BLAST219
ChainiPRO_0000039887724 – 930Protein VP1By similarityAdd BLAST207
ChainiPRO_0000039888931 – 948Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000310979949 – 1102Protein 2BSequence analysisAdd BLAST154
ChainiPRO_50000648501103 – 1420Protein 2CSequence analysisAdd BLAST318
ChainiPRO_50000648511421 – 1573Protein 3ASequence analysisAdd BLAST153
ChainiPRO_50000648521574 – 1596Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_50000648531597 – 1620Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_50000648541621 – 1644Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00000398891645 – 1857Picornain 3CSequence analysisAdd BLAST213
ChainiPRO_00000398901858 – 2327RNA-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 residuei1576O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1599O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1623O-(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
Sitei723 – 724Cleavage; by picornain 3CSequence analysis2
Sitei930 – 931Cleavage; by picornain 3CSequence analysis2
Sitei948 – 949Cleavage; by ribosomal skipSequence analysis2
Sitei1102 – 1103Cleavage; by picornain 3CSequence analysis2
Sitei1420 – 1421Cleavage; by picornain 3CSequence analysis2
Sitei1573 – 1574Cleavage; by picornain 3CSequence analysis2
Sitei1596 – 1597Cleavage; by picornain 3CSequence analysis2
Sitei1620 – 1621Cleavage; by picornain 3CSequence analysis2
Sitei1644 – 1645Cleavage; by picornain 3CSequence analysis2
Sitei1857 – 1858Cleavage; by picornain 3CSequence analysis2

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

12327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1859 – 1870Combined sources12
Beta strandi1878 – 1880Combined sources3
Helixi1882 – 1887Combined sources6
Beta strandi1890 – 1893Combined sources4
Helixi1909 – 1913Combined sources5
Turni1914 – 1916Combined sources3
Helixi1925 – 1946Combined sources22
Helixi1955 – 1960Combined sources6
Beta strandi1963 – 1965Combined sources3
Beta strandi1970 – 1972Combined sources3
Turni1976 – 1982Combined sources7
Helixi1985 – 1988Combined sources4
Turni1991 – 1994Combined sources4
Helixi1998 – 2008Combined sources11
Beta strandi2016 – 2020Combined sources5
Beta strandi2024 – 2026Combined sources3
Helixi2027 – 2031Combined sources5
Beta strandi2037 – 2040Combined sources4
Helixi2043 – 2062Combined sources20
Turni2066 – 2069Combined sources4
Helixi2076 – 2087Combined sources12
Beta strandi2090 – 2100Combined sources11
Turni2101 – 2104Combined sources4
Helixi2107 – 2117Combined sources11
Helixi2120 – 2122Combined sources3
Helixi2127 – 2133Combined sources7
Turni2134 – 2136Combined sources3
Beta strandi2137 – 2152Combined sources16
Beta strandi2157 – 2159Combined sources3
Helixi2160 – 2179Combined sources20
Beta strandi2180 – 2182Combined sources3
Helixi2185 – 2187Combined sources3
Beta strandi2189 – 2193Combined sources5
Beta strandi2196 – 2203Combined sources8
Turni2207 – 2210Combined sources4
Helixi2211 – 2215Combined sources5
Turni2216 – 2218Combined sources3
Beta strandi2221 – 2223Combined sources3
Beta strandi2228 – 2230Combined sources3
Helixi2237 – 2239Combined sources3
Beta strandi2245 – 2249Combined sources5
Turni2251 – 2253Combined sources3
Beta strandi2256 – 2259Combined sources4
Helixi2262 – 2269Combined sources8
Beta strandi2271 – 2273Combined sources3
Helixi2277 – 2288Combined sources12
Helixi2289 – 2291Combined sources3
Helixi2293 – 2300Combined sources8
Helixi2301 – 2303Combined sources3
Helixi2312 – 2323Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QGCelectron microscopy30.001724-930[»]
2287-504[»]
3505-723[»]
5859-879[»]
4WYLX-ray2.00A1858-2327[»]
4WYWX-ray1.80A1858-2327[»]
4WZMX-ray2.52A1858-2327[»]
4WZQX-ray2.80A1858-2327[»]
4X2BX-ray2.94A1858-2327[»]
5JXSX-ray2.80A1858-2327[»]
ProteinModelPortaliP03311.
SMRiP03311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03311.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 201Peptidase C28Add BLAST201
Domaini1184 – 1348SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1647 – 1831Peptidase C3Add BLAST185
Domaini2091 – 2209RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi864 – 866Cell attachment siteBy similarity3

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. 2 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.
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

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)DescriptionActionsGraphical viewLength
Sequence conflicti789 – 792LRAA → SRH no nucleotide entry (PubMed:6311686).Curated4
Sequence conflicti947P → L no nucleotide entry (PubMed:6311686).Curated1
Sequence conflicti1008Missing no nucleotide entry (PubMed:6311686).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1804A → V.1
Natural varianti1916K → R.1
Natural varianti1958A → V.1
Natural varianti1975G → S.1
Natural varianti2000V → A.1
Natural varianti2080W → R.1
Natural varianti2083F → S.1
Natural varianti2087F → L.1
Natural varianti2140H → Y.1
Natural varianti2163I → V.1
Natural varianti2261A → T.1
Natural varianti2299L → F.1
Natural varianti2326D → R.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0465321 – 28Missing in isoform Lb. CuratedAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133357 Genomic RNA. Translation: CAB60267.1.
M11027 Genomic RNA. Translation: AAA42654.1.
PIRiJC1328.
JC1330.
JC1331.
JC1334.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QGCelectron microscopy30.001724-930[»]
2287-504[»]
3505-723[»]
5859-879[»]
4WYLX-ray2.00A1858-2327[»]
4WYWX-ray1.80A1858-2327[»]
4WZMX-ray2.52A1858-2327[»]
4WZQX-ray2.80A1858-2327[»]
4X2BX-ray2.94A1858-2327[»]
5JXSX-ray2.80A1858-2327[»]
ProteinModelPortaliP03311.
SMRiP03311.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03311.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 2 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.
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_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: November 30, 2016
This is version 148 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.