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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Brazil/C3Indaial/1971 serotype C) (FMDV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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 sitei1691For picornain 3C activity; Proton donor/acceptorSequence analysisBy similarity1
Active sitei1729For picornain 3C activityBy similarity1
Active sitei1808For picornain 3C activitySequence analysisBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1213 – 1220ATPPROSITE-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

Protein family/group databases

MEROPSiC28.001.

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 -/Brazil/C3Indaial/1971 serotype C) (FMDV)
Taxonomic identifieri12117 [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
  • UP000012668 Componenti: Genome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1476CytoplasmicSequence analysisAdd BLAST1476
Intramembranei1477 – 1497Sequence analysisAdd BLAST21
Topological domaini1498 – 2328CytoplasmicSequence 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_00004225041 – 2328Genome polyproteinBy similarityAdd BLAST2328
ChainiPRO_00004225051 – 201Leader proteaseBy similarityAdd BLAST201
ChainiPRO_0000422506202 – 504Protein VP0Sequence analysisAdd BLAST303
ChainiPRO_0000422507202 – 286Protein VP4Sequence analysisAdd BLAST85
ChainiPRO_0000422508287 – 504Protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039869505 – 723Protein VP3Sequence analysisAdd BLAST219
ChainiPRO_0000039870724 – 931Protein VP1By similarityAdd BLAST208
ChainiPRO_0000039871932 – 949Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000422509950 – 1103Protein 2BSequence analysisAdd BLAST154
ChainiPRO_00004225101104 – 1421Protein 2CSequence analysisAdd BLAST318
ChainiPRO_00004225111422 – 1574Protein 3ASequence analysisAdd BLAST153
ChainiPRO_00004225121575 – 1597Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_00004225131598 – 1621Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_00004225141622 – 1645Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00004225151646 – 1858Picornain 3CSequence analysisAdd BLAST213
ChainiPRO_00004225161859 – 2328RNA-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 residuei1577O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1600O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1624O-(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
Sitei931 – 932Cleavage; by picornain 3CSequence analysis2
Sitei949 – 950Cleavage; by ribosomal skipSequence analysis2
Sitei1103 – 1104Cleavage; by picornain 3CSequence analysis2
Sitei1421 – 1422Cleavage; by picornain 3CSequence analysis2
Sitei1574 – 1575Cleavage; by picornain 3CSequence analysis2
Sitei1597 – 1598Cleavage; by picornain 3CSequence analysis2
Sitei1621 – 1622Cleavage; by picornain 3CSequence analysis2
Sitei1645 – 1646Cleavage; by picornain 3CSequence analysis2
Sitei1858 – 1859Cleavage; by picornain 3CSequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP03310.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP03310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 201Peptidase C28Add BLAST201
Domaini1185 – 1349SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1648 – 1832Peptidase C3Add BLAST185
Domaini2092 – 2210RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi865 – 867Cell 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: P03310-1) [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 VHAIREIKTH FFSRYTGRME FTLHNGEKKI FYSRPNNHDN
60 70 80 90 100
CWLNTILQLF RYVDEPFFDW VYNSPENLTL SAIEQLEKLT GLELREGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV
160 170 180 190 200
FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG GWKANVQRKL
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 GYATTEDSTS GPNTSGLETR VHQAERFFKM
360 370 380 390 400
TLFEWVPSQS FGHMHKVVLP SEPKGVYGGL VKSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG
460 470 480 490 500
VNRYDQYNQH KPWTLVVMVV APLTVNTSGA QQIKVYANIA PTNVHVAGEL
510 520 530 540 550
PSKEGIFPVA CADGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD
560 570 580 590 600
VAEACPTLLT FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
610 620 630 640 650
YTQYAGTINL HFMFTGPTDA KARYMVAYVP PGMEAPDNPE EAAHCIHAEW
660 670 680 690 700
DTGLNSKFTF SIPYISAADY AYTASSEAET TSVQGWVCVY QITHGKADAD
710 720 730 740 750
ALVVSASAGK DFELRLPVDA RQQTTTTGES ADPVTTTVEN YGGETQTQRR
760 770 780 790 800
HHTDVAFVLD RFVKVQVSGN QHTLDVMQVH KDSIVGALLR AATYYFSDLE
810 820 830 840 850
IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL PYTAPHRVLA
860 870 880 890 900
TAYTGTTAYT TGVRRGDLAH LAAAHARHLP TSFNFGAVKA ETITELLVRM
910 920 930 940 950
KRAELYCPRP VLPVQPAGDR HKQPLIAPAK QLLNFDLLKL AGDVESNPGP
960 970 980 990 1000
FFFSDVRSNF SKLVETINQM QEDMSTKHGP DFNRLVSAFE ELATGVKAIR
1010 1020 1030 1040 1050
TGLDEAKPWY KLIKLLSRLS CMAAVAARSK DPVLVAIMLA DTGLEILDST
1060 1070 1080 1090 1100
FVVKKISDSL SSLFHVPAPV FSFGAPILLA GLVKVASSFF RSTPEDLERA
1110 1120 1130 1140 1150
EKQLKARDIN DIFAILKNGE WLVKLILAIR DWIKAWIASE EKFVTMTDLV
1160 1170 1180 1190 1200
PGILEKQRDL NDPSKYKEAK EWLDNARQAC LKNGNTHIAN LCKVVAPAPS
1210 1220 1230 1240 1250
KSRPEPVVVC LRGKSGQGKS FLANVLAQAI STHFTGRTDS VWYCPPDPDH
1260 1270 1280 1290 1300
FDGYNQQTVV VMDDLGQNPD GKDFKYFAQM VSTTGFIPPM ASLEDKGKPF
1310 1320 1330 1340 1350
NSKVIIATTN LYSGFTPRTM VCPDALNRRF HFDIDVSAKD GYKINNKLDI
1360 1370 1380 1390 1400
IKALEDTHTN PVAMFQYDCA LLNGMAVEMK RMQQDMFKPQ PPLQNVYQLV
1410 1420 1430 1440 1450
QEVIERVELH EKVSSHPIFK QISIPSQKSV LYFLIEKGQH EAAIEFFEGM
1460 1470 1480 1490 1500
VHDSIKEELR PLIQQTSFVK RAFKRLKENF EIVALCLTLL ANIVIMIRET
1510 1520 1530 1540 1550
RKRQQMVDDA VNEYIEKANI TTDDKTLDEA EKNPLETSGA STVGFRERTL
1560 1570 1580 1590 1600
PGHKARDDVN SEPAQPVEEQ PQAEGPYAGP LERQKPLKVR AKLPQQEGPY
1610 1620 1630 1640 1650
AGPMERQKPL KVKAKAPVVK EGPYEGPVKK PVALKVKAKN LIVTESGAPP
1660 1670 1680 1690 1700
TDLQKMVMGN TKPVELILDG KTVAICCATG VFGTAYLVPR HLFAEKYDKI
1710 1720 1730 1740 1750
MLDGRAMTDS DYRVFEFEIK VKGQDMLSDA ALMVLHRGNR VRDITKHFRD
1760 1770 1780 1790 1800
TARMKKGTPV VGVINNADVG RLIFSGEALT YKDIVVCMDG DTMPGLFAYR
1810 1820 1830 1840 1850
AATKAGYCGG AVLAKDGADT FIVGTHSAGG NGVGYCSCVS RSMLLKMKAH
1860 1870 1880 1890 1900
IDPEPHHEGL IVDTRDVEER VHVMRKTKLA PTVAHGVFNP DFGPAALSNR
1910 1920 1930 1940 1950
DPRLNEGVVL DEVIFSKHKG DTKMSEEDKA LFRRCAADYA SRLHSVLGTA
1960 1970 1980 1990 2000
NAPLSIYEAI KGVDGLDAME PDTAPGLPWA LQGKRRGALI DFENGTVGPE
2010 2020 2030 2040 2050
VEAALKLMEK REYKFACQTF LKDEIRPMEK VRAGKTRIVD VLPVEHILYT
2060 2070 2080 2090 2100
RMMIGRFCAQ MHSNNGPQIG SAVGCNPDVD WQRFGTHFAQ YRNVWDVDYS
2110 2120 2130 2140 2150
AFDANHCSDA MNIMFEEVFR TEFGFHPNAE WILKTLVNTE HAYENKRITV
2160 2170 2180 2190 2200
EGGMPSGCSA TSIINTILNN IYVLYALRRH YEGVELDTYT MISYGDDIVV
2210 2220 2230 2240 2250
ASDYDLDFEA LKPHFKSIGQ TITPADKSDK GFVLGHSITD VTFLKRHFHM
2260 2270 2280 2290 2300
DYGTGFYKPV MASKTLEAIL SFARRGTIQE KLISVAGLAV HSGPDEYRRL
2310 2320
FEPFQGLFEI PSYRSLYLRW VNAVCGDA
Length:2,328
Mass (Da):258,282
Last modified:May 29, 2013 - v2
Checksum:iB2D0CE9A4BA94622
GO
Isoform Lb (identifier: P03310-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,300
Mass (Da):254,971
Checksum:i5D457B8195EFF8C8
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti330S → A.1
Natural varianti376V → A.1
Natural varianti420D → E.1
Natural varianti458N → K.1
Natural varianti515Y → F.1
Natural varianti560T → M.1
Natural varianti638N → S.1
Natural varianti677E → D.1
Natural varianti722Q → L.1
Natural varianti747T → I.1
Natural varianti766Q → H.1
Natural varianti805H → Q.1
Natural varianti825T → A.1
Natural varianti852A → T.1
Natural varianti861 – 863TGV → ASA.3
Natural varianti917A → T.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0465311 – 28Missing in isoform Lb. CuratedAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY593806 Genomic RNA. Translation: AAT01749.1.
M90376 Genomic RNA. Translation: AAA91492.1.
J02184 Genomic RNA. Translation: AAA42618.1.
PIRiA03912.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY593806 Genomic RNA. Translation: AAT01749.1.
M90376 Genomic RNA. Translation: AAA91492.1.
J02184 Genomic RNA. Translation: AAA42618.1.
PIRiA03912.

3D structure databases

ProteinModelPortaliP03310.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC28.001.

Proteomic databases

PRIDEiP03310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_FMDVI
AccessioniPrimary (citable) accession number: P03310
Secondary accession number(s): Q65066, Q6PMY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 29, 2013
Last modified: November 30, 2016
This is version 101 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

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.