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P03310

- POLG_FMDVI

UniProt

P03310 - POLG_FMDVI

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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: 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 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.
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.
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.
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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511For leader protease activity By similarity
Active sitei148 – 1481For leader protease activity By similarity
Active sitei163 – 1631For leader protease activity By similarity
Sitei201 – 2022Cleavage; by leader protease Reviewed prediction
Sitei286 – 2872Cleavage Reviewed prediction
Sitei504 – 5052Cleavage; by picornain 3C Reviewed prediction
Sitei723 – 7242Cleavage; by picornain 3C Reviewed prediction
Sitei931 – 9322Cleavage; by picornain 3C Reviewed prediction
Sitei949 – 9502Cleavage; by ribosomal skip Reviewed prediction
Sitei1103 – 11042Cleavage; by picornain 3C Reviewed prediction
Sitei1421 – 14222Cleavage; by picornain 3C Reviewed prediction
Sitei1574 – 15752Cleavage; by picornain 3C Reviewed prediction
Sitei1597 – 15982Cleavage; by picornain 3C Reviewed prediction
Sitei1621 – 16222Cleavage; by picornain 3C Reviewed prediction
Sitei1645 – 16462Cleavage; by picornain 3C Reviewed prediction
Active sitei1691 – 16911For picornain 3C activity Reviewed prediction
Active sitei1718 – 17181For picornain 3C activity Reviewed prediction
Active sitei1808 – 18081For picornain 3C activity Reviewed prediction
Sitei1858 – 18592Cleavage; by picornain 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1213 – 12208ATP Reviewed prediction

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 -/Brazil/C3Indaial/1971 serotype C) (FMDV)
Taxonomic identifieri12117 [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]
ProteomesiUP000012668: Genome

Subcellular locationi

Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B-1 : Virion Reviewed prediction
Chain Protein 3B-2 : Virion Reviewed prediction
Chain Protein 3B-3 : Virion Reviewed prediction
Chain Picornain 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14761476Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1477 – 149721 Reviewed predictionAdd
BLAST
Topological domaini1498 – 2328831Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  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 – 23282328Genome polyprotein By similarityPRO_0000422504Add
BLAST
Chaini1 – 201201Leader protease By similarityPRO_0000422505Add
BLAST
Chaini202 – 504303Protein VP0 Reviewed predictionPRO_0000422506Add
BLAST
Chaini202 – 28685Protein VP4 Reviewed predictionPRO_0000422507Add
BLAST
Chaini287 – 504218Protein VP2 Reviewed predictionPRO_0000422508Add
BLAST
Chaini505 – 723219Protein VP3 Reviewed predictionPRO_0000039869Add
BLAST
Chaini724 – 931208Protein VP1 By similarityPRO_0000039870Add
BLAST
Chaini932 – 94918Protein 2A Reviewed predictionPRO_0000039871Add
BLAST
Chaini950 – 1103154Protein 2B Reviewed predictionPRO_0000422509Add
BLAST
Chaini1104 – 1421318Protein 2C Reviewed predictionPRO_0000422510Add
BLAST
Chaini1422 – 1574153Protein 3A Reviewed predictionPRO_0000422511Add
BLAST
Chaini1575 – 159723Protein 3B-1 Reviewed predictionPRO_0000422512Add
BLAST
Chaini1598 – 162124Protein 3B-2 Reviewed predictionPRO_0000422513Add
BLAST
Chaini1622 – 164524Protein 3B-3 Reviewed predictionPRO_0000422514Add
BLAST
Chaini1646 – 1858213Picornain 3C Reviewed predictionPRO_0000422515Add
BLAST
Chaini1859 – 2328470RNA-directed RNA polymerase 3D-POL Reviewed predictionPRO_0000422516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by host By similarity
Disulfide bondi511 – 511Interchain; in VP3 dimer By similarity
Modified residuei1577 – 15771O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1600 – 16001O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1624 – 16241O-(5'-phospho-RNA)-tyrosine By 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.
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.

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

3D structure databases

ProteinModelPortaliP03310.
SMRiP03310. Positions 29-201, 216-931, 1652-1852, 1859-2328.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28Add
BLAST
Domaini1185 – 1349165SF3 helicaseAdd
BLAST
Domaini1648 – 1832185Peptidase C3Add
BLAST
Domaini2092 – 2210119RdRp catalyticAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi865 – 8673Cell attachment site By similarity

Sequence similaritiesi

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: 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

MNTTDCFIAL VHAIREIKTH FFSRYTGRME FTLHNGEKKI FYSRPNNHDN     50
CWLNTILQLF RYVDEPFFDW VYNSPENLTL SAIEQLEKLT GLELREGGPP 100
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG GWKANVQRKL 200
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
LTTRNGHTTS TTQSSVGVTY GYATTEDSTS GPNTSGLETR VHQAERFFKM 350
TLFEWVPSQS FGHMHKVVLP SEPKGVYGGL VKSYAYMRNG WDVEVTAVGN 400
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG 450
VNRYDQYNQH KPWTLVVMVV APLTVNTSGA QQIKVYANIA PTNVHVAGEL 500
PSKEGIFPVA CADGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD 550
VAEACPTLLT FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 600
YTQYAGTINL HFMFTGPTDA KARYMVAYVP PGMEAPDNPE EAAHCIHAEW 650
DTGLNSKFTF SIPYISAADY AYTASSEAET TSVQGWVCVY QITHGKADAD 700
ALVVSASAGK DFELRLPVDA RQQTTTTGES ADPVTTTVEN YGGETQTQRR 750
HHTDVAFVLD RFVKVQVSGN QHTLDVMQVH KDSIVGALLR AATYYFSDLE 800
IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL PYTAPHRVLA 850
TAYTGTTAYT TGVRRGDLAH LAAAHARHLP TSFNFGAVKA ETITELLVRM 900
KRAELYCPRP VLPVQPAGDR HKQPLIAPAK QLLNFDLLKL AGDVESNPGP 950
FFFSDVRSNF SKLVETINQM QEDMSTKHGP DFNRLVSAFE ELATGVKAIR 1000
TGLDEAKPWY KLIKLLSRLS CMAAVAARSK DPVLVAIMLA DTGLEILDST 1050
FVVKKISDSL SSLFHVPAPV FSFGAPILLA GLVKVASSFF RSTPEDLERA 1100
EKQLKARDIN DIFAILKNGE WLVKLILAIR DWIKAWIASE EKFVTMTDLV 1150
PGILEKQRDL NDPSKYKEAK EWLDNARQAC LKNGNTHIAN LCKVVAPAPS 1200
KSRPEPVVVC LRGKSGQGKS FLANVLAQAI STHFTGRTDS VWYCPPDPDH 1250
FDGYNQQTVV VMDDLGQNPD GKDFKYFAQM VSTTGFIPPM ASLEDKGKPF 1300
NSKVIIATTN LYSGFTPRTM VCPDALNRRF HFDIDVSAKD GYKINNKLDI 1350
IKALEDTHTN PVAMFQYDCA LLNGMAVEMK RMQQDMFKPQ PPLQNVYQLV 1400
QEVIERVELH EKVSSHPIFK QISIPSQKSV LYFLIEKGQH EAAIEFFEGM 1450
VHDSIKEELR PLIQQTSFVK RAFKRLKENF EIVALCLTLL ANIVIMIRET 1500
RKRQQMVDDA VNEYIEKANI TTDDKTLDEA EKNPLETSGA STVGFRERTL 1550
PGHKARDDVN SEPAQPVEEQ PQAEGPYAGP LERQKPLKVR AKLPQQEGPY 1600
AGPMERQKPL KVKAKAPVVK EGPYEGPVKK PVALKVKAKN LIVTESGAPP 1650
TDLQKMVMGN TKPVELILDG KTVAICCATG VFGTAYLVPR HLFAEKYDKI 1700
MLDGRAMTDS DYRVFEFEIK VKGQDMLSDA ALMVLHRGNR VRDITKHFRD 1750
TARMKKGTPV VGVINNADVG RLIFSGEALT YKDIVVCMDG DTMPGLFAYR 1800
AATKAGYCGG AVLAKDGADT FIVGTHSAGG NGVGYCSCVS RSMLLKMKAH 1850
IDPEPHHEGL IVDTRDVEER VHVMRKTKLA PTVAHGVFNP DFGPAALSNR 1900
DPRLNEGVVL DEVIFSKHKG DTKMSEEDKA LFRRCAADYA SRLHSVLGTA 1950
NAPLSIYEAI KGVDGLDAME PDTAPGLPWA LQGKRRGALI DFENGTVGPE 2000
VEAALKLMEK REYKFACQTF LKDEIRPMEK VRAGKTRIVD VLPVEHILYT 2050
RMMIGRFCAQ MHSNNGPQIG SAVGCNPDVD WQRFGTHFAQ YRNVWDVDYS 2100
AFDANHCSDA MNIMFEEVFR TEFGFHPNAE WILKTLVNTE HAYENKRITV 2150
EGGMPSGCSA TSIINTILNN IYVLYALRRH YEGVELDTYT MISYGDDIVV 2200
ASDYDLDFEA LKPHFKSIGQ TITPADKSDK GFVLGHSITD VTFLKRHFHM 2250
DYGTGFYKPV MASKTLEAIL SFARRGTIQE KLISVAGLAV HSGPDEYRRL 2300
FEPFQGLFEI PSYRSLYLRW VNAVCGDA 2328
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti330 – 3301S → A.
Natural varianti376 – 3761V → A.
Natural varianti420 – 4201D → E.
Natural varianti458 – 4581N → K.
Natural varianti515 – 5151Y → F.
Natural varianti560 – 5601T → M.
Natural varianti638 – 6381N → S.
Natural varianti677 – 6771E → D.
Natural varianti722 – 7221Q → L.
Natural varianti747 – 7471T → I.
Natural varianti766 – 7661Q → H.
Natural varianti805 – 8051H → Q.
Natural varianti825 – 8251T → A.
Natural varianti852 – 8521A → T.
Natural varianti861 – 8633TGV → ASA.
Natural varianti917 – 9171A → T.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb. VSP_046531Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AY593806 Genomic RNA. Translation: AAT01749.1 .
M90376 Genomic RNA. Translation: AAA91492.1 .
J02184 Genomic RNA. Translation: AAA42618.1 .
PIRi A03912.

3D structure databases

ProteinModelPortali P03310.
SMRi P03310. Positions 29-201, 216-931, 1652-1852, 1859-2328.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Evolution of the capsid protein genes of foot-and-mouth disease virus: antigenic variation without accumulation of amino acid substitutions over six decades."
    Martinez M.A., Dopazo J., Hernandez J., Mateu M.G., Sobrino F., Domingo E., Knowles N.J.
    J. Virol. 66:3557-3565(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 202-933.
  3. "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] OF 714-947.

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: July 9, 2014
This is version 89 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

External Data

Dasty 3

Similar proteinsi