SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P03305

- POLG_FMDVO

UniProt

P03305 - POLG_FMDVO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.4 Publications
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.4 Publications
Protein VP0: VP0 precursor is a component of immature procapsids By similarity.4 Publications
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity.4 Publications
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.4 Publications
Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity.4 Publications
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.4 Publications
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.4 Publications
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.4 Publications

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
Active sitei148 – 1481For leader protease activity
Active sitei163 – 1631For leader protease activity
Sitei201 – 2022Cleavage; by leader protease Reviewed prediction
Sitei286 – 2872Cleavage Reviewed prediction
Sitei504 – 5052Cleavage; by picornain 3C Reviewed prediction
Sitei724 – 7252Cleavage; by picornain 3C Reviewed prediction
Sitei935 – 9362Cleavage; by picornain 3C Reviewed prediction
Sitei953 – 9542Cleavage; by ribosomal skip Reviewed prediction
Sitei1107 – 11082Cleavage; by picornain 3C Reviewed prediction
Sitei1425 – 14262Cleavage; by picornain 3C Reviewed prediction
Sitei1578 – 15792Cleavage; by picornain 3C Reviewed prediction
Sitei1601 – 16022Cleavage; by picornain 3C Reviewed prediction
Sitei1625 – 16262Cleavage; by picornain 3C Reviewed prediction
Sitei1649 – 16502Cleavage; by picornain 3C Reviewed prediction
Active sitei1695 – 16951For picornain 3C activity Reviewed prediction
Active sitei1722 – 17221For picornain 3C activity Reviewed prediction
Active sitei1812 – 18121For picornain 3C activity Reviewed prediction
Sitei1862 – 18632Cleavage; by picornain 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1217 – 12248ATP 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 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 VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : 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 – 14801480Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1481 – 150121 Reviewed predictionAdd
BLAST
Topological domaini1502 – 2332831Cytoplasmic 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 – 23322332Genome polyproteinPRO_0000039872Add
BLAST
Chaini1 – 201201Leader proteasePRO_0000039873Add
BLAST
Chaini202 – 504303Protein VP0 Reviewed predictionPRO_0000374076Add
BLAST
Chaini202 – 28685Protein VP4 Reviewed predictionPRO_0000039876Add
BLAST
Chaini287 – 504218Protein VP2 Reviewed predictionPRO_0000039877Add
BLAST
Chaini505 – 724220Protein VP3 Reviewed predictionPRO_0000039878Add
BLAST
Chaini725 – 935211Protein VP1PRO_0000039879Add
BLAST
Chaini936 – 95318Protein 2A Reviewed predictionPRO_0000039880Add
BLAST
Chaini954 – 1107154Protein 2B Reviewed predictionPRO_0000310976Add
BLAST
Chaini1108 – 1425318Protein 2C Reviewed predictionPRO_0000039881Add
BLAST
Chaini1426 – 1578153Protein 3A Reviewed predictionPRO_0000039882Add
BLAST
Chaini1579 – 160123Protein 3B-1 Reviewed predictionPRO_0000039883Add
BLAST
Chaini1602 – 162524Protein 3B-2 Reviewed predictionPRO_0000310977Add
BLAST
Chaini1626 – 164924Protein 3B-3 Reviewed predictionPRO_0000310978Add
BLAST
Chaini1650 – 1862213Picornain 3C Reviewed predictionPRO_0000039884Add
BLAST
Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POL Reviewed predictionPRO_0000039885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by host By similarity
Disulfide bondi406 ↔ 858Interchain (between VP2 and VP1 chains)
Disulfide bondi511 – 511Interchain; in VP3 dimer
Modified residuei1581 – 15811O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1604 – 16041O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1628 – 16281O-(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.3 Publications
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.

Structurei

Secondary structure

1
2332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323
Beta strandi38 – 403
Beta strandi47 – 493
Helixi51 – 6313
Helixi66 – 683
Helixi69 – 724
Beta strandi73 – 764
Helixi79 – 9012
Helixi100 – 1078
Helixi108 – 1103
Beta strandi111 – 1133
Beta strandi115 – 1206
Beta strandi123 – 1264
Beta strandi129 – 1313
Helixi134 – 1363
Beta strandi137 – 1448
Turni145 – 1473
Beta strandi148 – 1536
Beta strandi158 – 1636
Beta strandi166 – 1694
Helixi174 – 1763
Beta strandi177 – 1826
Turni195 – 1973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP03305.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28Add
BLAST
Domaini1189 – 1353165SF3 helicaseAdd
BLAST
Domaini1652 – 1836185Peptidase C3Add
BLAST
Domaini2096 – 2214119RdRp catalyticAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi869 – 8713Cell 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: 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

MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN     50
CWLNAILQLF RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP 100
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQRKL 200
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT 350
HLFDWVTSDS FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN 400
QFNGGCLLVA MVPELYSIQK RELYQLTLFP HQFINPRTNM TAHITVPFVG 450
VNRYDQYKVH KPWTLVVMVV APLTVNTEGA PQIKVYANIA PTNVHVAGEF 500
PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ LPGRFTNLLD 550
VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ 600
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE 650
WDTGLNSKFT FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG 700
DALVVLASAG KDFELRLPVD ARAETTSAGE SADPVTTTVE NYGGETQIQR 750
RQHTDVSFIM DRFVKVTPQN QINILDLMQI PSHTLVGALL RASTYYFSDL 800
EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA LPYTAPHRVL 850
ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL 900
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES 950
NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV 1000
KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI 1050
LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP VLLAGLVKVA SSFFRSTPED 1100
LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM 1150
TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA 1200
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP 1250
DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK 1300
GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINS 1350
KLDIIKALED THANPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV 1400
YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF 1450
FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM 1500
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR 1550
ERTLPGQKAC DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ 1600
EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV KAKNLIVTES 1650
GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK 1700
YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK 1750
HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL 1800
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK 1850
MKAHIDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA 1900
LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV 1950
LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT 2000
VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT RIVDVLPVEH 2050
ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD 2100
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK 2150
RITVGGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD 2200
DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGH SITDVTFLKR 2250
HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE 2300
YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA 2332
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.

Show »
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. VSP_018982Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X00871 Genomic RNA. Translation: CAA25416.1 .
J02185 Genomic RNA. Translation: AAA42635.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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: July 9, 2014
This is version 154 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

Similar proteinsi