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P03307

- POLG_FMDV5

UniProt

P03307 - POLG_FMDV5

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Protein
Genome polyprotein
Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Germany/A5Westerwald/1951 serotype A) (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 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
Sitei725 – 7262Cleavage; 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. RNA binding Source: UniProtKB-KW
  3. RNA helicase activity Source: InterPro
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. cysteine-type endopeptidase activity Source: InterPro
  6. ion channel activity Source: UniProtKB-KW
  7. structural molecule activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB
  4. modulation by virus of host chromatin organization Source: UniProtKB-KW
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. protein oligomerization 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 RNA genome replication Source: InterPro
  11. viral protein processing 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 -/Germany/A5Westerwald/1951 serotype A) (FMDV)
Taxonomic identifieri12113 [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]
ProteomesiUP000012669: 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 – 14801480Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1481 – 150121 Reviewed prediction
Add
BLAST
Topological domaini1502 – 2332831Cytoplasmic Reviewed prediction
Add
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 – 23312331Genome polyprotein By similarity
PRO_0000422477Add
BLAST
Chaini1 – 201201Leader protease By similarity
PRO_0000422478Add
BLAST
Chaini202 – 504303Protein VP0 Reviewed prediction
PRO_0000422479Add
BLAST
Chaini202 – 28685Protein VP4 Reviewed prediction
PRO_0000422480Add
BLAST
Chaini287 – 504218Protein VP2 Reviewed prediction
PRO_0000422481Add
BLAST
Chaini505 – 725221Protein VP3 Reviewed prediction
PRO_0000039830Add
BLAST
Chaini726 – 935210Protein VP1 Reviewed prediction
PRO_0000039831Add
BLAST
Chaini936 – 95318Protein 2A Reviewed prediction
PRO_0000039832Add
BLAST
Chaini954 – 1107154Protein 2B Reviewed prediction
PRO_0000422482Add
BLAST
Chaini1108 – 1425318Protein 2C Reviewed prediction
PRO_0000422483Add
BLAST
Chaini1426 – 1578153Protein 3A Reviewed prediction
PRO_0000422484Add
BLAST
Chaini1579 – 160123Protein 3B-1 Reviewed prediction
PRO_0000422485Add
BLAST
Chaini1602 – 162524Protein 3B-2 Reviewed prediction
PRO_0000422486Add
BLAST
Chaini1626 – 164924Protein 3B-3 Reviewed prediction
PRO_0000422487Add
BLAST
Chaini1650 – 1862213Picornain 3C Reviewed prediction
PRO_0000422488Add
BLAST
Chaini1863 – 2332470RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000422489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by host By similarity
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.
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

ProteinModelPortaliP03307.
SMRiP03307. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28
Add
BLAST
Domaini1189 – 1353165SF3 helicase
Add
BLAST
Domaini1652 – 1836185Peptidase C3
Add
BLAST
Domaini2096 – 2214119RdRp catalytic
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi868 – 8703Cell 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: P03307-1) [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

MHTTDCFIAL VHAIREIRAL FLPRTTGKME LTLHNGEKKT FYSRPNNHDN     50
CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAINQLEELT GLELHEGGPP 100
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV 150
FACVTSNGWY AIDDEEFYPW TPDPSDVLVF VPYDQEPLNG DWKAMVQRKL 200
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI 300
LTTRNGHTIS TTQSSVGVTY GYSTGEDHVA GPNTSGLETR VVQAERFFKK 350
FLFDWTTDKP FGHLEKLELP ADHHGVFGHL VESYAYMRNG WDVEVSAVGN 400
QFNGGCLLVA MVPEWKEFEQ REKYQLTLFP HQFISPRTNM TAHITVPYLG 450
VNRYDQYKKH KPWTLVVMVV SPLTVSDTAA AQIKVYANIA PTYVHVAGEL 500
PSKEGIFPVA CSDGYGGLVT TDPKTADPAY GKVYNPPRTN YPGRFTNLLD 550
VAEACPTFLC FDDGKPYVVT RTDDTRLLAK FDVSLAAKHM SNTYLSGIAQ 600
YYAQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVEVPPDT PERAAHCIHA 650
EWDTGLNSKF TFSIPYVSAA DYAYTASDTA ETTNVQGWVC IYQITHGKAE 700
NDTLVVSASA GKDFELRLPI DPRQQTTAVG ESADPVTTTV ENYGGETQTQ 750
RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ THQHGLVGAL LRAATYYFSD 800
LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL ALPYTAPHRV 850
LATVYNGTNK YSTGGPRRGD TGSPAARAAK QLPASFNYGA IRAVTIHELL 900
VRMKRAELYC PRPLLAIEVS SQDRHKQKII APARQLLNFD LLKLAGDVES 950
NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAAGV 1000
KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI 1050
LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP ILLAGLVKVA SSFFRSTPED 1100
LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM 1150
TDLVPGILEK QHDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA 1200
PAPSKPRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RTDSVWYCPP 1250
DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK 1300
GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINN 1350
KLDITKALED THTNPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV 1400
YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIK KGQHEAAIEF 1450
FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM 1500
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKNPLE TSGASTVGFR 1550
ERTLPGQKAR DDVNSEPAQP AEEQPQAEGP YAGPLERQRP LKVRAKLPQQ 1600
EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV RAKNLIVTES 1650
GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK 1700
YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK 1750
HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL 1800
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK 1850
MKAHIDPEPH HEGLIVDTRD AEERVHVMRK TKLAPTVAHG VFNPEFGPAA 1900
LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV 1950
LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT 2000
VGPEVEAALK LMEKREYKFV CQTFLKDEIR PMEKVRAGKT RIVDVLPVEH 2050
ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD 2100
VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK 2150
RHTVEGGMPS 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):259,336
Last modified:May 29, 2013 - v2
Checksum:iCD295048EBAA0EFC
GO
Isoform Lb (identifier: P03307-2) [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):256,143
Checksum:i1EEAD5368F43ABE1
GO

Sequence cautioni

The sequence CAA24365.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti746 – 7461E → D.
Natural varianti753 – 7553HHT → YYM.
Natural varianti871 – 8711T → M.
Natural varianti874 – 8741P → A.
Natural varianti894 – 8941V → I.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb.
VSP_046529Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY593781 Genomic RNA. Translation: AAT01724.1.
V01135 Genomic RNA. Translation: CAA24365.1. Different initiation.
V01135 Genomic RNA. Translation: CAA24366.1. Sequence problems.
PIRiA03909.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY593781 Genomic RNA. Translation: AAT01724.1 .
V01135 Genomic RNA. Translation: CAA24365.1 . Different initiation.
V01135 Genomic RNA. Translation: CAA24366.1 . Sequence problems.
PIRi A03909.

3D structure databases

ProteinModelPortali P03307.
SMRi P03307. Positions 29-201, 216-286, 298-933, 1656-1856, 1863-2332.
ModBasei 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. "The molecular basis of the antigenic variation of foot-and-mouth disease virus."
    Beck E., Feil G., Strohmaier K.
    EMBO J. 2:555-559(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_FMDV5
AccessioniPrimary (citable) accession number: P03307
Secondary accession number(s): Q6PN05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 29, 2013
Last modified: July 9, 2014
This is version 91 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