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P15072

- POLG_FMDVT

UniProt

P15072 - POLG_FMDVT

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Protein
Genome polyprotein
Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (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 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.
Protein VP0: VP0 precursor is a component of immature procapsids 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
Sitei930 – 9312Cleavage; by picornain 3C Reviewed prediction
Sitei948 – 9492Cleavage; by ribosomal skip Reviewed prediction
Sitei1102 – 11032Cleavage; by picornain 3C Reviewed prediction
Sitei1420 – 14212Cleavage; by picornain 3C Reviewed prediction
Sitei1573 – 15742Cleavage; by picornain 3C Reviewed prediction
Sitei1596 – 15972Cleavage; by picornain 3C Reviewed prediction
Sitei1620 – 16212Cleavage; by picornain 3C Reviewed prediction
Sitei1644 – 16452Cleavage; by picornain 3C Reviewed prediction
Active sitei1690 – 16901For picornain 3C activity Reviewed prediction
Active sitei1717 – 17171For picornain 3C activity Reviewed prediction
Active sitei1807 – 18071For picornain 3C activity Reviewed prediction
Sitei1857 – 18582Cleavage; by picornain 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1212 – 12198ATP 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

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 8 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
OrganismiFoot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV)
Taxonomic identifieri12121 [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]
ProteomesiUP000012671: 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 – 14751475Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1476 – 149621 Reviewed prediction
Add
BLAST
Topological domaini1497 – 2327831Cytoplasmic 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 – 23272327Genome polyprotein By similarity
PRO_0000039891Add
BLAST
Chaini1 – 201201Leader protease
PRO_0000039892Add
BLAST
Chaini202 – 504303Protein VP0 Reviewed prediction
PRO_0000374077Add
BLAST
Chaini202 – 28685Protein VP4 Reviewed prediction
PRO_0000039895Add
BLAST
Chaini287 – 504218Protein VP2 Reviewed prediction
PRO_0000039896Add
BLAST
Chaini505 – 723219Protein VP3 Reviewed prediction
PRO_0000039897Add
BLAST
Chaini724 – 930207Protein VP1 Reviewed prediction
PRO_0000039898Add
BLAST
Chaini931 – 94818Protein 2A Reviewed prediction
PRO_0000039899Add
BLAST
Chaini949 – 1102154Protein 2B Reviewed prediction
PRO_0000310980Add
BLAST
Chaini1103 – 1420318Protein 2C Reviewed prediction
PRO_0000422519Add
BLAST
Chaini1421 – 1573153Protein 3A Reviewed prediction
PRO_0000422520Add
BLAST
Chaini1574 – 159623Protein 3B-1 Reviewed prediction
PRO_0000422521Add
BLAST
Chaini1597 – 162024Protein 3B-2 Reviewed prediction
PRO_0000422522Add
BLAST
Chaini1621 – 164424Protein 3B-3 Reviewed prediction
PRO_0000422523Add
BLAST
Chaini1645 – 1857213Picornain 3C Reviewed prediction
PRO_0000422524Add
BLAST
Chaini1858 – 2327470RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000422525Add
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 residuei1576 – 15761O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1599 – 15991O-(5'-phospho-RNA)-tyrosine By similarity
Modified residuei1623 – 16231O-(5'-phospho-RNA)-tyrosine By similarity

Post-translational modificationi

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.
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.

Keywords - PTMi

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

Interactioni

Subunit structurei

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi291 – 2933
Beta strandi302 – 3054
Beta strandi308 – 3114
Helixi332 – 3343
Turni342 – 3443
Beta strandi348 – 3558
Beta strandi364 – 3729
Helixi375 – 3839
Beta strandi384 – 39815
Beta strandi404 – 41310
Helixi421 – 4233
Beta strandi429 – 4346
Turni436 – 4383
Beta strandi440 – 4467
Beta strandi450 – 4556
Helixi457 – 4593
Beta strandi463 – 47412
Turni476 – 4783
Beta strandi483 – 49917
Helixi548 – 5547
Beta strandi561 – 5633
Beta strandi571 – 5744
Beta strandi576 – 5816
Turni587 – 5915
Helixi593 – 5986
Beta strandi601 – 6055
Beta strandi608 – 6147
Beta strandi621 – 6299
Beta strandi631 – 6333
Helixi639 – 6424
Beta strandi645 – 6517
Beta strandi659 – 6624
Beta strandi667 – 6693
Beta strandi671 – 6744
Beta strandi686 – 69611
Beta strandi701 – 7088
Beta strandi713 – 7175
Beta strandi863 – 8653

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJOX-ray2.30P859-873[»]
1FMDX-ray3.502287-504[»]
3505-723[»]
1QGCelectron microscopy30.002287-504[»]
3505-723[»]
ProteinModelPortaliP15072.
SMRiP15072. Positions 29-201, 216-930, 1651-1851, 1858-2327.

Miscellaneous databases

EvolutionaryTraceiP15072.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28
Add
BLAST
Domaini1184 – 1348165SF3 helicase
Add
BLAST
Domaini1647 – 1831185Peptidase C3
Add
BLAST
Domaini2091 – 2209119RdRp catalytic
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi864 – 8663Cell attachment site

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: P15072-1) [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

MNTTDCFIAV VNAIREIRAL FLPRTTGKME FTLHDGEKKV FYSRPNNHDN     50
CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP 100
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGQEHAV 150
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNE GWKANVQRKL 200
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE 250
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 300
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM 350
ALFDWVPSQN FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN 400
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG 450
VNRYDQYKQH RPWTLVVMVV APLTTNTAGA QQIKVYANIA PTNVHVAGEL 500
PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD 550
VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 600
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW 650
DTGLNSKFTF SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD 700
ALVVSASAGK DFELRLPVDA RQQTTATGES ADPVTTTVEN YGGETQVQRR 750
HHTDVAFVLD RFVKVTVSGN QHTLDVMQAH KDNIVGALLR AATYYFSDLE 800
IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL PYTAPHRVLA 850
TAYTGTTTYT ASTRGDSAHL TATRARHLPT SFNFGAVKAE TITELLVRMK 900
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF 950
FFSDVRSNFS KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT 1000
GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF 1050
VVKKISDSLS SLFHVPAPAF SFGAPILLAG LVKVASSFFR STPEDLERAE 1100
KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP 1150
GILEKQRDLN DPSKYKDAKE WLDNTRQACL KSGNVHIANL CKVVAPAPSK 1200
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF 1250
DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS 1300
SKVIIATTNL YSGFTPKTMV CPDALNRRFH FDIDVSAKDG YKINNKLDII 1350
KALEDTHTNP VAMFQYDCAL LNGMAVEMKR LQQDMFKPQP PLQNVYQLVQ 1400
EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV 1450
HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH 1500
KRQKMVDDAV NEYIEKANIT TDDKTLDEAE KNPLETSGAS TVGFRERTLP 1550
GQKARDDVNS EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPQQEGPYA 1600
GPMERQKPLK VKARAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT 1650
DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM 1700
LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDV 1750
ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA 1800
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI 1850
DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD 1900
PRLNEGVVLD EVIFSKHKGD TKMSEEDKAL FRRCAADYAS RLHSVLGTAN 1950
APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV 2000
EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR 2050
MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA 2100
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE 2150
GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA 2200
SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD 2250
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF 2300
EPFQGLFEIP SYRSLYLRWV NAVCGDA 2327
Length:2,327
Mass (Da):258,119
Last modified:May 29, 2013 - v2
Checksum:iA81AB150E79617DD
GO
Isoform Lb (identifier: P15072-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,299
Mass (Da):254,985
Checksum:iA0B0C0DD67DE5BA2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81I → T.
Natural varianti48 – 481H → Q.
Natural varianti307 – 3071H → Q.
Natural varianti408 – 4092LV → QA.
Natural varianti726 – 7261A → T.
Natural varianti852 – 8521A → G.
Natural varianti867 – 8671S → L.
Natural varianti876 – 8761R → G.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb.
VSP_018983Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY593805 Genomic RNA. Translation: AAT01748.1.
X00130 Genomic RNA. Translation: CAA24960.2.
PIRiA20288. GNNYC1.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure in complex with a fab fragment of a neutralizing antibody

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY593805 Genomic RNA. Translation: AAT01748.1 .
X00130 Genomic RNA. Translation: CAA24960.2 .
PIRi A20288. GNNYC1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EJO X-ray 2.30 P 859-873 [» ]
1FMD X-ray 3.50 2 287-504 [» ]
3 505-723 [» ]
1QGC electron microscopy 30.00 2 287-504 [» ]
3 505-723 [» ]
ProteinModelPortali P15072.
SMRi P15072. Positions 29-201, 216-930, 1651-1851, 1858-2327.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P15072.

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. "Structure of the FMDV translation initiation site and of the structural proteins."
    Beck E., Forss S., Strebel K., Cattaneo R., Feil G.
    Nucleic Acids Res. 11:7873-7885(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1011.
  3. "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.

Entry informationi

Entry nameiPOLG_FMDVT
AccessioniPrimary (citable) accession number: P15072
Secondary accession number(s): Q6PMY1
, Q84755, Q84756, Q84757, Q84758
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 29, 2013
Last modified: July 9, 2014
This is version 123 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.

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

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