Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15072 (POLG_FMDVT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 8 chains:

  1. Leader protease
    Short name=Lpro
    EC=3.4.22.46
  2. Protein VP0
    Alternative name(s):
    VP4-VP2
  3. Protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  4. Protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  5. Protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  6. Protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  7. Protein 2A
    Short name=P2A
    Alternative name(s):
    P52
  8. Protein 2B
    Short name=P2B
OrganismFoot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV) [Complete proteome]
Taxonomic identifier12121 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeAphthovirus
Virus hostBos 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]

Protein attributes

Sequence length2327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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).

Subunit structure

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

Subcellular location

Protein VP2: Virion. Host cytoplasm Potential.

Protein VP3: Virion. Host cytoplasm Potential.

Protein VP1: Virion. Host cytoplasm Potential.

Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 3B-1: Virion Potential.

Protein 3B-2: Virion Potential.

Protein 3B-3: Virion Potential.

Picornain 3C: Host cytoplasm Potential.

RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 1 peptidase C28 domain.

Contains 1 peptidase C3 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processClathrin- 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
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Membrane
Virion
   Coding sequence diversityAlternative initiation
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
Viral ion channel
   PTMCovalent protein-RNA linkage
Disulfide bond
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

modulation by virus of host chromatin organization

Inferred from electronic annotation. Source: UniProtKB-KW

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host RIG-I activity by RIG-I proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

suppression by virus of host translation initiation factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral protein processing

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

icosahedral viral capsid

Inferred from electronic annotation. Source: InterPro

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Lab (identifier: P15072-1)

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.
Isoform Lb (identifier: P15072-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23272327Genome polyprotein By similarity
PRO_0000039891
Chain1 – 201201Leader protease
PRO_0000039892
Chain202 – 504303Protein VP0 Potential
PRO_0000374077
Chain202 – 28685Protein VP4 Potential
PRO_0000039895
Chain287 – 504218Protein VP2 Potential
PRO_0000039896
Chain505 – 723219Protein VP3 Potential
PRO_0000039897
Chain724 – 930207Protein VP1 Potential
PRO_0000039898
Chain931 – 94818Protein 2A Potential
PRO_0000039899
Chain949 – 1102154Protein 2B Potential
PRO_0000310980
Chain1103 – 1420318Protein 2C Potential
PRO_0000422519
Chain1421 – 1573153Protein 3A Potential
PRO_0000422520
Chain1574 – 159623Protein 3B-1 Potential
PRO_0000422521
Chain1597 – 162024Protein 3B-2 Potential
PRO_0000422522
Chain1621 – 164424Protein 3B-3 Potential
PRO_0000422523
Chain1645 – 1857213Picornain 3C Potential
PRO_0000422524
Chain1858 – 2327470RNA-directed RNA polymerase 3D-POL Potential
PRO_0000422525

Regions

Topological domain1 – 14751475Cytoplasmic Potential
Intramembrane1476 – 149621 Potential
Topological domain1497 – 2327831Cytoplasmic Potential
Domain1 – 201201Peptidase C28
Domain1184 – 1348165SF3 helicase
Domain1647 – 1831185Peptidase C3
Domain2091 – 2209119RdRp catalytic
Nucleotide binding1212 – 12198ATP Potential
Motif864 – 8663Cell attachment site

Sites

Active site511For leader protease activity By similarity
Active site1481For leader protease activity By similarity
Active site1631For leader protease activity By similarity
Active site16901For picornain 3C activity Potential
Active site17171For picornain 3C activity Potential
Active site18071For picornain 3C activity Potential
Site201 – 2022Cleavage; by leader protease Potential
Site286 – 2872Cleavage Potential
Site504 – 5052Cleavage; by picornain 3C Potential
Site723 – 7242Cleavage; by picornain 3C Potential
Site930 – 9312Cleavage; by picornain 3C Potential
Site948 – 9492Cleavage; by ribosomal skip Potential
Site1102 – 11032Cleavage; by picornain 3C Potential
Site1420 – 14212Cleavage; by picornain 3C Potential
Site1573 – 15742Cleavage; by picornain 3C Potential
Site1596 – 15972Cleavage; by picornain 3C Potential
Site1620 – 16212Cleavage; by picornain 3C Potential
Site1644 – 16452Cleavage; by picornain 3C Potential
Site1857 – 18582Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue15761O-(5'-phospho-RNA)-tyrosine By similarity
Modified residue15991O-(5'-phospho-RNA)-tyrosine By similarity
Modified residue16231O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation2021N-myristoyl glycine; by host By similarity
Disulfide bond511Interchain; in VP3 dimer By similarity

Natural variations

Alternative sequence1 – 2828Missing in isoform Lb.
VSP_018983
Natural variant81I → T.
Natural variant481H → Q.
Natural variant3071H → Q.
Natural variant408 – 4092LV → QA.
Natural variant7261A → T.
Natural variant8521A → G.
Natural variant8671S → L.
Natural variant8761R → G.

Secondary structure

............................................................................ 2327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Lab [UniParc].

Last modified May 29, 2013. Version 2.
Checksum: A81AB150E79617DD

FASTA2,327258,119
        10         20         30         40         50         60 
MNTTDCFIAV VNAIREIRAL FLPRTTGKME FTLHDGEKKV FYSRPNNHDN CWLNTILQLF 

        70         80         90        100        110        120 
RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP ALVIWNIKHL LHTGIGTASR 

       130        140        150        160        170        180 
PSEVCMVDGT DMCLADFHAG IFMKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF 

       190        200        210        220        230        240 
VPYDQEPLNE GWKANVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG 

       250        260        270        280        290        300 
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 

       310        320        330        340        350        360 
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM ALFDWVPSQN 

       370        380        390        400        410        420 
FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN QFNGGCLLVA LVPEMGDISD 

       430        440        450        460        470        480 
REKYQLTLYP HQFINPRTNM TAHITVPYVG VNRYDQYKQH RPWTLVVMVV APLTTNTAGA 

       490        500        510        520        530        540 
QQIKVYANIA PTNVHVAGEL PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA 

       550        560        570        580        590        600 
LPGRFTNYLD VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY 

       610        620        630        640        650        660 
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW DTGLNSKFTF 

       670        680        690        700        710        720 
SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD ALVVSASAGK DFELRLPVDA 

       730        740        750        760        770        780 
RQQTTATGES ADPVTTTVEN YGGETQVQRR HHTDVAFVLD RFVKVTVSGN QHTLDVMQAH 

       790        800        810        820        830        840 
KDNIVGALLR AATYYFSDLE IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL 

       850        860        870        880        890        900 
PYTAPHRVLA TAYTGTTTYT ASTRGDSAHL TATRARHLPT SFNFGAVKAE TITELLVRMK 

       910        920        930        940        950        960 
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF FFSDVRSNFS 

       970        980        990       1000       1010       1020 
KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT GLDEAKPWYK LIKLLSRLSC 

      1030       1040       1050       1060       1070       1080 
MAAVAARSKD PVLVAIMLAD TGLEILDSTF VVKKISDSLS SLFHVPAPAF SFGAPILLAG 

      1090       1100       1110       1120       1130       1140 
LVKVASSFFR STPEDLERAE KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE 

      1150       1160       1170       1180       1190       1200 
KFVTMTDLVP GILEKQRDLN DPSKYKDAKE WLDNTRQACL KSGNVHIANL CKVVAPAPSK 

      1210       1220       1230       1240       1250       1260 
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF DGYNQQTVVV 

      1270       1280       1290       1300       1310       1320 
MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS SKVIIATTNL YSGFTPKTMV 

      1330       1340       1350       1360       1370       1380 
CPDALNRRFH FDIDVSAKDG YKINNKLDII KALEDTHTNP VAMFQYDCAL LNGMAVEMKR 

      1390       1400       1410       1420       1430       1440 
LQQDMFKPQP PLQNVYQLVQ EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE 

      1450       1460       1470       1480       1490       1500 
AAIEFFEGMV HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH 

      1510       1520       1530       1540       1550       1560 
KRQKMVDDAV NEYIEKANIT TDDKTLDEAE KNPLETSGAS TVGFRERTLP GQKARDDVNS 

      1570       1580       1590       1600       1610       1620 
EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPQQEGPYA GPMERQKPLK VKARAPVVKE 

      1630       1640       1650       1660       1670       1680 
GPYEGPVKKP VALKVKAKNL IVTESGAPPT DLQKMVMGNT KPVELILDGK TVAICCATGV 

      1690       1700       1710       1720       1730       1740 
FGTAYLVPRH LFAEKYDKIM LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV 

      1750       1760       1770       1780       1790       1800 
RDITKHFRDV ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA 

      1810       1820       1830       1840       1850       1860 
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI DPEPHHEGLI 

      1870       1880       1890       1900       1910       1920 
VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD PRLNEGVVLD EVIFSKHKGD 

      1930       1940       1950       1960       1970       1980 
TKMSEEDKAL FRRCAADYAS RLHSVLGTAN APLSIYEAIK GVDGLDAMEP DTAPGLPWAL 

      1990       2000       2010       2020       2030       2040 
QGKRRGALID FENGTVGPEV EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV 

      2050       2060       2070       2080       2090       2100 
LPVEHILYTR MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA 

      2110       2120       2130       2140       2150       2160 
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE GGMPSGCSAT 

      2170       2180       2190       2200       2210       2220 
SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA SDYDLDFEAL KPHFKSLGQT 

      2230       2240       2250       2260       2270       2280 
ITPADKSDKG FVLGHSITDV TFLKRHFHMD YGTGFYKPVM ASKTLEAILS FARRGTIQEK 

      2290       2300       2310       2320 
LISVAGLAVH SGPDEYRRLF EPFQGLFEIP SYRSLYLRWV NAVCGDA 

« Hide

Isoform Lb [UniParc].

Checksum: A0B0C0DD67DE5BA2
Show »

FASTA2,299254,985

References

[1]"Comparative genomics of foot-and-mouth disease virus."
Carrillo C., Tulman E.R., Delhon G., Lu Z., Carreno A., Vagnozzi A., Kutish G.F., Rock D.L.
J. Virol. 79:6487-6504(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY593805 Genomic RNA. Translation: AAT01748.1.
X00130 Genomic RNA. Translation: CAA24960.2.
PIRGNNYC1. A20288.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJOX-ray2.30P859-873[»]
1FMDX-ray3.502287-504[»]
3505-723[»]
1QGCelectron microscopy30.002287-504[»]
3505-723[»]
ProteinModelPortalP15072.
SMRP15072. Positions 29-201, 216-930, 1651-1851, 1858-2327.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProIPR015031. 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]
PfamPF05408. 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]
PRINTSPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15072.

Entry information

Entry namePOLG_FMDVT
AccessionPrimary (citable) accession number: P15072
Secondary accession number(s): Q6PMY1 expand/collapse secondary AC list , Q84755, Q84756, Q84757, Q84758
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references