UniProtKB - P03305 (POLG_FMDVO)
Genome polyprotein
Functioni
Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Cleaves also the host translation initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host DDX58, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this mofidier that can no longer be attached to target proteins. Cleaves also host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly.
By similarity6 PublicationsLies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks.
By similarityForms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.
1 PublicationCapsid protein V1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome. Mediates cell entry by attachment to an integrin receptor, usually host ITGAV/ITGB6, via a conserved arginine-glycine-aspartic acid (R-G-D) motif.
4 PublicationsCapsid protein V3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.
1 PublicationMediates self-processing of the polyprotein by a translational effect termed 'ribosome skipping'. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally 'trimmed' from the C-terminus of the upstream protein 1D by 3C proteinase.
1 PublicationPlays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.
1 PublicationAssociates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.
4 PublicationsPlays important roles in virus replication, virulence and host range.
2 PublicationsCovalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
1 PublicationCovalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
1 PublicationCovalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
1 PublicationCysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease.
1 PublicationRNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.
PROSITE-ProRule annotation1 PublicationMiscellaneous
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-. EC:3.4.22.46
- 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.PROSITE-ProRule annotation EC:3.4.22.28
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 51 | For leader protease activity | 1 | |
Active sitei | 148 | For leader protease activity | 1 | |
Active sitei | 163 | For leader protease activity | 1 | |
Active sitei | 1695 | For protease 3C activity; Proton donor/acceptorPROSITE-ProRule annotation | 1 | |
Active sitei | 1733 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1812 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2200 | For RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1217 – 1224 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: UniProtKB-EC
- ion channel activity Source: UniProtKB-KW
- ISG15-specific protease activity Source: UniProtKB
- nucleoside-triphosphatase activity Source: RHEA
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB
- modulation by virus of host chromatin organization Source: UniProtKB-KW
- modulation by virus of host protein ubiquitination Source: UniProtKB
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- positive stranded viral RNA replication Source: UniProtKB
- protein complex oligomerization Source: UniProtKB-KW
- proteolysis Source: UniProtKB
- regulation of translation Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- suppression by virus of host ISG15-protein conjugation Source: UniProtKB
- suppression by virus of host NF-kappaB cascade Source: UniProtKB
- suppression by virus of host translation initiation factor activity Source: UniProtKB
- suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB
- transcription, DNA-templated Source: InterPro
- viral protein processing Source: InterPro
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Enzyme and pathway databases
BRENDAi | 3.4.22.46, 2315 |
Protein family/group databases
MEROPSi | C03.008 |
TCDBi | 1.A.85.1.8, the poliovirus 2b viroporin (2b viroporin) family |
UniLectini | P03305 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 15 chains: 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 Alternative name(s): P52 Alternative name(s): Genome-linked protein VPg1 Alternative name(s): Genome-linked protein VPg2 Alternative name(s): Genome-linked protein VPg3 Protease 3C (EC:3.4.22.281 Publication) Alternative name(s): Picornain 3C Short name: P3C Protease P20B Alternative name(s): P56A |
Organismi | Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV) |
Taxonomic identifieri | 73482 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Aphthovirus › |
Virus hosti | Bos 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] |
Proteomesi |
|
Subcellular locationi
- Host nucleus 1 Publication
- Host cytoplasm 1 Publication
- Virion 1 Publication
- Host cytoplasm Curated
- Virion 1 Publication
- Host cytoplasm Curated
- Virion 1 Publication
- Host cytoplasm Curated
- Host endoplasmic reticulum membrane 1 Publication
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated 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).By similarity
- Host cytoplasm 2 Publications
- Host endoplasmic reticulum membrane 1 Publication Note: Interacts with host endoplasmic reticulum membranes through its hydrophobic stretch, while its N- and C-terminus face the cytosol being accessible to other viral proteins for viral replication.1 Publication
- Virion Curated
- Virion Curated
- Virion Curated
- Host cytoplasm Curated
- Host cytoplasm 1 Publication
- Host nucleus 1 Publication
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 1480 | CytoplasmicSequence analysisAdd BLAST | 1480 | |
Intramembranei | 1481 – 1501 | Sequence analysisAdd BLAST | 21 | |
Topological domaini | 1502 – 2332 | CytoplasmicSequence analysisAdd BLAST | 831 |
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000039872 | 1 – 2332 | Genome polyproteinAdd BLAST | 2332 | |
ChainiPRO_0000039873 | 1 – 201 | Leader proteaseAdd BLAST | 201 | |
ChainiPRO_0000374076 | 202 – 504 | Capsid protein VP0Sequence analysisAdd BLAST | 303 | |
ChainiPRO_0000039876 | 202 – 286 | Capsid protein VP4Sequence analysisAdd BLAST | 85 | |
ChainiPRO_0000039877 | 287 – 504 | Capsid protein VP2Sequence analysisAdd BLAST | 218 | |
ChainiPRO_0000039878 | 505 – 724 | Capsid protein VP3Sequence analysisAdd BLAST | 220 | |
ChainiPRO_0000039879 | 725 – 935 | Capsid protein VP1Add BLAST | 211 | |
ChainiPRO_0000039880 | 936 – 953 | Protein 2ASequence analysisAdd BLAST | 18 | |
ChainiPRO_0000310976 | 954 – 1107 | Protein 2BSequence analysisAdd BLAST | 154 | |
ChainiPRO_0000039881 | 1108 – 1425 | Protein 2CSequence analysisAdd BLAST | 318 | |
ChainiPRO_0000039882 | 1426 – 1578 | Protein 3ASequence analysisAdd BLAST | 153 | |
ChainiPRO_0000039883 | 1579 – 1601 | Protein 3B-1Sequence analysisAdd BLAST | 23 | |
ChainiPRO_0000310977 | 1602 – 1625 | Protein 3B-2Sequence analysisAdd BLAST | 24 | |
ChainiPRO_0000310978 | 1626 – 1649 | Protein 3B-3Sequence analysisAdd BLAST | 24 | |
ChainiPRO_0000039884 | 1650 – 1862 | Protease 3CSequence analysisAdd BLAST | 213 | |
ChainiPRO_0000039885 | 1863 – 2332 | RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST | 470 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 202 | N-myristoyl glycine; by hostBy similarity | 1 | |
Disulfide bondi | 406 ↔ 858 | Interchain (between VP2 and VP1 chains) | ||
Disulfide bondi | 511 | Interchain; in VP3 dimer | ||
Modified residuei | 1581 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 | |
Modified residuei | 1604 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 | |
Modified residuei | 1628 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 201 – 202 | Cleavage; by leader proteaseSequence analysis | 2 | |
Sitei | 286 – 287 | CleavageSequence analysis | 2 | |
Sitei | 504 – 505 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 724 – 725 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 935 – 936 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 953 – 954 | Cleavage; by ribosomal skipSequence analysis | 2 | |
Sitei | 1107 – 1108 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1425 – 1426 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1578 – 1579 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1601 – 1602 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1625 – 1626 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1649 – 1650 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1862 – 1863 | Cleavage; by picornain 3CSequence analysis | 2 |
Keywords - PTMi
Autocatalytic cleavage, Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, PhosphoproteinProteomic databases
PRIDEi | P03305 |
Interactioni
Subunit structurei
Interacts (via R-G-D motif) with host ITGAV/ITGB6 (PubMed:28534487).
1 PublicationProtein-protein interaction databases
ELMi | P03305 |
Structurei
Secondary structure
3D structure databases
BMRBi | P03305 |
SMRi | P03305 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03305 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 201 | Peptidase C28Add BLAST | 201 | |
Domaini | 1189 – 1353 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 165 | |
Domaini | 1652 – 1848 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 197 | |
Domaini | 2096 – 2214 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 119 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 197 – 218 | DisorderedSequence analysisAdd BLAST | 22 | |
Regioni | 237 – 265 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 1529 – 1584 | DisorderedSequence analysisAdd BLAST | 56 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 869 – 871 | Cell attachment site1 Publication | 3 | |
Motifi | 1879 – 1886 | Nuclear localization signal1 Publication | 8 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 203 – 218 | Polar residuesSequence analysisAdd BLAST | 16 |
Sequence similaritiesi
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
DisProti | DP00573 |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 2 hits 4.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR015031, Capsid_VP4_Picornavir IPR037080, Capsid_VP4_sf_Picornavirus IPR043502, DNA/RNA_pol_sf 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 IPR038765, Papain-like_cys_pep_sf IPR044067, PCV_3C_PRO IPR008739, Peptidase_C28 IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam 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 |
PRINTSi | PR00918, CALICVIRUSNS PR01542, FMDVP1COAT |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF54001, SSF54001, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51887, APHTHOVIRUS_LPRO, 1 hit PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative initiation. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN
60 70 80 90 100
CWLNAILQLF RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV
160 170 180 190 200
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQRKL
210 220 230 240 250
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE
260 270 280 290 300
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
310 320 330 340 350
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT
360 370 380 390 400
HLFDWVTSDS FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA MVPELYSIQK RELYQLTLFP HQFINPRTNM TAHITVPFVG
460 470 480 490 500
VNRYDQYKVH KPWTLVVMVV APLTVNTEGA PQIKVYANIA PTNVHVAGEF
510 520 530 540 550
PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ LPGRFTNLLD
560 570 580 590 600
VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ
610 620 630 640 650
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE
660 670 680 690 700
WDTGLNSKFT FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG
710 720 730 740 750
DALVVLASAG KDFELRLPVD ARAETTSAGE SADPVTTTVE NYGGETQIQR
760 770 780 790 800
RQHTDVSFIM DRFVKVTPQN QINILDLMQI PSHTLVGALL RASTYYFSDL
810 820 830 840 850
EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA LPYTAPHRVL
860 870 880 890 900
ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL
910 920 930 940 950
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES
960 970 980 990 1000
NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV
1010 1020 1030 1040 1050
KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI
1060 1070 1080 1090 1100
LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP VLLAGLVKVA SSFFRSTPED
1110 1120 1130 1140 1150
LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM
1160 1170 1180 1190 1200
TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
1210 1220 1230 1240 1250
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP
1260 1270 1280 1290 1300
DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK
1310 1320 1330 1340 1350
GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINS
1360 1370 1380 1390 1400
KLDIIKALED THANPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV
1410 1420 1430 1440 1450
YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF
1460 1470 1480 1490 1500
FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
1510 1520 1530 1540 1550
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR
1560 1570 1580 1590 1600
ERTLPGQKAC DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ
1610 1620 1630 1640 1650
EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV KAKNLIVTES
1660 1670 1680 1690 1700
GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK
1710 1720 1730 1740 1750
YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK
1760 1770 1780 1790 1800
HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
1810 1820 1830 1840 1850
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK
1860 1870 1880 1890 1900
MKAHIDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA
1910 1920 1930 1940 1950
LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV
1960 1970 1980 1990 2000
LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT
2010 2020 2030 2040 2050
VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT RIVDVLPVEH
2060 2070 2080 2090 2100
ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
2110 2120 2130 2140 2150
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK
2160 2170 2180 2190 2200
RITVGGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD
2210 2220 2230 2240 2250
DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGH SITDVTFLKR
2260 2270 2280 2290 2300
HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE
2310 2320 2330
YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
The sequence of this isoform differs from the canonical sequence as follows:
1-28: Missing.
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 780 | I → V in strain: Isolate O1BFS. | 1 | |
Natural varianti | 808 | G → R in strain: Isolate O1BFS. | 1 | |
Natural varianti | 861 | N → S in strain: Isolate O1BFS. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_018982 | 1 – 28 | Missing in isoform Lb. CuratedAdd BLAST | 28 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X00871 Genomic RNA Translation: CAA25416.1 J02185 Genomic RNA Translation: AAA42635.1 |
Genome annotation databases
KEGGi | ag:CAA25416 |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
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: EMBLi GenBanki DDBJi Links Updated | X00871 Genomic RNA Translation: CAA25416.1 J02185 Genomic RNA Translation: AAA42635.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
4QBB | X-ray | 1.60 | A/B/C | 29-195 | [»] | |
6FFA | X-ray | 1.50 | A | 29-195 | [»] | |
BMRBi | P03305 | |||||
SMRi | P03305 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
ELMi | P03305 |
Protein family/group databases
MEROPSi | C03.008 |
TCDBi | 1.A.85.1.8, the poliovirus 2b viroporin (2b viroporin) family |
UniLectini | P03305 |
Proteomic databases
PRIDEi | P03305 |
Genome annotation databases
KEGGi | ag:CAA25416 |
Enzyme and pathway databases
BRENDAi | 3.4.22.46, 2315 |
Miscellaneous databases
EvolutionaryTracei | P03305 |
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
DisProti | DP00573 |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 2 hits 4.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR015031, Capsid_VP4_Picornavir IPR037080, Capsid_VP4_sf_Picornavirus IPR043502, DNA/RNA_pol_sf 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 IPR038765, Papain-like_cys_pep_sf IPR044067, PCV_3C_PRO IPR008739, Peptidase_C28 IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam 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 |
PRINTSi | PR00918, CALICVIRUSNS PR01542, FMDVP1COAT |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF54001, SSF54001, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51887, APHTHOVIRUS_LPRO, 1 hit PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_FMDVO | |
Accessioni | P03305Primary (citable) accession number: P03305 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | February 23, 2022 | |
This is version 204 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families