UniProtKB - P03311 (POLG_FMDVS)
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 similarityLies 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.
By similarityForms 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. In addition, targets host MAVS to suppress type I IFN pathway.
By similarityForms 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.
By similarityMediates 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.
By similarityPlays 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.
By similarityAssociates 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.
By similarityPlays important roles in virus replication, virulence and host range.
By similarityCovalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
By similarityCovalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
By similarityCovalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
By similarityCysteine 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.
By similarityRNA-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.
By similarityMiscellaneous
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 activityBy similarity | 1 | |
Active sitei | 148 | For leader protease activityBy similarity | 1 | |
Active sitei | 163 | For leader protease activityBy similarity | 1 | |
Active sitei | 1690 | For protease 3C activity; Proton donor/acceptorPROSITE-ProRule annotation | 1 | |
Active sitei | 1728 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1807 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2195 | For RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1212 – 1219 | 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
- nucleoside-triphosphatase activity Source: RHEA
- RNA binding Source: UniProtKB
- 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
- 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
- regulation of translation Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- suppression by virus of host translation initiation factor activity 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
Protein family/group databases
MEROPSi | C03.008 |
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:3.4.22.28) Alternative name(s): Picornain 3C Short name: P3C Protease P20B Alternative name(s): P56A |
Organismi | Foot-and-mouth disease virus (isolate -/Spain/S8c1SantaPau/1970 serotype C) (FMDV) |
Taxonomic identifieri | 12120 [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 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 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 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
- Virion Curated
- Virion Curated
- Virion Curated
- Host cytoplasm Curated
- 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
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 1475 | CytoplasmicSequence analysisAdd BLAST | 1475 | |
Intramembranei | 1476 – 1496 | Sequence analysisAdd BLAST | 21 | |
Topological domaini | 1497 – 2327 | CytoplasmicSequence analysisAdd BLAST | 831 |
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000422517 | 1 – 2327 | Genome polyproteinBy similarityAdd BLAST | 2327 | |
ChainiPRO_5000064843 | 1 – 201 | Leader proteaseBy similarityAdd BLAST | 201 | |
ChainiPRO_0000422518 | 202 – 504 | Capsid protein VP0Sequence analysisAdd BLAST | 303 | |
ChainiPRO_5000064844 | 202 – 286 | Capsid protein VP4Sequence analysisAdd BLAST | 85 | |
ChainiPRO_5000064845 | 287 – 504 | Capsid protein VP2Sequence analysisAdd BLAST | 218 | |
ChainiPRO_0000039886 | 505 – 723 | Capsid protein VP3Sequence analysisAdd BLAST | 219 | |
ChainiPRO_0000039887 | 724 – 930 | Capsid protein VP1By similarityAdd BLAST | 207 | |
ChainiPRO_0000039888 | 931 – 948 | Protein 2ASequence analysisAdd BLAST | 18 | |
ChainiPRO_0000310979 | 949 – 1102 | Protein 2BSequence analysisAdd BLAST | 154 | |
ChainiPRO_5000064850 | 1103 – 1420 | Protein 2CSequence analysisAdd BLAST | 318 | |
ChainiPRO_5000064851 | 1421 – 1573 | Protein 3ASequence analysisAdd BLAST | 153 | |
ChainiPRO_5000064852 | 1574 – 1596 | Protein 3B-1Sequence analysisAdd BLAST | 23 | |
ChainiPRO_5000064853 | 1597 – 1620 | Protein 3B-2Sequence analysisAdd BLAST | 24 | |
ChainiPRO_5000064854 | 1621 – 1644 | Protein 3B-3Sequence analysisAdd BLAST | 24 | |
ChainiPRO_0000039889 | 1645 – 1857 | Protease 3CSequence analysisAdd BLAST | 213 | |
ChainiPRO_0000039890 | 1858 – 2327 | 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 | 511 | Interchain; in VP3 dimerBy similarity | ||
Modified residuei | 1576 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 | |
Modified residuei | 1599 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 | |
Modified residuei | 1623 | 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 | 723 – 724 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 930 – 931 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 948 – 949 | Cleavage; by ribosomal skipSequence analysis | 2 | |
Sitei | 1102 – 1103 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1420 – 1421 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1573 – 1574 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1596 – 1597 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1620 – 1621 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1644 – 1645 | Cleavage; by picornain 3CSequence analysis | 2 | |
Sitei | 1857 – 1858 | Cleavage; by picornain 3CSequence analysis | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, PhosphoproteinInteractioni
Subunit structurei
Interacts with host ISG15. Capsid protein VP1:
Interacts (via R-G-D motif) with host ITGAV/ITGB6.
Interacts with host MAVS; this interaction inhibits binding of host TRAF3 to MAVS, thereby suppressing interferon-mediated responses.
By similarityStructurei
Secondary structure
3D structure databases
SMRi | P03311 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03311 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 201 | Peptidase C28Add BLAST | 201 | |
Domaini | 1184 – 1348 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 165 | |
Domaini | 1647 – 1843 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 197 | |
Domaini | 2091 – 2209 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 119 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 196 – 218 | DisorderedSequence analysisAdd BLAST | 23 | |
Regioni | 237 – 265 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 1524 – 1584 | DisorderedSequence analysisAdd BLAST | 61 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 864 – 866 | Cell attachment siteBy similarity | 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 200 – 218 | Polar residuesSequence analysisAdd BLAST | 19 |
Sequence similaritiesi
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
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
MNTTDCFIAV VNAIKEVRAL FLPRTAGKME FTLHDGEKKV FYSRPNNHDN
60 70 80 90 100
CWLNTILQLF RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFMKGREHAV
160 170 180 190 200
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNE GWKASVQRKL
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 TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM
360 370 380 390 400
ALFDWVPSQN FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA LVPEMGDISD REKYQLTLYP HQFINPRTNM TAHITVPYVG
460 470 480 490 500
VNRYDQYKQH RPWTLVVMVV APLTTNTAGA QQIKVYANIA PTNVHVAGEL
510 520 530 540 550
PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA LPGRFTNYLD
560 570 580 590 600
VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
610 620 630 640 650
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW
660 670 680 690 700
DTGLNSKFTF SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD
710 720 730 740 750
ALVVSASAGK DFELRLPVDA RQQTTTTGES ADPVTTTVEN YGGETQVQRR
760 770 780 790 800
HHTDVAFVLD RFVKVTVSDN QHTLDVMQAH KDNIVGALLR AATYYFSDLE
810 820 830 840 850
IAVTHTGKLT WVPNGAPVSA LNNTTNPTAY HKGPVTRLAL PYTAPHRVLA
860 870 880 890 900
TAYTGTTTYT ASARGDLAHL TTTHARHLPT SFNFGAVKAE TITELLVRMK
910 920 930 940 950
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF
960 970 980 990 1000
FFSDVRSNFS KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT
1010 1020 1030 1040 1050
GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF
1060 1070 1080 1090 1100
VVKKISDSLS SLFHVPAPAF SFGAPILLAG LVKVASSFFR STPEDLERAE
1110 1120 1130 1140 1150
KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP
1160 1170 1180 1190 1200
GILEKQRDLN DPSKYKDAKE WLDNTRQVCL KSGNVHIANL CKVVAPAPSK
1210 1220 1230 1240 1250
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF
1260 1270 1280 1290 1300
DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS
1310 1320 1330 1340 1350
SKVIIATTNL YSGFTPKTMV CPDALNRRFH FDIDVSAKDG YKINNKLDII
1360 1370 1380 1390 1400
KALEDTHTNP VAMFQYDCAL LNGMAVEMKR LQQDMFKPQP PLQNVYQLVQ
1410 1420 1430 1440 1450
EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV
1460 1470 1480 1490 1500
HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH
1510 1520 1530 1540 1550
KRQKMVDDAV NEYIEKANIT TDDQTLDEAE KNPLETSGAS TVGFRERTLP
1560 1570 1580 1590 1600
GQKARDDVNS EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPRQEGPYA
1610 1620 1630 1640 1650
GPMERQKPLK VKARAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT
1660 1670 1680 1690 1700
DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM
1710 1720 1730 1740 1750
LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDV
1760 1770 1780 1790 1800
ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA
1810 1820 1830 1840 1850
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI
1860 1870 1880 1890 1900
DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD
1910 1920 1930 1940 1950
PRLNEGVVLD EVIFSKHKGD TKMSAEDKAL FRRCAADYAS RLHSVLGTAN
1960 1970 1980 1990 2000
APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV
2010 2020 2030 2040 2050
EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR
2060 2070 2080 2090 2100
MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA
2110 2120 2130 2140 2150
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE
2160 2170 2180 2190 2200
GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA
2210 2220 2230 2240 2250
SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD
2260 2270 2280 2290 2300
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF
2310 2320
EPFQGLFEIP SYRSLYLRWV NAVCGDA
The sequence of this isoform differs from the canonical sequence as follows:
1-28: Missing.
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 789 – 792 | LRAA → SRH no nucleotide entry (PubMed:6311686).Curated | 4 | |
Sequence conflicti | 947 | P → L no nucleotide entry (PubMed:6311686).Curated | 1 | |
Sequence conflicti | 1008 | Missing no nucleotide entry (PubMed:6311686).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 1804 | A → V. | 1 | |
Natural varianti | 1916 | K → R. | 1 | |
Natural varianti | 1958 | A → V. | 1 | |
Natural varianti | 1975 | G → S. | 1 | |
Natural varianti | 2000 | V → A. | 1 | |
Natural varianti | 2080 | W → R. | 1 | |
Natural varianti | 2083 | F → S. | 1 | |
Natural varianti | 2087 | F → L. | 1 | |
Natural varianti | 2140 | H → Y. | 1 | |
Natural varianti | 2163 | I → V. | 1 | |
Natural varianti | 2261 | A → T. | 1 | |
Natural varianti | 2299 | L → F. | 1 | |
Natural varianti | 2326 | D → R. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_046532 | 1 – 28 | Missing in isoform Lb. CuratedAdd BLAST | 28 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ133357 Genomic RNA Translation: CAB60267.1 M11027 Genomic RNA Translation: AAA42654.1 |
PIRi | JC1328 JC1330 JC1331 JC1334 |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ133357 Genomic RNA Translation: CAB60267.1 M11027 Genomic RNA Translation: AAA42654.1 |
PIRi | JC1328 JC1330 JC1331 JC1334 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QGC | electron microscopy | 30.00 | 1 | 724-930 | [»] | |
2 | 287-504 | [»] | ||||
3 | 505-723 | [»] | ||||
5 | 859-879 | [»] | ||||
4WYL | X-ray | 2.00 | A | 1858-2327 | [»] | |
4WYW | X-ray | 1.80 | A | 1858-2327 | [»] | |
4WZM | X-ray | 2.52 | A | 1858-2327 | [»] | |
4WZQ | X-ray | 2.80 | A | 1858-2327 | [»] | |
4X2B | X-ray | 2.94 | A | 1858-2327 | [»] | |
5JXS | X-ray | 2.80 | A | 1858-2327 | [»] | |
5N8X | X-ray | 2.40 | A | 1858-2327 | [»] | |
5N95 | X-ray | 2.60 | A | 1858-2327 | [»] | |
6GVV | X-ray | 2.35 | A | 1858-2327 | [»] | |
6GVY | X-ray | 2.20 | A | 1858-2327 | [»] | |
6KWK | X-ray | 2.50 | C | 440-448 | [»] | |
6KWL | X-ray | 1.80 | C | 440-448 | [»] | |
6S2L | X-ray | 2.30 | A | 1858-2327 | [»] | |
SMRi | P03311 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | C03.008 |
Protocols and materials databases
ABCDi | P03311, 1 sequenced antibody |
Miscellaneous databases
EvolutionaryTracei | P03311 |
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
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_FMDVS | |
Accessioni | P03311Primary (citable) accession number: P03311 Secondary accession number(s): Q84781, Q84782, Q9QCE2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | May 29, 2013 | |
Last modified: | May 25, 2022 | |
This is version 178 of the entry and version 2 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