UniProtKB - P03305 (POLG_FMDVO)

BLAST

>sp|P03305|POLG_FMDVO Genome polyprotein OS=Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) OX=73482 PE=1 SV=1
MNTTDCFIALVQAIREIKALFLSRTTGKMELTLYNGEKKTFYSRPNNHDNCWLNAILQLF
RYVEEPFFDWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIKHLLHTGIGTASR
PSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVF
VPYDQEPLNGEWKAKVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLG
DNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRI
LTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDS
FGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELYSIQK
RELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGA
PQIKVYANIAPTNVHVAGEFPSKEGIFPVACSDGYGGLVTTDPKTADPVYGKVFNPPRNQ
LPGRFTNLLDVAEACPTFLRFEGGVPYVTTKTDSDRVLAQFDMSLAAKQMSNTFLAGLAQ
YYTQYSGTINLHFMFTGPTDAKARYMVAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFT
FSIPYLSAADYAYTASGVAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVD
ARAETTSAGESADPVTTTVENYGGETQIQRRQHTDVSFIMDRFVKVTPQNQINILDLMQI
PSHTLVGALLRASTYYFSDLEIAVKHEGDLTWVPNGAPEKALDNTTNPTAYHKAPLTRLA
LPYTAPHRVLATVYNGECRYNRNAVPNLRGDLQVLAQKVARTLPTSFNYGAIKATRVTEL
LYRMKRAETYCPRPLLAIHPTEARHKQKIVAPVKQTLNFDLLKLAGDVESNPGPFFFSDV
RSNFSKLVETINQMQEDMSTKHGPDFNRLVSAFEELAIGVKAIRTGLDEAKPWYKLIKLL
SRLSCMAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKISDSLSSLFHVPAPVFSFGAP
VLLAGLVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAW
IASEEKFVTMTDLVPGILEKQRDLNDPSKYKEAKEWLDNARQACLKSGNVHIANLCKVVA
PAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRIDSVWYCPPDPDHFDGYNQ
QTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFT
PRTMVCPDALNRRFHFDIDVSAKDGYKINSKLDIIKALEDTHANPVAMFQYDCALLNGMA
VEMKRMQQDMFKPQPPLQNVYQLVQEVIDRVELHEKVSSHPIFKQISIPSQKSVLYFLIE
KGQHEAAIEFFEGMVHDSIKEELRPLIQQTSFVKRAFKRLKENFEIVALCLTLLANIVIM
IRETRKRQKMVDDAVNEYIEKANITTDDKTLDEAEKSPLETSGASTVGFRERTLPGQKAC
DDVNSEPAQPVEEQPQAEGPYAGPLERQKPLKVRAKLPQQEGPYAGPMERQKPLKVKAKA
PVVKEGPYEGPVKKPVALKVKAKNLIVTESGAPPTDLQKMVMGNTKPVELILDGKTVAIC
CATGVFGTAYLVPRHLFAEKYDKIMVDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLH
RGNRVRDITKHFRDTARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGL
FAYRAATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLLKMKAHIDPEPH
HEGLIVDTRDVEERVHVMRKTKLAPTVAHGVFNPEFGPAALSNKDPRLNEGVVLDEVIFS
KHKGDTKMSEEDKALFRRCAADYASRLHSVLGTANAPLSIYEAIKGVDGLDAMEPDTAPG
LPWALQGKRRGALIDFENGTVGPEVEAALKLMEKREYKFVCQTFLKDEIRPLEKVRAGKT
RIVDVLPVEHILYTRMMIGRFCAQMHSNNGPQIGSAVGCNPDVDWQRFGTHFAQYRNVWD
VDYSAFDANHCSDAMNIMFEEVFRTEFGFHPNAEWILKTLVNTEHAYENKRITVGGGMPS
GCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFK
SLGQTITPADKSDKGFVLGHSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRG
TIQEKLISVAGLAVHSGPDEYRRLFEPFQGLFEIPSYRSLYLRWVNAVCGDA

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History
Entry version 184 (10 Oct 2018)
Sequence version 1 (21 Jul 1986)
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Protein

Genome polyprotein

Gene

N/A

Organism

Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Leader protease: 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.6 Publications

Capsid protein VP4: Lies 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 similarity

Capsid protein VP2: Forms 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 Publication

Capsid 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 Publications

Capsid 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 Publication

Protein 2A: Mediates 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 Publication

Protein 2B: Plays 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 Publication

Protein 2C: Associates 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 Publications

Protein 3A: Plays important roles in virus replication, virulence and host range.2 Publications

Protein 3B-1: Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.1 Publication

Protein 3B-2: Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.1 Publication

Protein 3B-3: Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.1 Publication

Protease 3C: Cysteine 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 Publication

RNA-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 Publication

Miscellaneous

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.

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).PROSITE-ProRule annotation

Sites

Feature key	Position(s)	DescriptionActions	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 picornain 3C activity; Proton donor/acceptorSequence analysisBy similarity	1
Active siteⁱ	1733	For picornain 3C activityBy similarity	1
Active siteⁱ	1812	For picornain 3C activitySequence analysisBy 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: InterPro
ion channel activity Source: UniProtKB-KW
ISG15-specific protease activity
Source: UniProtKB
Inferred from direct assayⁱ
- 29463763
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

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
induction by virus of host autophagy
Source: UniProtKB
Inferred from direct assayⁱ
- 22993157
modulation by virus of host chromatin organization Source: UniProtKB-KW
modulation by virus of host protein ubiquitination
Source: UniProtKB
Inferred from direct assayⁱ
- 21307201
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
Inferred from direct assayⁱ
- 29463763
regulation of translation Source: UniProtKB-KW
RNA-protein covalent cross-linking Source: UniProtKB-KW
suppression by virus of host ISG15 activity
Source: UniProtKB
Inferred from direct assayⁱ
- 29463763
suppression by virus of host NF-kappaB transcription factor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 17881445
suppression by virus of host translation initiation factor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11034318
suppression by virus of host type I interferon-mediated signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 17881445
transcription, DNA-templated Source: InterPro
viral protein processing Source: InterPro
viral RNA genome replication Source: InterPro
virion attachment to host cell Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological process	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, Translation regulation, Transport, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	3.4.22.46 2315

BRENDAⁱ

3.4.22.46 2315

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	C03.008

MEROPSⁱ

C03.008

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Genome polyprotein Cleaved into the following 15 chains: Leader protease (EC:3.4.22.461 Publication) Short name: Lb(pro) Capsid protein VP0 Alternative name(s): VP4-VP2 Capsid protein VP4 Alternative name(s): P1A Virion protein 4 Capsid protein VP2 Alternative name(s): P1B Virion protein 2 Capsid protein VP3 Alternative name(s): P1C Virion protein 3 Capsid protein VP1 Alternative name(s): P1D Virion protein 1 Protein 2A Short name: P2A Alternative name(s): P52 Protein 2B Short name: P2B Protein 2C (EC:3.6.1.15) Short name: P2C Protein 3A Short name: P3A Protein 3B-1 Short name: P3B-1 Alternative name(s): Genome-linked protein VPg1 Protein 3B-2 Short name: P3B-2 Alternative name(s): Genome-linked protein VPg2 Protein 3B-3 Short name: P3B-3 Alternative name(s): Genome-linked protein VPg3 Protease 3C (EC:3.4.22.281 Publication) Alternative name(s): Picornain 3C Short name: P3C Protease P20B RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48) Short name: P3D-POL 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 › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Aphthovirus › Foot-and-mouth disease virus › Foot-and-mouth disease virus - type O
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	UP000008765 Componentⁱ: Genome

Subcellular locationⁱ

Protein 2B :

Host endoplasmic reticulum membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.24
  "Viroporin Activity of the Foot-and-Mouth Disease Virus Non-Structural 2B Protein."
  Ao D., Guo H.C., Sun S.Q., Sun D.H., Fung T.S., Wei Y.Q., Han S.C., Yao X.P., Cao S.Z., Liu D.X., Liu X.T.
  PLoS ONE 10:E0125828-E0125828(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION (PROTEIN 2B), SUBUNIT (PROTEIN 2B), SUBCELLULAR LOCATION (PROTEIN 2B), TOPOLOGY (PROTEIN 2B).

Protein 2C :

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

Protein 3A :

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

Protein 3B-1 :

Virion Curated

Protein 3B-2 :

Virion Curated

Protein 3B-3 :

Virion Curated

Protease 3C :

Host cytoplasm Curated

RNA-directed RNA polymerase 3D-POL :

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 1480	CytoplasmicSequence analysisAdd BLAST	1480
Intramembraneⁱ	1481 – 1501	Sequence analysisAdd BLAST	21
Topological domainⁱ	1502 – 2332	CytoplasmicSequence analysisAdd BLAST	831

GO - Cellular componentⁱ

host cell cytoplasm
Source: UniProtKB
Inferred from direct assayⁱ
- 17881445
host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
host cell nucleus
Source: UniProtKB
Inferred from direct assayⁱ
- 17881445
icosahedral viral capsid Source: InterPro
integral to membrane of host cell Source: UniProtKB-KW
membrane Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Virion

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	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	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

Leader protease: Removes six residues from its own C-terminus, generating sLb(pro).1 Publication

Genome polyprotein: 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.1 Publication

Capsid protein VP4: Myristoylation is required during RNA encapsidation and formation of the mature virus particle.By similarity

Protein 3B-1: 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.1 Publication

Protein 3B-2: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.1 Publication

Protein 3B-3: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.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	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, Phosphoprotein

Proteomic databases

PRIDEⁱ	P03305

PRIDEⁱ

P03305

Interactionⁱ

Subunit structureⁱ

Leader protease: Interacts with host ISG15 (PubMed:29463763). Capsid protein VP1: Interacts (via R-G-D motif) with host ITGAV/ITGB6 (PubMed:28534487). Protein 2B: Forms homooligomers. Protein 2C: Interacts with host VIM (PubMed:23576498). Interacts with host BECN1 (PubMed:22933281). Protein 3A: Interacts with host DCTN3 (PubMed:24352458).6 Publications

Protein-protein interaction databases

ELMⁱ	P03305

ELMⁱ

P03305

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	30 – 33	Combined sources	4
Beta strandⁱ	38 – 40	Combined sources	3
Beta strandⁱ	47 – 49	Combined sources	3
Helixⁱ	51 – 63	Combined sources	13
Helixⁱ	66 – 68	Combined sources	3
Helixⁱ	69 – 72	Combined sources	4
Beta strandⁱ	73 – 76	Combined sources	4
Helixⁱ	79 – 90	Combined sources	12
Helixⁱ	100 – 107	Combined sources	8
Helixⁱ	108 – 110	Combined sources	3
Beta strandⁱ	111 – 113	Combined sources	3
Beta strandⁱ	115 – 120	Combined sources	6
Beta strandⁱ	123 – 126	Combined sources	4
Beta strandⁱ	129 – 131	Combined sources	3
Helixⁱ	134 – 136	Combined sources	3
Beta strandⁱ	137 – 143	Combined sources	7
Beta strandⁱ	145 – 147	Combined sources	3
Beta strandⁱ	149 – 155	Combined sources	7
Beta strandⁱ	158 – 163	Combined sources	6
Beta strandⁱ	166 – 169	Combined sources	4
Helixⁱ	174 – 176	Combined sources	3
Beta strandⁱ	177 – 182	Combined sources	6
Turnⁱ	195 – 197	Combined sources	3
Helixⁱ	229 – 232	Combined sources	4
Helixⁱ	268 – 274	Combined sources	7
Helixⁱ	297 – 299	Combined sources	3
Beta strandⁱ	301 – 305	Combined sources	5
Beta strandⁱ	308 – 314	Combined sources	7
Helixⁱ	332 – 334	Combined sources	3
Helixⁱ	342 – 344	Combined sources	3
Beta strandⁱ	348 – 355	Combined sources	8
Beta strandⁱ	364 – 370	Combined sources	7
Helixⁱ	376 – 383	Combined sources	8
Beta strandⁱ	384 – 397	Combined sources	14
Beta strandⁱ	404 – 413	Combined sources	10
Helixⁱ	421 – 428	Combined sources	8
Beta strandⁱ	429 – 434	Combined sources	6
Turnⁱ	436 – 438	Combined sources	3
Beta strandⁱ	440 – 446	Combined sources	7
Beta strandⁱ	451 – 455	Combined sources	5
Turnⁱ	457 – 459	Combined sources	3
Beta strandⁱ	463 – 474	Combined sources	12
Turnⁱ	476 – 478	Combined sources	3
Beta strandⁱ	483 – 499	Combined sources	17
Helixⁱ	548 – 554	Combined sources	7
Turnⁱ	562 – 564	Combined sources	3
Beta strandⁱ	565 – 569	Combined sources	5
Beta strandⁱ	577 – 583	Combined sources	7
Helixⁱ	588 – 590	Combined sources	3
Helixⁱ	594 – 599	Combined sources	6
Beta strandⁱ	602 – 607	Combined sources	6
Beta strandⁱ	609 – 615	Combined sources	7
Beta strandⁱ	622 – 630	Combined sources	9
Helixⁱ	640 – 643	Combined sources	4
Beta strandⁱ	646 – 652	Combined sources	7
Beta strandⁱ	658 – 663	Combined sources	6
Beta strandⁱ	668 – 670	Combined sources	3
Beta strandⁱ	672 – 675	Combined sources	4
Beta strandⁱ	687 – 697	Combined sources	11
Beta strandⁱ	702 – 709	Combined sources	8
Beta strandⁱ	714 – 718	Combined sources	5
Helixⁱ	739 – 742	Combined sources	4
Helixⁱ	752 – 754	Combined sources	3
Helixⁱ	756 – 760	Combined sources	5
Beta strandⁱ	762 – 766	Combined sources	5
Helixⁱ	777 – 779	Combined sources	3
Helixⁱ	785 – 791	Combined sources	7
Beta strandⁱ	793 – 808	Combined sources	16
Beta strandⁱ	810 – 813	Combined sources	4
Helixⁱ	819 – 823	Combined sources	5
Beta strandⁱ	827 – 830	Combined sources	4
Beta strandⁱ	837 – 841	Combined sources	5
Beta strandⁱ	846 – 852	Combined sources	7
Beta strandⁱ	891 – 893	Combined sources	3
Beta strandⁱ	895 – 912	Combined sources	18
Beta strandⁱ	921 – 924	Combined sources	4

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00573
ProteinModelPortalⁱ	P03305
SMRⁱ	P03305
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P03305

EvolutionaryTraceⁱ

P03305

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	1 – 201	Peptidase C28Add BLAST	201
Domainⁱ	1189 – 1353	SF3 helicasePROSITE-ProRule annotationAdd BLAST	165
Domainⁱ	1652 – 1836	Peptidase C3Add BLAST	185
Domainⁱ	2096 – 2214	RdRp catalyticPROSITE-ProRule annotationAdd BLAST	119

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

Sequence similaritiesⁱ

Belongs to the picornaviruses polyprotein family.Curated

Phylogenomic databases

Database of Orthologous Groups More...OrthoDBⁱ	VOG090000RV

OrthoDBⁱ

VOG090000RV

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00205 rhv_like, 3 hits
Gene3Dⁱ	2.60.120.20, 3 hits 4.10.90.10, 1 hit
InterProⁱ	View protein in InterPro IPR015031 Capsid_VP4_Picornavir IPR037080 Capsid_VP4_sf_Picornavirus 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 IPR008739 Peptidase_C28 IPR000199 Peptidase_C3A/C3B_picornavir IPR009003 Peptidase_S1_PA IPR001676 Picornavirus_capsid IPR033703 Rhv-like IPR001205 RNA-dir_pol_C IPR007094 RNA-dir_pol_PSvirus IPR029053 Viral_coat
Pfam protein domain database More...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
PROSITEⁱ	View protein in PROSITE PS50507 RDRP_SSRNA_POS, 1 hit PS51218 SF3_HELICASE_2, 1 hit

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 Add to basket

Isoform Lab (identifier: P03305-1) [UniParc]FASTA Add 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

        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

Length:2,332

Mass (Da):258,927

Last modified:July 21, 1986 - v1

Checksum:ⁱ4A83176F43447D68

Isoform Lb (identifier: P03305-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MELTLYNGEK KTFYSRPNNH DNCWLNAILQ LFRYVEEPFF DWVYSSPENL 
        60         70         80         90        100
TLEAIKQLED LTGLELHEGG PPALVIWNIK HLLHTGIGTA SRPSEVCMVD 
       110        120        130        140        150
GTDMCLADFH AGIFLKGQEH AVFACVTSNG WYAIDDEDFY PWTPDPSDVL 
       160        170        180        190        200
VFVPYDQEPL NGEWKAKVQR KLKGAGQSSP ATGSQNQSGN TGSIINNYYM 
       210        220        230        240        250
QQYQNSMDTQ LGDNAISGGS NEGSTDTTST HTTNTQNNDW FSKLASSAFS 
       260        270        280        290        300
GLFGALLADK KTEETTLLED RILTTRNGHT TSTTQSSVGV TYGYATAEDF 
       310        320        330        340        350
VSGPNTSGLE TRVVQAERFF KTHLFDWVTS DSFGRCHLLE LPTDHKGVYG 
       360        370        380        390        400
SLTDSYAYMR NGWDVEVTAV GNQFNGGCLL VAMVPELYSI QKRELYQLTL 
       410        420        430        440        450
FPHQFINPRT NMTAHITVPF VGVNRYDQYK VHKPWTLVVM VVAPLTVNTE 
       460        470        480        490        500
GAPQIKVYAN IAPTNVHVAG EFPSKEGIFP VACSDGYGGL VTTDPKTADP 
       510        520        530        540        550
VYGKVFNPPR NQLPGRFTNL LDVAEACPTF LRFEGGVPYV TTKTDSDRVL 
       560        570        580        590        600
AQFDMSLAAK QMSNTFLAGL AQYYTQYSGT INLHFMFTGP TDAKARYMVA 
       610        620        630        640        650
YAPPGMEPPK TPEAAAHCIH AEWDTGLNSK FTFSIPYLSA ADYAYTASGV 
       660        670        680        690        700
AETTNVQGWV CLFQITHGKA DGDALVVLAS AGKDFELRLP VDARAETTSA 
       710        720        730        740        750
GESADPVTTT VENYGGETQI QRRQHTDVSF IMDRFVKVTP QNQINILDLM 
       760        770        780        790        800
QIPSHTLVGA LLRASTYYFS DLEIAVKHEG DLTWVPNGAP EKALDNTTNP 
       810        820        830        840        850
TAYHKAPLTR LALPYTAPHR VLATVYNGEC RYNRNAVPNL RGDLQVLAQK 
       860        870        880        890        900
VARTLPTSFN YGAIKATRVT ELLYRMKRAE TYCPRPLLAI HPTEARHKQK 
       910        920        930        940        950
IVAPVKQTLN FDLLKLAGDV ESNPGPFFFS DVRSNFSKLV ETINQMQEDM 
       960        970        980        990       1000
STKHGPDFNR LVSAFEELAI GVKAIRTGLD EAKPWYKLIK LLSRLSCMAA 
      1010       1020       1030       1040       1050
VAARSKDPVL VAIMLADTGL EILDSTFVVK KISDSLSSLF HVPAPVFSFG 
      1060       1070       1080       1090       1100
APVLLAGLVK VASSFFRSTP EDLERAEKQL KARDINDIFA ILKNGEWLVK 
      1110       1120       1130       1140       1150
LILAIRDWIK AWIASEEKFV TMTDLVPGIL EKQRDLNDPS KYKEAKEWLD 
      1160       1170       1180       1190       1200
NARQACLKSG NVHIANLCKV VAPAPSKSRP EPVVVCLRGK SGQGKSFLAN 
      1210       1220       1230       1240       1250
VLAQAISTHF TGRIDSVWYC PPDPDHFDGY NQQTVVVMDD LGQNPDGKDF 
      1260       1270       1280       1290       1300
KYFAQMVSTT GFIPPMASLE DKGKPFNSKV IIATTNLYSG FTPRTMVCPD 
      1310       1320       1330       1340       1350
ALNRRFHFDI DVSAKDGYKI NSKLDIIKAL EDTHANPVAM FQYDCALLNG 
      1360       1370       1380       1390       1400
MAVEMKRMQQ DMFKPQPPLQ NVYQLVQEVI DRVELHEKVS SHPIFKQISI 
      1410       1420       1430       1440       1450
PSQKSVLYFL IEKGQHEAAI EFFEGMVHDS IKEELRPLIQ QTSFVKRAFK 
      1460       1470       1480       1490       1500
RLKENFEIVA LCLTLLANIV IMIRETRKRQ KMVDDAVNEY IEKANITTDD 
      1510       1520       1530       1540       1550
KTLDEAEKSP LETSGASTVG FRERTLPGQK ACDDVNSEPA QPVEEQPQAE 
      1560       1570       1580       1590       1600
GPYAGPLERQ KPLKVRAKLP QQEGPYAGPM ERQKPLKVKA KAPVVKEGPY 
      1610       1620       1630       1640       1650
EGPVKKPVAL KVKAKNLIVT ESGAPPTDLQ KMVMGNTKPV ELILDGKTVA 
      1660       1670       1680       1690       1700
ICCATGVFGT AYLVPRHLFA EKYDKIMVDG RAMTDSDYRV FEFEIKVKGQ 
      1710       1720       1730       1740       1750
DMLSDAALMV LHRGNRVRDI TKHFRDTARM KKGTPVVGVI NNADVGRLIF 
      1760       1770       1780       1790       1800
SGEALTYKDI VVCMDGDTMP GLFAYRAATK AGYCGGAVLA KDGADTFIVG 
      1810       1820       1830       1840       1850
THSAGGNGVG YCSCVSRSML LKMKAHIDPE PHHEGLIVDT RDVEERVHVM 
      1860       1870       1880       1890       1900
RKTKLAPTVA HGVFNPEFGP AALSNKDPRL NEGVVLDEVI FSKHKGDTKM 
      1910       1920       1930       1940       1950
SEEDKALFRR CAADYASRLH SVLGTANAPL SIYEAIKGVD GLDAMEPDTA 
      1960       1970       1980       1990       2000
PGLPWALQGK RRGALIDFEN GTVGPEVEAA LKLMEKREYK FVCQTFLKDE 
      2010       2020       2030       2040       2050
IRPLEKVRAG KTRIVDVLPV EHILYTRMMI GRFCAQMHSN NGPQIGSAVG 
      2060       2070       2080       2090       2100
CNPDVDWQRF GTHFAQYRNV WDVDYSAFDA NHCSDAMNIM FEEVFRTEFG 
      2110       2120       2130       2140       2150
FHPNAEWILK TLVNTEHAYE NKRITVGGGM PSGCSATSII NTILNNIYVL 
      2160       2170       2180       2190       2200
YALRRHYEGV ELDTYTMISY GDDIVVASDY DLDFEALKPH FKSLGQTITP 
      2210       2220       2230       2240       2250
ADKSDKGFVL GHSITDVTFL KRHFHMDYGT GFYKPVMASK TLEAILSFAR 
      2260       2270       2280       2290       2300
RGTIQEKLIS VAGLAVHSGP DEYRRLFEPF QGLFEIPSYR SLYLRWVNAV 

CGDA

Show »

Length:2,304

Mass (Da):255,803

Checksum:ⁱ5372D197CC761349

Natural variant

Feature key	Position(s)	DescriptionActions	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

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

KEGGⁱ

ag:CAA25416

Keywords - Coding sequence diversityⁱ

Alternative initiation

Protein	Similar proteins		Species	Score	Length	Source
P03305	Isoform Lb of Genome polyprotein		FMDVO		2304	UniRef100_P03305
Polyprotein (Fragment)		Foot-and-mouth disease virus - type O		88
Capsid protein VP1 (Fragment)		Foot-and-mouth disease virus O/IND463/97		52
Capsid protein VP1 (Fragment)		Foot-and-mouth disease virus O/IND146/99		52
Foot and mouth disease virus VP1 (Fragment)		Foot-and-mouth disease virus		387
+8

Protein	Similar proteins		Species	Score	Length	Source
P03305	Genome polyprotein	)	FMDVZ		2336	UniRef90_P03305
Genome polyprotein	)	FMDVA		2333
Genome polyprotein		FMDVC		2333
Genome polyprotein	)	FMDV1		2332
Genome polyprotein		FMDV5		2332
+1398

Protein	Similar proteins		Species	Score	Length	Source
P03305	Genome polyprotein	)	FMDVZ		2336	UniRef50_P03305
Genome polyprotein		FMDVC		2333
Genome polyprotein	)	FMDVA		2333
Genome polyprotein	)	FMDV1		2332
Genome polyprotein		FMDV5		2332
+1599

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

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
DisProtⁱ	DP00573
ProteinModelPortalⁱ	P03305
SMRⁱ	P03305
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

ELMⁱ	P03305

ELMⁱ

P03305

Protein family/group databases

MEROPSⁱ	C03.008

MEROPSⁱ

C03.008

Proteomic databases

PRIDEⁱ	P03305

PRIDEⁱ

P03305

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

KEGGⁱ	ag:CAA25416

KEGGⁱ

ag:CAA25416

Phylogenomic databases

OrthoDBⁱ	VOG090000RV

OrthoDBⁱ

VOG090000RV

Enzyme and pathway databases

BRENDAⁱ	3.4.22.46 2315

BRENDAⁱ

3.4.22.46 2315

Miscellaneous databases

EvolutionaryTraceⁱ	P03305

EvolutionaryTraceⁱ

P03305

Family and domain databases

CDDⁱ	cd00205 rhv_like, 3 hits
Gene3Dⁱ	2.60.120.20, 3 hits 4.10.90.10, 1 hit
InterProⁱ	View protein in InterPro IPR015031 Capsid_VP4_Picornavir IPR037080 Capsid_VP4_sf_Picornavirus 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 IPR008739 Peptidase_C28 IPR000199 Peptidase_C3A/C3B_picornavir IPR009003 Peptidase_S1_PA IPR001676 Picornavirus_capsid 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
PROSITEⁱ	View protein in PROSITE PS50507 RDRP_SSRNA_POS, 1 hit PS51218 SF3_HELICASE_2, 1 hit
ProtoNetⁱ	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:	October 10, 2018
	This is version 184 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P03305 (POLG_FMDVO)

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Genome polyprotein

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

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<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ