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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription. Increases translation driven by the viral internal ribosome entry site (IRES) (By similarity).By similarity3 Publications
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.
Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).By similarity
Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei51For leader protease activity1
Active sitei148For leader protease activity1
Active sitei163For leader protease activity1
Active sitei1695For picornain 3C activity; Proton donor/acceptorSequence analysisBy similarity1
Active sitei1733For picornain 3C activityBy similarity1
Active sitei1812For picornain 3C activitySequence analysisBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1217 – 1224ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Clathrin- and caveolin-independent endocytosis of virus by host, Clathrin-mediated endocytosis of virus by host, Host-virus interaction, Ion transport, Modulation of host chromatin by virus, 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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BRENDAi3.4.22.46. 2315.

Protein family/group databases

MEROPSiC03.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 15 chains:
Leader protease (EC:3.4.22.46)
Short name:
Lpro
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
P52
Protein 2B
Short name:
P2B
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
Alternative name(s):
Protease 3C
Short name:
P3C
Protease P20B
Alternative name(s):
P56A
OrganismiFoot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)
Taxonomic identifieri73482 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeAphthovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Capra hircus (Goat) [TaxID: 9925]
Cervidae (deer) [TaxID: 9850]
Erinaceidae (hedgehogs) [TaxID: 9363]
Loxodonta africana (African elephant) [TaxID: 9785]
Ovis aries (Sheep) [TaxID: 9940]
Rattus norvegicus (Rat) [TaxID: 10116]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008765 Componenti: Genome

Subcellular locationi

Protein 2B :
Protein 2C :
Protein 3A :
RNA-directed RNA polymerase 3D-POL :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1480CytoplasmicSequence analysisAdd BLAST1480
Intramembranei1481 – 1501Sequence analysisAdd BLAST21
Topological domaini1502 – 2332CytoplasmicSequence analysisAdd BLAST831

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000398721 – 2332Genome polyproteinAdd BLAST2332
ChainiPRO_00000398731 – 201Leader proteaseAdd BLAST201
ChainiPRO_0000374076202 – 504Protein VP0Sequence analysisAdd BLAST303
ChainiPRO_0000039876202 – 286Protein VP4Sequence analysisAdd BLAST85
ChainiPRO_0000039877287 – 504Protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039878505 – 724Protein VP3Sequence analysisAdd BLAST220
ChainiPRO_0000039879725 – 935Protein VP1Add BLAST211
ChainiPRO_0000039880936 – 953Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000310976954 – 1107Protein 2BSequence analysisAdd BLAST154
ChainiPRO_00000398811108 – 1425Protein 2CSequence analysisAdd BLAST318
ChainiPRO_00000398821426 – 1578Protein 3ASequence analysisAdd BLAST153
ChainiPRO_00000398831579 – 1601Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_00003109771602 – 1625Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_00003109781626 – 1649Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00000398841650 – 1862Picornain 3CSequence analysisAdd BLAST213
ChainiPRO_00000398851863 – 2332RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi202N-myristoyl glycine; by hostBy similarity1
Disulfide bondi406 ↔ 858Interchain (between VP2 and VP1 chains)
Disulfide bondi511Interchain; in VP3 dimer
Modified residuei1581O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1604O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1628O-(5'-phospho-RNA)-tyrosineBy similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei201 – 202Cleavage; by leader proteaseSequence analysis2
Sitei286 – 287CleavageSequence analysis2
Sitei504 – 505Cleavage; by picornain 3CSequence analysis2
Sitei724 – 725Cleavage; by picornain 3CSequence analysis2
Sitei935 – 936Cleavage; by picornain 3CSequence analysis2
Sitei953 – 954Cleavage; by ribosomal skipSequence analysis2
Sitei1107 – 1108Cleavage; by picornain 3CSequence analysis2
Sitei1425 – 1426Cleavage; by picornain 3CSequence analysis2
Sitei1578 – 1579Cleavage; by picornain 3CSequence analysis2
Sitei1601 – 1602Cleavage; by picornain 3CSequence analysis2
Sitei1625 – 1626Cleavage; by picornain 3CSequence analysis2
Sitei1649 – 1650Cleavage; by picornain 3CSequence analysis2
Sitei1862 – 1863Cleavage; by picornain 3CSequence analysis2

Keywords - PTMi

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

Interactioni

Subunit structurei

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

Structurei

Secondary structure

12332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi47 – 49Combined sources3
Helixi51 – 63Combined sources13
Helixi66 – 68Combined sources3
Helixi69 – 72Combined sources4
Beta strandi73 – 76Combined sources4
Helixi79 – 90Combined sources12
Helixi100 – 106Combined sources7
Helixi107 – 110Combined sources4
Beta strandi111 – 113Combined sources3
Beta strandi115 – 120Combined sources6
Beta strandi123 – 126Combined sources4
Beta strandi129 – 131Combined sources3
Helixi134 – 136Combined sources3
Beta strandi137 – 145Combined sources9
Beta strandi149 – 153Combined sources5
Beta strandi158 – 163Combined sources6
Beta strandi166 – 169Combined sources4
Helixi174 – 176Combined sources3
Beta strandi177 – 185Combined sources9
Turni195 – 197Combined sources3
Helixi229 – 232Combined sources4
Helixi268 – 274Combined sources7
Helixi297 – 299Combined sources3
Beta strandi301 – 305Combined sources5
Beta strandi308 – 314Combined sources7
Helixi332 – 334Combined sources3
Helixi342 – 344Combined sources3
Beta strandi348 – 355Combined sources8
Beta strandi364 – 370Combined sources7
Helixi376 – 383Combined sources8
Beta strandi384 – 397Combined sources14
Beta strandi404 – 413Combined sources10
Helixi421 – 428Combined sources8
Beta strandi429 – 434Combined sources6
Turni436 – 438Combined sources3
Beta strandi440 – 446Combined sources7
Beta strandi451 – 455Combined sources5
Turni457 – 459Combined sources3
Beta strandi463 – 474Combined sources12
Turni476 – 478Combined sources3
Beta strandi483 – 499Combined sources17
Helixi548 – 554Combined sources7
Turni562 – 564Combined sources3
Beta strandi565 – 569Combined sources5
Beta strandi577 – 583Combined sources7
Helixi588 – 590Combined sources3
Helixi594 – 599Combined sources6
Beta strandi602 – 607Combined sources6
Beta strandi609 – 615Combined sources7
Beta strandi622 – 630Combined sources9
Helixi640 – 643Combined sources4
Beta strandi646 – 652Combined sources7
Beta strandi658 – 663Combined sources6
Beta strandi668 – 670Combined sources3
Beta strandi672 – 675Combined sources4
Beta strandi687 – 697Combined sources11
Beta strandi702 – 709Combined sources8
Beta strandi714 – 718Combined sources5
Helixi739 – 742Combined sources4
Helixi752 – 754Combined sources3
Helixi756 – 760Combined sources5
Beta strandi762 – 766Combined sources5
Helixi777 – 779Combined sources3
Helixi785 – 791Combined sources7
Beta strandi793 – 808Combined sources16
Beta strandi810 – 813Combined sources4
Helixi819 – 823Combined sources5
Beta strandi827 – 830Combined sources4
Beta strandi837 – 841Combined sources5
Beta strandi846 – 852Combined sources7
Beta strandi891 – 893Combined sources3
Beta strandi895 – 912Combined sources18
Beta strandi921 – 924Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QMYX-ray1.90A/B/C29-195[»]
1QOLX-ray3.00A/B/C/D/E/F/G/H29-201[»]
1QQPX-ray1.901725-937[»]
2287-504[»]
3505-724[»]
4202-286[»]
2JQFNMR-R/S29-201[»]
2JQGNMR-R29-195[»]
4QBBX-ray1.60A/B/C29-195[»]
DisProtiDP00573.
ProteinModelPortaliP03305.
SMRiP03305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03305.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 201Peptidase C28Add BLAST201
Domaini1189 – 1353SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1652 – 1836Peptidase C3Add BLAST185
Domaini2096 – 2214RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi869 – 871Cell attachment siteBy similarity3

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C28 domain.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 2 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004080. FMDV_VP1_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR008739. Peptidase_C28.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF05408. Peptidase_C28. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Lab (identifier: P03305-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
GO
Isoform Lb (identifier: P03305-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,304
Mass (Da):255,803
Checksum:i5372D197CC761349
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti780I → V in strain: Isolate O1BFS. 1
Natural varianti808G → R in strain: Isolate O1BFS. 1
Natural varianti861N → S in strain: Isolate O1BFS. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189821 – 28Missing in isoform Lb. CuratedAdd BLAST28

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

KEGGiag:CAA25416.

Keywords - Coding sequence diversityi

Alternative initiation

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 entryMethodResolution (Å)ChainPositionsPDBsum
1QMYX-ray1.90A/B/C29-195[»]
1QOLX-ray3.00A/B/C/D/E/F/G/H29-201[»]
1QQPX-ray1.901725-937[»]
2287-504[»]
3505-724[»]
4202-286[»]
2JQFNMR-R/S29-201[»]
2JQGNMR-R29-195[»]
4QBBX-ray1.60A/B/C29-195[»]
DisProtiDP00573.
ProteinModelPortaliP03305.
SMRiP03305.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA25416.

Enzyme and pathway databases

BRENDAi3.4.22.46. 2315.

Miscellaneous databases

EvolutionaryTraceiP03305.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 2 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004080. FMDV_VP1_coat.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR008739. Peptidase_C28.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF05408. Peptidase_C28. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_FMDVO
AccessioniPrimary (citable) accession number: P03305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The capsid protein VP1 contains the main antigenic determinants of the virion; therefore, changes in its sequence must be responsible for the high antigenic variability of the virus.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.