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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate -/Azerbaijan/A22-550/1965 serotype A) (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 cleaves the host translation initiation factors 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
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta6, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity).By similarity
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 activityBy similarity1
Active sitei148For leader protease activityBy similarity1
Active sitei163For leader protease activityBy similarity1
Active sitei1696For picornain 3C activity; Proton donor/acceptorSequence analysisBy similarity1
Active sitei1734For picornain 3C activityBy similarity1
Active sitei1813For picornain 3C activitySequence analysisBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1218 – 1225ATPPROSITE-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-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

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 -/Azerbaijan/A22-550/1965 serotype A) (FMDV)
Taxonomic identifieri73481 [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
  • UP000008621 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1481CytoplasmicSequence analysisAdd BLAST1481
Intramembranei1482 – 1502Sequence analysisAdd BLAST21
Topological domaini1503 – 2336CytoplasmicSequence analysisAdd BLAST834

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_00000398501 – 2336Genome polyproteinAdd BLAST2336
ChainiPRO_00000398511 – 201Leader proteaseAdd BLAST201
ChainiPRO_0000374075202 – 504Protein VP0Sequence analysisAdd BLAST303
ChainiPRO_0000039854202 – 286Protein VP4Sequence analysisAdd BLAST85
ChainiPRO_0000039855287 – 504Protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039856505 – 725Protein VP3Sequence analysisAdd BLAST221
ChainiPRO_0000039857726 – 936Protein VP1Sequence analysisAdd BLAST211
ChainiPRO_0000039858937 – 954Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000039859955 – 1108Protein 2BSequence analysisAdd BLAST154
ChainiPRO_00000398601109 – 1426Protein 2CSequence analysisAdd BLAST318
ChainiPRO_00000398611427 – 1579Protein 3ASequence analysisAdd BLAST153
ChainiPRO_00000398621580 – 1602Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_00000398631603 – 1626Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_00000398641627 – 1650Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00000398651651 – 1863Picornain 3CSequence analysisAdd BLAST213
ChainiPRO_00000398661864 – 2336RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi202N-myristoyl glycine; by hostBy similarity1
Disulfide bondi511Interchain; in VP3 dimer
Modified residuei1582O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1605O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1629O-(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
Sitei725 – 726Cleavage; by picornain 3CSequence analysis2
Sitei936 – 937Cleavage; by picornain 3CSequence analysis2
Sitei954 – 955Cleavage; by ribosomal skipSequence analysis2
Sitei1108 – 1109Cleavage; by picornain 3CSequence analysis2
Sitei1426 – 1427Cleavage; by picornain 3CSequence analysis2
Sitei1579 – 1580Cleavage; by picornain 3CSequence analysis2
Sitei1602 – 1603Cleavage; by picornain 3CSequence analysis2
Sitei1626 – 1627Cleavage; by picornain 3CSequence analysis2
Sitei1650 – 1651Cleavage; by picornain 3CSequence analysis2
Sitei1863 – 1864Cleavage; 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.By similarity

Structurei

Secondary structure

12336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi229 – 232Combined sources4
Helixi269 – 274Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FMDX-ray3.504202-286[»]
ProteinModelPortaliP49303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 201Peptidase C28Add BLAST201
Domaini1190 – 1354SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1653 – 1837Peptidase C3Add BLAST185
Domaini2097 – 2215RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi869 – 871Cell attachment site3

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: P49303-1) [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 LYALREIKAF LLSRTQGKME LTLYNGEKKT FYSRPNNHDN
60 70 80 90 100
CWLNTILQLF RYVDEPFFDW VYDSPENLTC EAIRQLEEIT GLELHEGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV
160 170 180 190 200
FACVTSDGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQKRL
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 GYSTQEDHVS GPNTSGLETR VVQAERFFKK
360 370 380 390 400
YLFDWTPDKA FGHLEKLELP TDHKGVYGHL VDSFAYMRNG WDVEVSAVGN
410 420 430 440 450
QFNGGCLLVA MVPEWKELTP REKYQLTLFP HQFISPRTNM TAHIVVPYLG
460 470 480 490 500
VNRYDQYKKH KPWTLVVMVV SPLTTNTVSA GQIKVYANIA PTHVHVAGEL
510 520 530 540 550
PSKEGIVPVA CSDGYGGLVT TDPKTADPVY GMVYNPPRTN YPGRFTNLLD
560 570 580 590 600
VAEACPTFLC FDDGKPYVVT RTDEQRLLAK FDLSLAAKHM SNTYLSGIAQ
610 620 630 640 650
YYAQYSGTIN LHFMFTGSTD SKARYMVAYV PPGVETPPDT PEKAAHCIHA
660 670 680 690 700
EWDTGLNSKF TFSIPYVSAA DYAYTASDVA ETTNVQGWVC IYQITHGKAE
710 720 730 740 750
QDTLVVSVSA GKDFELRLPI DPRSQTTSTG ESADPVTTTV ENYGGETQVQ
760 770 780 790 800
RRQHTDVTFI MDRFVKIQNL NPIHVIDLMQ THQHGLVGAL LRAATYYFSD
810 820 830 840 850
LEIVVRHDGN LTWVPNGAPE AALSNMGNPT AYPKAPFTRL ALPYTAPHRV
860 870 880 890 900
LATVYNGTGK YSAGGMGRRG DLEPLAARVA AQLPTSFNFG AIQATTIHEL
910 920 930 940 950
LVRMKRAELY CPRPLLAVEV SSQDRHKQKI IAPAKQLLNF DLLKLAGDVE
960 970 980 990 1000
SNPGPFFFSD VRSNFSKLVE TINQMQEDMS TKHGPDFNRL VSAFEELATG
1010 1020 1030 1040 1050
VKAIRTGLDE AKPWYKLIKL LSRLSCMAAV AARSKDPVLV AIMLADTGLE
1060 1070 1080 1090 1100
ILDSTFVVKK ISDSLSSLFH VPAPVFSFGA PILLAGLVKV ASSFFRSTPE
1110 1120 1130 1140 1150
DLERAEKQLK ARDINDIFAI LKNGEWLVKL ILAIRDWIKA WIASEEKFVT
1160 1170 1180 1190 1200
MTDLVPGILE KQRDLNDPSK YKEAKEWLDS ARQACLKNGN VHIANLCKVV
1210 1220 1230 1240 1250
TPAPSKSRPE PVVVCLRGKS GQGKSFLANV LAQAISTHFT GRIDSVWYCP
1260 1270 1280 1290 1300
PDPDHFDGYN QQTVVVMDDL GQNPDGKDFK YFAQMVSTTG FIPPMASLED
1310 1320 1330 1340 1350
KGKPFNSKVI ITTTNLYSGF TPRTMVCPDA LNRRFHFDID VSAKDGYKVN
1360 1370 1380 1390 1400
NKLDITKALE DTHTNPVAMF KYDCALLNGM AVEMKRMQQD MFKPQPPLQN
1410 1420 1430 1440 1450
VYQLVQEVIE RVELHEKVSS HQIFKQISIP SQKSVLYFLI EKGQHEAAIE
1460 1470 1480 1490 1500
FFEGLVHDSI KEELRPLIQQ TSFVKRAFKR LKENFEIVAL CLTLLANIVI
1510 1520 1530 1540 1550
MIRETRKRQQ MVDDAVNEYI EKANITTDDK TLDEAEKNPL ETSGVSIVGF
1560 1570 1580 1590 1600
RERTLPGHRA SDDVNSEPAR PVEEQPQAEG PYTGPLERQK PLKVKAKLPQ
1610 1620 1630 1640 1650
QEGPYAGPME RQKPLKVKVK APVVKEGPYE GPVKKPVALK VKAKNLIVTE
1660 1670 1680 1690 1700
SGAPPTDLQK MVMGNTKPVE LILDGKTVAI CCATGVFGTA YLVPRHLFAE
1710 1720 1730 1740 1750
KYDKIMLDGR AMTDSDYRVF EFEIKVKGQD MLSDAALMVL HRGNRVRDIT
1760 1770 1780 1790 1800
KHFRDTARMK KGTPVVGVIN NADVGRLIFS GEALTYKDIV VCMDGDTMPG
1810 1820 1830 1840 1850
LFAYKAATKA GYCGGAVLAK DGADTFIVGT HSAGGNGVGY CSCVSRSMLL
1860 1870 1880 1890 1900
KMKAHIDPEP HHEGLIVDTR DVEERVHVMR KTKLAPTVAH GVFNPEFGPA
1910 1920 1930 1940 1950
ALSNKDPRLN EGVVLDEVIF SKHKGDTKMT EEDKALFRRC AADYASRLHN
1960 1970 1980 1990 2000
VLGTANAPLS IYEAIKGVDG LDAMEPDTAP GLPWALQGKR RGTLIDFENG
2010 2020 2030 2040 2050
TVGPEVASAL ELMEKRQYKF TCQTFLKDEV RPMEKVRAGK TRIVDVLPVE
2060 2070 2080 2090 2100
HILYTRMMIG RFCAQMHSNN GPQIGSAVGC NPDVDWQRFG THFAQYKNVW
2110 2120 2130 2140 2150
DVDYSAFDAN HCSDAMNIMF EEVFRTEFGF HPNAEWILKT LVNTEHAYEN
2160 2170 2180 2190 2200
KRITVEGGMP SGCSATSIIN TILNNIYVLY ALRRHYEGVE LDTYTMISYG
2210 2220 2230 2240 2250
DDIVVASDYD LDFEALKPHF KSLGQTITPA DKSDKGFVLG QSITDVTFLK
2260 2270 2280 2290 2300
RHFRMDYGTG FYKPVMASKT LEAILSFARR GTIQEKLISV AGLAVHSGPD
2310 2320 2330
EYRRLFEPFQ GLFEIPSYRS LYLRWVNAVC GDAQSL
Length:2,336
Mass (Da):259,985
Last modified:February 1, 1996 - v1
Checksum:i15AC2AB022B5B954
GO
Isoform Lb (identifier: P49303-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,308
Mass (Da):256,785
Checksum:iFD33D0633D64D309
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti726 – 728TTS → NTT.3
Natural varianti804V → L.1
Natural varianti859G → S.1
Natural varianti919E → V.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189811 – 28Missing in isoform Lb. CuratedAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74812 Genomic RNA. Translation: CAA52812.1.
M38362 Genomic RNA. Translation: AAA42664.1.
PIRiS37077.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74812 Genomic RNA. Translation: CAA52812.1.
M38362 Genomic RNA. Translation: AAA42664.1.
PIRiS37077.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FMDX-ray3.504202-286[»]
ProteinModelPortaliP49303.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_FMDVZ
AccessioniPrimary (citable) accession number: P49303
Secondary accession number(s): Q65094
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 133 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.By similarity

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.