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P49303

- POLG_FMDVZ

UniProt

P49303 - POLG_FMDVZ

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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: 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 (By similarity).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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511For leader protease activityBy similarity
Active sitei148 – 1481For leader protease activityBy similarity
Active sitei163 – 1631For leader protease activityBy similarity
Sitei201 – 2022Cleavage; by leader proteaseSequence Analysis
Sitei286 – 2872CleavageSequence Analysis
Sitei504 – 5052Cleavage; by picornain 3CSequence Analysis
Sitei725 – 7262Cleavage; by picornain 3CSequence Analysis
Sitei936 – 9372Cleavage; by picornain 3CSequence Analysis
Sitei954 – 9552Cleavage; by ribosomal skipSequence Analysis
Sitei1108 – 11092Cleavage; by picornain 3CSequence Analysis
Sitei1426 – 14272Cleavage; by picornain 3CSequence Analysis
Sitei1579 – 15802Cleavage; by picornain 3CSequence Analysis
Sitei1602 – 16032Cleavage; by picornain 3CSequence Analysis
Sitei1626 – 16272Cleavage; by picornain 3CSequence Analysis
Sitei1650 – 16512Cleavage; by picornain 3CSequence Analysis
Active sitei1696 – 16961For picornain 3C activitySequence Analysis
Active sitei1723 – 17231For picornain 3C activitySequence Analysis
Active sitei1813 – 18131For picornain 3C activitySequence Analysis
Sitei1863 – 18642Cleavage; by picornain 3CSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1218 – 12258ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. RNA helicase activity Source: InterPro
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. induction by virus of host autophagy Source: UniProtKB
  3. modulation by virus of host chromatin organization Source: UniProtKB-KW
  4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  5. protein oligomerization Source: UniProtKB-KW
  6. RNA-protein covalent cross-linking Source: UniProtKB-KW
  7. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  8. suppression by virus of host translation initiation factor activity Source: UniProtKB
  9. transcription, DNA-templated Source: InterPro
  10. viral protein processing Source: InterPro
  11. viral RNA genome replication Source: InterPro
  12. virion attachment to host cell Source: UniProtKB-KW
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, 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

Protein family/group databases

MEROPSiC28.001.

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 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]
ProteomesiUP000008621: Genome

Subcellular locationi

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

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. icosahedral viral capsid Source: InterPro
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23362336Genome polyproteinPRO_0000039850Add
BLAST
Chaini1 – 201201Leader proteasePRO_0000039851Add
BLAST
Chaini202 – 504303Protein VP0Sequence AnalysisPRO_0000374075Add
BLAST
Chaini202 – 28685Protein VP4Sequence AnalysisPRO_0000039854Add
BLAST
Chaini287 – 504218Protein VP2Sequence AnalysisPRO_0000039855Add
BLAST
Chaini505 – 725221Protein VP3Sequence AnalysisPRO_0000039856Add
BLAST
Chaini726 – 936211Protein VP1Sequence AnalysisPRO_0000039857Add
BLAST
Chaini937 – 95418Protein 2ASequence AnalysisPRO_0000039858Add
BLAST
Chaini955 – 1108154Protein 2BSequence AnalysisPRO_0000039859Add
BLAST
Chaini1109 – 1426318Protein 2CSequence AnalysisPRO_0000039860Add
BLAST
Chaini1427 – 1579153Protein 3ASequence AnalysisPRO_0000039861Add
BLAST
Chaini1580 – 160223Protein 3B-1Sequence AnalysisPRO_0000039862Add
BLAST
Chaini1603 – 162624Protein 3B-2Sequence AnalysisPRO_0000039863Add
BLAST
Chaini1627 – 165024Protein 3B-3Sequence AnalysisPRO_0000039864Add
BLAST
Chaini1651 – 1863213Picornain 3CSequence AnalysisPRO_0000039865Add
BLAST
Chaini1864 – 2336473RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi202 – 2021N-myristoyl glycine; by hostBy similarity
Disulfide bondi511 – 511Interchain; in VP3 dimer
Modified residuei1582 – 15821O-(5'-phospho-RNA)-tyrosineBy similarity
Modified residuei1605 – 16051O-(5'-phospho-RNA)-tyrosineBy similarity
Modified residuei1629 – 16291O-(5'-phospho-RNA)-tyrosineBy similarity

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

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

1
2336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi229 – 2324Combined sources
Helixi269 – 2746Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FMDX-ray3.504202-286[»]
ProteinModelPortaliP49303.
SMRiP49303. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14811481CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1503 – 2336834CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1482 – 150221Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 201201Peptidase C28Add
BLAST
Domaini1190 – 1354165SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1653 – 1837185Peptidase C3Add
BLAST
Domaini2097 – 2215119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi869 – 8713Cell attachment site

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

Gene3Di2.60.120.20. 3 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.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti726 – 7283TTS → NTT.
Natural varianti804 – 8041V → L.
Natural varianti859 – 8591G → S.
Natural varianti919 – 9191E → V.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform Lb. CuratedVSP_018981Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X74812 Genomic RNA. Translation: CAA52812.1 .
M38362 Genomic RNA. Translation: AAA42664.1 .
PIRi S37077.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FMD X-ray 3.50 4 202-286 [» ]
ProteinModelPortali P49303.
SMRi P49303. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C28.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProi IPR015031. 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.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami 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.
[Graphical view ]
PRINTSi PR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Primary structure of the DNA copy of the protein VP1 gene of the foot-and-mouth disease virus A22."
    Onishchenko A.M., Petrov N.A., Blinov V.M., Vassilenko S.K., Sandakhchiev L.S., Burdov A.N., Ivanyushchenkov V.N., Perevozchikova N.A.
    Bioorg. Khim. 12:416-419(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 702-955.

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: October 29, 2014
This is version 122 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

External Data

Dasty 3