P49303 (POLG_FMDVZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 15 chains: Leader protease Short name=Lpro EC=3.4.22.46 Protein VP0 Alternative name(s): VP4-VP2 Protein VP4 Alternative name(s): P1A Virion protein 4 Protein VP2 Alternative name(s): P1B Virion protein 2 Protein VP3 Alternative name(s): P1C Virion protein 3 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 Short name=P2C EC=3.6.1.15 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 Picornain 3C EC=3.4.22.28 Alternative name(s): Protease 3C Short name=P3C Protease P20B RNA-directed RNA polymerase 3D-POL Short name=P3D-POL EC=2.7.7.48 Alternative name(s): P56A
Organism	Foot-and-mouth disease virus (isolate -/Azerbaijan/A22-550/1965 serotype A) (FMDV) [Complete proteome]
Taxonomic identifier	73481 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Aphthovirus › Foot-and-mouth disease virus › Foot-and-mouth disease virus - type A
Virus host	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]

Protein attributes

Sequence length	2336 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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. 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. 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. Protein 3C is a 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 co-operatively to the protease By similarity. RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
Catalytic activity	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).
Subunit structure	VP1 interacts (via RGD) with integrins heterodimers alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8 By similarity.
Subcellular location	Protein VP2: Virion. Host cytoplasm Potential. Protein VP3: Virion. Host cytoplasm Potential. Protein VP1: Virion. Host cytoplasm Potential. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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. Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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. Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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. Protein 3B-1: Virion Potential. Protein 3B-2: Virion Potential. Protein 3B-3: Virion Potential. Picornain 3C: Host cytoplasm Potential. RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.
Post-translational modification	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. 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.
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.
Sequence similarities	Belongs to the picornaviruses polyprotein family. Contains 1 peptidase C28 domain. Contains 1 peptidase C3 domain. Contains 1 RdRp catalytic domain. Contains 1 SF3 helicase domain.

Ontologies

Keywords
Biological process	Clathrin-mediated endocytosis of virus by host Host-virus interaction Ion transport Modulation of host chromatin by virus Transport Viral RNA replication Viral attachment to host cell Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host cytoplasm Host cytoplasmic vesicle Host membrane Membrane Virion
Coding sequence diversity	Alternative initiation
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Capsid protein Helicase Hydrolase Ion channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase Viral ion channel
PTM	Covalent protein-RNA linkage Disulfide bond Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW modulation by virus of host chromatin organization Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro viral protein processing Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell icosahedral viral capsid Inferred from electronic annotation. Source: InterPro membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Lab (identifier: P49303-1)

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.

Isoform Lb (identifier: P49303-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2336

2336

Genome polyprotein

PRO_0000039850

Chain

1 – 201

201

Leader protease

PRO_0000039851

Chain

202 – 504

303

Protein VP0 Potential

PRO_0000374075

Chain

202 – 286

85

Protein VP4 Potential

PRO_0000039854

Chain

287 – 504

218

Protein VP2 Potential

PRO_0000039855

Chain

505 – 725

221

Protein VP3 Potential

PRO_0000039856

Chain

726 – 936

211

Protein VP1 Potential

PRO_0000039857

Chain

937 – 954

18

Protein 2A Potential

PRO_0000039858

Chain

955 – 1108

154

Protein 2B Potential

PRO_0000039859

Chain

1109 – 1426

318

Protein 2C Potential

PRO_0000039860

Chain

1427 – 1579

153

Protein 3A Potential

PRO_0000039861

Chain

1580 – 1602

23

Protein 3B-1 Potential

PRO_0000039862

Chain

1603 – 1626

24

Protein 3B-2 Potential

PRO_0000039863

Chain

1627 – 1650

24

Protein 3B-3 Potential

PRO_0000039864

Chain

1651 – 1863

213

Picornain 3C Potential

PRO_0000039865

Chain

1864 – 2336

473

RNA-directed RNA polymerase 3D-POL Potential

PRO_0000039866

Regions

Topological domain

1 – 1481

1481

Cytoplasmic Potential

Intramembrane

1482 – 1502

21

Potential

Topological domain

1503 – 2336

834

Cytoplasmic Potential

Domain

1 – 201

201

Peptidase C28

Domain

1190 – 1354

165

SF3 helicase

Domain

1653 – 1837

185

Peptidase C3

Domain

2097 – 2215

119

RdRp catalytic

Nucleotide binding

1218 – 1225

8

ATP Potential

Motif

869 – 871

3

Cell attachment site

Sites

Active site

51

1

For leader protease activity By similarity

Active site

148

1

For leader protease activity By similarity

Active site

163

1

For leader protease activity By similarity

Active site

1696

1

For picornain 3C activity Potential

Active site

1723

1

For picornain 3C activity Potential

Active site

1813

1

For picornain 3C activity Potential

Site

201 – 202

2

Cleavage; by leader protease Potential

Site

286 – 287

2

Cleavage Potential

Site

504 – 505

2

Cleavage; by picornain 3C Potential

Site

725 – 726

2

Cleavage; by picornain 3C Potential

Site

936 – 937

2

Cleavage; by picornain 3C Potential

Site

954 – 955

2

Cleavage; by ribosomal skip Potential

Site

1108 – 1109

2

Cleavage; by picornain 3C Potential

Site

1426 – 1427

2

Cleavage; by picornain 3C Potential

Site

1579 – 1580

2

Cleavage; by picornain 3C Potential

Site

1602 – 1603

2

Cleavage; by picornain 3C Potential

Site

1626 – 1627

2

Cleavage; by picornain 3C Potential

Site

1650 – 1651

2

Cleavage; by picornain 3C Potential

Site

1863 – 1864

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue

1582

1

O-(5'-phospho-RNA)-tyrosine By similarity

Modified residue

1605

1

O-(5'-phospho-RNA)-tyrosine By similarity

Modified residue

1629

1

O-(5'-phospho-RNA)-tyrosine By similarity

Lipidation

202

1

N-myristoyl glycine; by host By similarity

Disulfide bond

511

Interchain; in VP3 dimer

Natural variations

Alternative sequence

1 – 28

28

Missing in isoform Lb.

VSP_018981

Natural variant

726 – 728

3

TTS → NTT.

Natural variant

804

1

V → L.

Natural variant

859

1

G → S.

Natural variant

919

1

E → V.

Secondary structure

1

.

.

.

.

.

2336

Helix Strand Turn

Details...

Helix

229 – 232

4

Helix

269 – 274

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform Lab [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 15AC2AB022B5B954	FASTA	2,336	259,985
	10 20 30 40 50 60 MNTTDCFIAL LYALREIKAF LLSRTQGKME LTLYNGEKKT FYSRPNNHDN CWLNTILQLF 70 80 90 100 110 120 RYVDEPFFDW VYDSPENLTC EAIRQLEEIT GLELHEGGPP ALVIWNIKHL LHTGIGTASR 130 140 150 160 170 180 PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSDGWY AIDDEDFYPW TPDPSDVLVF 190 200 210 220 230 240 VPYDQEPLNG EWKAKVQKRL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG 250 260 270 280 290 300 DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI 310 320 330 340 350 360 LTTRNGHTTS TTQSSVGVTY GYSTQEDHVS GPNTSGLETR VVQAERFFKK YLFDWTPDKA 370 380 390 400 410 420 FGHLEKLELP TDHKGVYGHL VDSFAYMRNG WDVEVSAVGN QFNGGCLLVA MVPEWKELTP 430 440 450 460 470 480 REKYQLTLFP HQFISPRTNM TAHIVVPYLG VNRYDQYKKH KPWTLVVMVV SPLTTNTVSA 490 500 510 520 530 540 GQIKVYANIA PTHVHVAGEL PSKEGIVPVA CSDGYGGLVT TDPKTADPVY GMVYNPPRTN 550 560 570 580 590 600 YPGRFTNLLD VAEACPTFLC FDDGKPYVVT RTDEQRLLAK FDLSLAAKHM SNTYLSGIAQ 610 620 630 640 650 660 YYAQYSGTIN LHFMFTGSTD SKARYMVAYV PPGVETPPDT PEKAAHCIHA EWDTGLNSKF 670 680 690 700 710 720 TFSIPYVSAA DYAYTASDVA ETTNVQGWVC IYQITHGKAE QDTLVVSVSA GKDFELRLPI 730 740 750 760 770 780 DPRSQTTSTG ESADPVTTTV ENYGGETQVQ RRQHTDVTFI MDRFVKIQNL NPIHVIDLMQ 790 800 810 820 830 840 THQHGLVGAL LRAATYYFSD LEIVVRHDGN LTWVPNGAPE AALSNMGNPT AYPKAPFTRL 850 860 870 880 890 900 ALPYTAPHRV LATVYNGTGK YSAGGMGRRG DLEPLAARVA AQLPTSFNFG AIQATTIHEL 910 920 930 940 950 960 LVRMKRAELY CPRPLLAVEV SSQDRHKQKI IAPAKQLLNF DLLKLAGDVE SNPGPFFFSD 970 980 990 1000 1010 1020 VRSNFSKLVE TINQMQEDMS TKHGPDFNRL VSAFEELATG VKAIRTGLDE AKPWYKLIKL 1030 1040 1050 1060 1070 1080 LSRLSCMAAV AARSKDPVLV AIMLADTGLE ILDSTFVVKK ISDSLSSLFH VPAPVFSFGA 1090 1100 1110 1120 1130 1140 PILLAGLVKV ASSFFRSTPE DLERAEKQLK ARDINDIFAI LKNGEWLVKL ILAIRDWIKA 1150 1160 1170 1180 1190 1200 WIASEEKFVT MTDLVPGILE KQRDLNDPSK YKEAKEWLDS ARQACLKNGN VHIANLCKVV 1210 1220 1230 1240 1250 1260 TPAPSKSRPE PVVVCLRGKS GQGKSFLANV LAQAISTHFT GRIDSVWYCP PDPDHFDGYN 1270 1280 1290 1300 1310 1320 QQTVVVMDDL GQNPDGKDFK YFAQMVSTTG FIPPMASLED KGKPFNSKVI ITTTNLYSGF 1330 1340 1350 1360 1370 1380 TPRTMVCPDA LNRRFHFDID VSAKDGYKVN NKLDITKALE DTHTNPVAMF KYDCALLNGM 1390 1400 1410 1420 1430 1440 AVEMKRMQQD MFKPQPPLQN VYQLVQEVIE RVELHEKVSS HQIFKQISIP SQKSVLYFLI 1450 1460 1470 1480 1490 1500 EKGQHEAAIE FFEGLVHDSI KEELRPLIQQ TSFVKRAFKR LKENFEIVAL CLTLLANIVI 1510 1520 1530 1540 1550 1560 MIRETRKRQQ MVDDAVNEYI EKANITTDDK TLDEAEKNPL ETSGVSIVGF RERTLPGHRA 1570 1580 1590 1600 1610 1620 SDDVNSEPAR PVEEQPQAEG PYTGPLERQK PLKVKAKLPQ QEGPYAGPME RQKPLKVKVK 1630 1640 1650 1660 1670 1680 APVVKEGPYE GPVKKPVALK VKAKNLIVTE SGAPPTDLQK MVMGNTKPVE LILDGKTVAI 1690 1700 1710 1720 1730 1740 CCATGVFGTA YLVPRHLFAE KYDKIMLDGR AMTDSDYRVF EFEIKVKGQD MLSDAALMVL 1750 1760 1770 1780 1790 1800 HRGNRVRDIT KHFRDTARMK KGTPVVGVIN NADVGRLIFS GEALTYKDIV VCMDGDTMPG 1810 1820 1830 1840 1850 1860 LFAYKAATKA GYCGGAVLAK DGADTFIVGT HSAGGNGVGY CSCVSRSMLL KMKAHIDPEP 1870 1880 1890 1900 1910 1920 HHEGLIVDTR DVEERVHVMR KTKLAPTVAH GVFNPEFGPA ALSNKDPRLN EGVVLDEVIF 1930 1940 1950 1960 1970 1980 SKHKGDTKMT EEDKALFRRC AADYASRLHN VLGTANAPLS IYEAIKGVDG LDAMEPDTAP 1990 2000 2010 2020 2030 2040 GLPWALQGKR RGTLIDFENG TVGPEVASAL ELMEKRQYKF TCQTFLKDEV RPMEKVRAGK 2050 2060 2070 2080 2090 2100 TRIVDVLPVE HILYTRMMIG RFCAQMHSNN GPQIGSAVGC NPDVDWQRFG THFAQYKNVW 2110 2120 2130 2140 2150 2160 DVDYSAFDAN HCSDAMNIMF EEVFRTEFGF HPNAEWILKT LVNTEHAYEN KRITVEGGMP 2170 2180 2190 2200 2210 2220 SGCSATSIIN TILNNIYVLY ALRRHYEGVE LDTYTMISYG DDIVVASDYD LDFEALKPHF 2230 2240 2250 2260 2270 2280 KSLGQTITPA DKSDKGFVLG QSITDVTFLK RHFRMDYGTG FYKPVMASKT LEAILSFARR 2290 2300 2310 2320 2330 GTIQEKLISV AGLAVHSGPD EYRRLFEPFQ GLFEIPSYRS LYLRWVNAVC GDAQSL
	Isoform Lb [UniParc]. Checksum: FD33D0633D64D309	FASTA	2,308	256,785
	10 20 30 40 50 60 MELTLYNGEK KTFYSRPNNH DNCWLNTILQ LFRYVDEPFF DWVYDSPENL TCEAIRQLEE 70 80 90 100 110 120 ITGLELHEGG PPALVIWNIK HLLHTGIGTA SRPSEVCMVD GTDMCLADFH AGIFLKGQEH 130 140 150 160 170 180 AVFACVTSDG WYAIDDEDFY PWTPDPSDVL VFVPYDQEPL NGEWKAKVQK RLKGAGQSSP 190 200 210 220 230 240 ATGSQNQSGN TGSIINNYYM QQYQNSMDTQ LGDNAISGGS NEGSTDTTST HTTNTQNNDW 250 260 270 280 290 300 FSKLASSAFS GLFGALLADK KTEETTLLED RILTTRNGHT TSTTQSSVGV TYGYSTQEDH 310 320 330 340 350 360 VSGPNTSGLE TRVVQAERFF KKYLFDWTPD KAFGHLEKLE LPTDHKGVYG HLVDSFAYMR 370 380 390 400 410 420 NGWDVEVSAV GNQFNGGCLL VAMVPEWKEL TPREKYQLTL FPHQFISPRT NMTAHIVVPY 430 440 450 460 470 480 LGVNRYDQYK KHKPWTLVVM VVSPLTTNTV SAGQIKVYAN IAPTHVHVAG ELPSKEGIVP 490 500 510 520 530 540 VACSDGYGGL VTTDPKTADP VYGMVYNPPR TNYPGRFTNL LDVAEACPTF LCFDDGKPYV 550 560 570 580 590 600 VTRTDEQRLL AKFDLSLAAK HMSNTYLSGI AQYYAQYSGT INLHFMFTGS TDSKARYMVA 610 620 630 640 650 660 YVPPGVETPP DTPEKAAHCI HAEWDTGLNS KFTFSIPYVS AADYAYTASD VAETTNVQGW 670 680 690 700 710 720 VCIYQITHGK AEQDTLVVSV SAGKDFELRL PIDPRSQTTS TGESADPVTT TVENYGGETQ 730 740 750 760 770 780 VQRRQHTDVT FIMDRFVKIQ NLNPIHVIDL MQTHQHGLVG ALLRAATYYF SDLEIVVRHD 790 800 810 820 830 840 GNLTWVPNGA PEAALSNMGN PTAYPKAPFT RLALPYTAPH RVLATVYNGT GKYSAGGMGR 850 860 870 880 890 900 RGDLEPLAAR VAAQLPTSFN FGAIQATTIH ELLVRMKRAE LYCPRPLLAV EVSSQDRHKQ 910 920 930 940 950 960 KIIAPAKQLL NFDLLKLAGD VESNPGPFFF SDVRSNFSKL VETINQMQED MSTKHGPDFN 970 980 990 1000 1010 1020 RLVSAFEELA TGVKAIRTGL DEAKPWYKLI KLLSRLSCMA AVAARSKDPV LVAIMLADTG 1030 1040 1050 1060 1070 1080 LEILDSTFVV KKISDSLSSL FHVPAPVFSF GAPILLAGLV KVASSFFRST PEDLERAEKQ 1090 1100 1110 1120 1130 1140 LKARDINDIF AILKNGEWLV KLILAIRDWI KAWIASEEKF VTMTDLVPGI LEKQRDLNDP 1150 1160 1170 1180 1190 1200 SKYKEAKEWL DSARQACLKN GNVHIANLCK VVTPAPSKSR PEPVVVCLRG KSGQGKSFLA 1210 1220 1230 1240 1250 1260 NVLAQAISTH FTGRIDSVWY CPPDPDHFDG YNQQTVVVMD DLGQNPDGKD FKYFAQMVST 1270 1280 1290 1300 1310 1320 TGFIPPMASL EDKGKPFNSK VIITTTNLYS GFTPRTMVCP DALNRRFHFD IDVSAKDGYK 1330 1340 1350 1360 1370 1380 VNNKLDITKA LEDTHTNPVA MFKYDCALLN GMAVEMKRMQ QDMFKPQPPL QNVYQLVQEV 1390 1400 1410 1420 1430 1440 IERVELHEKV SSHQIFKQIS IPSQKSVLYF LIEKGQHEAA IEFFEGLVHD SIKEELRPLI 1450 1460 1470 1480 1490 1500 QQTSFVKRAF KRLKENFEIV ALCLTLLANI VIMIRETRKR QQMVDDAVNE YIEKANITTD 1510 1520 1530 1540 1550 1560 DKTLDEAEKN PLETSGVSIV GFRERTLPGH RASDDVNSEP ARPVEEQPQA EGPYTGPLER 1570 1580 1590 1600 1610 1620 QKPLKVKAKL PQQEGPYAGP MERQKPLKVK VKAPVVKEGP YEGPVKKPVA LKVKAKNLIV 1630 1640 1650 1660 1670 1680 TESGAPPTDL QKMVMGNTKP VELILDGKTV AICCATGVFG TAYLVPRHLF AEKYDKIMLD 1690 1700 1710 1720 1730 1740 GRAMTDSDYR VFEFEIKVKG QDMLSDAALM VLHRGNRVRD ITKHFRDTAR MKKGTPVVGV 1750 1760 1770 1780 1790 1800 INNADVGRLI FSGEALTYKD IVVCMDGDTM PGLFAYKAAT KAGYCGGAVL AKDGADTFIV 1810 1820 1830 1840 1850 1860 GTHSAGGNGV GYCSCVSRSM LLKMKAHIDP EPHHEGLIVD TRDVEERVHV MRKTKLAPTV 1870 1880 1890 1900 1910 1920 AHGVFNPEFG PAALSNKDPR LNEGVVLDEV IFSKHKGDTK MTEEDKALFR RCAADYASRL 1930 1940 1950 1960 1970 1980 HNVLGTANAP LSIYEAIKGV DGLDAMEPDT APGLPWALQG KRRGTLIDFE NGTVGPEVAS 1990 2000 2010 2020 2030 2040 ALELMEKRQY KFTCQTFLKD EVRPMEKVRA GKTRIVDVLP VEHILYTRMM IGRFCAQMHS 2050 2060 2070 2080 2090 2100 NNGPQIGSAV GCNPDVDWQR FGTHFAQYKN VWDVDYSAFD ANHCSDAMNI MFEEVFRTEF 2110 2120 2130 2140 2150 2160 GFHPNAEWIL KTLVNTEHAY ENKRITVEGG MPSGCSATSI INTILNNIYV LYALRRHYEG 2170 2180 2190 2200 2210 2220 VELDTYTMIS YGDDIVVASD YDLDFEALKP HFKSLGQTIT PADKSDKGFV LGQSITDVTF 2230 2240 2250 2260 2270 2280 LKRHFRMDYG TGFYKPVMAS KTLEAILSFA RRGTIQEKLI SVAGLAVHSG PDEYRRLFEP 2290 2300 FQGLFEIPSY RSLYLRWVNA VCGDAQSL

References

[1]	Sosnovtsev S.V., Onischenko A.M., Petrov N.A., Kalashnikova T.I., Mamaeva N.V., Drygin V.Y., Perevozchikova N.A., Vasilenko S.K. Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"The DNA-copy primary structure for the gene of the FMDV A-22 serotype VP1-protein." 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X74812 Genomic RNA. Translation: CAA52812.1.
M38362 Genomic RNA. Translation: AAA42664.1.

PIR

S37077.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FMD	X-ray	3.50	4	202-286	[»]

ProteinModelPortal

P49303.

SMR

P49303. Positions 29-201, 216-286, 298-934, 1657-1857, 1864-2333.

ModBase

Search...

Protein family/group databases

MEROPS

C03.008.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

4.10.90.10. 1 hit.

InterPro

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.
[Graphical view]

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.
[Graphical view]

PRINTS

PR00918. CALICVIRUSNS.
PR01542. FMDVP1COAT.

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.
SSF52540. SSF52540. 1 hit.

PROSITE

PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

POLG_FMDVZ

Accession

Primary (citable) accession number: P49303
Secondary accession number(s): Q65094

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program