ID Q6PMY3_9PICO Unreviewed; 2336 AA.
AC Q6PMY3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Foot-and-mouth disease virus A.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Caphthovirinae; Aphthovirus;
OC Foot-and-mouth disease virus.
OX NCBI_TaxID=12111 {ECO:0000313|EMBL:AAT01746.1, ECO:0000313|Proteomes:UP000134908};
RN [1] {ECO:0000313|EMBL:AAT01746.1, ECO:0000313|Proteomes:UP000134908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A Venceslau {ECO:0000313|EMBL:AAT01746.1};
RX PubMed=15858032; DOI=10.1128/JVI.79.10.6487-6504.2005;
RA Carrillo C., Tulman E.R., Delhon G., Lu Z., Carreno A., Vagnozzi A.,
RA Kutish G.F., Rock D.L.;
RT "Comparative genomics of foot-and-mouth disease virus.";
RL J. Virol. 79:6487-6504(2005).
CC -!- FUNCTION: Associates with and induces structural rearrangements of
CC intracellular membranes. Triggers host autophagy by interacting with
CC host BECN1 and thereby promotes viral replication. Participates in
CC viral replication and interacts with host DHX9. Displays RNA-binding,
CC nucleotide binding and NTPase activities. May play a role in virion
CC morphogenesis and viral RNA encapsidation by interacting with the
CC capsid protein VP3. {ECO:0000256|ARBA:ARBA00003578}.
CC -!- FUNCTION: Covalently linked to the 5'-end of both the positive-strand
CC and negative-strand genomic RNAs. Acts as a genome-linked replication
CC primer. {ECO:0000256|ARBA:ARBA00002573}.
CC -!- FUNCTION: Cysteine protease that generates mature viral proteins from
CC the precursor polyprotein. In addition to its proteolytic activity,
CC binds to viral RNA and thus influences viral genome replication. RNA
CC and substrate bind cooperatively to the protease.
CC {ECO:0000256|ARBA:ARBA00004047}.
CC -!- FUNCTION: Forms an icosahedral capsid of pseudo T=3 symmetry with
CC capsid proteins VP0 and VP3. The capsid is composed of 60 copies of
CC each capsid protein organized in the form of twelve pentamers and
CC encloses the viral positive strand RNA genome.
CC {ECO:0000256|ARBA:ARBA00033732}.
CC -!- FUNCTION: Forms an icosahedral capsid of pseudo T=3 symmetry with
CC capsid proteins VP1 and VP3. The capsid is composed of 60 copies of
CC each capsid protein organized in the form of twelve pentamers and
CC encloses the viral positive strand RNA genome.
CC {ECO:0000256|ARBA:ARBA00033735}.
CC -!- FUNCTION: Lies on the inner surface of the capsid shell. After binding
CC to the host receptor, the capsid undergoes conformational changes.
CC Capsid protein VP4 is released, capsid protein VP1 N-terminus is
CC externalized, and together, they shape a pore in the host membrane
CC through which the viral genome is translocated into the host cell
CC cytoplasm. After genome has been released, the channel shrinks.
CC {ECO:0000256|ARBA:ARBA00033716}.
CC -!- FUNCTION: Mediates self-processing of the polyprotein by a
CC translational effect termed 'ribosome skipping'. Mechanistically, 2A-
CC mediated cleavage occurs between the C-terminal glycine and the proline
CC of the downstream protein 2B. In the case of foot-and-mouth disease
CC virus, the 2A oligopeptide is post-translationally 'trimmed' from the
CC C-terminus of the upstream protein 1D by 3C proteinase.
CC {ECO:0000256|ARBA:ARBA00002616}.
CC -!- FUNCTION: Plays an essential role in the virus replication cycle by
CC acting as a viroporin. Creates a pore in the host reticulum endoplasmic
CC and as a consequence releases Ca2+ in the cytoplasm of infected cell.
CC In turn, high levels of cytoplasmic calcium may trigger membrane
CC trafficking and transport of viral ER-associated proteins to
CC viroplasms, sites of viral genome replication.
CC {ECO:0000256|ARBA:ARBA00003379}.
CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC Covalently attaches UMP to a tyrosine of VPg, which is used to prime
CC RNA synthesis. The positive stranded RNA genome is first replicated at
CC virus induced membranous vesicles, creating a dsRNA genomic replication
CC form. This dsRNA is then used as template to synthesize positive
CC stranded RNA genomes. ss(+)RNA genomes are either translated,
CC replicated or encapsidated. {ECO:0000256|ARBA:ARBA00004027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytically cleaves itself from the polyprotein of the
CC foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but
CC then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-
CC Arg- and -Lys-|-Arg-.; EC=3.4.22.46;
CC Evidence={ECO:0000256|ARBA:ARBA00001868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000256|ARBA:ARBA00011175}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Host cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004295}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000256|ARBA:ARBA00008303}.
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DR EMBL; AY593803; AAT01746.1; -; Genomic_RNA.
DR MEROPS; C28.001; -.
DR Proteomes; UP000134908; Genome.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23210; Aphthovirus_RdRp; 1.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 4.10.90.10; Capsid protein VP4 superfamily, Picornavirus; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR015031; Capsid_VP4_Picornavir.
DR InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004080; FMDV_VP1_coat.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR008739; Peptidase_C28.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF05408; Peptidase_C28; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 3.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF08935; VP4_2; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR PRINTS; PR01542; FMDVP1COAT.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51887; APHTHOVIRUS_LPRO; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Clathrin-mediated endocytosis of virus by host
KW {ECO:0000256|ARBA:ARBA00022570};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Modulation of host chromatin by virus {ECO:0000256|ARBA:ARBA00023330};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022706};
KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 32..185
FT /note="Peptidase C28"
FT /evidence="ECO:0000259|PROSITE:PS51887"
FT DOMAIN 1193..1357
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1656..1852
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 2100..2218
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2336 AA; 259836 MW; B2F0043CA9B19486 CRC64;
MNYMDTTDCF IALVHAIREI KTLFFPRHTG KMEFTLHNGE KKVFYSRPNK HDNCWLNTIL
QLFRYVDEPF FDWVYNSPEN LTLSAIRQLE ELTGLELHEG GPPALVIWNI KHLLHTGIGT
ASRPSEVCMV DGTDMCLADF HAGIFLKGKE HAVFACVTSN GWYAVDDEDF YPWTPDPSDV
LVFVPYDQEP LNGEWKANVQ RKLKGAGQSS PATGSQNQSG NTGSIINNYY MQQYQNSMDT
QLGDNAISGG SNEGSTDTTS THTTNTQNND WFSKLASSAF TGLFGALLAD KKTEETTLLE
DRILTTRNGH TTSTTQSSVG VTYGYSTGED HVAGPNTSGL ETRVVQAERF YKKFLFDWTT
DRPFGHLEKL ELPTDHHGVF GHLVDSYAYM RNGWDVEVSA VGNQFNGGCL LVAMVPEWKD
FDTREKYQLT LFPHQFISPR TNMTAHITVP YLGVNRYDQY KKHKPWTLVV MVVSPLTVNT
AGASQIKVYA NIAPTYVHVA GELPSKEGIF PVACADGYGG LVTTDPKTAD PVYGKVYNPP
RTNYPGRFTN LLDVAEACPT FLCFDDGKPY VTTRTDQTRL LAKFDLSLAA KHMSNTYLAG
LAQYYTQYSG TINLHFMFTG STDSKARYMV AYIPPGVETP PETPEMAAHC IHAEWDTGLN
SKFTFSIPYV SAADYAYTAS DVAETTNVQG WVCIYQITHG KAENDALVVS VSAGKDFELR
LPIDPRLQTT ATGESADPVT TTVENYGGET QVQRRHHTDI GFIMDRFVKI KDVTPTHVID
LMQTHQHGLV GAMLRAATYY FSDLEIVVQH DGNLTWVPNG APVSALENTS NPTAYNKAPF
TRLALPYTAP HRVLATVYNG TSKYTVSGSG RRGDMGSLAA RVAKQLPASF NYGAIKATAI
HELLVRMKRA ELYCPRPLLA VEVSSQDRHK QSIIAPAKQL LNFDLLKLAG DVESNPGPFF
FSDVRSNFTK LVETINQMQE DMSTKHGPDF NRLVSAFEEL ATGVKAIRTG LDEAKPWYKL
IKLLSRLSCM AAVAARSKDP VLVAIMLADT GLEILDSTFV VKKISDSLSS LFHVPAPVFS
FGAPILLAGL VKVASSFFRS TPEDLERAEK QLKARDINDI FAILKNGEWL VKLILAIRDW
IKAWIASEEK FVTMTDLVPG ILEKQRDLDD PSKYKEAKEW LDNARQACLK SGNVHIANLC
KVVTPAPSKS RPEPVVVCLR GKSGQGKSFL ANVLAQAIST HFTGRTDSVW YCPPDPDHFD
GYNQQTVVVM DDLGQNPDGK DFKYFAQMVS TTGFIPPMAS LEDKGKPFNS KVIIATTNLY
SGFTPRTMVC PDALNRRFHF DIDVSAKDGY KVNNKLDIIK ALEDTHTNPV AMFQYDCALL
NGMAVEMKRM QQDMFKPQPP LQNVYQLVQE VIERVELHEK VSSHPIFKQI SIPSQKSVLY
FLIEKGQHEA AIEFFEGMVH DSIKEELRPL IQQTSFVKRA FKRLKENFEI VALCLTLLAN
IVIMIRETRK RQKMVDDAVN EYIEKANITT DDKTLDEAEK NPLETSGAST VGFRERTLPG
HKASDDVNSE PAQPVGEQPH AEGPYAGPLE RQKPLKVRAK LPQQEGPYAG PMERQKPLKV
KAKAPVVKEG PYEGPVKKPV ALKVKAKNLI VTESGAPPTD LQKMVMGNTK PVELILDGKT
VAICCATGVF GTAYLVPRHL FAEKYDKIML DGRAMTDSDY RVFEFEIKVK GQDMLSDAAL
MVLHRGNRVR DITKHFRDTA RMKKGTPVVG VINNADVGRL IFSGEALTYK DIVVCMDGDT
MPGLFAYRAA TKAGYCGGAV LAKDGADTFI VGTHSAGGNG VGYCSCVSRS MLLKMKAHID
PEPHHEGLIV DTRDVEERVH VMRKTKLAPT VAHGVFNPEF GPAALSNKDP RLNEGVVLDE
VIFSKHKGDT KMSEEDKALF RRCAADYASR LHSVLGTANA PLSIYEAIKG VDGLDAMEPD
TAPGLPWALQ GKRRGALIDF ENGTVGPEVE AALKLMEKRE YKFACQTFLK DEIRPMEKVR
AGKTRIVDVL PVEHILYTRM MIGRFCAQMH SNNGPQIGSA VGCNPDVDWQ RFGTHFAQYR
NVWDVDYSAF DANHCSDAMN IMFEEVFRTE FGFHPNAEWI LKTLVNTEHA YENKRITVEG
GMPSGCSATS IINTILNNIY VLYALRRHYE GVELDTYTMI SYGDDIVVAS DYDLDFEALK
PHFKSLGQTI TPADKSDKGF VLGHSITDVT FLKRHFHMDY GTGFYKPVMA SKTLEAILSF
ARRGTIQEKL ISVAGLAVHS GPDEYRRLFE PFQGLFEIPS YRSLYLRWVN AVCGDA
//
