ID E4W501_9PICO Unreviewed; 2332 AA.
AC E4W501;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Foot-and-mouth disease virus O.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Caphthovirinae; Aphthovirus;
OC Foot-and-mouth disease virus.
OX NCBI_TaxID=12118 {ECO:0000313|EMBL:ADR51742.1, ECO:0000313|Proteomes:UP000101507};
RN [1] {ECO:0000313|EMBL:ADR51742.1, ECO:0000313|Proteomes:UP000101507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel 07-6380 {ECO:0000313|EMBL:ADR51742.1};
RA Xu L., Bieker J., Rowland J., Hurtle W., Carrillo C., Hagai Y., Perez A.,
RA Beckham T., McIntosh M.T., Metwally S.A.;
RT "Sequence identification and genetic profile of FMDV in a 2007 disease
RT outbreak in Israel using full length genomic analysis.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ175662; ADR51742.1; -; Genomic_RNA.
DR Proteomes; UP000101507; 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 29..182
FT /note="Peptidase C28"
FT /evidence="ECO:0000259|PROSITE:PS51887"
FT DOMAIN 1189..1353
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1652..1848
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 2096..2214
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 198..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2332 AA; 259191 MW; 2DDA3F099565FE8C CRC64;
MNTTDCFIAL LHALREIKTL FRTRTHGKME FTLYNGEKKT FYSRPNRHDN CWLNTILQLF
RYVDEPFFDW VYDSPENLTL EAIRQLEELT GLELHEGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSDGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG EWQTKVQKRL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSSHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTY GYATTEDFVS GPNTSGLETR VVQAERFFKT HLFDWVTSDS
FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN QFNGGCLLVA MVPELCSISK
RELYQLTLFP HQFINPRTNM TAHITVPFVG VNRYDQYKVH KPWTLVVMVV APLTVNTEGA
PQIKVYANIA PTNVHVAGEF PSKEGIFPVA CSDGYGGLVT TDPKTADPAY GKVFNPPRNM
LPGRFTNFLD VAEACPTFLH FEGDVPYVTT KTDSDRVLAQ FDLSLAAKHM SNTFLAGLAQ
YYTQYSGTIN LHFMFTGPTD AKARYMIAYA PPGMEPPKTP EAAAHCIHAE WDTGLNSKFT
FSIPYLSAAD YAYTASDTAE TTNVQGWVCL FQITHGKADG DALVVLASAG KDFELRLPVD
ARTQTTSTGE SADPVTATVE NYGGETQVQR RQHTDVSFIL DRFVKVTPKD QINVLDLMQT
PAHTLVGALL RAATYYFADL EVAVKHEGNL TWVPNGAPET ALDNTTNPTA YHKAPLTRLA
LPYTAPHRVL ATVYNGNCKY GESHTTNVRG DLQVLAQKAA ITLPTSFNYG AIKATRVTEL
LYRMKRAETY CPRPLLAIHP DEARHKQKIV APVKQLLNFD LLKLAGDVES NPGPFFFSDV
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELATGV KAIRTGLDEA KPWYKLIKLL
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP
ILLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
IASEEKFVTM TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RTDSVWYCPP DPDHFDGYNQ
QAVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
PRTMVCPDAL NRRFHFDIDV SAKDGYKINN KLDIVKALED THTNPVAMFQ YDCALLNGMA
VEMKRMQQDM FKPQPPLQNV YQLVQEVIER VELHEKVSSH PIFKQISIPS QKSVLYFLIE
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
IRETRKRQQM VDDAVSEYIE KANITTDDKT LDEAEKNPLE TSGTSAVGFR ERALPGHKVS
DDVNSEPAKP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ EGPYAGLMER QKPLKVKAKA
PVVKEGPYEG PVKKPVALKV KARNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC
CATGVFGTAY LVPRHLFAEK YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
FAYKAATKAG YCGGAVLAKD GAETFILGTH SAGGNGVGYC SCVSRSMLLK MKVHIDPEPH
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNRDPRLNE GVALDEVIFS
KHKGDTKMSE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG
LPWALQGKRR GALIDFENGT VGPEVEAALE LMEKREYKFA CQTFLKDEIR PMEKVRAGKT
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK RITVEGGMPS
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
//
