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Genome polyprotein

 T1RTJ1_9PICO            Unreviewed;      2332 AA.
T1RTJ1;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00711595};
Foot-and-mouth disease virus - type O.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=12118 {ECO:0000313|EMBL:AGO58290.1, ECO:0000313|Proteomes:UP000121296};
[1] {ECO:0000313|EMBL:AGO58290.1, ECO:0000313|Proteomes:UP000121296}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MOG/7/2010 {ECO:0000313|EMBL:AGO58290.1};
PubMed=24007643;
Valdazo-Gonzalez B., Timina A., Scherbakov A., Abdul-Hamid N.F.,
Knowles N.J., King D.P.;
"Multiple introductions of serotype O foot-and-mouth disease viruses
into East Asia in 2010--2011.";
Vet. Res. 44:76-76(2013).
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00817576}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- CATALYTIC ACTIVITY: 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.
{ECO:0000256|SAAS:SAAS00711755}.
-!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane
{ECO:0000256|SAAS:SAAS00711512}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS00711512}; Cytoplasmic side
{ECO:0000256|SAAS:SAAS00711512}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00803776}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000256|SAAS:SAAS00782306}.
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EMBL; KF112881; AGO58290.1; -; Genomic_RNA.
Proteomes; UP000121296; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
InterPro; IPR015031; Capsid_VP4_Picornavir.
InterPro; IPR004080; FMDV_VP1_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008739; Peptidase_C28.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF05408; Peptidase_C28; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF08935; VP4_2; 1.
PRINTS; PR00918; CALICVIRUSNS.
PRINTS; PR01542; FMDVP1COAT.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|SAAS:SAAS00124676};
Capsid protein {ECO:0000256|SAAS:SAAS00803779};
Complete proteome {ECO:0000313|Proteomes:UP000121296};
Helicase {ECO:0000256|SAAS:SAAS00124676};
Host cytoplasm {ECO:0000256|SAAS:SAAS00711571};
Host cytoplasmic vesicle {ECO:0000256|SAAS:SAAS00711589};
Host membrane {ECO:0000256|SAAS:SAAS00795395};
Host-virus interaction {ECO:0000256|SAAS:SAAS00711583};
Hydrolase {ECO:0000256|SAAS:SAAS00124676,
ECO:0000256|SAAS:SAAS00482329};
Ion channel {ECO:0000256|SAAS:SAAS00711569};
Ion transport {ECO:0000256|SAAS:SAAS00711569};
Membrane {ECO:0000256|SAAS:SAAS00795395};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00124676};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|SAAS:SAAS00482329};
RNA-binding {ECO:0000256|SAAS:SAAS00711776};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Thiol protease {ECO:0000256|SAAS:SAAS00482329};
Transferase {ECO:0000256|SAAS:SAAS00510600};
Transport {ECO:0000256|SAAS:SAAS00711569};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00711583};
Viral ion channel {ECO:0000256|SAAS:SAAS00711569};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00711583, ECO:0000256|SAAS:SAAS00803779};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00711583}.
DOMAIN 1189 1353 SF3 helicase.
{ECO:0000259|PROSITE:PS51218}.
DOMAIN 2096 2214 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
SEQUENCE 2332 AA; 259108 MW; A9C666B7CFDE3D76 CRC64;
MNTTDCFIAL LHAIREIKAR LFLKTQEKME FTLYNGERKT FYSRPNNNDN CWLNAILQLF
RYVDEPFFDW VYESPENRTL EAIEQLEGIT GLELHEGGPP ALVVWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG DWKAKVQRRL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT HLFDWVTSDP
FGRCHLLELP TDHKGVYGGL TDSYAYMRNG WDVEVTAVGN QFNGGCLLVA MVPELCSIQK
RELYQLTLFP HQFINPRTNM TAHIKVPFVG VNRYDQYKVH KPWTLVVMVV APLTVNTEGA
PQIKVYANIA PTDVHVAGEF PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNM
LPGRFTNFLD VAEACPTFLH FEGDVPYVTT KTDSDRILAQ FDLSLAAKHM SNTFLAGLAQ
YYTQYSGTIN LHFMFTGPTD AKARYMIAYA PPGMEPPRTP EAAAHCIHAE WDTGLNSKFT
FSIPYLSAAD YAYTASDTAE TTNVQGWVCL FQITHGKADG DALVVLASAG KDFELRLPVD
ARQQTTSTGE SADPVTATVE NYGGETQVQR RHHTDVSFIL DRFVKVTPQD QINVLDLMQT
PPHTLVGALL RAATYYFADL EVAVKHEGDL TWVPNGAPEA ALGNTTNPTA YHKAPLTRLA
LPYTAPHRVL ATVYNGNCKY AGGPLTNVRG DLQVLAQKAA RPLPTSFNYG AIKATRVAEL
LYRMKRAETY CPRPLLAVHP DQARHKQKIV APVKQSWKFD LLKLAGDVES NPGPFFFSDV
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELATGV KAIRTGLDEA KPWYKLIKLL
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP
ILLAGLVKVA SGFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
IASEEKFVTM TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RTDSVWYCPP DPDHFDGYNQ
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
PRTMVCPDAL NRRFHFDIDV SAKDGYKTNN KLDIIKALED THTNPVAMFQ YDCALLNGMA
VEMKRMQQDM FKPQPPLQNV YQLVQEVIDR VELHEKVSSH SIFKQISIPS QKSVLYFLIE
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRGFKRL KENFEIVALC LTLLANIVIM
IRETRKRQQM VDDAVNEYIE KANITTDDKT LDEAEKNPLE TSGASTVGFR ERTLPGHKTR
DDVDSEPAKP VEEHPQAEGP YAGPLERQKP LKVRAKLPRQ EGPYAGPMER QKPLKVKVNA
PVVKEGPYEG PVKKPVALKV KAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC
CATGVFGTAY LVPRHLFAEK YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALIVLH
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
FAYKAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK MKAHIDPEPH
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEYGPAA LSNKDPRLNE GVVLDEVIFS
KHKGDTKMTP EDKALFRRCA ADYASRLHSV LGTANAPLSV YEAIKGVDGL DAMEPDTAPG
LPWALQGRRR GALIDFENGT VGPEVQAALE LMEKREYKFA CQTFLKDEIR PMEKVRAGKT
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK RITVEGGMPS
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA


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