ID X5CBY0_9PICO Unreviewed; 1397 AA.
AC X5CBY0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=p2/P3 polyprotein {ECO:0000313|EMBL:AHW45745.1};
DE Flags: Fragment;
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:AHW45745.1};
RN [1] {ECO:0000313|EMBL:AHW45745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=O/ETH/03/96 {ECO:0000313|EMBL:AHW45745.1};
RX PubMed=25818579; DOI=10.1016/j.vetmic.2015.03.007;
RA Nsamba P., de Beer T.A., Chitray M., Scott K., Vosloo W., Maree F.F.;
RT "Determination of common genetic variants within the non-structural
RT proteins of foot-and-mouth disease viruses isolated in sub-Saharan
RT Africa.";
RL Vet. Microbiol. 177:106-122(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
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DR EMBL; KJ144929; AHW45745.1; -; Genomic_RNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; 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:InterPro.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23210; Aphthovirus_RdRp; 1.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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 Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022706}.
FT DOMAIN 254..418
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 717..913
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 1161..1279
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 594..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHW45745.1"
SQ SEQUENCE 1397 AA; 155613 MW; DDABF2FD89D0965A CRC64;
LLNFDLLKLA GDVEPNPGPF FFSDVRSNFS KLVETINQMQ EDMSTKHGPD FNRLVSAFEE
LATGVKAIRT GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF
VVKKISDSLS SLFHVPAPVF SFGAPILLAG LVKVASSFFR STPEDLERAE KQLKARDIND
IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP GILEKQRDLN DPSKYKEAKE
WLDNARQACL KSGNTHIANL CKVTAPAPSK SRPEPVVVCL RGKSGQGKSF LANVLAQALS
THFTGRTDSV WYCPPDPDHF DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFIPPMA
SLEDKGKPFN SKVIIATTNL YSGFTPRTMV CPDALNRRFH FDIDVSAKDG YKVNNRLDII
KALEDTHTNP VAMFQYDCAL LNGMAVDMKR MQQDVFKPKP PLQNVYQLVQ EVIDQVELHE
KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIDFFEGMV HDSIKEELRP LIQQTSFVKR
AFKRLKENFE IVALCLTLLA NIVIMIRETR KRQKMVDDAV NDYIEKANIT TDDKTLDEAE
KNPLETSGAS TIGFRERALP GQVARDDVDS EPAKPVEEQP QAEGPYSGPL ERQKPLKVRA
KLPQQEGPYA GPMERQKPLK VTAKAPVVKE GPYEGPVKKP VALKVKAKNL IVTESGPPPT
DLQKLVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM LDGRAMTDSD
YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDT ARMKKGTPVV GVINNADVGR
LIFSGDALTY KDIVVCMDGD TMPGLFAYRA ATKAGYCGGA VLAKDGADTF IVGTHSAGGN
GVGYCSCVSR SMLLKMKAHI DPEPHHEGLI IDTRDVEERV HVMRKTKLAP TVAHGVFNPE
FGPAALSNRD PRLNEGVVLD EVIFSKHKGD TKMSEEDKAL FRRCAADYAS HLHSVLGMAN
APLSVYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV TAALELMEKR
EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR MMIGRFCAQM HSNNGPQIGS
AVGCNPDVDW QRFGTHFSQY RNVWDVDYSA FDANHCSDAM NIMFEEVFRT DFGFHPNAEW
ILKTLVNTEH AYENKRITVE GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM
ISYGDDIVVA SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF EPFQGLFEIP
SYRSLYLRWV NAVCGDA
//
