ID X5CZT3_9PICO Unreviewed; 1397 AA.
AC X5CZT3;
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:AHW45753.1};
DE Flags: Fragment;
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:AHW45753.1};
RN [1] {ECO:0000313|EMBL:AHW45753.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/TAN/04/80 {ECO:0000313|EMBL:AHW45753.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ144937; AHW45753.1; -; 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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHW45753.1"
SQ SEQUENCE 1397 AA; 155704 MW; 65BD223A43E118D6 CRC64;
LLNFDLLKLA GDVESNPGPF FFSDVRSNFA KLVDTINQMQ EDMSTKHGPD FNRLVSAFEE
LATGVKAIRT GLDEAKPWYK LIKLLSRLSC MAAVAARSKD PVLVAIMLAD TGLEILDSTF
VVKKISDSLS SLFHVPAPVF SFGAPILLAG LVKIASSFFR STPEELERAE KQLKARDIND
IFAILKNGEW LVKLILAIRD WIKAWIASEE KFVTMTDLVP GILEKQRDLN DPSKYKEAKE
WLDNARQACL KSGNVHIANL CKVVAPAPSK SRPEPVVVCL RGKSGQGKSF LANVLAQAIS
THFTGRTDSV WYCPPDPDHF DGYNQQTVVV MDDLGQNPDG KDFKYFAQMV STTGFVPPMA
SLEDKGKPFN SKVIIATTNL YSGFTPRTMV CPDALNRRFH FDIDVSAKDG YRINNKLDII
KALEDTHTNP VAMFQYDCAL LNGMAVEMKR MQQDMFKPQP PIQNVYQLVQ EVIERVELHE
KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE AAIEFFEGMV HDSIKEELRP LIQQTSFVKR
AFKRLKENFE IVALCLTLLA NIVIMIRETR KRQQMVDNAV NEYIEKANIT TDDKTLDEAE
KNPLETSGAS TVGFRERTLP GHNASDDVNS EPAKPVEEQP QAEGPYAGPF ERQKPLKVKA
RLPQQEGPYA GPMERQKPLK VKVKTPVVKE GPYEGPVKKP VALKVKAKNL IVTESGAPPT
DLQKMVMGNT KPVELILDGK TVAICCATGV FGTAYLVPRH LFAEKYDKIM LDGRAMTDSD
YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV RDITKHFRDT ARMKKGTPVV GVVNNADVGR
LIFSGEALTY KDIVVCMDGD TMPGLFAYRA ATKAGYCGGA VLAKDGADTF IVGTHSAGGN
GVGYCSCVSK SMLLKMKAHV DPEPHHEGLI VDTRDVEERV HVMRKTKLAP TVAHGVFNPE
FGPAALSNKD PRLNEGVVLD EVIFSKHKGD TKMTEEDKAL FRRCAADYAS RLHSVLGTAN
APLSIYEAIK GVDGLDAMEP DTAPGLPWAL QGKRRGALID FENGTVGPEV AAPLELMEKR
EYKFACQTFL KDEIRPMEKV RAGKTRIVDV LPVEHILYTR MMIGRFCAQM HSNNGPQIGS
AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA FDANHCSDAM NIMFEEVFRT EFGFHPNAEW
ILKTLVNTEH AYENKRITVE GGMPSGCSAT SIINTILNNI YVLYALRRHY EGVELDTYTM
ISYGDDIVVA SDYDLDFEAL KPHFKSLGQT ITPADKSDKG FVLGHSITDV TFLKRHFHMD
YGTGFYKPVM ASKTLEAILS FARRGTIQEK LISVAGLAVH SGPDEYRRLF EPFQGLFEIP
SYRSLYLRWV NAVCGDA
//
