ID A0A1I9W7D2_SCPMV Unreviewed; 534 AA. AC A0A1I9W7D2; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 19-JAN-2022, entry version 12. DE SubName: Full=Polyprotein P2a {ECO:0000313|EMBL:APA23083.1}; DE Flags: Fragment; OS Southern cowpea mosaic virus (SCPMV) (Southern bean mosaic virus (strain OS cowpea)). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Sobelivirales; Solemoviridae; Sobemovirus. OX NCBI_TaxID=196398 {ECO:0000313|EMBL:APA23083.1}; OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida). OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean). OH NCBI_TaxID=3915; Vigna mungo (Black gram) (Phaseolus mungo). OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea). RN [1] {ECO:0000313|EMBL:APA23083.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BE250 {ECO:0000313|EMBL:APA23083.1}; RX PubMed=27764211; RA Palanga E., Filloux D., Martin D.P., Fernandez E., Gargani D., RA Ferdinand R., Zabre J., Bouda Z., Neya J.B., Sawadogo M., Traore O., RA Peterschmitt M., Roumagnac P.; RT "Metagenomic-Based Screening and Molecular Characterization of Cowpea- RT Infecting Viruses in Burkina Faso."; RL PLoS ONE 11:E0165188-E0165188(2016). CC -!- FUNCTION: covalently attached to the 5' extremity of the genomic and CC subgenomic RNAs. It may serve as a primer for the replicase. CC {ECO:0000256|ARBA:ARBA00003319}. CC -!- FUNCTION: responsible for cleavages of polyprotein P2A and replicase CC polyprotein P2AB. {ECO:0000256|ARBA:ARBA00003816}. CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|ARBA:ARBA00004301}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}. 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; KX599170; APA23083.1; -; Genomic_RNA. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0016032; P:viral process; IEA:InterPro. DR Gene3D; 2.40.10.10; -; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR000382; Peptidase_S39B_luteovirus. DR Pfam; PF02122; Peptidase_S39; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR PROSITE; PS51868; PEPTIDASE_S39; 1. PE 4: Predicted; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|ARBA:ARBA00022870}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758}. FT DOMAIN 97..292 FT /note="Peptidase S39" FT /evidence="ECO:0000259|PROSITE:PS51868" FT REGION 460..534 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 465..486 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:APA23083.1" SQ SEQUENCE 534 AA; 57870 MW; 9609E5875A40A767 CRC64; IVALVTLCAT GLWLSTSAVS FGIRYVRVRV SPEKTQNRTI YVSSGLPHFD PVYGVIMKCE PMGGGPAIEL QVNPSWIHLL PTSPAINKVE AGQESAILGS TYSVVETGGE PKSLVAIKSG DSTLGFGARV YHEGMDVLMV PHHVWYNDKP HTALAKNGRS VDTEDWEVEA ACADPRIDFV LVKVPTAVWA KLAVRSTRVL APVHGTAVQT FGGQDSKHLF SGLGKAKALD NAWEFTHTAP TAKGWSGTPL YTRDGIVGMH TGYVDIGTSN RAINMHFIMS CLVSKMETLP PELGYREISL EDVGLRSFEF LEVEIENRGK VKLGKREFAW VPKGKAWADM LDDDDLPPPP KMVNGNLVWA DAQESFDGAL PLNCLRAAGR NVLPPKLNLV TINSPVDPPT KQVACHSEIV DHRLASLEKC LENLLQTLSQ PQQKFSQSSP NSGGLKGDQE LKLAPCYSKQ ESLFPPKPRV TSSKPATTSL PGTPGQSPSP ALGKELGPST QSSSKLSRKQ RRRRSTKRPV QGSPSPVSPP PTRT //