P2A_SCPMV
ID P2A_SCPMV Reviewed; 572 AA.
AC Q83470;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Polyprotein P2A;
DE Contains:
DE RecName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Serine protease;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=VPg;
DE Contains:
DE RecName: Full=Putative protein p10;
DE Contains:
DE RecName: Full=Putative protein p8;
GN ORFNames=ORF2A;
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;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2823471; DOI=10.1016/0042-6822(87)90172-3;
RA Wu S., Rinehart C.A., Kaesberg P.;
RT "Sequence and organization of southern bean mosaic virus genomic RNA.";
RL Virology 161:73-80(1987).
RN [2]
RP SEQUENCE REVISION TO 555, GENOME REANNOTATION, AND RIBOSOMAL FRAMESHIFT.
RX PubMed=17115301; DOI=10.1007/s00705-006-0867-z;
RA Meier M., Truve E.;
RT "Sobemoviruses possess a common CfMV-like genomic organization.";
RL Arch. Virol. 152:635-640(2007).
CC -!- FUNCTION: [Serine protease]: Responsible for cleavages of polyprotein
CC P2A and replicase polyprotein P2AB.
CC -!- FUNCTION: [VPg]: Covalently attached to the 5' extremity of the genomic
CC and subgenomic RNAs. It may serve as a primer for the replicase.
CC -!- SUBCELLULAR LOCATION: [Polyprotein P2A]: Host membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [N-terminal protein]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Polyprotein P2A;
CC IsoId=Q83470-1; Sequence=Displayed;
CC Name=Replicase polyprotein P2AB;
CC IsoId=P21405-1; Sequence=External;
CC -!- PTM: The polyprotein is proteolytically cleaved into several chains by
CC the viral protease. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Polyprotein P2A]: Produced by conventional
CC translation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46566.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M23021; AAA46566.1; ALT_SEQ; Genomic_RNA.
DR PIR; C33739; C33739.
DR RefSeq; NP_042301.2; NC_001625.2. [Q83470-1]
DR RefSeq; NP_042302.3; NC_001625.2.
DR SMR; Q83470; -.
DR GeneID; 1481842; -.
DR GeneID; 1481843; -.
DR KEGG; vg:1481842; -.
DR KEGG; vg:1481843; -.
DR Proteomes; UP000008033; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
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 Covalent protein-RNA linkage; Host membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Ribosomal frameshifting; Serine protease; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..572
FT /note="Polyprotein P2A"
FT /id="PRO_0000338015"
FT CHAIN 1..132
FT /note="N-terminal protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409833"
FT CHAIN 133..325
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409834"
FT CHAIN 326..402
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409835"
FT CHAIN 403..499
FT /note="Putative protein p10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409836"
FT CHAIN 500..572
FT /note="Putative protein p8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409837"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 135..330
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT REGION 498..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 216
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 284
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT SITE 132..133
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 325..326
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 402..403
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 499..500
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 572 AA; 62182 MW; 019F112AE0CB0F99 CRC64;
MYRPSCLSYV LLVANMWSFA VCANAFIYGS YDPSHNIPIV ALMTLCATGL WLSTSVVSFG
IRYVRVRVSP EKTQNRTIYV SSGLPHFDPV YGVVKKCEPM GGGPAIELQV NPSWIHLLPT
SPAINKVEVG QESAILGSTY SVVETGGEPK SLVAVKSGDS TLGFGARVYH EGMDVLMVPH
HVWYNDKPHT ALAKNGRSVD TEDWEVEAAC ADPRIDFVLV KVPTAVWAKL AVRSTKVLAP
VHGTAVQTFG GQDSKQLFSG LGKAKALDNA WEFTHTAPTA KGWSGTPLYT RDGIVGMHTG
YVDIGTSNRA INMHFIMSCL VSKMETLPPE LGYREISLED VGLRSFEFLE VEIENRGKVK
LGKREFAWVP KGKAWADMLD DDDLPLPPKM VNGNLVWADA QESFDGALPL NCLRAAGRNV
LPPKLNLVTI NSPVDPPTKQ VACPSEIVDH RLASLEKCLE NLLQTLSQPQ QKFSQNSLSS
GGLKGDQELK LAPCYSKQES LFPPKPRATS SKPITTSSPG TPGRSPLPVS GKELGPSTQS
SSKLSRKQRR RRSTKRPVQG SPSPASPPPT RT
