P2A_SBMVA
ID P2A_SBMVA Reviewed; 575 AA.
AC O73564;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 65.
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 bean mosaic virus (isolate Bean/United States/Arkansas) (SBMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Sobemovirus.
OX NCBI_TaxID=652938;
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].
RC STRAIN=SBMV-B, and SBMV-S;
RX PubMed=9856101; DOI=10.1007/s007050050451;
RA Lee L., Anderson E.J.;
RT "Nucleotide sequence of a resistance breaking mutant of southern bean
RT mosaic virus.";
RL Arch. Virol. 143:2189-2201(1998).
RN [2]
RP SEQUENCE REVISION TO 557, 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=O73564-1; Sequence=Displayed;
CC Name=Replicase polyprotein P2AB;
CC IsoId=O72157-1; 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=AAC15984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC15988.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AF055887; AAC15984.1; ALT_SEQ; Genomic_RNA.
DR EMBL; AF055888; AAC15988.1; ALT_SEQ; Genomic_RNA.
DR SMR; O73564; -.
DR Proteomes; UP000001671; 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; 2.
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..575
FT /note="Polyprotein P2A"
FT /id="PRO_0000402469"
FT CHAIN 1..132
FT /note="N-terminal protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409838"
FT CHAIN 133..325
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409839"
FT CHAIN 326..402
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409840"
FT CHAIN 403..497
FT /note="Putative protein p10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409841"
FT CHAIN 498..575
FT /note="Putative protein p8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409842"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 135..335
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT REGION 513..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
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 497..498
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 575 AA; 62722 MW; 08956ADAFA40D1EC CRC64;
MYHPGRSPSF LITLANVICA AILFDIHTGG YQPGSLIPIV AWMTPFVTLL WLSASFATYL
YKYVRTRLLP EEKVARVYYT AQSAPYFDPA LGVMMQFAPS HGGASIEVQV NPSWISLLGG
SLKINGDDAS NESAVLGSFY SSVKPGDEPA SLVAIKSGPQ TIGFGCRTKI DGDDCLFTAN
HVWNNSMRPT ALAKRGKQVA IEDWETPLSC DHKMLDFVVV RVPKHVWSKL GVKATQLVCP
SDKDAVTCYG GSSSDNLLSG TGVCSKVDFS WKLTHSCPTA AGWSGTPIYS SRGVVGMHVG
FEDIGKLNRG VNAFYVSNYL LRSQETLPPE LSVIEIPFED VETRSYEFIE VEIKGRGKAK
LGKREFAWIP ESGKYWADDD DDSLPPPPKV VDGKMVWSSA QETVAEPLNY QRAAGSRPLP
PFLNLQATTS KKEKQPLQEE CPLDLLGSRL ASLESCVEKI LQMKSLELLG SSQNCQTSPG
PSEAPKQSFT PCYSKQESLI PLESQGILKE LVKTSLSATP PPNPVTVSVE KPGPSTQSTK
KSARRRNRRK STRKPVQESP SPASPQPTKT SLRGI
