RDRP_SBMVA
ID RDRP_SBMVA Reviewed; 962 AA.
AC O72157;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Replicase polyprotein P2AB;
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=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=RdRp;
GN ORFNames=ORF2A-2B;
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 PROTEIN SEQUENCE OF 326-345, AND CHARACTERIZATION OF VPG.
RX PubMed=9778784; DOI=10.1023/a:1008044715899;
RA van der Wilk F., Verbeek M., Dullemans A., van den Heuvel J.;
RT "The genome-linked protein (VPg) of southern bean mosaic virus is encoded
RT by the ORF2.";
RL Virus Genes 17:21-24(1998).
RN [3]
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 -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome.
CC {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48;
CC -!- SUBCELLULAR LOCATION: [N-terminal protein]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Replicase polyprotein P2AB]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein P2AB;
CC IsoId=O72157-1; Sequence=Displayed;
CC Name=Polyprotein P2A;
CC IsoId=O73564-1; Sequence=External;
CC -!- PTM: The polyprotein is proteolytically cleaved into several chains by
CC the viral protease.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein P2AB]: Produced by -1
CC ribosomal frameshifting at the 2A-2B genes boundary.
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DR EMBL; AF055887; AAC15983.1; -; Genomic_RNA.
DR SMR; O72157; -.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR Pfam; PF02122; Peptidase_S39; 1.
DR Pfam; PF02123; RdRP_4; 1.
DR PRINTS; PR00914; LVIRUSRNAPOL.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51868; PEPTIDASE_S39; 1.
PE 1: Evidence at protein level;
KW Covalent protein-RNA linkage; Direct protein sequencing; Host membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Reference proteome; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW Serine protease; Transferase; Transmembrane; Transmembrane helix;
KW Viral RNA replication.
FT CHAIN 1..962
FT /note="Replicase polyprotein P2AB"
FT /id="PRO_0000402470"
FT CHAIN 1..132
FT /note="N-terminal protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409847"
FT CHAIN 133..325
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409848"
FT CHAIN 326..402
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409849"
FT CHAIN 403..962
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409850"
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 DOMAIN 692..806
FT /note="RdRp catalytic"
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"
SQ SEQUENCE 962 AA; 106566 MW; BF840BC106F9CF82 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 QETVAEPLNL PAGGRVKALA
ALSQLAGYDF KEGEAASTRG MPLRFVGQSA CKFRELCRKD TPDEVLRATR VFPELSDFSW
PERGSKAELH SLLLQAGKFN PTGIPRNLEG ACQNLLERYP ASKSCYCLRG EAWSFDAVYE
EVCKKAQSAE INEKASPGVP LSRLASTNKD LLKRHLELVA LCVTERLFLL SEAEDLLDES
PVDLVRRGLC DPVRLFVKQE PHASRKVREG RFRLISSVSL VDQLVERMLF GPQNQLEIAE
WEHIPSKPGM GLSLRQQAKS LFDDLRVKHS RCPAAEADIS GFDWSVQDWE LWADVEMRIV
LGGFGHKLAK AAQNRFSCFM NSVFQLSDGT LIEQQLPGIM KSGSYCTSST NSRIRCLMAE
LIGSPWCIAM GDDSVEGWVD GAKDKYMRLG HTCKDYKPCA TTISGRLYEV EFCSHVIRED
RCWLASWPKT LFKYLSEGKW FFEDLERDVS SSPHWPRIRH YVVGNTPSPH KTNLQNQSPR
YGEEVDKTTV NQGYSEHSGS PGHSIEEAQE PEAAPFCCEA ASVYPGWGVH GPYCSGDYGS
LT
