RDRP_SCPMV
ID RDRP_SCPMV Reviewed; 956 AA.
AC P21405;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
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 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 cleavage 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:0000255|PROSITE-ProRule:PRU00539}.
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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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=P21405-1; Sequence=Displayed;
CC Name=Polyprotein P2A;
CC IsoId=Q83470-1; 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; M23021; AAA46565.1; -; Genomic_RNA.
DR PIR; B33739; RRBWSC.
DR RefSeq; NP_042301.2; NC_001625.2.
DR RefSeq; NP_042302.3; NC_001625.2. [P21405-1]
DR SMR; P21405; -.
DR PRIDE; P21405; -.
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: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:0039694; P:viral RNA genome replication; 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 InterPro; IPR007094; RNA-dir_pol_PSvirus.
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.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Covalent protein-RNA linkage; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..956
FT /note="Replicase polyprotein P2AB"
FT /id="PRO_0000222496"
FT CHAIN 1..132
FT /note="N-terminal protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409843"
FT CHAIN 133..325
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409844"
FT CHAIN 326..402
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409845"
FT CHAIN 403..956
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409846"
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 DOMAIN 694..808
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
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:0000250"
FT SITE 402..403
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 956 AA; 104849 MW; 4670F3E7CDB7C85C 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 NLLAGGRTQC
LAAQIELGDY KFSCGPTHET GGMPFRNCGS STCKFREVSR KPVADAVTAA TKVFPELSEL
GWPERGSGAE IGSLLLQAGK FVPTKAPSNL EQAYNNLLSR YPRSKPLACF RQGTWSFDAI
FEQVVSKATS AEINQKASPG VPLSRLATTN KDLMAQHMQF VAACVTGRVP LLASFEDIHA
LSPTEMVEMG LCDPVRLFVK QEPHPSRKLK EGRYRLISSV SIVDQLVERM LFGAQNELEI
AEWQSIPSKP GMGLSVIHQA DAIFRDLRVK HTVCPAAEAD ISGFDWSVQD WELWADVEMR
IVLGSFPPMM ARAARNRFSC FMNSVLQLSN GQLLQQELPG IMKSGSYCTS STNSRIRCLM
AELIGSPWCI AMGDDSVEGF VEGAREKYAG LGHLCKDYKP CATTPTGQLY AVEFCSHVIK
RNKAFLTSWP KTLYRFLSTP RETLEDLERE LASSPMWHKI QSYVRSIPSP DKTARDKSIC
NGYPLDQEAI STSYSEYSSK SASAEATREA ACCAGAQAYP SWGIHGPYCS GDHGEA
