RDRP_CFMVN
ID RDRP_CFMVN Reviewed; 942 AA.
AC Q0PW25;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 Cocksfoot mottle virus (isolate Dactylis glomerata/Norway/CfMV-NO/1995)
OS (CfMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Sobemovirus.
OX NCBI_TaxID=1005059;
OH NCBI_TaxID=4509; Dactylis glomerata (Orchard grass) (Cock's-foot grass).
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7595389; DOI=10.1099/0022-1317-76-11-2817;
RA Maekinen K., Tamm T., Naess V., Truve E., Puurand U., Munthe T., Saarma M.;
RT "Characterization of cocksfoot mottle sobemovirus genomic RNA and sequence
RT comparison with related viruses.";
RL J. Gen. Virol. 76:2817-2825(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16732485; DOI=10.1007/s11262-005-6917-x;
RA Meier M., Paves H., Olspert A., Tamm T., Truve E.;
RT "P1 protein of Cocksfoot mottle virus is indispensable for the systemic
RT spread of the virus.";
RL Virus Genes 32:321-326(2006).
RN [3]
RP PROTEIN SEQUENCE OF 320-336, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND
RP CHARACTERIZATION OF VPG.
RX PubMed=11038392; DOI=10.1099/0022-1317-81-11-2783;
RA Maekinen K., Maekelaeinen K., Arshava N., Tamm T., Merits A., Truve E.,
RA Zavriev S., Saarma M.;
RT "Characterization of VPg and the polyprotein processing of cocksfoot mottle
RT virus (genus Sobemovirus).";
RL J. Gen. Virol. 81:2783-2789(2000).
RN [4]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=7886961; DOI=10.1006/viro.1995.1118;
RA Maekinen K., Naess V., Tamm T., Truve E., Aaspollu A., Saarma M.;
RT "The putative replicase of the cocksfoot mottle sobemovirus is translated
RT as a part of the polyprotein by -1 ribosomal frameshift.";
RL Virology 207:566-571(1995).
RN [5]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=10848968; DOI=10.1046/j.1432-1327.2000.01379.x;
RA Lucchesi J., Makelainen K., Merits A., Tamm T., Makinen K.;
RT "Regulation of -1 ribosomal frameshifting directed by cocksfoot mottle
RT sobemovirus genome.";
RL Eur. J. Biochem. 267:3523-3529(2000).
RN [6]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=19748532; DOI=10.1016/j.virusres.2009.09.002;
RA Tamm T., Suurvali J., Lucchesi J., Olspert A., Truve E.;
RT "Stem-loop structure of Cocksfoot mottle virus RNA is indispensable for
RT programmed -1 ribosomal frameshifting.";
RL Virus Res. 146:73-80(2009).
RN [7]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND PHOSPHORYLATION AT THR-339 AND
RP SER-390.
RX PubMed=21068217; DOI=10.1099/vir.0.026476-0;
RA Olspert A., Peil L., Hebrard E., Fargette D., Truve E.;
RT "Protein-RNA linkage and post-translational modifications of two
RT sobemovirus VPgs.";
RL J. Gen. Virol. 92:445-452(2011).
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: [Replicase polyprotein P2AB]: Host membrane
CC {ECO:0000305}; 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=Replicase polyprotein P2AB;
CC IsoId=Q0PW25-1; Sequence=Displayed;
CC Name=Polyprotein P2A;
CC IsoId=Q89504-1; Sequence=External;
CC -!- PTM: The polyprotein is proteolytically cleaved into several chains by
CC the viral protease. {ECO:0000269|PubMed:11038392,
CC ECO:0000269|PubMed:21068217}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein P2AB]: Produced by -1
CC ribosomal frameshifting at the 2A-2B genes boundary.
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DR EMBL; Z48630; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; DQ680848; ABG73619.1; -; Genomic_RNA.
DR SMR; Q0PW25; -.
DR MEROPS; S39.001; -.
DR iPTMnet; Q0PW25; -.
DR PRIDE; Q0PW25; -.
DR Proteomes; UP000001461; Genome.
DR Proteomes; UP000008994; 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; 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.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW Covalent protein-RNA linkage; Direct protein sequencing; Host membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Serine protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..942
FT /note="Replicase polyprotein P2AB"
FT /id="PRO_0000409857"
FT CHAIN 1..130
FT /note="N-terminal protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409858"
FT CHAIN 131..319
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409859"
FT CHAIN 320..397
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409860"
FT CHAIN 398..942
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409861"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 129..326
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT DOMAIN 691..805
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 888..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 209
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 276
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT SITE 130..131
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 319..320
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 324
FT /note="Interacts with viral RNA (covalent)"
FT SITE 397..398
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT MOD_RES 339
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:21068217"
FT MOD_RES 390
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:21068217"
FT CONFLICT 27
FT /note="I -> V (in Ref. 1; Z48630)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="CE -> WQ (in Ref. 1; Z48630)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> A (in Ref. 1; Z48630)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="K -> R (in Ref. 1; Z48630)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="T -> A (in Ref. 1; Z48630)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 103355 MW; 392D8EACFD0BCF76 CRC64;
MGCSVVGNCK SVMLMSRMSW SKLALLISVA MAAAMTDSPP TLICMGILVS VVLNWIVCAV
CEEASELILG VSLETTRPSP ARVIGEPVFD PRYGYVAPAI YDGKSFDVIL PISALSSAST
RKETVEMAVE NSRLQPLESS QTPKSLVALY SQDLLSGWGS RIKGPDGQEY LLTALHVWET
NISHLCKDGK KVPISGCPIV ASSADSDLDF VLVSVPKNAW SVLGVGVARL ELLKRRTVVT
VYGGLDSKTT YCATGVAELE NPFRIVTKVT TTGGWSGSPL YHKDAIVGLH LGARPSAGVN
RACNVAMAFR VVRKFVTVEN SELYPDQSSG PARELDAETY TERLEQGIAF TEYNISGITV
KTSDREWTTA EALRVARYKP LGGGKAWGDS DDEDTQETAI RPLNLPAGGL PTGQSALGQL
IEYAGYVWRD EGIINSNGMP FRSAGKSSCR FREAVCRAVH RDVRAAETEF PELKELAWPS
RGSKAEIGSL LFQAGRFERV EAPANLQLAI TNLQAQYPRS RPRSCFRREP WCREDFVAEI
EKIAHSGEIN LKASPGVPLA EIGVSNQQVI DVAWPLVCEA VVERLHALAS VDPRQHDWSP
EELVKRGLCD PVRLFVKQEP HSRQKIEQGR FRLISSVSLV DQLVERMLFG PQNTTEIALW
HSNPSKPGMG LSKASQVALL WEDLARKHQT HPGAMADISG FDWSVQDWEL WADVSMRIEL
GSFPALMAKA AISRFYCLMN ATFQLTNGEL LTQELPGLMK SGSYCTSSSN SRIRCLMAEL
IGSPWCIAMG DDSVEGWVDD APRKYSALGH LCKEYEACPV LPNGDLKEVS FCSHLISKGR
AELETWPKCL FRYLSGPHDV ESLEMELSSS RRWGQIVRYL RRIGRVSGND GEERSSNESP
ATTKTQGSAA AWGPPQEAWP VDGASLSTFE PSSSGWFHLE GW
