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 02-OCT-2024, entry version 73. 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; Cocksfoot mottle virus. 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. 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; Z48630; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; DQ680848; ABG73619.1; -; Genomic_RNA. DR SMR; Q0PW25; -. DR MEROPS; S39.001; -. DR iPTMnet; Q0PW25; -. DR Proteomes; UP000001461; Segment. DR Proteomes; UP000008994; Segment. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW. DR CDD; cd23180; ps-ssRNAv_Solemoviridae_RdRp; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 //