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 14-MAY-2014, entry version 39. 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 OS glomerata/Norway/CfMV-NO/1995) (CfMV). OC Viruses; ssRNA positive-strand viruses, no DNA stage; 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; RA Maekinen K., Tamm T., Naess V., Truve E., Puurand U., Munthe T., RA Saarma M.; RT "Characterization of cocksfoot mottle sobemovirus genomic RNA and RT sequence 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 RT systemic spread of the virus."; RL Virus Genes 32:321-326(2006). RN [3] RP PROTEIN SEQUENCE OF 320-336, PROTEOLYTIC PROCESSING OF POLYPROTEIN, RP AND CHARACTERIZATION OF VPG. RX PubMed=11038392; RA Maekinen K., Maekelaeinen K., Arshava N., Tamm T., Merits A., RA Truve E., Zavriev S., Saarma M.; RT "Characterization of VPg and the polyprotein processing of cocksfoot RT mottle 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 RT translated 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 RT for programmed -1 ribosomal frameshifting."; RL Virus Res. 146:73-80(2009). RN [7] RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND PHOSPHORYLATION AT THR-339 RP AND 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 cleavages of CC polyprotein P2A and replicase polyprotein P2AB. CC -!- FUNCTION: VPg: covalently attached to the 5' extremity of the CC genomic and subgenomic RNAs. It may serve as a primer for the CC replicase. CC -!- FUNCTION: RNA-directed RNA polymerase: replicates the viral genome CC (Potential). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBCELLULAR LOCATION: Replicase polyprotein P2AB: Host membrane; CC Multi-pass membrane protein (Potential). CC -!- SUBCELLULAR LOCATION: N-terminal protein: Host membrane; Multi- CC pass membrane protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Ribosomal frameshifting; Named isoforms=2; CC Name=Replicase polyprotein P2AB; CC IsoId=Q0PW25-1; Sequence=Displayed; CC Note=Produced by -1 ribosomal frameshifting at the 2A-2B genes CC boundary; CC Name=Polyprotein P2A; CC IsoId=Q89504-1; Sequence=External; CC Note=Produced by conventional translation; CC -!- PTM: The polyprotein is proteolytically cleaved into several CC chains by the viral protease. CC -!- SIMILARITY: Contains 1 peptidase S39A domain. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. 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 MEROPS; S39.001; -. 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 RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. 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 InterPro; IPR000382; Peptidase_S39B_luteovirus. DR InterPro; IPR001795; RNA-dir_pol_luteovirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR Pfam; PF02122; Peptidase_S39; 1. DR Pfam; PF02123; RdRP_4; 1. DR PRINTS; PR00914; LVIRUSRNAPOL. DR SUPFAM; SSF50494; SSF50494; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 1: Evidence at protein level; KW Complete proteome; Covalent protein-RNA linkage; KW Direct protein sequencing; Host membrane; Hydrolase; Membrane; KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; KW Reference proteome; Ribosomal frameshifting; KW RNA-directed RNA polymerase; Serine protease; Transferase; KW Transmembrane; Transmembrane helix; Viral RNA replication. FT CHAIN 1 942 Replicase polyprotein P2AB. FT /FTId=PRO_0000409857. FT CHAIN 1 130 N-terminal protein (Potential). FT /FTId=PRO_0000409858. FT CHAIN 131 319 Serine protease (Potential). FT /FTId=PRO_0000409859. FT CHAIN 320 397 VPg (Potential). FT /FTId=PRO_0000409860. FT CHAIN 398 942 RNA-directed RNA polymerase (Potential). FT /FTId=PRO_0000409861. FT TRANSMEM 10 30 Helical; (Potential). FT TRANSMEM 41 61 Helical; (Potential). FT DOMAIN 155 305 Peptidase S39A. FT DOMAIN 691 805 RdRp catalytic. FT ACT_SITE 176 176 For protease activity (Potential). FT ACT_SITE 209 209 For protease activity (Potential). FT ACT_SITE 276 276 For protease activity (Potential). FT BINDING 324 324 Viral RNA (covalent). FT SITE 130 131 Cleavage; by viral serine protease FT (Potential). FT SITE 319 320 Cleavage; by viral serine protease FT (Potential). FT SITE 397 398 Cleavage; by viral serine protease FT (Potential). FT MOD_RES 339 339 Phosphothreonine; by host. FT MOD_RES 390 390 Phosphoserine; by host. FT CONFLICT 27 27 I -> V (in Ref. 1; Z48630). FT CONFLICT 61 62 CE -> WQ (in Ref. 1; Z48630). FT CONFLICT 75 75 T -> A (in Ref. 1; Z48630). FT CONFLICT 217 217 K -> R (in Ref. 1; Z48630). FT CONFLICT 752 752 T -> A (in Ref. 1; Z48630). 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 //