ID   RDRP_CMVAS              Reviewed;         858 AA.
AC   O39436;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   29-SEP-2021, entry version 63.
DE   RecName: Full=RNA-directed RNA polymerase 2a;
DE            Short=protein 2a;
DE            EC=2.7.7.48;
GN   ORFNames=ORF2a;
OS   Cucumber mosaic virus (strain As) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=117118;
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Kim S.H., Park Y.I.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-dependent RNA polymerase which replicates the viral
CC       genome composed of 3 RNA segments, RNA1, RNA2 and RNA3. {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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- SUBUNIT: Interacts with replication protein 1a. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; AF033667; AAB86650.1; -; Genomic_RNA.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF00978; RdRP_2; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication.
FT   CHAIN           1..858
FT                   /note="RNA-directed RNA polymerase 2a"
FT                   /id="PRO_0000083271"
FT   DOMAIN          511..624
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          772..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  96809 MW;  5AF06495CBABA473 CRC64;
     MAFPAPAFSL ANLLNGSYGV DTPEEVERVR SEQRDEAAAA CRNYRPLPAV DVSESVPEDA
     HSLRTPDGAP SEEVSVEFVT YGAEDYLEKS DDELLVAFET MVKPMRIGQL WCPAFNKCSF
     ISSIAMARAL LLAPRTSHRT MKCFEDLVAA IYTKSDFYYD DECEADDVQI DISSRDVPGY
     SFEPWSRTSG FEPPPICEAC DMIMYQCPCF DFNALKKSCA ERTFADDYVI EGLDGVVNNA
     TLSSNLGPFL VPVKCPYEKC PTPVGEIPPD LNRATDRVDI NLVQSICDST LPTHSNYDDS
     FHQVFVESAD YSIDLDHVRL RQSDLIAKIP DSGHMIPVLN TGSGHKRVGT TKEVLTAIKK
     RNADVPELGD SVNLSRLSKA VAERFFISYI NGNSLASSNF VNVVSNFHDY MEKWKSSGLS
     YDDLPDLHAE NLQFYDHMIK SDVKPVVSDT LNIDRPVPAT ITYHKKGITS QFSPLFTALF
     ERFQRCLRER IILPVGKISS LEMAGFDVKN KHCFEIDLSK FDKSQGEFPF KIQEHILNGL
     GCPAPITKWW CDFHRFSYIR DRRAGVGMPI SFQRRTGDAF TYFGNTIVTM AEFAWCYDTD
     QFEKLLFSGD DSLGFSVLPP VGDPSKFTTL FNMEAKVMEP AVPYICSKFL LSDEFGNTFS
     VPDPLREVQR LGTKKIPCSD NDEFLFAHFM SFVDRLKFLD RMTQSCIDQL SLFFELKYRK
     SGEEAALMLG AFKKYTANFQ SYKELYYSDR RQCELINSFS CVELRIERSS STKQREKKDG
     IERRRNDKRR TPTGSYGGGE EAETKVSQAE STGTRSQKSQ REGAFKSQAV PLPTILSSRW
     FGTDRDVPPC EHGGIVRV