RDRP_CMVMB
ID RDRP_CMVMB Reviewed; 857 AA.
AC Q66145;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 64.
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 MB-8) (CMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Cucumovirus.
OX NCBI_TaxID=117122;
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 Karasawa A., Ito A., Okada I., Hase S., Ehara Y.;
RL Submitted (JUL-1996) 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; D86613; BAA13141.1; -; Genomic_RNA.
DR PRIDE; Q66145; -.
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..857
FT /note="RNA-directed RNA polymerase 2a"
FT /id="PRO_0000083278"
FT DOMAIN 511..624
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 780..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 96671 MW; 658EC9F705C463D6 CRC64;
MAFPAPAFSL ANLLNGSYGV DTPEDVERLR SEQREEAAAA CRNYRPLSAV DVSESVTEDA
HSLQTPDGAP AEAVSDEFVT YGAEDYLEKS DDELLVAFET MVKPMRIGQL WCPAFNKCSF
ISSIAMARAL LLAPRTSHRT MKCFEDLVAA IYTKSDFYYS EECEADDVQM DISSRDVPGY
SFEPWSRTSG FEPPPICEAC DMIMYQCPCF DFNALKKSCA ERTFADDYVI EGLDGVVDNA
TLLSNLGPFL VPVKCQYEKC PTPPIAIPPN LNRATDRVDI NLVQSICDST LPTHSNYDDS
FHQVFVESAD YSIDLDHVRL RQSDLIAKIP DSGHMIPVLN TGSGHKRVGT TKEVLTAIKK
RNADVPELGD SVNLSRLSKA VAERFFISYI NGNSLASSNF VNVVSNFHDY MEKWKSSGLS
YDDLPDLHAE NLQFYDHMIK SDVKPVVSDT LNIDRPIPAT ITYHKKSITS QFSPLFTALF
ERFQRCLRER IILPVGKISS LEMAGFDVKN KYCLEIDLSK FDKSQGEFHL LIQEHILNGL
GCPAPITKWW CDFHRFSYIR DRRAGVGMPI SFQRRTGDAF TYFGNTIVTM AEFAWCYDTD
QFEKLLFSGD DSLGFSLLPP VGDSSKFTTL YNMEAKVMEP SVPYICSKFL LSDEFGNTFS
VPDPLREVQR LGTKKIPYSD NDEFLFAHFM SFVDRLKFLD RMSQSCIDQL SIFFELKYKK
SGEEAALMLG AFKKYTANFQ SYKELYYSDR HQCELINSFC STEFRVERVN SNKQRKKYGI
ERRCDDKRRT PTGSYGGGEE AETKVSQTKS TGTRSQKSQR ESAFESQTVP LPTVLSSGWS
GTDRVVPPCE RGGVTRA
