ID   RDRP_MCMVK              Reviewed;         965 AA.
AC   P11640; Q9IBM2;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE            EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE   AltName: Full=111 kDa protein;
DE   AltName: Full=Protein p111;
DE   Contains:
DE     RecName: Full=Protein p50;
GN   ORFNames=ORF2;
OS   Maize chlorotic mottle virus (isolate United States/Kansas/1987) (MCMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Machlomovirus.
OX   NCBI_TaxID=882210;
OH   NCBI_TaxID=4577; Zea mays (Maize).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2726455; DOI=10.1093/nar/17.8.3163;
RA   Nutter R.C., Scheets K., Panganiban L.C., Lommel S.A.;
RT   "The complete nucleotide sequence of the maize chlorotic mottle virus
RT   genome.";
RL   Nucleic Acids Res. 17:3163-3177(1989).
RN   [2]
RP   FUNCTION.
RX   PubMed=27242072; DOI=10.1016/j.virusres.2016.04.024;
RA   Scheets K.;
RT   "Analysis of gene functions in Maize chlorotic mottle virus.";
RL   Virus Res. 222:71-79(2016).
CC   -!- FUNCTION: RNA-dependent RNA polymerase that plays an essential role in
CC       the virus replication. {ECO:0000269|PubMed:27242072}.
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   -!- MISCELLANEOUS: Readthrough of the terminator UAG occurs at position
CC       439.
CC   -!- SIMILARITY: Belongs to the tombusviridae RNA polymerase family.
CC       {ECO:0000305}.
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DR   EMBL; X14736; CAA32862.1; -; Genomic_RNA.
DR   EMBL; X14736; CAB55589.1; -; Genomic_RNA.
DR   PIR; JQ0058; JQ0058.
DR   RefSeq; NP_619718.1; NC_003627.1.
DR   RefSeq; NP_619719.1; NC_003627.1.
DR   PRIDE; P11640; -.
DR   GeneID; 2652939; -.
DR   GeneID; 2652940; -.
DR   KEGG; vg:2652939; -.
DR   KEGG; vg:2652940; -.
DR   Proteomes; UP000007071; Genome.
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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002166; RNA_pol_HCV.
DR   Pfam; PF00998; RdRP_3; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA suppression of termination; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..965
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000040211"
FT   CHAIN           1..438
FT                   /note="Protein p50"
FT                   /id="PRO_0000040212"
FT   DOMAIN          662..778
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   965 AA;  110880 MW;  8507E5D2DF86C612 CRC64;
     MATLPSIHAF WKLWWPTFSE ERKMTVVQAL RNGLTRKLFQ ITQIAQQILR WPPYIRERMT
     SSLGQSLVKT FQTLLGIRKA LSRLCLTRNM NVDIFTMLLI PFKFLSQLCS QIVASANFVI
     QTFRHGLSRG LCLARCRNPE TMRSGWSKHT LQMQNCSSTS PLMTPFQPQI ARDLSNPHGL
     WMSTRNKLTR TGGSAIQQTS RYVRLAVRFS LLAAGAYISC VLARKALKEY VYRWELKSDQ
     ELPTREQSQI SQVEQAMEQN GAMMVMKLNG PTAPILSLQD CLTKHVLVPE IVDEEGTVTQ
     KEQSTFLIRE FGPAVRNLVT LAKLEFGGIP KKTTANELTV WRFLVRKCEH ANMNPTDSRT
     AISMALPYVF MPCRTDVGRA SIPLRDESIE ICRQYRAQFV EETPLRRVFN NPLSGKAWRN
     WVRHLGGLDD PALFQELKXG CLEEWLGVQS RRTRARHPKL RSHFKDTRHK TRRVFRIAGL
     GNLYEFGVHN NSAVNLERGL MERVFYVKDD KGELVSCPEP ISGIFWKNLK GFRNSIVHHV
     GHRHPVSRET FLAYYTGPKR TMYEKAVNSL YEMPVSYDDA KLKTFVKAEK INLTKKADPV
     PRVIQPRAPR YNVELGRYLR PVEHPIYHAI DKIWGGPTIM KGYSVEQIGR HIENAFRSFT
     DPVAIGFDAS RFDQHVSVEA LRWEHSVYSR IYGYPELLTQ LLRWQIHNRG TAYASDGAFN
     YQVDGKRMSG DMNISLGNCI LATAITHDFV TKLGIPARLI NNGDDNVLIC PAVEVGRVRQ
     ELYRHWLNYG FEVISEEPVY ILEQVEFCQM RPVFDGTQYT MMRDPRTTMS KDAYAVTPFN
     TPTAARRWMR AVGECGLSLT GGLPVKQEYY TALVKHGLDP KNIKQGKDFD SGLYYLSKLS
     NRKWQEVQES ARYSFWLAFG YTPDEQRALE EYFKSWTPTF EWSTTGILAE IPECLLLKHN
     PLPPT