ID   RDRP_MNSV               Reviewed;         791 AA.
AC   Q83424; Q83423; Q83426;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=p89 {ECO:0000303|PubMed:2212985};
DE   Contains:
DE     RecName: Full=p29 {ECO:0000303|PubMed:2212985, ECO:0000303|PubMed:25372121};
GN   Name=ORF1 {ECO:0000312|EMBL:AAB02430.1};
OS   Melon necrotic spot virus (MNSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Gammacarmovirus.
OX   NCBI_TaxID=11987;
OH   NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2584953; DOI=10.1099/0022-1317-70-11-3033;
RA   Riviere C.J., Pot J., Tremaine J.H., Rochon D.M.;
RT   "Coat protein of melon necrotic spot carmovirus is more similar to those of
RT   tombusviruses than those of carmoviruses.";
RL   J. Gen. Virol. 70:3033-3042(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2212985; DOI=10.1099/0022-1317-71-9-1887;
RA   Riviere C.J., Rochon D.M.;
RT   "Nucleotide sequence and genomic organization of melon necrotic spot
RT   virus.";
RL   J. Gen. Virol. 71:1887-1896(1990).
RN   [3]
RP   FUNCTION (P29), AND SUBCELLULAR LOCATION (P29).
RX   PubMed=25372121; DOI=10.1094/mpmi-09-14-0274-r;
RA   Gomez-Aix C., Garcia-Garcia M., Aranda M.A., Sanchez-Pina M.A.;
RT   "Melon necrotic spot virus Replication Occurs in Association with Altered
RT   Mitochondria.";
RL   Mol. Plant Microbe Interact. 28:387-397(2015).
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase
CC       that plays an essential role in the virus replication.
CC       {ECO:0000250|UniProtKB:P11640}.
CC   -!- FUNCTION: [p29]: Induces the reorganization of host mitochondria and
CC       the formation of structures with numerous dilations surrounded by
CC       double membranes, which may provide a protected environment to viral
CC       replication. {ECO:0000269|PubMed:25372121}.
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: [p29]: Host mitochondrion
CC       {ECO:0000269|PubMed:25372121}.
CC   -!- MISCELLANEOUS: This protein is translated as a fusion protein by
CC       episodic readthrough of P29 termination codon. Readthrough of the
CC       terminator codon TAG occurs between the codons for 268-Asn and 270-Gly.
CC       {ECO:0000305|PubMed:2212985}.
CC   -!- SIMILARITY: Belongs to the tombusviridae RNA polymerase family.
CC       {ECO:0000305}.
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DR   EMBL; M29671; AAB02430.1; -; Genomic_RNA.
DR   EMBL; M29671; AAB02431.1; -; Genomic_RNA.
DR   EMBL; D12536; BAA02099.1; -; Genomic_RNA.
DR   EMBL; D12536; BAA02100.1; -; Genomic_RNA.
DR   RefSeq; NP_041226.1; NC_001504.1.
DR   RefSeq; NP_041227.1; NC_001504.1.
DR   GeneID; 1491976; -.
DR   GeneID; 1491977; -.
DR   KEGG; vg:1491976; -.
DR   KEGG; vg:1491977; -.
DR   Proteomes; UP000202003; Genome.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
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   Host mitochondrion; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..791
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000455298"
FT   CHAIN           1..268
FT                   /note="p29"
FT                   /id="PRO_0000455299"
FT   DOMAIN          491..607
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   791 AA;  88683 MW;  D803CDD7E8D3886E CRC64;
     MDTGLKFLVS GGLATSSVIR KVSAVSSLDS SLPSSSILSA IHGSWTSAIS HDCSKIAKVA
     AIVGIGYLGV RIGAAWCRRT PGITNSIITY GEEVVEQVKV DIDEDAEEES DIGEEIVVGT
     IGIGIHTNVN PEVRAKRRHR SRPFIKKIVN LTKNHFGGCP DSSKSNVMAV SKFVYEQCKQ
     HNCLPHQTRL IMSIAVPLVL SPDMYDISSK ALLNSEILTE NRATLDRLKT LDGWLTHLVC
     HPLSAKAWRR AIDNLCGLPD WKAFKLVNXG CLEELAGFCT SVRRGTHPDM TEFPQDRPIK
     TRKLYCLGGV GTSVKFNVHN NSLANLRRGL VERVFFVEND KKELEPAPKP LSGAFDRLTW
     FRRKLHSIVG THSSISPGQF LDFYTGRRRT IYEGAVKSLE GLSVQRRDAY LKTFVKAEKI
     NTTKKPDPAP RVIQPRNVRY NVEVGRYLRR FEHYLYRGID EIWNGPTIIK GYTVEQIGKI
     ARDAWDSFVS PVAIGFDMKR FDQHVSSDAL KWEHSVYLDA FCHDSYLAEL LKWQLVNKGV
     GYASDGMIKY KVDGCRMSGD MNTAMGNCLI ACAITHDFFR SRGIRARLMN NGDDCVVICE
     KECAAVVKAD MVRHWRQFGF QCELECDAEI FEQIEFCQMR PVYDGEKYVM VRNPLVSLSK
     DSYSVGPWNG INHARKWVNA VGLCGLSLTG GIPVVQSYYN MMIRNTQSVN SSGILRDVSF
     ASGFRELARL GNRKSGAISE DARFSFYLAF GITPDLQRAM ESDYDAHTIE WGFVPQGNPR
     IQPISWTLNE L