ID   RDRP_LRVLG              Reviewed;         874 AA.
AC   Q02382;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 69.
DE   RecName: Full=Probable RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
GN   Name=ORF3;
OS   Leishmania RNA virus 1 - 1 (isolate Leishmania guyanensis) (LRV-1-1).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC   Ghabrivirales; Totiviridae; Leishmaniavirus; Leishmania RNA virus 1.
OX   NCBI_TaxID=58103;
OH   NCBI_TaxID=5664; Leishmania major.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1382295; DOI=10.1073/pnas.89.18.8596;
RA   Stuart K.D., Weeks R., Guilbride L., Myler P.J.;
RT   "Molecular organization of Leishmania RNA virus 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8596-8600(1992).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which replicates the viral
CC       genome. Catalyzes the transcription of fully conservative plus-strand
CC       genomic RNAs that are extruded from the virion into the cytoplasm where
CC       they function as mRNAs for translation of viral proteins and also as
CC       substrates for encapsidation to form new virions. Once encapsidated,
CC       the positive strand is converted to dsRNA by the RNA-directed RNA
CC       polymerase. Displays ssRNA-binding activity (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the totiviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; M92355; AAB50024.1; -; Genomic_RNA.
DR   PIR; C46171; C46171.
DR   RefSeq; NP_041191.1; NC_002063.1.
DR   GeneID; 1446405; -.
DR   KEGG; vg:1446405; -.
DR   OrthoDB; 9167at10239; -.
DR   Proteomes; UP000006721; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR   Pfam; PF02123; RdRP_4; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-binding; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..874
FT                   /note="Probable RNA-directed RNA polymerase"
FT                   /id="PRO_0000404517"
SQ   SEQUENCE   874 AA;  98321 MW;  A21CABDF4AA1A009 CRC64;
     MQCPNQNHML VNRAMVVAAL DSFEDARRII SGVLDLSRLT NTSVKGQHTN DTNYFSRYSN
     FFSQMPAIIL NQLKCCIKAQ VDDAVKMVLQ KAKKVEVSKP VEKMLTFTTL NTYLGYPEST
     GCVMEYTEEQ SGPIAAKLLI TLLSSTLNAM VRPKSDPNIS QNKIPRHYYQ LKVHVGAQKK
     VNLTAIEVIR GCQHECSVVY CEFVRYSAYF AGLYDDQVAA ILLYAVAAHN VQGFGARFCV
     LWALMCVRIA GFADDINIYI KHRGMSGLLP QLVEMKCLLG RGVNEIDVET EARRRLDVGS
     LSMQRLDENE LRAAVRLIYS EELRRPVTYP LICDFWSSRW LWAANGSHSR ALEHAHPELA
     TRKEGQAYRK AVMEQWQHNP MDRWDGTVYV TPSAKLEHGK TRLLLACDTL SYMWFEYALR
     PVERIWENSN VILDPGSMGN CGIATRINGW RNGMPGQSFF AVDYDDFNSQ HTLMSQKIVF
     EELFHHIGYN ASWVKTLVDS FDSMELWIKG KCAGIMAGTL MSGHRATSFI NSVLNRAYII
     CAGGHVPTSM HVGDDILMSC TLGHADNLIA NLNRKGVRLN ASKQVFSKTS GEFLRVAHRE
     HTSHGYLARV ISSAVSGNWV SDHTLNQQEA LMNAIVCCRG ILNRSLPGEK NPVVRVISRS
     VSKRTKIEEK TIRLLLSGRA CLKGGVVYGE QTNYIQVYRI NCRVERSEEK LPPYRHATED
     YLNNHLADIE VMAVRQYGSD IADIMAQASW KKSMSTEGAE DVSRLSLQRD KTLPCLHCIT
     EKETSLLPVR YGLFSSYPIL MMLKDRIPIK EALKLAVTIG YRPQPNSDLE LDLWGESNNS
     CAIEGVLPYN EATSLAQKLP CGGVVIQVIH NVYV
//