ID   L_SV41                  Reviewed;        2269 AA.
AC   P35341;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-SEP-2026, entry version 131.
DE   RecName: Full=RNA-directed RNA polymerase L;
DE            Short=Protein L;
DE   AltName: Full=Large structural protein;
DE   AltName: Full=Replicase;
DE   AltName: Full=Transcriptase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48 {ECO:0000250|UniProtKB:P28887};
DE   Includes:
DE     RecName: Full=GTP phosphohydrolase {ECO:0000250|UniProtKB:P03523};
DE              EC=3.6.1.- {ECO:0000250|UniProtKB:P03523};
DE   Includes:
DE     RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE              EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
DE     AltName: Full=PRNTase {ECO:0000305};
DE   Includes:
DE     RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE     AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE              Short=G-N7-MTase {ECO:0000250|UniProtKB:P03523};
DE     AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE              Short=N1-2'-O-MTase {ECO:0000250|UniProtKB:P03523};
GN   Name=L;
OS   Simian virus 41 (SV41).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus.
OX   NCBI_TaxID=3052561;
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Toshiba/Chanock;
RX   PubMed=1328485; DOI=10.1099/0022-1317-73-10-2743;
RA   Ogawa M., Mutsuga N., Tsurudome M., Kawano M., Matsumura H., Kusagawa S.,
RA   Komada H., Nishio M., Ito Y.;
RT   "Nucleotide sequence analysis of the simian virus 41 gene encoding the
RT   large (L) protein and construction of a phylogenetic tree for the L
RT   proteins of paramyxoviruses.";
RL   J. Gen. Virol. 73:2743-2750(1992).
CC   -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC       of viral mRNAs, their capping and polyadenylation. The template is
CC       composed of the viral RNA tightly encapsidated by the nucleoprotein
CC       (N). The viral polymerase binds to the genomic RNA at the 3' leader
CC       promoter, and transcribes subsequently all viral mRNAs with a
CC       decreasing efficiency. The first gene is the most transcribed, and the
CC       last the least transcribed. The viral phosphoprotein acts as a
CC       processivity factor. Capping is concomitant with initiation of mRNA
CC       transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase)
CC       adds the cap structure when the nascent RNA chain length has reached
CC       few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC       facilitates subsequent guanine-N-7 methylation, both activities being
CC       carried by the viral polymerase. Polyadenylation of mRNAs occur by a
CC       stuttering mechanism at a slipery stop site present at the end viral
CC       genes. After finishing transcription of a mRNA, the polymerase can
CC       resume transcription of the downstream gene.
CC       {ECO:0000250|UniProtKB:P03523}.
CC   -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of
CC       viral genomic RNA. The template is composed of the viral RNA tightly
CC       encapsidated by the nucleoprotein (N). The replicase mode is dependent
CC       on intracellular N protein concentration. In this mode, the polymerase
CC       replicates the whole viral genome without recognizing transcriptional
CC       signals, and the replicated genome is not caped or polyadenylated.
CC       {ECO:0000250|UniProtKB:P03523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC         adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC         triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC         adenosine in mRNA + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC         Evidence={ECO:0000250|UniProtKB:P03523};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC         mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC         adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC         Evidence={ECO:0000250|UniProtKB:P28887};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC         adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC         5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC         adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC         ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P28887};
CC   -!- SUBUNIT: Interacts with the P protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxovirus L protein family.
CC       {ECO:0000305}.
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DR   EMBL; X64275; CAA45569.1; -; Genomic_RNA.
DR   PIR; JQ1750; JQ1750.
DR   RefSeq; YP_138510.1; NC_006428.1.
DR   AlphaFoldDB; P35341; -.
DR   SMR; P35341; -.
DR   GeneID; 3159460; -.
DR   KEGG; vg:3159460; -.
DR   Proteomes; UP000108270; Segment.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0062105; F:RNA 2'-O-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR039736; L_poly_C.
DR   InterPro; IPR026890; Mononeg_mRNAcap.
DR   InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR   InterPro; IPR025786; Mononega_L_MeTrfase.
DR   InterPro; IPR016269; RNA-dir_pol_paramyxovirus.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR04198; paramyx_RNAcap; 1.
DR   Pfam; PF14318; Mononeg_mRNAcap; 1.
DR   Pfam; PF00946; Mononeg_RNA_pol; 1.
DR   PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR   PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW   Viral RNA replication; Virion; Zinc.
FT   CHAIN           1..2269
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000142741"
FT   DOMAIN          666..850
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          1785..1998
FT                   /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT   REGION          1226..1262
FT                   /note="priming-capping loop"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   ACT_SITE        1302
FT                   /note="Nucleophile; for GDP polyribonucleotidyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   ACT_SITE        1796
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:Q06996"
FT   ACT_SITE        1921
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:Q06996"
FT   ACT_SITE        1957
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   ACT_SITE        1994
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:Q06996"
FT   BINDING         673
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RNA-directed RNA polymerase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P28887"
FT   BINDING         783
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RNA-directed RNA polymerase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P28887"
FT   BINDING         1146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   BINDING         1815..1824
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   2269 AA;  256432 MW;  3BD60C14AA161F5B CRC64;
     MAASADILLP EVHLNSPIVK HKLVYFLLLG KLPHNLSEDE ITPLHNQNWD QIAHEESNLS
     ERLFAVRSEL TRRIAQLRAT RWRSEIAVLL WPNSLPYLCT FKPYNRLNTI DEWNKLVSAA
     SNILSSPLSK CMQDISTKLI GRTNLFSRSQ SRPGQSADNT ITLNKIAAVW ADNKWQPLVS
     LWLTIKYQMR QMIANQSKRT CSELVYVVDT RSGIIIITPE LVTCFDKDHS VLMYFTFEMV
     LMISDLFEGR MNVTALCTVS NYLSPLLSRI ERLFDIVDHL AHLLGDNVYK IIASLESLVY
     GCLQLHDPVI DLAGTFYSFV AQEIVDGLQQ GNILSPEEAY TVTEQLLECF SGLSPDLTAE
     LLCLMRLWGH PNLTAAQAAK KVRDTMCAGK VLDFQIIMKT LAFFHTILIN GYRRKKNGIW
     PPLSLPGNAS KSLIELHHDN SEISYEYTLR HWKELSLIEF KKCFDFDPGE ELSIFMKDKA
     ISAPKEDWMS VFRKSLIKQR HQRHHIPMPN PFNRRLLLNF IEDPSFDPAK ELEYVTSGEY
     LRDPHFCASY SLKEKEIKPD GRIFAKLTNR MRSCQVIAEA LLANHAGKLM KENGVVMNQI
     SLTKSLLTMS QIGLISEKAQ RYTRDNIALG ALFSKGQRTR AHPQTQLSSI DSSQNRELPD
     DSLELSACFI TTDLTKYCPQ WRYQTIIPFA KTLNRMYGVP HLFEWIHLRL LRSTLYVGDP
     FNPPADTSVF DLDQVLNGDI FIVSPKGGIE GLCQKMWTMI SISVIILSSA ESKTRVMSMV
     QGDNQAIAVT TKVPRSVPLT EKRNLAYNAS KLFFDRLKHN NFGLGHQLKA QETIISSQFF
     IYSKRVFYQG RILTQALKNA SKLCLTADVL GECTQASCSN AATTIMRLTE NGVEKDVCYM
     LNVYQAIRQL CFDLYYPQYS IPGEQISQHY LKHPSIVARL VILPSQLGGL NYLSCSRLFN
     RNIGDPLGTA VADLKRLIKC GALESWVLSN LLSRKPGTGS WATLAADPYS LNIDYLYPPT
     TILKRHTQNT LMEVCKNPML KGVFTDNARE EENNLAKFLL DRDIVLPRVA HIVIEQSSVG
     RKKQIQGFFD TTRTIMRKSF EIKPLSSKRT LSVIECNINY LAYNFNIIHH PNPIPGYLQC
     ITTDNCSVDI ARSLRKLSWS SLLNGRTLEG LETPDPIEVV NGALVIGVGE CDYCMQGDTK
     FTWFFLPKGI EIDGDPEKNP PIRVPYVGSK TEERRVASMA YVKGATSSLK AALRGAGVFI
     WAYGDTDANW DDALDLANTR VQISKEQLQA LTPLPTSANI THRLDDGATT IKFTPASSYA
     FSSYTHISND QQYLEVDNRV VDSNIIYQQL MITGLGIIET YNNPPIRTSS EELTLHLHTS
     SSCCIRPVDG CIICESPSLL PQLTVPYTNP FVYDPNPLAD YEIAHLDYLS YQARIGSIEH
     YSLQDRIDLL AHLTAKQMIN SIIGLDESVS LLNDAVVTSD YTNNWISECS YTKIDLVFKM
     MAWNLLLELS FQMYYLRITT WSNIFDYTYM TLRRIPGNAL TNIAATISHP KLLRRAMNLD
     VITPVHAPYL ASLDYIKLSI DAIQWGIKQV LADLHNGIDY EILILSEDSL ELSDRAMNLI
     ARKLTLLALI QGNQLVLPKI KGLSPDEKCL VLTEHLMSEY QLLLLDDAEL SKRSYNLTNP
     RITAFPSNNF YLTRKVLNSI RDSEEGQYLI GAYYDSFQQM ETDIILHSTL IAPYDTSETL
     TKFDLCISLF PHDDNLEKYP LPVDHDSQSA VSTIVPGPPI HHVLRPLGVS STSWYKGLSY
     VRYLELCKVP TGDHLYLAEG SGASMSLVEM LIPGQKVYYN SLFSSGENPP QRNYAPLPTQ
     FVQSVPYKLW QADLTNKEGI IEDFIPLWNG NGAVTDLSNK DCVAFIIHKV GAEQASLVHV
     DLESTANLNQ QSLSRSQIHA LIIATTVLKR GGFLVYKTSW LPFSRLSQLA CVLWSFFDKI
     TMIRSSYSDP NSHEIYLVCR LAADFKTIGF SAALASAIAI AIHGDGFTTI HPDVVSNYWQ
     HHLENVGRVG KAIDDVIDGV STNFYSGDNG LILRCGGTPS SRKWLDIDLL PTFSSLQETL
     VNLVTVHLKE IIEIQTSSME DYTSLLFTPY NIGSVGKIRT IVKLILERSL MYVIRNWLVM
     PSSYQDSVRQ DLELGSFRLS SVLQEDTFWK LTENRKYLAS QLTRDYITTF FTTHSILPIH
     RSYQKRIWKA LGSVIYCSEV PGESQQNWDS IPLVYEEDQI ERGIDGEEL
//