ID   L_RINDR                 Reviewed;        2183 AA.
AC   P41357;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 125.
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   Rinderpest virus (strain RBOK) (RDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus; Morbillivirus pecoris; Rinderpest morbillivirus.
OX   NCBI_TaxID=36409;
OH   NCBI_TaxID=9915; Bos indicus (Zebu).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9933; Gazella (gazelles).
OH   NCBI_TaxID=9894; Giraffa camelopardalis (Giraffe).
OH   NCBI_TaxID=9832; Hippopotamus.
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
OH   NCBI_TaxID=9821; Suidae (pigs).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7897350; DOI=10.1099/0022-1317-76-3-593;
RA   Baron M.D., Barrett T.;
RT   "Sequencing and analysis of the nucleocapsid (N) and polymerase (L) genes
RT   and the terminal extragenic domains of the vaccine strain of rinderpest
RT   virus.";
RL   J. Gen. Virol. 76:593-602(1995).
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; Z30698; CAA83184.1; -; Genomic_RNA.
DR   EMBL; Z30697; CAA83183.1; -; Genomic_RNA.
DR   PIR; S47307; S47307.
DR   SMR; P41357; -.
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   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   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; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion; Zinc.
FT   CHAIN           1..2183
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000142735"
FT   DOMAIN          656..840
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          1755..1958
FT                   /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT   REGION          1212..1248
FT                   /note="priming-capping loop"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   ACT_SITE        1288
FT                   /note="Nucleophile; for GDP polyribonucleotidyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   ACT_SITE        1766
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:Q06996"
FT   ACT_SITE        1881
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:Q06996"
FT   ACT_SITE        1917
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P03523"
FT   ACT_SITE        1954
FT                   /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT                   (nucleoside-2'-O-)-methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:Q06996"
FT   BINDING         663
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:Q997F0"
FT   BINDING         773
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:Q997F0"
FT   BINDING         1132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q997F0"
FT   BINDING         1785..1794
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   2183 AA;  248110 MW;  EF2C7D7E9E867F89 CRC64;
     MDSLSVNQIL YPEVHLDSPI VTNKLVAILE YARIPHKYVL EDPTLCKNIK HRLDSGFSNQ
     MVINNVEIGN VVQSKLKGYP NHEHIPYPEC NQELFIARDK KATEKIRSLF KKGTTLYTKI
     SDKVCTCLET ANSRLGLGAD LGIGIKEKIL SLSLYMQSSQ WYEPFLFWFT IKTEMRSTIK
     SSVHTSHRRR YVPSFFSGDS FEILISRDLV AIVHRRLHHV YYLTFELVLM YCDIIEGRLM
     TETAMVIDPR YTELLERVRY MWKLIDGFFP TLGNSTYQVV ALLEPLSLAY LQLRDVTTEL
     RGAFLNHCFT EIREILNQNG VTDDNTYHEI VEALDYIFIT DDIHLTGEIF SFFRSFGHPR
     LEAITAADNV RKHMNQPKVI VYETLMKGHA IFCGIIINGY RDRHGGSWPP IHLPVHAATS
     IRNAQASGEG LTYEQCVDNW KSFAGIRFGC FMPLSLDSDL TMYLKDKALA ALKKEWDSAY
     PKEFLRYNPP KSTSSRRLVD VFLNDSTFDP YNMIMYVVSG DYLRDPDFNS SYSLKEKEIK
     ETGRLFAKMT YKMRACQVIA ENLISNGIGK YFRDNGMAKD EHDLTKALHT LAVSGVPKDF
     KDNYRGGPRA KTFSSKKTHT GAGISRVSRN EANYRSPEQR GCNTGGPDQI ESYETVSAFI
     TADLKKYCLN WRYETISLFA QRLNEIYGLP SFFQWLHRRL ERSVLYVSDP HCPPDLDSHA
     NLDNVPNDQI FIKYPMGGIE GYCQKLWTIS TIPYLYLAAH ESGVRIASLV QGDNQTIAVT
     KRVPSSWPYH LKKREAARVT REYFCLLRQR LHDIGHHLKA NETIVSSHFF VYSKGIYYDG
     LLISQSLKSI ARCVFWSETI VDETRAACSN IATTIAKSIE RGFDRYLAYS LNILKVIQQI
     LISLGFTINS TMTQDVVVPL LSNHDLLIRM ALLPAPIGGM NYLNMSRLFV RNIGDPVTSS
     IADLKRMIGA SLMPEETLHQ VMTQQPGDSS FLDWASDPYS ANLVCIQSIT RLLKNITAKY
     VLINSPNPML RGLFHDDSKE EDEQLATFLM DRSVIVPRAA HEILDHSITG AREAIAGMLD
     TTKGLIRTSS RRGGLTTRVI ARLSTYDYEQ FRSGMVLLTG SKRNYLIDRD SCSVQLARAL
     RSHMWARLAR GRPIYGLEVP DVLESMRGHL IQRHATCILC DFGSANYGWF FVPSNCQLDD
     IDRETSALRV PYIGSTTDER TDMKLAFVKS PSQSLRSAVR IATVYSWAYG DDDKSWNEAL
     KLAQQRAKVS LEELKMITPI STSTNLAHRL RDRSTQVKYS GTSLVRVARY TTISNDNLSF
     VISDKKVDTN FIYQQGMLLG LGVLETLFRL DKDTGPSNTV LHLHVETDCC VIPMVDHPRI
     PSLHELKFRR ELCTNPLIYD SAPIIDREAT KLYTQSHRRH LVEFVTWSTS QLYHILAKST
     ALSMIDLVTK FEKDHMNEVS ALIGDDDINS FITEFLLVEP RLFTVYLGQC TAINWAFDIH
     YHRPSGKYQM GELLTSFLAR MSKSVFKVFV NALSHPKIYR KFWHSGIIEP IHGPSLDTQN
     LHITVCNMIY SCYMTYLDLL LNDELDEFTY LLCESDEDIV ADRFDNIQAR HLCVLSDLYC
     NPRGCPTIRG LQPVEKCAIM TKHIEAEAKL SPAGPSWNIG PIVIDHFSCS LTYLRRGSIK
     QIRLRVDPGF IFEALTVTDP QKPNFQHEQA ADMHISNFRP PYDGVAELLG TINSSKHNLP
     ILGTGVYNYE VHAFRRIGLN SSACYKAVEI STLIKSSMDP EEDSLFLGEG SGSMLITYKE
     ILKLKKCFYN SGVSAESRSG QRELAPYPSE VSLVEHQLGA EKTVKVLFNG RPEVTWIGSV
     DCFNYIISNI QTSSLGLIHS DIETLPTKDI TEKLEELSAI LALALLLGKV GSVLVIKVMP
     ISGDYVQGFM SYMVPYYREV LIIYPRYSNF ISTEAYLVLL GLRANRLIDP ERIKQQVMES
     GIRTIPGLVG HILSIKQLNC IQSQAGPAIT RGEINPILRK LTSIERILIS CGLTINGTKI
     CSDVVHHDIS SGPDGLLNSS IILLQELARF KDNQRSQQGM FHAYPVLLSS RQRELISRVA
     RKFWGYILLY SSDRRLLSRL VSNLKSGYLL FDLHQNLFMK NLSKSEKQLI RTGGLKREWL
     FKLTTKEIKE WFKLIGYSAL IRE
//