L_RINDR
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 03-AUG-2022, entry version 110.
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 EC=2.1.1.375 {ECO:0000250|UniProtKB:P03523};
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.
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 concommitant 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=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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000250|UniProtKB:P03523};
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 + H(+) + S-adenosyl-L-homocysteine;
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 + H(+) + phosphate; 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 Proteomes; UP000008654; Genome.
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; IEA:RHEA.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR024352; L_methyltrans_paramyxo.
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 Pfam; PF12803; G-7-MTase; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 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; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
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 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
