L_CDVO
ID L_CDVO Reviewed; 2184 AA.
AC P24658;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 117.
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 Canine distemper virus (strain Onderstepoort) (CDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11233;
OH NCBI_TaxID=9646; Ailuropoda melanoleuca (Giant panda).
OH NCBI_TaxID=9649; Ailurus fulgens (Lesser panda) (Red panda).
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9665; Mustela.
OH NCBI_TaxID=9689; Panthera leo (Lion).
OH NCBI_TaxID=9654; Procyon lotor (Raccoon).
OH NCBI_TaxID=9704; Zalophus californianus (California sealion).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8438585; DOI=10.1006/viro.1993.1102;
RA Sidhu M.S., Menonna J.P., Cook S.D., Dowling P.C., Udem S.A.;
RT "Canine distemper virus L gene: sequence and comparison with related
RT viruses.";
RL Virology 193:50-65(1993).
RN [2]
RP SEQUENCE REVISION.
RA Sidhu M.S.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-63.
RX PubMed=1993883; DOI=10.1099/0022-1317-72-2-443;
RA Curran M.D., Clarke D.K., Rima B.K.;
RT "The nucleotide sequence of the gene encoding the attachment protein H of
RT canine distemper virus.";
RL J. Gen. Virol. 72:443-447(1991).
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; AF014953; AAC26996.1; -; Genomic_RNA.
DR EMBL; D00758; BAA00655.1; -; Genomic_RNA.
DR PIR; A45389; A45389.
DR RefSeq; NP_047207.1; NC_001921.1.
DR SMR; P24658; -.
DR PRIDE; P24658; -.
DR GeneID; 1489795; -.
DR KEGG; vg:1489795; -.
DR Proteomes; UP000007634; 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; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2184
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000142726"
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 595..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1785..1794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 44
FT /note="T -> R (in Ref. 3; BAA00655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2184 AA; 248190 MW; BEF45756BBF0D37D CRC64;
MDSVSVNQIL YPEVHLDSPI VTNKLVSILE YARIRHNYQL LDTTLVRNIK ERISEGFSNQ
MIINCIEIGS IINQTLLSYP KHNHVIYPNC NKLLFHAQDR VISLRLRNIF KRGNSIYSKI
TDGVKKCLND INLNIGLGGA LDKTIGTKID EAGIIMQSSQ WFEPFLLWFT IKTEMRSVIK
SSTHNCRKRR QNPVFVKGES LNVLVSRDLV CIIDLTSHIV YYLTFEMVLM YCDVIEGRLM
TDTAMAIDQR YSTLHVRIRY LWDLIDGFFP DLGNSTYQLV ALLEPLSLAY LQLKDITFSL
RGAFLSHCFA EIQEILQDNG FYTEETFQTL TQALDFVFIT EDIHITGEIF SFFRSFGHPR
LEAITAAENV RKHMNQPKVV SYETMMKGHA IFCGIIINGY RDRHGGTWPP MDLPVHASPI
IRNAHASGEG ITYSQCIENW KSFAGIRFKC FMPLSLDSDL TMYLKDKALA ALRKEWDSVY
PKEFLRYNPP RSTESRRLVN VFLEDSQFDP YNMIMYVISG QYLEDPDFNL SYSLKEKEIK
EVGRLFAKMT YKMRACQVIA ENLISNGIGK YFKDNGMAKD EHDLTKSLHT LAVSGVPKDK
KDSHRGLTNQ RKSLKPAPYR GTRHSVSSPS SRYIDPNPNF CTSRREDNDI EIYETVSAFI
TTDLKKYCLN WRYETISIFA QRLNEIYGLP SFFQWLHRRL EQSILYVSDP HCPPDLDRHV
DLNTAPNSQI FIKYPMGGVE GYCQKLWTIS TIPYLYLAAH ESGVRIASLV QGDNQTIAVT
KRVPSTWSYA LKKSEASRVT TEYFIALRQR LHDVGHHLKA NETIISSHFF VYSKGIYYDG
MLISQSLKSI ARCVFWSETI VDETRAACSN ISTTLAKAIE KGFDRYLAYT LNILKIIQQV
LISLGFTINS AMTRDVIEPL LQDHCLLTKM AILPAPIGGF NYLNMSRLFV RNIGDPVTSS
IADLKRMIRS GLLGVEILHQ VMTQYPGDSS YLDWASDPYS ANLPCVQSIT RLLKNITARH
VLINSPNPML RGLFHDESQD EDEALAAFLM DRKIIIPRAA HEILDNTITG AREAIAGMLD
TTKGLIRASM KRGGLTPRII TRLSTYDYEQ FRAGIRLFSG KGHDQLIDQD SCSVQLARAL
RNHMWAKLAK GRPIYGLEVP DILESMKGYM IRRHESCLLC ASGSHNYGWF FIPANCQLDS
ITEGTSALRV PYIGSTTEER TDMKLAFVKS PSRSLKSAVR IATVYSWAYG DDDESWQEAW
TLAKQRADIS LEELRMITPI STSTNLAHRL RDKSTQVKYS GTSLIRVARY ATISNDNLSF
IIDDKKVDTN FIYQQGMLLG LGILEHLFRL SSTTGDSNTV LHLHVETDCC VIPMSDHPRV
PGLRKVVIPR NICTNPLIYD SNPIIEKDAV RLYNQSHRKH IVEFVTWTTG QLYHVLAKST
AMSMVEMITK FEKDHLNEVT ALIGDDDINS FITEFLLVEP RLFTVYLGQC AAINWGFEIH
YHRPSGKYQM GELLFSFLSR MSKGVFKILA NALSHPKVYR RFWDSGMIEP VHGPSLDSQN
LHITVCNLIY NCYMIYLDLL LNDELDDFSF ILCESDEDVI PERFDNIQAR HLCILSDLYC
NPRDCPQIRG LTPTQKCAVL SGYLKSKALE SHVGLTWNDK PILIDQYSCS LTYLRRGSIK
QIRLRVDPGF ITDAVGCLER RPLRNNSTSK ASELTSGFDP PKDDLAKLLS QLSTRTHNLP
ITGLGVRNYE VHSFRRIGIN STACYKAVEI ASVIKNEFTS EEHGLFLGEG SGAMLTVYKE
LLRLSRCYYN SGVSVESRTG QREISPYPSE VSLVEHQLGL DKLVTVLFNG RPEVTWVGSV
DCYKYILSQI SASSLGLIHS DIESLPDKDI IEKLEELSAI LSMTLILGKV GSVLVIKIMP
VSGDWVQGFI LYALPHFLRS FIVYPRYSNF VSTEAYLVFT GLRAGRLINP EGIKQQILRV
GIRTSPGLVG HILSSKQTAC VQSLHGPPFH AKSFNPHLQG LTSIEKVLIN CGLTINGLKV
CKNLLHHDIS SGEEGLKGSI TILYRELARF KDNHQSSHGM FHAYPVLIAS QERELVSIIA
KKYCGYILLY SGDLYEITRI VRNLKANHII FDLHRNLFMD NLSRSDRSLI LTTIPKKNWL
FQLETKEIKE WFKLLGYSAL IRNH
