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   25-NOV-2008, entry version 53.
DE   RecName: Full=Large structural protein;
DE            Short=Protein L;
DE   AltName: Full=Transcriptase;
DE   AltName: Full=Replicase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.56;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.-;
GN   Name=L;
OS   Canine distemper virus (strain Onderstepoort) (CDV).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Paramyxoviridae; Paramyxovirinae; 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 familiaris (Dog).
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   MEDLINE=93174968; 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   MEDLINE=91132146; PubMed=1993883;
RA   Curran M.D., Clarke D.K., Rima B.K.;
RT   "The nucleotide sequence of the gene encoding the attachment protein H
RT   of canine distemper virus.";
RL   J. Gen. Virol. 72:443-447(1991).
CC   -!- FUNCTION: Displays RNA-directed RNA polymerase, mRNA guanylyl
CC       transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A)
CC       synthetase activities. The viral mRNA guanylyl transferase
CC       displays a different biochemical reaction than the cellular
CC       enzyme. The template is composed of the viral RNA tightly
CC       encapsidated by the nucleoprotein (N). Functions either as
CC       transcriptase or as replicase. The transcriptase synthesizes
CC       subsequently the subgenomic RNAs, assuring their capping and
CC       polyadenylation by a stuttering mechanism. The transcriptase
CC       stutters on a specific sequence, resulting on a cotranscriptional
CC       editing of the phosphoprotein (P) mRNA. The replicase mode is
CC       dependent on intracellular N protein concentration. In this mode,
CC       the polymerase replicates the whole viral genome without
CC       recognizing the transcriptional signals (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBUNIT: Interacts with the P protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Virion (Potential). Cytoplasm (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the paramyxoviruses L protein family.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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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; -.
DR   GeneID; 1489795; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR016269; RNA-dir_RNA_pol_paramyxovir.
DR   InterPro; IPR014023; RNA_pol_cat.
DR   InterPro; IPR001016; RNA_pol_L_viral.
DR   Pfam; PF00946; Paramyx_RNA_pol; 1.
DR   PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN         1   2184       Large structural protein.
FT                                /FTId=PRO_0000142726.
FT   DOMAIN      656    840       RdRp catalytic.
FT   NP_BIND    1785   1794       ATP (Potential).
FT   CONFLICT     44     44       T -> R (in Ref. 3; BAA00655).
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
//