L_NDVB1
ID L_NDVB1 Reviewed; 2204 AA.
AC Q9DLD3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Newcastle disease virus (strain Chicken/United States/B1/48) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=652953;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Sellers H.S., Seal B.S.;
RT "Complete sequence for the B1 strain of Newcastle disease virus.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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; AF309418; AAG36980.1; -; Genomic_RNA.
DR RefSeq; NP_071471.1; NC_002617.1.
DR SMR; Q9DLD3; -.
DR PRIDE; Q9DLD3; -.
DR Proteomes; UP000002328; 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..2204
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000390627"
FT DOMAIN 634..818
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1745..1958
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT BINDING 1775..1784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2204 AA; 248740 MW; 9683868FD495A2D2 CRC64;
MASSGPERAE HQIILPESHL SSPLVKHKLL YYWKLTGLPL PDECDFDHLI LSRQWKKILE
SASPDTERMI KLGRAVHQTL NHNSRITGVL HPRCLEELAN IEVPDSTNKF RKIEKKIQIH
NTRYGELFTR LCTHIEKKLL GSSWSNNVPR SEEFSSIRTD PAFWFHSKWS TAKFAWLHIK
QIQRHLIVAA RTRSAANKLV MLTHKVGQVF VTPELVVVTH TNENKFTCLT QELVLMYADM
MEGRDMVNII STTAVHLRSL SEKIDDILRL IDALAKDLGN QVYDVVSLME GFAYGAVQLL
EPSGTFAGDF FAFNLQELKD ILIGLLPNDI AESVTHAIAT VFSGLEQNQA AEMLCLLRLW
GHPLLESRIA AKAVRSQMCA PKMVDFDMIL QVLSFFKGTI INGYRKKNAG VWPRVKVDTI
YGKVIGQLHA DSAEISHDIM LREYKSLSAL EFEPCIEYDP VTNLSMFLKD KAIAHPNDNW
LASFRRNLLS EDQKKHVKEA TSTNRLLIEF LESNDFDPYK EMEYLTTLEY LRDDNVAVSY
SLKEKEVKVN GRIFAKLTKK LRNCQVMAEG ILADQIAPFF QGNGVIQDSI SLTKSMLAMS
QLSFNSNKKR ITDCKERVSS NRNHDPKSKN RRRVATFITT DLQKYCLNWR YQTIKLFAHA
INQLMGLPHF FEWIHLRLMD TTMFVGDPFN PPSDPTDCDL SRVPNDDIYI VSARGGIEGL
CQKLWTMISI AAIQLAAARS HCRVACMVQG DNQVIAVTRE VRSDDSPEMV LTQLHQASDN
FFKELIHVNH LIGHNLKDRE TIRSDTFFIY SKRIFKDGAI LSQVLKNSSK LVLVSGDLSE
NTVMSCANIA STVARLCENG LPKDFCYYLN YIMSCVQTYF DSEFSITNNS HPDLNQSWIE
DISFVHSYVL TPAQLGGLSN LQYSRLYTRN IGDPGTTAFA EIKRLEAVGL LSPNIMTNIL
TRPPGNGDWA SLCNDPYSFN FETVASPNIV LKKHTQRVLF ETCSNPLLSG VHTEDNEAEE
KALAEFLLNQ EVIHPRVAHA IMEASSVGRR KQIQGLVDTT NTVIKIALTR RPLGIKRLMR
IVNYSSMHAM LFRDDVFSSS RSNHPLVSSN MCSLTLADYA RNRSWSPLTG GRKILGVSNP
DTIELVEGEI LSVSGGCTRC DSGDEQFTWF HLPSNIELTD DTSKNPPMRV PYLGSKTQER
RAASLAKIAH MSPHVKAALR ASSVLIWAYG DNEVNWTAAL TIAKSRCNVN LEYLRLLSPL
PTAGNLQHRL DDGITQMTFT PASLYRCHLT FTYPMILKGC SLKKESKRGM WFTNRVMLLG
LSLIESIFPM TTTRTYDEIT LHLHSKFSCC IREAPVAVPF ELLGVAPELR TVTSNKFMYD
PSPVSEGDFA RLDLAIFKSY ELNLESYPTI ELMNILSISS GKLIGQSVVS YDEDTSIKND
AIIVYDNTRN WISEAQNSDV VRLFEYAALE VLLHRSYQLY YLRVRGLDNI VLYMGDLYKN
MPGILLSNIA ATISHPVIHS RLHAVGLVNH DGSHQLADTD FIEMSAKLLV SCTRRVISGL
YSGNKYDLLF PSVLDDNLNE KMLQLISRLC CLYTVLFATT REIPKIRGLT AEEKCSILTE
YLLSDAVKPL LSPDQVSSIM SPNIITFPAN LYYMSRKSLN LIREREDRDT ILALLFPQEP
LLEFPSVQDI GARVKDPFTR QPAAFLQELD LSAPARYDAF TLSQIHPELT SPNPEEDYLV
RYLFRGIGTA SSSWYKASHL LSVPEVRCAR HGNSLYLAEG SGAIMSLLEL HVPHETIYYN
TLFSNEMNPP QRHFGPTPTQ FLNSVVYRNL QAEVTCKDGF VQEFRPLWRE NTEESDLTSD
KAVGYITSAV PYRSVSLLHC DIEIPPGSNQ SLLDQLAINL SLIAMHSVRE GGVVIIKVLY
AMGYYFHLLM NLFAPCSTKG YILSNGYACR GDMECYLVFV MGYLGGPTFV HEVVRMAKTL
VQRHGTLLSK SDEITLTRLF TSQRQRVTDI LSSPLPRLIK YLRKNIDTAL IEAGGQPVRP
FCAESLVSTL ANITQITQII ASHIDTVIRS VIYMEAEGDL ADTVFLFTPY NLSTDGKKRT
SLKQCTRQIL EVTILGLRVE NLNKIGDIIS LVLKGMISME DLIPLRTYLK HSTCPKYLKA
VLGITKLKEM FTDTSVLYLT RAQQKFYMKT IGNAVKGYYS NCDS
