L_NIPAV
ID L_NIPAV Reviewed; 2244 AA.
AC Q997F0; Q5K4D7; Q914E5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Nipah virus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=121791;
OH NCBI_TaxID=58060; Cynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis).
OH NCBI_TaxID=58065; Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9405; Pteropus hypomelanus (Island flying fox) (Variable flying fox).
OH NCBI_TaxID=132908; Pteropus vampyrus (Large flying fox).
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10827955; DOI=10.1126/science.288.5470.1432;
RA Chua K.B., Bellini W.J., Rota P.A., Harcourt B.H., Tamin A., Lam S.K.,
RA Ksiazek T.G., Rollin P.E., Zaki S.R., Shieh W., Goldsmith C.S.,
RA Gubler D.J., Roehrig J.T., Eaton B., Gould A.R., Olson J., Field H.,
RA Daniels P., Ling A.E., Peters C.J., Anderson L.J., Mahy B.W.;
RT "Nipah virus: a recently emergent deadly paramyxovirus.";
RL Science 288:1432-1435(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11504554; DOI=10.1006/viro.2001.1026;
RA Harcourt B.H., Tamin A., Halpin K., Ksiazek T.G., Rollin P.E.,
RA Bellini W.J., Rota P.A.;
RT "Molecular characterization of the polymerase gene and genomic termini of
RT Nipah virus.";
RL Virology 287:192-201(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate UMMC1, and Isolate UMMC2;
RX PubMed=11514724; DOI=10.1099/0022-1317-82-9-2151;
RA Chan Y.P., Chua K.B., Koh C.L., Lim M.E., Lam S.K.;
RT "Complete nucleotide sequences of Nipah virus isolates from Malaysia.";
RL J. Gen. Virol. 82:2151-2155(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NiV/MY/99/UM-0128, Isolate NiV/MY/99/VRI-2794, and
RC Isolate NV/MY/99/VRI-1413;
RX PubMed=15663869; DOI=10.3201/eid1012.040452;
RA Abubakar S., Chang L.Y., Mohdali A.R., Sharifah S.H., Yusoff K., Zamrod Z.;
RT "Isolation and molecular identification of Nipah virus from pigs.";
RL Emerg. Infect. Dis. 10:2228-2230(2004).
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; AF212302; AAK29089.1; -; Genomic_RNA.
DR EMBL; AY029768; AAK50555.1; -; Genomic_RNA.
DR EMBL; AJ564622; CAD92358.1; -; Genomic_RNA.
DR EMBL; AY029767; AAK50546.1; -; Genomic_RNA.
DR EMBL; AJ564621; CAD92352.1; -; Genomic_RNA.
DR EMBL; AJ564623; CAD92364.1; -; Genomic_RNA.
DR EMBL; AJ627196; CAF25498.1; -; Genomic_RNA.
DR RefSeq; NP_112028.1; NC_002728.1.
DR SMR; Q997F0; -.
DR PRIDE; Q997F0; -.
DR GeneID; 920950; -.
DR KEGG; vg:920950; -.
DR Proteomes; UP000002330; Genome.
DR Proteomes; UP000007527; Genome.
DR Proteomes; UP000008676; Genome.
DR Proteomes; UP000100567; Genome.
DR Proteomes; UP000110983; Genome.
DR Proteomes; UP000130871; Genome.
DR Proteomes; UP000170143; 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 GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0039697; P:negative stranded viral RNA transcription; IDA:UniProtKB.
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..2244
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000236011"
FT DOMAIN 715..899
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1810..2017
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT BINDING 1840..1849
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 223
FT /note="T -> N (in strain: Isolate NiV/MY/99/VRI-0626)"
FT VARIANT 1645
FT /note="S -> F (in strain: Isolate NiV/MY/99/UM-0128,
FT Isolate NiV/MY/99/VRI-2794, Isolate UMMC1 and Isolate NiV/
FT MY/99/VRI-0626)"
FT VARIANT 1753
FT /note="M -> V (in strain: Isolate NiV/MY/99/VRI-0626)"
FT VARIANT 2039
FT /note="H -> N (in strain: Isolate NiV/MY/99/VRI-0626)"
SQ SEQUENCE 2244 AA; 257233 MW; 1DE123E651A738C9 CRC64;
MADELSISDI IYPECHLDSP IVSGKLISAI EYAQLRHNQP SDDKRLSENI RLNLHGKRKS
LYILRQSKQG DYIRNNIKNL KEFMHIAYPE CNNILFSITS QGMTSKLDNI MKKSFKAYNI
ISKKVIGMLQ NITRNLITQD RRDEIINIHE CRRLGDLGKN MSQSKWYECF LFWFTIKTEM
RAVIKNSQKP KFRSDSCIIH MRDKSTEIIL NPNLICIFKS DKTGKKCYYL TPEMVLMYCD
VLEGRMMMET TVKSDIKYQP LISRSNALWG LIDPLFPVMG NRIYNIVSMI EPLVLALLQL
KDEARILRGA FLHHCIKEMH QELSECGFTD QKIRSMFIDD LLSILNIDNI HLLAEFFSFF
RTFGHPILEA KVAAEKVREH MLADKVLEYA PIMKAHAIFC GTIINGYRDR HGGAWPPLYL
PAHASKHIIR LKNSGESLTI DDCVKNWESF CGIQFDCFME LKLDSDLSMY MKDKALSPIK
DEWDSVYPRE VLSYTPPKST EPRRLVDVFV NDENFDPYNM LEYVLSGAYL EDEQFNVSYS
LKEKETKQAG RLFAKMTYKM RACQVIAEAL IASGVGKYFK ENGMVKDEHE LLKTLFQLSI
SSVPRGNSQG NDPQSINNIE RDFQYFKGVT TNVKDKKNNS FNKVKSALNN PCQADGVHHN
MSPNTRNRYK CSNTSKSFLD YHTEFNPHNH YKSDNTEAAV LSRYEDNTGT KFDTVSAFLT
TDLKKFCLNW RYESMAIFAE RLDEIYGLPG FFNWMHKRLE RSVIYVADPN CPPNIDKHME
LEKTPEDDIF IHYPKGGIEG YSQKTWTIAT IPFLFLSAYE TNTRIAAIVQ GDNESIAITQ
KVHPNLPYKV KKEICAKQAQ LYFERLRMNL RALGHNLKAT ETIISTHLFI YSKKIHYDGA
VLSQALKSMS RCCFWSETLV DETRSACSNI STTIAKAIEN GLSRNVGYCI NILKVIQQLL
ISTEFSINET LTLDVTSPIS NNLDWLITAA LIPAPIGGFN YLNLSRIFVR NIGDPVTASL
ADLKRMIDHS IMTESVLQKV MNQEPGDASF LDWASDPYSG NLPDSQSITK TIKNITARTI
LRNSPNPMLK GLFHDKSFDE DLELASFLMD RRVILPRAAH EILDNSLTGA REEIAGLLDT
TKGLIRSGLR KSGLQPKLVS RLSHHDYNQF LILNKLLSNR RQNDLISSNT CSVDLARALR
SHMWRELALG RVIYGLEVPD ALEAMVGRYI TGSLECQICE QGNTMYGWFF VPRDSQLDQV
DREHSSIRVP YVGSSTDERS DIKLGNVKRP TKALRSAIRI ATVYTWAYGD NEECWYEAWY
LASQRVNIDL DVLKAITPVS TSNNLSHRLR DKSTQFKFAG SVLNRVSRYV NISNDNLDFR
IEGEKVDTNL IYQQAMLLGL SVLEGKFRLR LETDDYNGIY HLHVKDNCCV KEVADVGQVD
AELPIPEYTE VDNNHLIYDP DPVSEIDCSR LSNQESKSRE LDFPLWSTEE LHDVLAKTVA
QTVLEIITKA DKDVLKQHLA IDSDDNINSL ITEFLIVDPE LFALYLGQSI SIKWAFEIHH
RRPRGRHTMV DLLSDLVSNT SKHTYKVLSN ALSHPRVFKR FVNCGLLLPT QGPYLHQQDF
EKLSQNLLVT SYMIYLMNWC DFKKSPFLIA EQDETVISLR EDIITSKHLC VIIDLYANHH
KPPWIIDLNP QEKICVLRDF ISKSRHVDTS SRSWNTSDLD FVIFYASLTY LRRGIIKQLR
IRQVTEVIDT TTMLRDNIIV ENPPIKTGVL DIRGCIIYNL EEILSMNTKS ASKKIFNLNS
RPSVENHKYR RIGLNSSSCY KALNLSPLIQ RYLPSGAQRL FIGEGSGSMM LLYQSTLGQS
ISFYNSGIDG DYIPGQRELK LFPSEYSIAE EDPSLTGKLK GLVVPLFNGR PETTWIGNLD
SYEYIINRTA GRSIGLVHSD MESGIDKNVE EILVEHSHLI SIAINVMMED GLLVSKIAYT
PGFPISRLFN MYRSYFGLVL VCFPVYSNPD STEVYLLCLQ KTVKTIVPPQ KVLEHSNLHD
EVNDQGITSV IFKIKNSQSK QFHDDLKKYY QIDQPFFVPT KITSDEQVLL QAGLKLNGPE
ILKSEISYDI GSDINTLRDT IIIMLNEAMN YFDDNRSPSH HLEPYPVLER TRIKTIMNCV
TKKVIVYSLI KFKDTKSSEL YHIKNNIRRK VLILDFRSKL MTKTLPKGMQ ERREKNGFKE
VWIVDLSNRE VKIWWKIIGY ISII
