L_HENDH
ID L_HENDH Reviewed; 2244 AA.
AC O89344;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 03-AUG-2022, entry version 107.
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 Hendra virus (isolate Horse/Autralia/Hendra/1994).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=928303;
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11024125; DOI=10.1128/jvi.74.21.9972-9979.2000;
RA Wang L.-F., Yu M., Hansson E., Pritchard L.I., Shiell B., Michalski W.P.,
RA Eaton B.T.;
RT "The exceptionally large genome of Hendra virus: support for creation of a
RT new genus within the family Paramyxoviridae.";
RL J. Virol. 74:9972-9979(2000).
RN [2]
RP SEQUENCE REVISION TO 1299-1325.
RA Wang L.-F., Yu M., Pritchard L.I., Hansson E., Eaton B.T.;
RL Submitted (AUG-2013) 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; AF017149; AAC83194.3; -; Genomic_RNA.
DR PIR; T08212; T08212.
DR RefSeq; NP_047113.3; NC_001906.3.
DR SMR; O89344; -.
DR PRIDE; O89344; -.
DR GeneID; 1446468; -.
DR KEGG; vg:1446468; -.
DR Proteomes; UP000008771; 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 Gene3D; 3.40.50.150; -; 1.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
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_0000236010"
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"
SQ SEQUENCE 2244 AA; 257496 MW; E13833A04271A1DD CRC64;
MAHELSISDI IYPECHLDSP IVSGKLISAI EYAQLRHNQP NGDKRLTENI KINLQGKRRS
VYISRQSRLG NYIRDNIKNL KEFLHVSYPE CNKSLFSLKS PGMTSKLSNI MKKSFKAYNI
VSRKIIEMLQ NITRNLITQD QKDEVLGIYE QDRLSNIGKY MSQSQWYECF LFWFTIKTEM
RAVIKNSQKP KFRSDSCIIH MKDNNMEIVM NPNLVCIYKN DKDGKRCYYL TPEIVLMCCD
VLEGRMMIET SIKSDIKYQS LITRSNALWT FIDSLFPIMG NRIYNIVSMI EPLVLALLQL
KDEARILRGA FLHHCIKEIH QELIGCGFTD QKTRSIFIDD LLSVMNIDNI HLLAEFFSFF
RTFGHPILEA KTAADKVREH MLADKVLEYG PIMKAHAVFC GTIINGYRDR HRGAWPPLYL
PSHASKHIIR LKNSGESLTV DDCVKNWESF CGIQFDCFME LKLDSDLSMY MKDKALSPIK
EEWDSVYPRE VLNYTPPRST EPRRLVDVFV NDENFDPYNM LEYVLTGDYL TDEQFNVSYS
LKEKETKQAG RLFAKMTYKM RACQVIAEAL IASGVGKYFK ENGMVKDEHE LLKTLFQLSI
SSVPRGNSQG RDSEFSNNTE KSLISLKRTT GRLLNNEVPC RMNIMSALID KNQSDQKKHN
ILPNTRNRHK CDNTSQTFLD YHMEFSPYKS DRMDRTETSD FSKYDDGTGT KFDTVSAFLT
TDLKKFCLNW RYESMAIFAE RLDEIYGLPG FFNWMHKRLE KSVIYVADPN CPPDIGKHIN
LDDTPEDDIF IHSPKGGIEG YSQKTWTIAT IPFLFLSAYE TNTRIAAIVQ GDNESIAITQ
KVHPNLPYKV KKEICARQAQ LYFDRLRMNL RALGLNLKAT ETIISTHLFV YSKKIHYDGA
VLSQALKSMS RCCFWSETLV DETRSACSNI STTIAKAIEN GLSRNVGYCI NVLKVIQQLL
ISTEFSINET LTADVTSPIS NNLDWLVTAS RIPAPIGGFN YLNLSRIFVR NIGDPVTASL
ADLKRMIEHD LMTDKVLQKV MNQEPGDASF LDWASDPYSG NLPDSQSITK TIKNITARTI
LRTSPNPMLK GLFHDKSFEE DLELATFLMD RRIILPRAAH EILDNSLTGA REEIAGLLDT
TKGLIRSGLK KSGIQPKLVS RLSNHDYNQF LILNRLLSNK KRNDLISPKT CSVDLAKALR
CHMWRDLALG RSIYGLEVPD ALEAMTGRYI TGSMECQLCD QGNTMYGWFF VPRDSQLDQV
NKEHSSIRVP YVGSSTDERS DIKLGNVKRP TRALRSAIRI ATVYTWAYGD SEESWYEAWY
LASQRVNIDI DVLKAITPVS TSNNLSHRLR DRSTQFKLPG SVLNRVSRYV NISNDNLDFR
VEGEKVDTNL IYQQTMLLGL SVLEGKFRLR TETDDYNGIY HLHVRDNCCV KEVADIGGVN
AELPVPEYTE VENNRLIYDP DPVSEIDCDR LSKQESKARE LDFPLWSTEE LHDVLAKTVA
QTVLEIITKA DKDVLKQHLA IDSDDSINSL ITEFLMVDPE LFALYLGQSI SVKWAFEIHH
RRPHGRHTMV DLLSDLISNT SKHTYKVLSN ALSHPRVFKR FVNCGLLLPT QGPYLHQQDF
EKLSQNLLIT SYMNYLMNWC DFKKFPFLIA EQDEAVVELR EDIITSKHLC MIIDLYANHH
KPPWIIDLNP QEKICVLRDF ISKCRHTDVS SRSWNITDLD FMVFYASLTY LRRGIIKQLR
IRQVTEVIDT TTMLRDNILV ENPPIKTGVL DIRGCIIYNL EEILSMNTKS TSRKVFNLGS
KLSVENHKYR RIGLNSSSCY KALNLSPLIQ RYLPAGSQRL FVGEGSGSMM LLYQQTLGCS
ISFYNSGIDG DYIPGQRELR LFPSEYSIAE DDPSQSDKLK GLVVPLFNGR PETTWIGNLD
SYEYIINRTA GRNIGLVHSD MESGIDKQVE EIMIEHSHLI SIAINVMIED GVLVSKIAFA
PGFPISRLLN MYRSYFGLVL VCFPVYSNPE STEVYLICLQ KTIKTIIPPQ KVLDHSYLSD
EINDQGITSV IFKIKNIQSK QFHEDLVKHY QVEQPFFVPS HITCDEKLLM QAGLKMNGPE
ILKNEVGYDI GSDINTLRST IIILLNEAMN YFDDERSPSH HLEPFPVLEK TRVKTIMGRV
TRKVTVYSLI KLKETKSPEL YNIKNYIRRK VLILDFRSHT MIKLLPKGMK ERREKSGFKE
IWIFDLSNRE VKIWWKIIGY LSLV
