L_EBLV2
ID L_EBLV2 Reviewed; 2127 AA.
AC A4UHQ7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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 European bat lyssavirus 2 (strain Human/Scotland/RV1333/2002) (EBLV2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=453116;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17374776; DOI=10.1099/vir.0.82692-0;
RA Marston D.A., McElhinney L.M., Johnson N., Muller T., Conzelmann K.K.,
RA Tordo N., Fooks A.R.;
RT "Comparative analysis of the full genome sequence of European bat
RT lyssavirus type 1 and type 2 with other lyssaviruses and evidence for a
RT conserved transcription termination and polyadenylation motif in the G-L 3'
RT non-translated region.";
RL J. Gen. Virol. 88:1302-1314(2007).
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: May form homodimer. Interacts with the P protein.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged
CC asymmetrically towards the blunt end of the virus.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SIMILARITY: Belongs to the rhabdoviridae protein L family.
CC {ECO:0000305}.
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DR EMBL; EF157977; ABO65252.1; -; Genomic_RNA.
DR RefSeq; YP_001285397.1; NC_009528.2.
DR SMR; A4UHQ7; -.
DR PRIDE; A4UHQ7; -.
DR GeneID; 5219912; -.
DR KEGG; vg:5219912; -.
DR Proteomes; UP000007206; 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; ISS:UniProtKB.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
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; IPR017234; RNA-dir_pol_rhabdovirus.
DR Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 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..2127
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297835"
FT DOMAIN 611..799
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1674..1871
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2127 AA; 242663 MW; EC05E7C49284B0DD CRC64;
MIDPLEVYDD PVDPVEPEID ARSNSVVPNI LRNSDYNLNS PLIEDPSKLM LDWLITGNKP
ARLNLTDNSL RSYKVLKSYF KKLDVGSLRV GGLGAQSMMS LWLHGAHSES TRSRKCLSDL
ALFYQRSAPI EKLLNYTLEN RGLAIPTDGV LSSLKKVNYD RAFGRYLGNL YSSYLFFHVI
ILYMNALDWE EEKTILALWK DLNSVDIKKD QVKFRDQIWG SLLVTKDFVY SQSANCLFDR
NYTLMLKDLF LSRFNSLLIL LSPPEPRYSE DLISQLCQLY IAGDNVLSTC GNSGYDVIKM
LEPYVVNSLV QRAEGFRPMI HSLGDFPTFI KDKVSQLEGT FGPSARNFFF VLDQLDNIHD
LVFVYGCYRH WGHPYIDYRK GLSKLYDQVH VKKVIDGDYQ ECLASDLAKR ILRWGFDKYS
KWYLDPKLLE KDHPLIPYIQ TQTWPPKHIV DIVGNTWHKL PITQIFEIPE SMDPSEILDD
KSHSFTRTKL ASWLSDHRGG PVPSEKVIIT ALSRPPVNPR EFLKSIDLGG LPDDDLIIGL
KPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
TGQGLQDYSR VTYAFHLDYE KWNNHQRLES TKDVFSVLDY VFGLKKVFSR THEFFQKSWV
YYSDRSDLIG LWEDQIYCLD MSDGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQTRNT
RTKILAQGDN QVLCPTYMLS SGLTQEGLIY ELDSISRNAL SIYRAIEEGA SKLGLIIKKE
ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCISNDQI VNLANIMSTV STNALTVAQH
SQSLIKPMRD FLLMAVQAVF HYLLFSPILK DRVYKILSAE GDNFLLAMSR IIYLDPSLGG
VSGMSLGRFH IRQFSDPVSE GLAFWKEIWS SSSESWIHSL CQEAGNPDLG DRSLESFTRL
LEDPTTLNIR GGASPTILLK EAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLKSI
EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRRS LSRTLEESFF NSEIHGINRM
TQVPQRVGRV WNCSAERADL LREISWGRKV VGTTVPHPGE MLVLLPKSSV SCVCKQTGED
SPRISVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
WFIARDSNLA QTLIRNITSL TGPQFPLEET PVFKRTGSAL HRFKSARYSE GGYSSICPNL
LSHISVSTDT MSDLTQDGKN FDFMFQPLML YAQTWTSELV QKDIRLRDST FHWHLRCLKC
IRPIDDIILD APQVFMFPDV SKRISRMVSG AVPQFQRLPE INLKPGKFEA LDSKDKSRHI
GTAQGLLYSI LVAIHDSGYN DATIFPMNIY SKISPRDYLR GLSRGILIGS SICFLTRMTN
ININRPLELI SGVISYILLR LDNHPSLYVM LREPSLRSEI FSIPQKIPAA YPTTMKEGNR
SVLCYLQHVL RYERDVITAS PENDWLWIFS DFRSAKMTYL TLVTYQSHIL LQKIEKNLPK
QMRIRLRQLS SLMRQILGGH GEDTLDSDED IQGLLRDALQ RTRWVDQEVR HAAKTMTGDH
SPSKKVSRKA GCSEWICSAQ QVAISTSSNP APTSEMDVRA LSRRFQNPLI SGLRVVQWAT
GAHYKLKPIL DNLEAYPSLC LVVGDGSGGI SRTVLSMFPD AKLVFNSLLE VNDFMASGTH
PLPPSAIVSG GDDIVSRVID FGSIWEKPSD LRNLSTWRYF QSIQTVNNMS YDLIVCDAEV
TDIPSVNKIT LLMSDFSLSI NGPLNLIFKT YGTMLVNPDY KAIQHLSRAF PSVTGYITQM
TSSFSSELYL KFSKRGKFFR DAEYLTSSTL REMSLVLFNC SSPKSEMQRA RSLNYQDLVR
GFPEEIISNP YNEMIITLID SEVESFLVHK MVDDLELQRG TLAKMSIIIA IVMVFSNRVF
NVSKPLTDPM FYPPSDPKIL RHFNICCSTL MYLSTALGDV LNFARLHELY NNPITYYFKK
QVIRGSIYLS WSWCDTTSVF KKVACNSNLS LSSHWIRLIY KIVRTTRLAG SSNDLSKEVE
KHLKGYNRWI SFDDIRSRSS LLDYSCL
