L_TIBVC
ID L_TIBVC Reviewed; 2119 AA.
AC D8V078;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 59.
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 Tibrogargan virus (strain CS132) (TIBV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Tibrovirus.
OX NCBI_TaxID=1559361;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=469753; Culicoides brevitarsis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=CS132;
RX PubMed=21593274; DOI=10.1099/vir.0.026120-0;
RA Gubala A., Davis S., Weir R., Melville L., Cowled C., Boyle D.;
RT "Tibrogargan and Coastal Plains rhabdoviruses: genomic characterization,
RT evolution of novel genes and seroprevalence in Australian livestock.";
RL J. Gen. Virol. 92:2160-2170(2011).
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; GQ294472; ADG86355.1; -; Viral_cRNA.
DR RefSeq; YP_007641376.1; NC_020804.1.
DR SMR; D8V078; -.
DR GeneID; 14857905; -.
DR KEGG; vg:14857905; -.
DR Proteomes; UP000029770; 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:0019083; P:viral transcription; IEA:UniProtKB-KW.
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 Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 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;
KW Viral transcription; Virion.
FT CHAIN 1..2119
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000432052"
FT DOMAIN 612..798
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1658..1855
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2119 AA; 244351 MW; B01916DDEC636B3D CRC64;
MDHNFEFYDD GGYDYDFSEE NVDDCIENVD CTDYCSLNLI NSYDYNLNSP ITPEKLNNCL
SYCQGLPYDQ IFYNPDYVKV KLMISHFKTV NVDDIPYYSE LVKIWPKIIS NVNCPQKGRE
FLVNAFDNFE FIYTIIRSFY KGWYKKEPET TYLDVLTNLN RLLDRDLSWF SMFLDLFFII
NLMNAKTVME QKNICLKRKW KAYKLNDEII YFSGQTETLG VFALSGEFVL IESQNLLLDR
NTTLMIKDTL VGRFQTILSM ICLQNEYQYQ ENEISYLRQL YDLGDQILST YGSEGYDIIK
TLEMICNNWI CDESFKYFRP MPDFTSFRSH VTNTIQDLVN NGYALASAWF NHIMNTTSIN
LVLVFYGSFR HWGHPPIEVL QGLRNLEGLV NEKHDVDDNY CQALASDLAF KVLKKKFRED
KKWYVDHKKM DQNNLLYTHI KNNTWPNPQT RIQFGDNWHK LPLIKCFELP DMIDLSSIYS
DKSHSLTRSQ VVEHVRYNSD KPIPTKRVLN TLLETENVNW PEFLKSVNDF GLPPEDLVIG
LKPKEREMKR TGRFFSLMTW NLRNYFVMTE LLIKEHFIGL FNGLTMADDL QGLIKKLLDR
TTGQGDSKIK KINIANGLDY TKWNNYQRYD SNRYVFRVMG QFLGYDMLIE RTHQFFEQSL
IYYPQRPDLM MVQNNTLENR GNEIVCWNGQ LGGLEGLRQK GWSVLNYLMI ERESKVRNSQ
IKILAQGDNQ IIFTSCFLDP YYSDEELLDN MMRAKDNNEA IMNAVMKGAE KIGLVINMDE
TIQSCCYANY GKVIIFRGKI LGLSTKRWSR VTCSSNDQIP SLGTLLASVS TNAMTVGNFS
ETPHDAILGH LIFGLIVLEV LAQHNPAIRG DPSKYIVQHK LMSHPLFKII LLYLDPSLGG
IGGTSVNRFL IRAFADPVTE SLSFWKLIYE NCNDNVIKNL CLEVGNPSLA VYNDDHFLKL
VEKPESLNIP KGISSTNMIK EQIKLSLINN AHNIKNKIIH DVTVRIREEE PALIAWLKSI
KPVFPRFLSE MASSTFYGLS NNLISLFTNS RTIRNCFKTK CLKEVDYLII KSEVIGIVSC
LKLVIKTHTN KPDNIWTCSA AHADKLRKQS WNEDIIGMTV PHPIEMHKIG YVVNGECLHC
YENKLSQCYI SILTPRGIPN TDYYCEGGPY KPYLGSSTNE GTSVLQPWEK ETKIPIIRRA
ARLRDVISWF VGEDSNLSES IINNLEALTG ENWGNYMRGF KRTGSALHRF RCARVSNGGF
SACSPTKSSW MIVTTDTMTG LDESNYDFMF QASIIFSQVT VGSIQRSTSQ IYHMHLNCQE
CLREIKEPLL ESDWVLKPRP VHELLKQWRP DPDLPWGFKN QICEIKNHST EWDLEPNTSK
CYFVGLILGF LFGDKVLSNG IQTENNLFPL SIRSRLDPSY FYGGLLRGFK LIAAIHLTHR
RNVISGQDSK SMLYGTLYYL IEEVSCDTDF VQFVSTGNLH NELFYSPHKI PPSYPLSGKD
LGSLCRSYLK YQLKDSDMSS ELRYVWVFAD IRSPKLLCTL GISLYVERLL FKESLTKKDK
ELIKRYQEDY ILGNNNELPT DMLNFYISNL RFCESEVRHS CKFSLPKIEY SLNQATSTWG
QECWGYVNEL DIICVADTIS YPKIQVPQYR NPVISGLRLF QCATGAHYKI RSILKHYSVQ
YRDALIGGDG SGGISALCLR YNARSRIIFN SLLQLEDSIL SGSRPTGPSA VASMGDMKLR
CVNFDSVWQE PSDLRELQTW KYFLRLKQDF NLKIDLAIFD MEVTDEISIS QIDDMLISHL
HCIFTTQTNT LIYKTYLDRV LNYPDMLLKL CQNFKSVKAV TTEFSSFKTS EIYLVCQNIE
TYPILSRTAL EEETRQRLLK LAYANSPLSH EISRAFKIYS RKDLMDGVPN HLISDPFLDL
STLFVMSGSL TSDACAILQL KNRSNLLNIL ISELCKLTNI IFELTVIHPK KIKVPSSPNI
NNYFALVIGI GTWFAFVLND PDYIRLIDAI INKQVYTDIY FYAQKNNKGI INQWKVSDNQ
SGKLICKKKF HISHKLATIG QVIRSCELSY RTITNPLPIQ STSVNQLIQQ KNKKLKLKYI
FKSCDLFFYL PDSILDTST
