L_SHRV
ID L_SHRV Reviewed; 1983 AA.
AC Q9QJT4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Snakehead rhabdovirus (SHRV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC Novirhabdovirus.
OX NCBI_TaxID=103603;
OH NCBI_TaxID=203314; Gobiosoma bosc (Naked goby) (Gobius bosc).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10666265; DOI=10.1128/jvi.74.5.2343-2350.2000;
RA Johnson M.C., Simon B.E., Kim C.H., Leong J.A.;
RT "Production of recombinant snakehead rhabdovirus: the NV protein is not
RT required for viral replication.";
RL J. Virol. 74:2343-2350(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF147498; AAD56771.1; -; Genomic_RNA.
DR RefSeq; NP_050585.1; NC_000903.1.
DR SMR; Q9QJT4; -.
DR PRIDE; Q9QJT4; -.
DR GeneID; 1457774; -.
DR KEGG; vg:1457774; -.
DR Proteomes; UP000007219; 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; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 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..1983
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297840"
FT DOMAIN 559..756
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1588..1785
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 1983 AA; 225025 MW; 3158F671B780B50D CRC64;
MEFFDLDLEV SQERLPAECS LNAPLNLSLS LQLFGRIEPK TENIRRQSRR ITKVLRERHN
GYRLQDLIID STRTQANLIP HLVSSASGDL NTPILEHWEM LSKYYQSLGY SLPSLDKFDF
KESAGYWNAA CSFRDMLLKS QKVEKKVNKQ QTYVIYDITF EFVEGVVFIH GGEDGFNDGF
LAGGAIAAMT YTELLALFKI LNQRAQALLM CNISKGLEPD MVPSPSTIHS IYAEADHMLR
MAGQGAIDLL KLWEPLVLTQ LGDVLGDRFG LEDDFKLTIR TEAALLADQL NLKRSFARMT
ELIKSETRKQ PLFQLFGLFK HFAYPRVYSR DTINTILGVS DKPSANDPEE YLHDQCEIRK
EFYTRYVKAY HRAPQLDLGG LSPGSYLRRA LEAGKMPNEK SPLYTNLEWF FVKFKKSIEW
PLSDTLSTFL SDKAITQNRS TWLDNETSSR DNSEKRLLLK FIKENEDSVA RVVAQAKEIY
DNEDDRIIAL KVKEMELKLK GRGFGLMTFK PRLLQVLRES IAKKTSKLFP EITMTASDLD
LKKRKFLVSR KSDDRRGYVH MSKSLDINKF CTSQRQFNSQ AVFQCLDELL GTGALFSRVH
EIFEKTWIVD GSASDPPNLK KFKDRYQKLK DLGIDAPHTW GDGVFSGLMG GIEGLCQYVW
TICLLLRVER VLSKTSLTHF VMAQGDNVII NLIIPIEIER DGSISPSEHR RVKSLSTSID
TQLAMELEKS GLTLKIEETL SSEHISIYGK DLHCPHHLTL SLKKAGSASI ISSEQYQDVP
TFLAGLSTSI ETISECVNDK VSAHLFGVIL AHAGWKSLCV SQTWKGWEYP YQKDETINRV
RSQGIKLTEG EQVTVEKRLE RNPDKRCLEW ILATSFLGSA LGMLPFPTPV DLEKRGVGDY
ITHRLALTKK ALSSRVLPRR IEKLIRSMVN LPHSRETDLA KLFDSPFSLN LATEEDATSV
IKRLARSTLR DLDIKNERLR AHIDIMDRGL QDLDRELGDS ETINPRVAHL IRDITDEKES
EMFVTKFATA RTMRTVALEN PQDVSVVSLL NKKSRAKETY TIWRSKRAPA EDWECSTQRA
KIERDSSWGK NVIGVTSPSP VEAMSYRLVD PSTWEEEKKD QDFTINYYLS KPSLISHQAR
LERGPLVPYY GTQTQPLIAK AYNELKGNPK TNKALMLLSL RETIVKSGSN LDKLIMRLCE
RALDLDLNTL PSLRAQEEAS SGEGIRGGIK ESMSPVGPDN FYTNITHKVF NRRWLSGFHI
NIADFIIWGL TCTRKSITTQ GTLSGNLPIC IPACRGCLRR KEREFLDIDN PPRWECKEGV
KDKAYMYFTT WCDLPRLSTL PSLDPQDAVF MIGRQLACSK GQDSGAATKF YNVSPESLGL
LHPRMLLLGY SEGLIFSYLR SQHIVLGCLY HPTITELLPS LEKYTLETID QHARQLGYLF
QEEETAKELL NAGLCPYTPR AIPLTITELK NAVCITVSRS ISVTLETKKS IHLMPESGIS
EEEVVAGRHA ARTLGGLLNI KVPNLVYIDC DLTKGLLPWE PELPSEVLQS ENFKIDGKRV
TLYAKSQKRD NSIWEERGWT CSNSREILAK GVKTKSLFIH QSVPSHLDID PALIVVIGGG
LGGCVVPYLQ HWRRPPVIFT TLFSERERIS EDGDLIIPPE LLVRGLSGRM VERELLEAEL
CDVTVPGNRK AIVDAVKRRI KPNESVLLID EIENRGDAED VLQQSISTLL QSLEKHCSLT
SVHTIRESNV KHFTQRLNIL RRGRYEANLF WNRYNRRDQY EALIVIPSES RMTECTFSVA
SVQAAFQKID DGIEVEAKLE AHSWGLPELP PREKKILLGY VSSVFLKLGL VVIERHMSST
KLIDLLESAG PQMISWEEKQ THRSWASTDS IKEKGVTQDR IMALLCFAWT LKGLKHGVWD
TNMDAVVEKT VYITHGPRLC ALDEKPRVQY AEFKLQSKKR VEDLKGYLGA LLHLETFFPL
GDR
