L_IHNVO
ID L_IHNVO Reviewed; 1986 AA.
AC Q82707;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Infectious hematopoietic necrosis virus (strain Oregon69) (IHNV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC Novirhabdovirus.
OX NCBI_TaxID=429315;
OH NCBI_TaxID=8028; Salmo.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8683214; DOI=10.1099/0022-1317-77-6-1259;
RA Schutze H., Enzmann P.J., Mundt E., Mettenleiter T.C.;
RT "Identification of the non-virion (NV) protein of fish rhabdoviruses viral
RT haemorrhagic septicaemia virus and infectious haematopoietic necrosis
RT virus.";
RL J. Gen. Virol. 77:1259-1263(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7595355; DOI=10.1099/0022-1317-76-10-2519;
RA Schutze H., Enzmann P.J., Kuchling R., Mundt E., Niemann H.,
RA Mettenleiter T.C.;
RT "Complete genomic sequence of the fish rhabdovirus infectious
RT haematopoietic necrosis virus.";
RL J. Gen. Virol. 76:2519-2527(1995).
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; X89213; CAA61500.1; -; Genomic_RNA.
DR SMR; Q82707; -.
DR PRIDE; Q82707; -.
DR Proteomes; UP000007211; 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; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..1986
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000282897"
FT DOMAIN 560..757
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1592..1788
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT BINDING 1619..1628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1986 AA; 225021 MW; 25FE029E810846F9 CRC64;
MDFFDLDIEI KQERLPAECS LNSPLNYSLS AQLTDRMTPR TENVRRQRER LRSHMREHFR
VKDLSTLDND STRLHARLTE DLITIQSPEI DSSVLENWTP LKSYYASLDY TLPEKTAFKW
EHAAPYWNLF AQLRAILLQS QKIKKQETGT RELYSCGPLQ IEFVEGVVLY FTDRGSKEEF
TKSGELPSVT PYADFLAWIK IISQRAQAVL MAVILRVTDK GLSPLPESLL AIYQNVDDIL
KRAGQPAIDL LKLWEPLVIT KLGELLGDRF GLEEDFRNTI RGEATKLAKN LFISRGLNRL
MDILDQQTDA QPLFQFFGLF KHFAYPRVFS RDTIQAIQEV SDRPSSISAV DFLHDQCEIR
KEFYVRYINA YHRAPGLDLS ALSPSSFLRD SLERGKIPNE RSPLYSNKEW YFVKFTKSIE
WPVSDTLSTF LSDKAITRDR PAWIEDGHSG RDMSEKRLLL KFIKENFSSV ADIVGAAEAI
YNNQEDRLIA LKVKEMELKI KGRGFGLMTF MPRLLQVLRE SIAKKTQKLF PEITMTSSDL
DMKKRKFMLS KKSDDRRGFI HVNKSLDINK FCTSQRQFNS NAVFSSLDEL MGTFPLFSRV
HEIFEKTWIV DGSSSDPPNL AHFTRILDEC TALGLDTPHI WADGVFSGLK GGIEGLCQYV
WTICLLLRVE RVMQKTALTH YILAQGDNVI ITIIVPVEIH RDGTIPEQES RRILALSRDI
DLSLESELEK SGLTLKIEET LTSENISIYG KDLHCPQHLT LAIKKAASAA IISSEQYQDV
PTFLSGLGTS LEALSECVNN KVGVHLFGVI MGVAGWRDLA THQTWRGWRY PYHKKAITGR
IRASEMKLSK GEPTELSISV LSKRRRETET LIELLSNSLL GSALGMLAFP TPLDLEKRGV
GDYITHRLTI ARKALLSGHL DPRIGRKVES ACNIPLSSRT DLSKLFDSPF SLNIATEEDA
TAVIKRQATK ILRLQEIKNE KLKAQIDNMD KGIATLDAAL AGATNINPRL NYMIRSITDE
KESEMFVTKF ASARTMRTLA MNHSSELPIV ILLEMKSQQK ETYTIWRTKR PPVTMWKCST
VLAKELRDTS WGKNIIGGTS PSPIEAMETI QIDPTEWEDR RSQDAMSINY YLSRAGMDEQ
TAKLTRGFLV PYYGTQTKPL VAKAYLELKG NPRTNKALLL LSVRESLVKT GSNLDKLIIK
LCSHALDIDV ASLPALRAQE EAAAGEGLRG GIKESMSPVG PDNFYTNITH KVFNRKWATP
YHVNIADFII QGLIETRRHL LVNERMNGLL PVSSVKCTSC FRKKEREFFD IPEEFTWKNE
SKTSDPAYTY FTTWCDLPRV SNLPEMDQRS ATRLLGRGLA LNRSSSGEII TKFYSMPMES
QRLLHPVELL LGYGEGVIFG YLRSQHINHG ALFHIGDESL AKKLRRYVLD TKTQHAKQIG
YLFQDEDSLH ELLGQGLCPY IPRSIPLTIT ELTNACAITT IRATEVILST KARIHHMPVQ
AIDESDVDTS RLAANTMQTI LGDPRPMNLV HLDCDLTHNM VAWESEVELD ILKSENFHID
GLLVELTARE LPIGDTPWKQ RDWTCSNDPK IIAKGIKTKS LFIHQGVTGA INLIPDLLVV
IGGGLGGCAV PYLQEWPDTP IIFATLFDER ERISEDGDLI VPPELLVRGM APRMIEREIL
EAELCDITNE GNRRLLIRLV TKNKGGGKVV LIDEIENRGA PESLLQSSLQ DLFEKLDKVC
KLTSVHTVRE STVEQFSQRV NSIKRSRKAV TLHWNRYNRR DQFEALVIVK GEEAKSDYRI
STITSAKAFR KIDEQLEIDG RLSSTQWSLP ALPSREKNIL FGYVSSVFLK MNLALSANDM
DRERLIETIE GTAPGLISWK EKLEHRDHAH RSDIEEKGIT QDKIFNLICL SWVLKGLRYG
VWDTDAQSIV AQTVYITRGP KLCPLGEKPK RIFASFKLQS GKRVEDAKGF LSALLHLEGF
FPLGEQ
