ID   L_IHNVW                 Reviewed;        1986 AA.
AC   Q82685;
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 WRAC) (IHNV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC   Novirhabdovirus.
OX   NCBI_TaxID=429314;
OH   NCBI_TaxID=8028; Salmo.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8578857; DOI=10.1016/0168-1702(95)00056-v;
RA   Morzunov S.P., Winton J.R., Nichol S.T.;
RT   "The complete genome structure and phylogenetic relationship of infectious
RT   hematopoietic necrosis virus.";
RL   Virus Res. 38:175-192(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; L40883; AAC42155.1; -; Genomic_RNA.
DR   RefSeq; NP_042681.1; NC_001652.1.
DR   SMR; Q82685; -.
DR   GeneID; 1489850; -.
DR   KEGG; vg:1489850; -.
DR   Proteomes; UP000007212; 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..1986
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000282898"
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;  225243 MW;  79E758B0B81474AA CRC64;
     MDFFDLDIEI KQERLPAECS LNSPLNYSLS AQLTDRMTPR TENVRRQRER LRSHMREHFR
     VKDLSTLDND STRLHARLTE DLITIQSPEI DSSVLENWPP LKSYIASLDY TLPEKTAFKW
     EQAAPYWNLF AQLRAILLQS QKIKKQETGT RELYSCVPLQ IEFVEGVVLY FTDRGSKEEF
     TKSGELPSVT PYADFLAWIK IISQRAQAVL MAVILRVTDK GLSPLPESLL AIYQNVDDIL
     KRAGQPAIDL LKLWEPLVIT KLGELLGDRF GLEEDFRNTI RGEATKLAKN LFISRGLNRL
     MDILDQQTDA QPLFQFFGLF KHFAYPRVFS RDTIQAIQEV SDRPSSISAV DFLHDQCEIR
     KEFYIRYINA YHRAPGLDLS ALSPSSFLRD SLERGKIPNE RSPLYSNKEW YFVKFTKSIE
     WPVSDTLSTF LSDKAITRDR PAWIEDGHSG RDMSEKRLLL KFIKENFSSV ADIVGAAEAI
     YNKEEDLLIA LKVKEMELKI KGRGFGLMTF MPRLLQVLRE SIAKKTQKLF PEITMTSSDL
     DMKKRKFMLS KKSDDRRGFI HVNKSLDINK FCTSQRQFNS NAVFSSLDEL MGTFPLFSRV
     HEIFEKTWIV DGSSSDPPNL AHFTRILDEC TALGLDTPHI WADGVFSGLK GGIEGLCQYV
     WTICLLLRVE RVMQKTALTH YILAQGDNVI ITIIVPVEIH RDGTIPEQES RRILSLSREI
     DLSLESELEK SGLTLKIEET LTSENISIYG KDLHCPQHLT LAIKKAASAA IISSEQYQDV
     PTFLSGLGTS LEALSECVNN KVGVHLFGVI MGVAGWRDLA THQTWRGWRY PYHKKAITGR
     IRASEMKLSK GEPTELSISV LSKRRRERET LIELLSNSLL GSALGMLAFP TPLDLEKRGV
     GDYITHRLTI ARKAILSGHL DPRIGRKVES ACNIPLSSRT DLSKLFDSPF SLNIATEEDA
     TAVIKRQATK ILRLQEIKNE KLRAQIDNMD KGIATLDAAL AGATNINPRL NYMIRSITDE
     KESEMFVTKF ASARTMRTLA MNHSSELPIV TLLEMKSQQK ETYTIWRTKR PPVTMWKCST
     VLAKELRDTS WGKNIIGGTS PSPIEAMETI QIDPTEWEDR RSQDAMSINY YLSRAGMDEQ
     TAKLTRGFLV PYYGTQTKPL VAKAYLELKG NPRTNKALLL LSVRESLVKT GSNLDKLIIK
     LCSHALDIDV ASLPALRAQE EAAAGEGLRG GIKESMSPVG PDNFYTNITH KVFNRKWATP
     YHVNIADFII QGLIETRRHL LVNERMNGLL PVSSVKCTSC FREKEREFFD IPEEFTWKNE
     SKTSDPAYTY FTTWCDLPRV SNLPEMDQRS ATRLLGRGLA LNRSSSGEII TKFYSMPMES
     QRLLHPVELL LGYGEGVIFG YLRSQHINHG ALFHIGDESL AKKLRRYVLD TKTQHAKQIG
     YLFQDEDSLH ELLGQGLCPY IPRSIPLTIT ELTNACAITT IRATEVILST KTRIHHMPVQ
     AIDESDVDTS RLAANNMQTI LGDPRPMNLV HLDCDLTHNM VAWESEVELD ILKSENFHID
     GLLVELTARE LPIGDTPWKQ RDWTCSNDPK IIAKGIKTKS LFIHQGVTGA INLIPDLLVV
     IGGGLGGCAV PYLQEWPDTP IIFATLFDER ERISEDGDLI VPPELLVRGM APRMIEREIL
     EAELCDITNE GNRRLLIRLV TKNKRGGKVV LIDEIENRGA PESLLQSSLQ DLFEKLDKVC
     KLNSVHTVRE STVEQFSQRV NSIKRSRKAV TLHWNRYNRR DQFEALVIVK GEEAKSDYRI
     STITSAKAFR KIDEQLEIDG RLSSTQWSLP ALPSREKNIL FGYVSSVFLK MNLALSANDM
     DRERLIETIE GTAPGLISWK EKLEHRDHAH RSDIEEKGIT QDKIFNLICL SWVLKGLRYG
     VWDTDAQSIV AQTVYITRGP KLCPLGEKPK RIFASFKLQS GKRVEDAKGF LSALLHLEGF
     FPLGEQ