L_HIRRV
ID L_HIRRV Reviewed; 1986 AA.
AC Q77SJ8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
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 Hirame rhabdovirus (strain Korea/CA 9703/1997) (HIRRV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC Novirhabdovirus.
OX NCBI_TaxID=453457;
OH NCBI_TaxID=72011; Acanthopagrus schlegelii (Black porgy).
OH NCBI_TaxID=8255; Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OH NCBI_TaxID=61084; Plecoglossus altivelis (Ayu).
OH NCBI_TaxID=160818; Sebastes inermis (Dark-banded rockfish).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15567027; DOI=10.1016/j.virusres.2004.06.004;
RA Kim D.H., Oh H.K., Eou J.I., Seo H.J., Kim S.K., Oh M.J., Nam S.W.,
RA Choi T.J.;
RT "Complete nucleotide sequence of the hirame rhabdovirus, a pathogen of
RT marine fish.";
RL Virus Res. 107:1-9(2005).
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; AF104985; AAQ73462.1; -; Genomic_RNA.
DR SMR; Q77SJ8; -.
DR Proteomes; UP000008118; 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_0000297836"
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"
SQ SEQUENCE 1986 AA; 224461 MW; 3A6254B6704D0C59 CRC64;
MDFFDLDIEI KQERLPAECS LNSPLNISLS SQLTDRMTPQ NENIRRQRER IRTHTKTHSR
IKHLSKLDND STRLHARLTE DLIKLQHLEV DSPVFDNWAL LTSYYAALDY TLPERASFDW
GQAAPYWNLY TQLRTILLQS QKIRKKDRGV REIYSCGPLR LEFVEGTVLY FTDKQSGGEF
TKSGELPSIT PYADFLAWVK IISQRAQAVL MAVILRVTDK GLSPLPESLL SVYQTVDDIL
KRAGQPAIDL LKLWEPLVIT KLGELLGDRF GLEEDFRLTI RGEATRLAKK LAITNGLNRL
MTVLDSQTEA QPLFQFFGLF KHFAYPRVFS RDTIQAIQEV SDRPSSISAA EFLHDQCEIR
KEFYIRYLKA YHRAPGLDLS ALSPSSFLRE SLEHGKIPNE KSPHYSNKEW YFIKFTKSIE
WPISDTLSTF LSDKAITRDR AAWIEEGHSG RDMSEKRLLL KFIKENFSSV AEIVAAADAI
YNNEGDRLIA LKVKEMELKI KGRGFGLMTF MPRLLQVLRE SIAKKTSKLF PEITMTSSDL
DMKKRKFMLS KRSDDRRGFI HINKSLDINK FCTSQRQFNS SAVFSSLDEM MGTFPLFSRV
HEIFEKTWIV DGSASDPPDL SHFTRILEEC RLHGIEAPHV WADGVFSGLK GGIEGLCQYV
WTICLLLRVE RVMQKTKLTH YILAQGDNVI ITIIVPVEIH RDGIISDQES RRLLTLSRNI
DLSLESELEK SGLTLKIEET LTSENISIYG KDLHCPQHLT LALKKAASAA IISSEQYQDI
PTFLSGLGTS LESLSECVNS KTGAHLFGVL MGVAGWKDLA THQTWRGWRY PYHKAPLSGR
VRASDMKIGK GEAVELTIPV MSPRQQGKET LRELLANSLL GSALGMLAFP TPIDLEKRGV
GDYITHRLAI ARKALLSEKL DPHIEKRVRS ACNLPLSSRV DLSKLFDSPF SLNLATEEDA
TAVIKRQAKK TLRLQEIGND KLRAQIGNMD KGIAALDADL AGAETINPRL NHMIRDITDE
KESEMFVTKF ASARTMRTLA MGDSSEVPIV VLLEKKSQQK ELYTIWRARR PHATMWKCST
VLAKGLRDIS WGKTIVGVTS PSPIEAMETT HIDPTDWEDS RSRETLSINY YLSRAGIDEQ
TAKLTRGSLV PYYGTQTKPL IAKAYLELKG NPRTNKALLL LSVRESLVKT GSNLDELIMQ
LCSHALDIDA ASLPALRAQE EATAGEGLRG GIKESMSPVG PDNFYTNITH KVFNRKWVTP
YHVNIADFII QGLIETRKHL ILNEKMDGLL PLSSVKCTAC FRKKEREFFD IPEGPTWKND
STTSDPAYTY FTTWCDLPRV STLPTMDQQS ATRLLGRGLS LNRPTAGEII TKFYSMSMES
QRLLHPVDLL LGYGEGVVFG YIRSQHIHHG ALFQTKRETL TNKLRKFILD TKTQHAKQIG
YLFQDEDSLH ELMAQGLCPY VPRSIPLTIT ELTNACAITT IRATEVILSA GSRVALMPVQ
AIDETDVDNS RLAANTMQTI LGDSRPMNPV YLDCDLTTNM TAWESSIELD VLKSENFHID
GLLMDLTARE LPISDTPWKQ RDWTCSNDPR IIAKGIKTKS LFIHQGVAEA LNMTPDLLVV
IGGGLGGCAV PYLQEWADVP LIFATLFDER ERISEDGDLV VPPEILVRGM APRMIERELL
EAELCDVTND GNRRLLTRLV KKNRGKGTVV LIDEIENRGA PESLLQSSLQ DLVRRLDKVC
TLTSIHTVRE STVEQFAQRT NSIKRDRKTV TLHWNRYNRR DQFEALVIVK GEETRSDYHV
STATAAQAFR KIDEQLEVEG RLSATRWSLP TLPAREKEIL FGYVSSVFLK TNLVLSADDM
DRETLLETIE DTAPGLISWK EKLEHRDHAF RSDIDEKGIT QDKVFNLICL AWVITGLRYG
IWETDAQSII TKTVYITRGP KLCPLGEKPK RVFASFKLQS DKRVEDAKGF LSALLHLEGF
FPLGRQ
