L_SVCV
ID L_SVCV Reviewed; 2095 AA.
AC Q91DR9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Spring viremia of carp virus (Rhabdovirus carpia).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Sprivivirus.
OX NCBI_TaxID=696863;
OH NCBI_TaxID=7962; Cyprinus carpio (Common carp).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Fijan reference;
RX PubMed=11900842; DOI=10.1016/s0168-1702(01)00441-5;
RA Hoffmann B., Schutze H., Mettenleiter T.C.;
RT "Determination of the complete genomic sequence and analysis of the gene
RT products of the virus of Spring Viremia of Carp, a fish rhabdovirus.";
RL Virus Res. 84:89-100(2002).
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; AJ318079; CAC51337.1; -; Genomic_RNA.
DR PDB; 5H5Z; X-ray; 1.74 A; C=828-836.
DR PDB; 5Y91; X-ray; 1.90 A; C=828-836.
DR PDB; 6LBE; X-ray; 2.60 A; E/F=828-836.
DR PDBsum; 5H5Z; -.
DR PDBsum; 5Y91; -.
DR PDBsum; 6LBE; -.
DR SMR; Q91DR9; -.
DR PRIDE; Q91DR9; -.
DR Proteomes; UP000007541; 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:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
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 InterPro; IPR017234; RNA-dir_pol_rhabdovirus.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase;
KW mRNA capping; 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..2095
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000287261"
FT DOMAIN 587..773
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1625..1822
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT BINDING 1652..1661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2095 AA; 238192 MW; EB43D47D061379AC CRC64;
MFEWESQDTP SGLPDEESYF PTSKLSVEER MHYLNNVDYN LNSPLISDDI EYLTLKHFGR
AIPSLWKVKN WEIPLEMLKG VGIIKTWDQI HPWMGKWFDS EHNCPQGESF LRTVQAESEL
TSEIPVTFIK GWIGKEIKFP VKRGHHAVHL LMQKVLDLHK LTLLINSVDS GETEKLCESF
GLNSKQSKFE TYSLGTVRYC PGWIFIDKAE ILLDRNFLLM MKDTLIGRLQ TLLSMLGNCE
MEVEQIYTHT ETMLSLYSYG DQIIEKAGNN GYSKIKLLEP ICNLRLSELA HKYRPLVPDF
PHFQEHVETS VREEDTTDGL LSAILSLVNN TEDIQLILTI YGSFRHWGHP FISYFEGLQK
LHDQVTLPKQ IDKEYAAALA SDLAYTVLQR KFSEEKKWYV DSIALSSKHP LKEHVDNGTW
PTAAQIQDFG DRWHLLPLTK CFEVPDLLDP SVIYSDKSHS MNRKEVIDHV ISTPNKPIPS
KKVLETMINN PATDWPTFLK AVDEEGLPRD NLIIGLKGKE RELKIAGRFF SLMSWQLREY
FVITEYLIKT HYVPLFKGLT MADDLTSVVK KMLDNTNGQG LDDYSSICIA NHIDYEKWNN
HQRKESNGPV FRVMGQFLGY PRLFERTHEF FESSLIYYNG RPDLMDVRGD SLVNTTDKMV
CWEGQAGGLE GLRQKGWSVL NLLVINRESS IRNTVVKVLA QGDNQVICTQ YKTKNYKNED
ELKMLLTAMV ENNQTIMNGI ITGTGKLGLI INNDETMQSA DYLNYGKVPV FRGILRGLET
KRWSRVTCIT NDQIPTLAGV MSSVSTNALT VAHFAASPIN AILQYHYFAN FCLMMIAMHN
PAIRSSMYTK MFRKCHIMSK EFKAATLYLD PSLGGVCGIS LARFLIRSFP DPVTEGLAFW
KMIHHNCQSD WLKALSKRCG NPKLARFRPE HIPKIIEDPA ALNISMGMSA SNLLKTEVKG
HLIRTADTIQ NQIIREAAEY LGQEEASLNE FLWDIEPFFP RFLSEFRSST FVGVTDSLIG
LFQNSKTIRG LFKSYYKREL DRLVVKSELS SLEHLGSYRK ETPDSIWECS STQADLLREK
SWGRSVIGMT VPHPLEMFGK GHQKELECIP CQTSGLTYIS SYCPRGINNW YSTVGSLAAY
LGSKTSETTS ILQPWEKDSK IPIIKRATKL RDSISWFVPP DSKLAKSIQQ NLKALTGEDW
EEDIQGFKRT GSALHRFTTS RVSNGGFSAQ SPAKLTRIMT TTDTMRDLGD QNYDFMFQAG
ILYSQMTTGE LRENSTNSTA THYHITCKSC LREIQEPMLE SRIVYNPPSS SRVIKSWIPN
ATEIMEESKP IKLREVDWDP LTRYEKSYHI GRCQGFLYGD LTYQKTGRSE ESSIFPLSIQ
YKVEGSGFMR GFCDGIIRAS AVQALHRRVS SIVSTADVIY GGALYLTNQV GDSPPFQNLC
RSGPLREELE RIPHKMTSSY PTSNSDMGYL IRNYLKRSLK QLSRGRYETK EGPIWVFSDV
RTKKFLGPFS LSTDALNCLY KNKLSKRDKN AVRNLSQLSS RMRSGDLSDE EIGKVEARFS
FTPAEMRHAC KFTIGKTQVP IVMSEWGQEA YGNITMYPVF YSTTKTEKPD WTFSRLQNPT
ISGLRISQQA TGAHYKLRSL LKGMKIHYQD AIGCGDGSGG LSSCLLRENK HCRVIFNSLL
ELTGNTLRGS TPDPPSAING IPQIRDRCVN LNNVWEHPSD LSHPDTWKYF GELKAQFNMD
VDLIVMDMEV QDIDISRRIE QNLRDHVHSL LSRHGTVIYK TYMTIMSENE KSVLDIVGVL
FEDVQLCQTQ YSSSQTSEVY CVMRRLRQKV DSQHVDWQSL VRQGINSKVY CNLPLDKEFE
RALNLYQIDT LVGVPRGLIP NLAVELETLL EIGGLSGGIL GKLVLNIEEG KLGFTMALIV
SCILISESAI CTTRLSNKRE VPSSGACQRM AVCLIGAAIL LSVHHRSIEN HKGAIRMLRH
SVPIRISSKL RKDGKLQSRW SSISREGLAK DVRLNSNMAG VGAWIRVWSR MKDRERRWEA
READSWLKTH NKGLSMEHVR RHTGVLDILH GTGDRLDRSV PTVSSAPRES GTWVE
