L_SV41
ID L_SV41 Reviewed; 2269 AA.
AC P35341;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Simian virus 41 (SV41).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus.
OX NCBI_TaxID=2560766;
OH NCBI_TaxID=314293; Simiiformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Toshiba/Chanock;
RX PubMed=1328485; DOI=10.1099/0022-1317-73-10-2743;
RA Ogawa M., Mutsuga N., Tsurudome M., Kawano M., Matsumura H., Kusagawa S.,
RA Komada H., Nishio M., Ito Y.;
RT "Nucleotide sequence analysis of the simian virus 41 gene encoding the
RT large (L) protein and construction of a phylogenetic tree for the L
RT proteins of paramyxoviruses.";
RL J. Gen. Virol. 73:2743-2750(1992).
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: Interacts with the P protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxovirus L protein family.
CC {ECO:0000305}.
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DR EMBL; X64275; CAA45569.1; -; Genomic_RNA.
DR PIR; JQ1750; JQ1750.
DR SMR; P35341; -.
DR Proteomes; UP000108270; 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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR024352; L_methyltrans_paramyxo.
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; IPR016269; RNA-dir_pol_paramyxovirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF12803; G-7-MTase; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 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..2269
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000142741"
FT DOMAIN 666..850
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1785..1998
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT BINDING 1815..1824
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2269 AA; 256432 MW; 3BD60C14AA161F5B CRC64;
MAASADILLP EVHLNSPIVK HKLVYFLLLG KLPHNLSEDE ITPLHNQNWD QIAHEESNLS
ERLFAVRSEL TRRIAQLRAT RWRSEIAVLL WPNSLPYLCT FKPYNRLNTI DEWNKLVSAA
SNILSSPLSK CMQDISTKLI GRTNLFSRSQ SRPGQSADNT ITLNKIAAVW ADNKWQPLVS
LWLTIKYQMR QMIANQSKRT CSELVYVVDT RSGIIIITPE LVTCFDKDHS VLMYFTFEMV
LMISDLFEGR MNVTALCTVS NYLSPLLSRI ERLFDIVDHL AHLLGDNVYK IIASLESLVY
GCLQLHDPVI DLAGTFYSFV AQEIVDGLQQ GNILSPEEAY TVTEQLLECF SGLSPDLTAE
LLCLMRLWGH PNLTAAQAAK KVRDTMCAGK VLDFQIIMKT LAFFHTILIN GYRRKKNGIW
PPLSLPGNAS KSLIELHHDN SEISYEYTLR HWKELSLIEF KKCFDFDPGE ELSIFMKDKA
ISAPKEDWMS VFRKSLIKQR HQRHHIPMPN PFNRRLLLNF IEDPSFDPAK ELEYVTSGEY
LRDPHFCASY SLKEKEIKPD GRIFAKLTNR MRSCQVIAEA LLANHAGKLM KENGVVMNQI
SLTKSLLTMS QIGLISEKAQ RYTRDNIALG ALFSKGQRTR AHPQTQLSSI DSSQNRELPD
DSLELSACFI TTDLTKYCPQ WRYQTIIPFA KTLNRMYGVP HLFEWIHLRL LRSTLYVGDP
FNPPADTSVF DLDQVLNGDI FIVSPKGGIE GLCQKMWTMI SISVIILSSA ESKTRVMSMV
QGDNQAIAVT TKVPRSVPLT EKRNLAYNAS KLFFDRLKHN NFGLGHQLKA QETIISSQFF
IYSKRVFYQG RILTQALKNA SKLCLTADVL GECTQASCSN AATTIMRLTE NGVEKDVCYM
LNVYQAIRQL CFDLYYPQYS IPGEQISQHY LKHPSIVARL VILPSQLGGL NYLSCSRLFN
RNIGDPLGTA VADLKRLIKC GALESWVLSN LLSRKPGTGS WATLAADPYS LNIDYLYPPT
TILKRHTQNT LMEVCKNPML KGVFTDNARE EENNLAKFLL DRDIVLPRVA HIVIEQSSVG
RKKQIQGFFD TTRTIMRKSF EIKPLSSKRT LSVIECNINY LAYNFNIIHH PNPIPGYLQC
ITTDNCSVDI ARSLRKLSWS SLLNGRTLEG LETPDPIEVV NGALVIGVGE CDYCMQGDTK
FTWFFLPKGI EIDGDPEKNP PIRVPYVGSK TEERRVASMA YVKGATSSLK AALRGAGVFI
WAYGDTDANW DDALDLANTR VQISKEQLQA LTPLPTSANI THRLDDGATT IKFTPASSYA
FSSYTHISND QQYLEVDNRV VDSNIIYQQL MITGLGIIET YNNPPIRTSS EELTLHLHTS
SSCCIRPVDG CIICESPSLL PQLTVPYTNP FVYDPNPLAD YEIAHLDYLS YQARIGSIEH
YSLQDRIDLL AHLTAKQMIN SIIGLDESVS LLNDAVVTSD YTNNWISECS YTKIDLVFKM
MAWNLLLELS FQMYYLRITT WSNIFDYTYM TLRRIPGNAL TNIAATISHP KLLRRAMNLD
VITPVHAPYL ASLDYIKLSI DAIQWGIKQV LADLHNGIDY EILILSEDSL ELSDRAMNLI
ARKLTLLALI QGNQLVLPKI KGLSPDEKCL VLTEHLMSEY QLLLLDDAEL SKRSYNLTNP
RITAFPSNNF YLTRKVLNSI RDSEEGQYLI GAYYDSFQQM ETDIILHSTL IAPYDTSETL
TKFDLCISLF PHDDNLEKYP LPVDHDSQSA VSTIVPGPPI HHVLRPLGVS STSWYKGLSY
VRYLELCKVP TGDHLYLAEG SGASMSLVEM LIPGQKVYYN SLFSSGENPP QRNYAPLPTQ
FVQSVPYKLW QADLTNKEGI IEDFIPLWNG NGAVTDLSNK DCVAFIIHKV GAEQASLVHV
DLESTANLNQ QSLSRSQIHA LIIATTVLKR GGFLVYKTSW LPFSRLSQLA CVLWSFFDKI
TMIRSSYSDP NSHEIYLVCR LAADFKTIGF SAALASAIAI AIHGDGFTTI HPDVVSNYWQ
HHLENVGRVG KAIDDVIDGV STNFYSGDNG LILRCGGTPS SRKWLDIDLL PTFSSLQETL
VNLVTVHLKE IIEIQTSSME DYTSLLFTPY NIGSVGKIRT IVKLILERSL MYVIRNWLVM
PSSYQDSVRQ DLELGSFRLS SVLQEDTFWK LTENRKYLAS QLTRDYITTF FTTHSILPIH
RSYQKRIWKA LGSVIYCSEV PGESQQNWDS IPLVYEEDQI ERGIDGEEL
