L_PIV5
ID L_PIV5 Reviewed; 2255 AA.
AC Q88434;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mammalian orthorubulavirus 5.
OX NCBI_TaxID=11208;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1320792; DOI=10.1016/0168-1702(92)90057-g;
RA Parks G.D., Ward C.D., Lamb R.A.;
RT "Molecular cloning of the NP and L genes of simian virus 5: identification
RT of highly conserved domains in paramyxovirus NP and L proteins.";
RL Virus Res. 22:259-279(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M81721; AAA47879.1; -; Genomic_RNA.
DR EMBL; AF052755; AAC95518.1; -; Genomic_RNA.
DR PDB; 6V85; EM; 4.38 A; A=1-2255.
DR PDB; 6V86; EM; 4.63 A; A=1-2255.
DR PDBsum; 6V85; -.
DR PDBsum; 6V86; -.
DR SMR; Q88434; -.
DR PRIDE; Q88434; -.
DR Proteomes; UP000007232; 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; 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 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 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; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2255
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000142742"
FT DOMAIN 656..840
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1775..1988
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 618..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1805..1814
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2255 AA; 255926 MW; 63EE2994D68DDE38 CRC64;
MAGSREILLP EVHLNSPIVK HKLYYYILLG NLPNEIDLDD LGPLHNQNWN QIAHEESNLA
QRLVNVRNFL ITHIPDLRKG HWQEYVNVIL WPRILPLIPD FKINDQLPLL KNWDKLVKES
CSVINAGTSQ CIQNLSYGLT GRGNLFTRSR ELSGDRRDID LKTVVAAWHD SDWKRISDFW
IMIKFQMRQL IVRQTDHNDS DLITYIENRE GIIIITPELV ALFNTENHTL TYMTFEIVLM
VSDMYEGRHN ILSLCTVSTY LNPLKKRITY LLSLVDNLAF QIGDAVYNII ALLESFVYAQ
LQMSDPIPEL RGQFHAFVCS EILDALRGTN SFTQDELRTV TTNLISPFQD LTPDLTAELL
CIMRLWGHPM LTASQAAGKV RESMCAGKVL DFPTIMKTLA FFHTILINGY RRKHHGVWPP
LNLPGNASKG LTELMNDNTE ISYEFTLKHW KEVSLIKFKK CFDADAGEEL SIFMKDKAIS
APKQDWMSVF RRSLIKQRHQ HHQVPLPNPF NRRLLLNFLG DDKFDPNVEL QYVTSGEYLH
DDTFCASYSL KEKEIKPDGR IFAKLTKRMR SCQVIAESLL ANHAGKLMKE NGVVMNQLSL
TKSLLTMSQI GIISEKARKS TRDNINQPGF QNIQRNKSHH SKQVNQRDPS DDFELAASFL
TTDLKKYCLQ WRYQTIIPFA QSLNRMYGYP HLFEWIHLRL MRSTLYVGDP FNPPADTSQF
DLDKVINGDI FIVSPRGGIE GLCQKAWTMI SIAVIILSAT ESGTRVMSMV QGDNQAIAVT
TRVPRSLPTL EKKTIAFRSC NLFFERLKCN NFGLGHHLKE QETIISSHFF VYSKRIFYQG
RILTQALKNA SKLCLTADVL GECTQSSCSN LATTVMRLTE NGVEKDICFY LNIYMTIKQL
SYDIIFPQVS IPGDQITLEY INNPHLVSRL ALLPSQLGGL NYLSCSRLFN RNIGDPVVSA
VADLKRLIKS GCMDYWILYN LLGRKPGNGS WATLAADPYS INIEYQYPPT TALKRHTQQA
LMELSTNPML RGIFSDNAQA EENNLARFLL DREVIFPRVA HIIIEQTSVG RRKQIQGYLD
STRSIMRKSL EIKPLSNRKL NEILDYNINY LAYNLALLKN AIEPPTYLKA MTLETCSIDI
ARNLRKLSWA PLLGGRNLEG LETPDPIEIT AGALIVGSGY CEQCAAGDNR FTWFFLPSGI
EIGGDPRDNP PIRVPYIGSR TDERRVASMA YIRGASSSLK AVLRLAGVYI WAFGDTLENW
IDALDLSHTR VNITLEQLQS LTPLPTSANL THRLDDGTTT LKFTPASSYT FSSFTHISND
EQYLTINDKT ADSNIIYQQL MITGLGILET WNNPPINRTF EESTLHLHTG ASCCVRPVDS
CILSEALTVK PHITVPYSNK FVFDEDPLSE YETAKLESLS FQAQLGNIDA VDMTGKLTLL
SQFTARQIIN AITGLDESVS LTNDAIVASD YVSNWISECM YTKLDELFMY CGWELLLELS
YQMYYLRVVG WSNIVDYSYM ILRRIPGAAL NNLASTLSHP KLFRRAINLD IVAPLNAPHF
ASLDYIKMSV DAILWGCKRV INVLSNGGDL ELVVTSEDSL ILSDRSMNLI ARKLTLLSLI
HHNGLELPKI KGFSPDEKCF ALTEFLRKVV NSGLSSIENL SNFMYNVENP RLAAFASNNY
YLTRKLLNSI RDTESGQVAV TSYYESLEYI DSLKLTPHVP GTSCIEDDSL CTNDYIIWII
ESNANLEKYP IPNSPEDDSN FHNFKLNAPS HHTLRPLGLS STAWYKGISC CRYLERLKLP
QGDHLYIAEG SGASMTIIEY LFPGRKIYYN SLFSSGDNPP QRNYAPMPTQ FIESVPYKLW
QAHTDQYPEI FEDFIPLWNG NAAMTDIGMT ACVEFIINRV GPRTCSLVHV DLESSASLNQ
QCLSKPIINA IITATTVLCP HGVLILKYSW LPFTRFSTLI TFLWCYFERI TVLRSTYSDP
ANHEVYLICI LANNFAFQTV SQATGMAMTL TDQGFTLISP ERINQYWDGH LKQERIVAEA
IDKVVLGENA LFNSSDNELI LKCGGTPNAR NLIDIEPVAT FIEFEQLICT MLTTHLKEII
DITRSGTQDY ESLLLTPYNL GLLGKISTIV RLLTERILNH TIRNWLILPP SLRMIVKQDL
EFGIFRITSI LNSDRFLKLS PNRKYLIAQL TAGYIRKLIE GDCNIDLTRP IQKQIWKALG
CVVYCHDPMD QRESTEFIDI NINEEIDRGI DGEEI
