L_ISFV
ID L_ISFV Reviewed; 2093 AA.
AC Q5K2K3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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:P03523};
DE Includes:
DE RecName: Full=GTP phosphohydrolase {ECO:0000250|UniProtKB:P28887};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P28887};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase;
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 Isfahan virus (ISFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=290008;
OH NCBI_TaxID=10045; Gerbillinae (gerbils).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15614433; DOI=10.1007/s00705-004-0452-2;
RA Marriott A.C.;
RT "Complete genome sequences of Chandipura and Isfahan vesiculoviruses.";
RL Arch. Virol. 150:671-680(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=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 -!- 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)-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 (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 -!- 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; AJ810084; CAH17548.1; -; Genomic_RNA.
DR RefSeq; YP_007641386.1; NC_020806.1.
DR SMR; Q5K2K3; -.
DR PRIDE; Q5K2K3; -.
DR GeneID; 14857914; -.
DR KEGG; vg:14857914; -.
DR Proteomes; UP000204017; 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; ISS:UniProtKB.
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 3: Inferred from homology;
KW ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase; mRNA capping;
KW 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..2093
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000287260"
FT DOMAIN 587..773
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1629..1826
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1656..1665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2093 AA; 237644 MW; B65373A9AB43E2C9 CRC64;
MDEYSEEKWG DSDEESFGTG KYSDESRIRG LNSVDYNLNS PLIQDDLYYL MERVRGRPVP
PIWKAKNWTE TIHLVQESRL DYLPTQKLHS WYAEWLMEES HDSSQGLAFL KEVDKDSLET
YEVVMSFLRG WCGGAPAYKK KEGRHIAKIG SLCQKFLDLH RVILIMNAST QMELSNLAET
FQASSVSKKI ITTPSMGKME MSGQFALAYQ QKVILDRNFL LMMKDVVIGR MQTLLSMVSR
TDDKFSDGDI SYLIKIYQLG DKIIQSLGND GYELIKTIEP MCNLRLSDLA REYRPLIPEF
PHFRQHIEGT VSELRKKTAL IVDMFKMIDR TPGVDITLVI YGSFRHWGHP FIDYFAGLTK
LNSQVTMGKQ IDDEYVACLA SDLARIVLTK EFNEKKRWSV NYNLVPQDHP FHEHIRDNTW
PTPAVIQDFG DKWHELPLTQ CFEIPDLIDP SIIYSDKSHS MNRQDVLNHV KRKPDQPIPS
RKVLQTMIDT PATNWLEFLE EIDKNGLSDD DLVIGLKGKE RELKIAGRFF SLMSWKLREY
FVITEYLIKT HFVPLFHGLT MADDMTAVIK KMLESSSGQG LKDYSAVCIA NHIDYEKWNN
HQRKRSNEPI FKVMGQFLGF PNLISRTHEF FEKSLIYYNG RPDLMKVQDG RLVNTTKQLV
CWEGQAGGLE GLRQKGWSIL NLLVIQRESK IRNTAVKVLA QGDNQVICTQ YKTKQHRNET
ELRSALTQMK LNNDAVMKAI ESGTNKLGLL INQDETMQSA DYLNYGKVPI FRGVIRGLET
KRWSRVTCVT NDQLPTCANL MSSVSTNALT VAHFDVTPLN AMIQYNYFGN FSRLLLNMHD
PAVRCSLFQL SQKHKIDLFS FEFKVGVLYL DPSIGGVCGT ALSRFLIRGF PDPVTESISF
WKVIYNNTQD NRLKKLCTAF GNPKIAQFRY SHIEKLLEDP TSLNISMGMS AANLLKSEIK
KNLLRKRRTI GNSIVRDAVT YIHSEDEKIR SYLWSINPLF PRFLSEFKSG TFMGVASSVV
SLFQNSRTIR NVFKDYMSSA IDELITKSEV NSLEHLCKYK GVRNFDQVWK CSASQADYLR
RLSWGRKVLG TTIPHPLEML GAGTIKNNSS TCCEHSGQDY ISVFCPKGIS NVLIERGPMA
AYLGSKTSES TSILQPWEKE SKIPIIKRAT RLRDAIHWFV EPSSNLAKSI LQNITALTGE
EWGSSLEGFK RTGSALHRFT TSRMSHGGFC AQSPAALTRM MATTDTMSDY AKDNYDFMFQ
ACLLFSQITT SVLLLETTIS NTVHFHTRCI NCVRKIEEPW LESPSVLQSK DVSNVLASWR
NGGGSWGEQL HQLKPLKGDW EILTPAEKSY HVGRTLGFLF GDLTGQSSIR ADDSSLFPLS
IQKRLRGRGF LRGVLDGLVR ASACQVIHRR SLTQLKRPAN AVYGGLIFLI DKISASSTFI
NLCRDGPIRE ELSSIPHKIP TSYPTSNADL GLHIRNYFKF QCKSVELGKY QSDLEDLWLF
SDLLSSGFAG PYALSSKVLK SLYKPSLSRR DRNNIRKLGA LSRLLRSHEN WSELHKEFLT
SQLLLCQEEV RHACKFGIPK NVSAKSSMVW GKEAVSYVLD IPVEFTSQKQ TKHLNACPRI
QDPTISGLRL GQLPTGAHYK IRTILNAYNI KCRDVLCGGD GSGGMTAACL RYYSNSRAIF
NSILEFDGSS MKGSSPDPPS ALETVDQGMV RCVNATTCWE NPSDLSQERT WDYFLHLKKS
FNMKIDLIIL DMEVRDFQIS KLIEGNLRLK ISKLLEKNGT LIYKTYGTII CSETSNVLTT
LGPLFHSVYI VQTGYSSSFT SEVYVLFSKQ KSFVDSPYVD WGSLQYNWEK LACFRNPRQE
FKRALRIRSS RSLMGIPSSF LPDPLVNLET LLQISGVPSG VSHQLVTDVK SSGASGLSSA
IGLLGLISHF TLDVTKLYVQ EYRPPSDNRL IKMASAITGI SYWISIAYHD QQLNQALTSV
IKKSFPIRWG LINHRLHWSV SDRFHRSKDV RLSDCLAGIG NWIRGMELMK LPAGMFSHKE
VNMILSKYIR GLNYHTISSR TGILEILKSQ FSIIDRSLMT ITTDNIQSSD WTD
