L_MOKV
ID L_MOKV Reviewed; 2127 AA.
AC P0C568;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Large structural protein;
DE Short=Protein L;
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 Mokola virus (MOKV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=12538;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=269271; Chodsigoa caovansunga (Van Sung's shrew).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9989; Rodentia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9225031; DOI=10.1099/0022-1317-78-7-1571;
RA Le Mercier P., Jacob Y., Tordo N.;
RT "The complete Mokola virus genome sequence: structure of the RNA-dependent
RT RNA polymerase.";
RL J. Gen. Virol. 78:1571-1576(1997).
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 rhabdoviruses protein L family.
CC {ECO:0000305}.
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DR EMBL; Y09762; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; YP_142354.1; NC_006429.1.
DR SMR; P0C568; -.
DR GeneID; 3159474; -.
DR KEGG; vg:3159474; -.
DR Proteomes; UP000006826; 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 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 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; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2127
FT /note="Large structural protein"
FT /id="PRO_0000294416"
FT DOMAIN 611..799
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1674..1871
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..2127
FT /note="Interaction with P protein"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2127 AA; 242160 MW; ACE7284E16A95328 CRC64;
MMDVTEVYDD PIDPVEPEGE WNSSPVVPNI LRNSDYNLNS PLLEDPANLM IQWLTSGNRP
SRMNVTENTT RSYKVLRALF KGVDIATIKI GGVGAQAMMG LWVLGSHSES SRSRKCLADL
SAFYQRTLPI ESILNHTLMN RGLQTPREGV LSGLNRVSYD QSFGRYLGNL YSSYLLFHVI
ILYMNALDWE EEKTILALWR DITSIDIKND RVYFKDPLWG KLLVTKDFVY AHNSNCLFDK
NYTLMLKDLF LSRFNSLLIL VSPPDSRYSD DLAANLCRLY ISGDRLLSSC GNAGYDVIKM
LEPCVVDLLV QRAETFRPLI HSLGEFPAFI KDKTTQLIGT FGPCASQFFS MLQQFDNIHD
LVFIYGCYRH WGHPYIDYRK GLSKLFDQVH MKKTIDQQYQ ERLASDLARK ILRWGFEKYS
KWYLDTGVIP KDHPLAPYIA TQTWPPKHVV DLLGDSWHTL PMTQIFEVPE SMDPSEILDD
KSHSFTRTKL SSWSSEHRGG PVPSEKVIIT ALSRPPVNPR DFLKSIDQGG LPDDDLIIGL
KPKERELKID GRFFALMSWN LRLYFVITEK LLANHIIPLF DALTMTDNLN KVFKKLIDRV
TGQGLKDYSR VTYAFHLDYE KWNNHQRLES TKDVFSVLDR AFGMKKVFSR THEFFQKSWI
YYSDRSDLIG IWKDQIYCLD MTEGPTCWNG QDGGLEGLRQ KGWSLVSLLM IERESKTRNT
RTKILAQGDN QVLCPTYMLS SGLNNEGLRY ELENISKNAM SIYRAIEDGA SKLGLIIKKE
ETMCSFDFLI YGKTPLFRGN ILVPESKRWA RVSCISNDQI VNLANIMSTV STNALTVAQH
SQSLVKPMRD FLLMSVQAIY HYLLFSPIIK DRVYKVLNSK DDDFLLAMSR IIYLDPSLGG
VSGMSLGRFP IRQFSDPVSE GLTFWKEIWL SSSETWIHHL CQEAGNPDLG DRSLESFTRL
LEDPTTLNIR GGASPTILLK EAIRKALYDE VDRVENSEFR EAIILSKTHR DNFILFLKSI
EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTVRRQFRKS LSKTLEESFL NSEIHGINRV
TQTPQRLGRV WTCSAERADQ LREISWGRKV VGTTVPNPSE MLTLVPKSSV ACGCYTREVG
NPRISVSVLP SFDPSFLSRG PLKGYLGSST SMSTQLFHSW EKVTNVHVVK RALSLKESIN
WFVSRESNLA KTLIGNILSL TGPSFPIEEA PVFKRTGSAL HRFKSARYSE GGYSAVCPNL
LSHISVSTDT MSDLTQDGTN FDFMFQPLML YAQTWTSELV QKDFRLADST FHWHLRCQKC
IRPIEEVTLD APQLFDFPDI SSRISRMVSG AVPQFRKLPE VGLKAGDLTA LSSSERSYHI
GTAQGLLYSI LVAVHDPGYN DNSLFPVNIY GKVSARGYLR GLARGILIGS SICFLTRMTN
ININRPLELI SGVISYILLK LDNHPSLYIM LKEPELRAEI FSIPQKVPAA YPTTMEEGNR
SVLCYLQQVL RYERDSMSFP PGNDILWIFS DFRSIKMTYL TLITFQAYLW LQRVERNLSK
QVRVRLRQLN SLMRQVLGGH GEDTIDSDDE ILSLLKESLR RTRWVDQEVR HAAKSMTPDL
NPVPKISRRM GSSEWICSAQ QIAISTSLNP ASASDIDLRS LSRQYQNPLI SGLRVVQWAT
GAHYKIKPIL NDLDVCPCLS LVIGDGSGGI SRVVLSMFPD SKLVFNSLLE VNDLMASGTH
PLPPSALMRG GDDITSRVID FESIWEKPSD LRNPLTWKYF HSIQSKLRSQ FDLIVCDAEV
TDIESVNKIT LLLSDFSMSI KGPLYLIFKT YGTMLVNPDY KAIHHLSRAF PNVTGFVTQM
TSSFSSEIYL RFSKTGYFFR DHELLTASTV REMSLVLFNC SNPKSEMLRA RTLNYQDLIR
GFPPEIISNP YNEMIITLID SEVESFLVHK VVDDLELKRG APSKMAIIIA VAILFSNSVL
NVSKSLNEPK FFPPSDPKLL RHFNICSSTL LFLSTALGDL SNFTRLHELY NSPVTYYFGK
QTIKGRRYLS WSWANSSPIF KKVACNSSIS LSSHWIRLIY KIVKTTRLNC SPRDMLRETE
ACLRTYNKWI NIRDTRSRTS ILDYCCL
