L_RABVD
ID L_RABVD Reviewed; 2127 AA.
AC Q0GBX5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
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 Rabies virus (strain China/DRV) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=445792;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Zhao Y.J., Guo L., Huang Y., Qian A.D.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ875051; ABI47946.1; -; Other_RNA.
DR SMR; Q0GBX5; -.
DR Proteomes; UP000008618; 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; 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_0000294419"
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..28
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; 242199 MW; B91DD2FD7C7631B1 CRC64;
MLDPGEVYDD PIDPVESDAE PRGAPTVPNI LRNSDYNLNS PLIEDPAGLM LEWLKTGNRP
YRMTLTDNCS RSYKVLKDYF KKVDLGSLKV GGTAAQSMIS LWLYGAHSES NRSRRCITDL
AHFYSKSSPI EKLLNCTLGN RGLRIPPEGV LSCLEKVDYD KAFGRYLANT YSSYLFFHVI
ILYMNALDQD EEKTILALWK DLTSVDIGKD LVKFKDQIWG LLIVTKDFVY SQSSNCLFDR
NYTLMLKDLF LSRFNSLMIL LSPPEPLYSD DLISQLCQLY IAGDQVLSMC GNSGYEVIKI
LEPYVVNSLV QRAEKFRPLI HSLGDFPVFI KDEVSQLEGT FGPSAKRFFR VLYQFDNIHD
LVFVYGCYRH WGHPYIDYRK GLSKLYDQVH MKKVIDKSYQ ECLASDLARR ILRWGFDKYS
KWYLDSRFLA QDHPLTPYVK TQTWPPRHIV DLVGDTWHKL PITQIFEIPE SMDPSEILDD
KSHSLTRTRL ASWLSGNRGG PVPSEKVIIT ALSKPPINPR EFLKSIDLGG LPDEDLIIGL
KPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
TGQGLSDYSR VTYAFHLDYE KWNNHQRLES PEDVFSVLDQ VFGLKRVFSR THEFFQKSWI
YYSDRSDLIG LWEDQIYCLD ISNGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQTRNT
RTKILAQGDN QVLCPTYMLS PGLSLEGLLY ELESISRNAL SIYRAIEEGA SKLGLIIKKE
ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCISNDQI VNLANIMSTV STNALTVAQH
SQSLIKPMRD FLLVSVQAVF HYLLFSPILK GRVYKILSAE GESFLLAMSR IIYLDPSLGG
VSGMSLGRFH IRQFSDPVSE GLSFWREIWL SSHESWIHAL CQEAGNPDLG ERTLESFTRL
LEDPTTLNIK GGASPTILLK DAIRKALYDE VDKVKNSEFR EAILLSKTHR DNFILFLKSV
EPLFPRFLSE LFSSSFLGIP ESVIGLIQNS RTIRRQFRKS LSRTLEESFY NSEIHGINRM
TQTPQRVGRV WPCSSERADL LREISWGRKV VGTTVPHPSE MLGLLPKSSI SCSCGATGGG
NPRVSVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
WFITRNSNLA QTLIRNIISL TGPDFPLEEA PVFKRTGSAL HRFKSARYSE GGYSSVCPNL
LSHISVSTDT MSDLTQDGKN YDFMFQPLML YAQTWTSELV QRDTRLRDST FHWHLRCNRC
VRPIDDITLE TSQIFEFPDV SKRISRMVSG AVPHFRKLPD IRLRPGDFES LSGREKSRHI
GSAQGLLYSI LVAIHDSGYN DGTIFPVNIY GKVSPRDYLR GLARGVLIGS SICFLTRMTN
ININRPLELI SGVISYILLR LDNHPSLYVM LREPSLRGEI FSIPQKIPAA YPTTMKEGNR
SILCYLQHVL RYEREVITAS PENDWLWIFS DFRSAKMTYL TLITYQSHLL LRRVERSLSK
GMRANLQQLS SLMRQVLGGH GEDTLESYDD IQRLLKDSLR RTRWVDQEVR HAAKTMTGDY
SPNKKVSRKV GCSEWVCSAQ QIAVSTSANP APVSELDLRA LSKRFQNPLI SGLRVVQWAT
GAHYKLKPIL DDLKVFPSLC LVVGDGSGGI SRAVLNMFPD AKLVFNSLLE VNDLMASGTH
PLPPSAIMSG GDDIVSRVID VDSIWEKPSD LRNLTTWGYF QSVQKQVNMS FDLIICDAEV
HDIASINQIT LLMSDFALSI DGPLYLVFKT YGTMLVNPDY KAIQHLSRAF PSVTGFVTQV
TSSFSSELYL RFSKRGKFFR DAEYLTSSTL REMSLVLFNC SSPKSEMQRA RSLNYQDLVR
GFPEEIISNP YNEMIITLID NDVESFLVHK MVDDLELQRG TLSKVAIIIA IMIVFSNRVF
NISKPLADPL FYPPSDPKIL RHFNICCSTL MYLSTALGDV PSFARLHDLY NRPITYYFRK
QVIRGNIYLS WSWSGDTPVF KRVACNSSLS LSSHWIRLIY KIVKTTRLVG NIEDLSGEVE
RHLHGYNRWI TLKDIRSRSS LLDYSCL
