L_CHAV
ID L_CHAV Reviewed; 2092 AA.
AC P13179; Q5K2K8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 Chandipura virus (strain I653514) (CHPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11273;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=7198; Phlebotominae (sandflies).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-11.
RX PubMed=2741347; DOI=10.1016/0042-6822(89)90540-0;
RA Masters P.S., Bhella R.S., Butcher M., Patel B., Ghosh H.P., Banerjee A.K.;
RT "Structure and expression of the glycoprotein gene of Chandipura virus.";
RL Virology 171:285-290(1989).
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; AJ810083; CAH17543.1; -; Genomic_RNA.
DR EMBL; J04350; AAA42917.1; -; Genomic_RNA.
DR SMR; P13179; -.
DR PRIDE; P13179; -.
DR BRENDA; 2.7.7.88; 14215.
DR Proteomes; UP000008448; 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; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2092
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000222839"
FT DOMAIN 588..774
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"
SQ SEQUENCE 2092 AA; 238532 MW; AE9091D6CFF0B206 CRC64;
MDLNPVDDAA ELSEENFFSG KLSKECRIRG LNSVDYNLNS PLVSDDLTYL LDKFKGKPVP
IRWKMKKWDS ILDQLRKHDL EYLRPSDLHQ WFAEWMLYSK HGSKQGEDFL KTVDEEASDT
FEVVRSFIRG WTGGEINFVR KSGKHMGYCA ELCQKFLDLH KLTLLGNAAT DNELLQLSKT
FGDDKIYKKR LIKLPSLGRV IFDSGFFIVL DQRVLMDRNF MLMMKDVIIG RMQTVLSMIS
RCDDKFSSKD IDFLLKVYST GDKIIRKLGN DGYELIKTVE PMCNLRLSDL ARRFRPLIPP
FPHFRRHIES TVDELSAKTP LIRELFSLID TSPNVDSTLV VYGSFRHWGH PFINYFEGLE
KLHKQVTMEK EIDTNYSEAL ASDLARIVLT KEFNEKKQWA VDYHRVPTNH PFKNHIRDNT
WPTAAVIQDF GDHWHELPLI QCFDIPDLID PSIIYSDKSH SMNRSEVLNH VRTKPHTPIP
SKKVLESMID KPATNWLEFL EEIDKNGLSD EDLVIGLKGK ERELKIAGRF FSLMSWKLRE
YFVVTEYLIK THFVPLFHGL TMADDMTAVI KKMLESSSGQ GLTNYESVCI ANHIDYEKWN
NHQRKLSNGP VFKVMGQFLG YPNLIYRTHE FFEKSLIYYN ERPDLMKVKN GILENSTHQR
VCWNGQAGGL EGLRQKGWSI LNLLVIQREA KIRNTAVKVL AQGDNQVICT QYKTKQYRND
IELRQALNQM AANNDVIMKA IESGTNKLGL LINQDETMQS ADYLNYGKVP IFRGVIRGLE
TKRWSRVTCV TNDQLPTCAN LMSSVSTNAL TVAHFDVHPL NAMIQFNFFG NFARLLLIMH
DPAIRQSLNQ LKGPNINVHS YGFKVAMLYL DPSIGGVCGT ALSRFLIRSF PDPVTESLSF
WKLIHHSTSD IRLKNLSEQF GNPKIAVFRE SHIEKLLEDP TSLNISMGMS AANLLKTEIK
KNLLQKKSSI GNQIVKDAVY YIHSEDEKLR TFLWSITPLF PRFLSEFKAG TFMGVASSIV
SLFQNSRTIR NVFRDYMSQT IDDLIVKSEL TSLEHLSNYT DRKGSGGIWG CSAEQADKLR
RMSWKRPVLG TTVPHPLEMH GRGTLKSPLS KCCKESRMDY ISVHIPEGLN KVLDGRGSLP
AYLGSKTSES TSILQPWEKE SKIPIIRRAT RLRDAIHWFV DPDSNLARSI LNNIESLTGE
KWEGALKGYK RTGSALHRFS TSRVSHGGFS SQSPACLTRM MATTDTMRDY AQLNYDFMFQ
ASLLYSQMTS SVILMGTTVS NTIHFHVTCR KCIREITEPM LESPREYRGK DVHLVLAKWK
NSSNGWGETL QLLKPVEGDW DTIPPVEKSY HVGRILGFLY GDLKSQNSSR ADDSSIFPLS
IQMRLRGRGF LRGILDGLVR ASACQVIHRR SVALLSKPAN AIYGGLIYLI DKISASTSFT
TLCRDGPIRE ELSSIPHKIP TSYPTSNSDM GLHIRNYLKF QCKTVELGKY QSDIKDLWLF
SDVMTSNIAG PFALSTKILK CLYKPALSQK DRNNIRKISN FSKMMRSQLS WDPTSSEFIT
SQILVCNEEI RHACKFGIPK LSLKFDDPVW GPEDYGLIWS IPVDYSSQSV PKNLKPCPRI
QNPSISGFRL GQLPTGAHYK LRSILRKKNI HYRDALCGGD GSGGMTAAVL RYNLKARAIF
NSILDFDGST MKGASPDPPS ALETVVNGRT RCVNAESCWE NPSDLSEQRT WDYFKFLKTH
HGLKIDLIVL DMEVRDFAIS ASIEKCVRHN VSSILEEDGV LIYKTYGSTI AAESSNAVVN
IGVLFESVEL IQTEYSSTST SEVYMYCRKI KKFVDAPHPD WISLDYYWSK LLCFRSYKEE
FFRSYEVSRK ESLKGIPNSF IPDPLVNLET LLQIAGVPSG ISHQLAIDIK ESQLTQITAA
MVLCGMIANY TLDVTKKRDS YNPPSDGRLI RMSAALVGIS FWISVKYYDK ELNFELEQIL
SRSFPIRWML SHNYLFWTTK KGFRNAKDVR LSGNMANIGN WIRCMELLHL PPGSLSKDEV
TTTCGKYIRN LKYSVILQQT GIIDLWKSRV ASDDRSLMEV KTEFIESEHW VD
