L_ABLVB
ID L_ABLVB Reviewed; 2128 AA.
AC Q9QSP0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 25-MAY-2022, entry version 88.
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 Australian bat lyssavirus (isolate Bat/AUS/1996) (ABLV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=446561;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=328804; Pteropus conspicillatus (Spectacled flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
OH NCBI_TaxID=446909; Saccolaimus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12367747; DOI=10.1016/s0168-1702(02)00056-4;
RA Gould A.R., Kattenbelt J.A., Gumley S.G., Lunt R.A.;
RT "Characterisation of an Australian bat lyssavirus variant isolated from an
RT insectivorous bat.";
RL Virus Res. 89:1-28(2002).
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; AF081020; AAD47900.2; -; Genomic_RNA.
DR RefSeq; NP_478343.1; NC_003243.1.
DR SMR; Q9QSP0; -.
DR PRIDE; Q9QSP0; -.
DR GeneID; 926729; -.
DR KEGG; vg:926729; -.
DR Proteomes; UP000006934; 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..2128
FT /note="Large structural protein"
FT /id="PRO_0000294415"
FT DOMAIN 612..800
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1675..1872
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..2128
FT /note="Interaction with P protein"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2128 AA; 242984 MW; C7AB91F58AF2B948 CRC64;
MIDPGEVYDD PIDPVEPEPE LKTNNAVIPN ILRNSDYNLN SPLIEHPSRL MLEWLTTGNK
PMRLTLTDNC IRSYKTLKCY FRKVDIGSVK VGGPAAQAMT SLWLHGEHSE SNRSRKCLSD
LTQFYQKSSP IEKLLNYTLG NRGLRIPPEG VLLCLKKVDY DRSFGRYLAN IYSSYLFFHV
IILYMNALDW DEEKTILALW RDLNSVDIKK DQVKFRDSIW GSLIVTKEFV YSQNSNCLFD
RNYTLMLKDL FLSRFNSLLI LLSPPEPRYS DDLISLLCQL YIAGDHVLSM CGNSGYDVIK
MLEPYVINSL VQRAEEFRPL IHSLGDFPLF IREKVGQLEG TFGPSARRFF QVLDQVDNIH
DLVFVYGCYR HWGHPYIDYR KGLLKLYDQV HVKKMIDGAY QECLASDLAK RILRWGFDKY
SKWYLDPKLL APDHPLAPYI KTQTWPPKHI VDLVGNTWHK LPITQIFEIP ESMDPSEILD
DKSHSFTRTK LASWLAENRG GPVPSEKVII TALSKPPVNP REFLKSIDLG GLPDDDLIIG
LKPKERELKI EGRFFALMSW NLRLYFVITE KLLANYILPL FDALTMTDNL NKVFKKLIDR
VTGQGLQDYS RVTYAFHLDY EKWNNHQRLE STKDVFPVLD QVFGLKKVFS RTHEFFQKSW
IYYSDRSDLI GLWEDQIYCL DMSDGPTCWN GQDGGLEGLR QKGWSLVSLL MIDRESQTRN
TRTKDFAQGD NQVLCPTYML SSGLSHEGLL YELESISRNA LSIYRAIEDG ASKLGLIIKK
EETMCSYDFL IYGKTPLFRG NILVPESKRW ARVSCISNDQ IVNLANIMST VSTNALTVAQ
HSQSLIKPMR GFLLMAVQAV FHYLLFSPIL KGRVYKILSA EGDDFLLAMS RIVYLDPSLG
GVSGMSLGRF HIRQFSDPVS EGLSFWKEIW TSSSESWIHS LCQEAGNPDL GDRSLEKFTR
LLEDPTTLNI RGGASPTILL KDAIRKALYD EVDKVENSEF REAILLSRHH RDNFILFLKS
IEPLFPRFLS ELFSSSFLGI PESIIGLIQN SRTIRRQFRR SLSRSLEESF YNSEIHGISR
MTQVPQRIGR VWSCSSERAH LLREISWGRK RVGTTVPHPS EMLALLPKSS ISCPCGLTGS
ENPRVSISVL PSIYQSFFSR GPLKGYLGSS TSMSTQTFHA WEKVTNVHVV KRALSLKESI
NWFISRNSNL AQTLIRNIIS LTGPQFPLEE APVFKRTGSA LHRFKSARYS EGGYSSICPN
LLSHISVSTD TMSDLTHDGR NFDFMFQPLM LYAQTWTSEL VQKDIRLKDS TFHWHLRCPK
CIRSIDDVIL VHPQVFDFPD VSKRISRMVS GAVPSSQILP EVNLLPGHFE SLCGRDKSRH
IGSAQGLLYS ILVATHDPGY NDGTIFPVNI YSKISPKDYL RGLARGILIG SSICLLTRMT
NININRPLEL ISGVITYILL RLDNHPSLYV MLREPSLRSE IFSIPQKIPA AYPTTMKEGN
RSVLCYLQHV LRYEREIITS SPENDWLWIF SDFRSMKMTY LTLITYQSHI FLQRIERSLS
KKMRADLRQL SSLMRQVLGG HGEDTLDSGE DIQRLLRDAI QRTKWVDQEV RHAAKTMTND
HSPSKKTSRK VGCSEWICSA QQVSISTSSN PAPVSEMDVR TLSRKLQNPL ISGLRVVQCA
TGAHYKLKPI LDNLNTYPSF CLVVGDGSGG ISRTVLNMFP DAKLVFNSLL EVSDLMASGT
HPLPPSAIMS GGEDITSRVI DFESIWEKPS DLRNLSTWRY FQSVQSQLNM SYDLIICDAE
VTDIASVNKI TLLMSDFVLS IDGPVDLIFK SYGSMLVDPD YKAIQHLSRA FPQVTGYITQ
LTSSFSSELY LRFSKRGKFF RDAEYLTSST LREMSLVLFN CSSPKSELQR ARSLNYQDLV
RGFPEEIVSN PYNEMIITLI DSEVESFLVH KMVDDLELQR GTLSRMSIII AIVIVYSNRV
FNVSKPLNDP LFYPPSDPKI LRHFNICCST MMYLSTVLGD VPNFARQHEL YNGPITYYFK
RQIIRGSIYL SWSWSDDTSV FKRVSCNSNL SLSSHWIRLI YKIVKTTRLT GSPVDLSKEV
EKHLRGYNRW ITLNDVKSRS SLLDYSCL
