L_ABLVH
ID L_ABLVH Reviewed; 2127 AA.
AC Q8JTG9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Human/AUS/1998) (ABLV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=446562;
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=12083841; DOI=10.1006/viro.2002.1417;
RA Warrilow D., Smith I.L., Harrower B., Smith G.A.;
RT "Sequence analysis of an isolate from a fatal human infection of Australian
RT bat lyssavirus.";
RL Virology 297:109-119(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; AF418014; AAN05310.1; -; Genomic_RNA.
DR SMR; Q8JTG9; -.
DR PRIDE; Q8JTG9; -.
DR Proteomes; UP000006884; 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_0000294414"
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 1562..2127
FT /note="Interaction with P protein"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2127 AA; 242676 MW; E3777CFCDA404F4E CRC64;
MIDPGEVYDD PIDPVEPEPE LKNNTVIPNI LRNSDYNLNS PLIEDSARLM LEWLTTGNRP
GRLTLTDNCI RSYKTLKCYF RKVDVGSLKV GGLAAQAMIS LWLHGEHSES NRSRKCLSDL
TQFYQKSSPI EKLLNYTLGN RGLRIPPEGV LFCLKKVDYD RAFGRYLANI YASYLFFHVI
ILYMNALDWD EEKTILALWK DLSSVDIKKD QVKFRDPIWG SLIVTKDFVY SQNANCLFDR
NYTLMLKDLF LSRFNSLLIL LSPPEPRYSD DLISQLCQLY IAGDNVLSMC GNSGYDVIKM
LEPYVVNSLV QRAEGFRPLI HSLGDFPLFI RDKVGQLEGT FGPSARKFFQ VLDQFDNIHD
LVFVYGCYRH WGHPYIDYRK GLSKLYDQVH IKKVIDGTYQ ECLASDLAKR VLRWGFDKYS
KWYLDPKLLA QDHPLTPYIR TQTWPPKHIV DLVGNTWHRL PITQIFEIPE SMDPSEILDD
KSHSLTRTKL ASWLAENRGG PVPSEKVIIT ALSKPPVNPR EFLKSIDLGG LPDDDLIIGL
KPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
TGQGLQDYSR VTYAFHLDYE KWNNHQRLES TKDVFSVLDQ VFGLKKVFSR THEFFQKSWV
YYSDRSDLIG LWEDQIYCLD MSDGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQTRNT
RTKILAQGDN QVLCPTYMLS SGLSQEGLLY ELESISRNAL SIYRAIEDGA SKLGLIIKKE
ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCISNDQI VNLANIMSTV STNALTVAQH
SQSLIKPMRD FLLMSVQAVF HYLLFSPILK GRVYKILSAD GDDFLLAMSR IIYLDPSLGG
VSGMSLGRFH IRQFSDPVSE GLSFWKEIWS SSSEPWIHSL CQEAGNPDLG DRSLESFTRL
LEDPTTLNIR GGASPTILLK DAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLKSI
EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRRS LSRSLEESFY NSEIHGINRM
TQVPQRIGRV WSCSSERADL LREISWGRKV VGTTVPHPSE MLTLLPKSSI SCVCGPTGSE
NPRVSVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
WFIARDSNLA QTLIKNIISL TGPQFPLEEA PVFKRTGSAL HRFKSARYSE GGYSSICPNL
LSHISVSTDT MSDLTQDGRN FDFMFQPLML YAQTWTSELV QKDIRLKDST FHWHLRCQKC
IRSIDDITLD TSQVFEFPDV SKRISRMVSG AVPQFQKLPE VYLKPGHFDS LCGKDKSRHI
GSAQGLLYSI LVATHDPGYN DGTIFPVNIY SKISPKDYLR GLARGVLIGS SICFLTRMTN
ININRPLELI SGVISYILLR LDNHPSLYVM LRESSLRSEI FSIPQKIPAA YPTTMKEGNR
SVLCYLQHVL RYERDIITSS PENDWLWIFS DFRSTKMTYL TLITYQSHIL LQRIERSLSK
KMRADLRQLS SLMRQVLGGH GEDSLDSGED IQRLLRDALQ RTRWVDQEVR HAAKTMTGDH
SPSKKTSRKA GCSEWICSAQ QVAISTSSNP APVSEMDIRT LSRKLQNPLI SGLRVVQWAT
GAHYKLKPIL DDLNAYPSFC LVVGDGSGGI SRTVLNMFPD AKLVFNSLLE VSDLMASGTH
PLPPSAIMSG GDDIVSRVVD FESIWEKPSD LRNLSTWRYF QSVQSKLNMS YDLIICDAEV
TDIISVNKIT LLMSDFVLSI DGPLDLIFKS YGTMLVNPDY KAIQHLSRAF PKATGYITQL
TSSFSSELYL RFSKRGKFFR DVEYLTSSTL REMSLVLFNC SSPKSELQRA RSLNYQDLIR
GFPEEIVSNP YNEMIITLID SEVESFLVHK MVDDLELQRG TLSKMSIIIA IVIVYSNRVF
NVSKPLSDPV FYPPSDPKIL RHFNICCSTM LYLSTILGDV PNFARLHELY NSPITYYFKK
QIIRGSIYLS WSWSDDTSVF KRVSCNSNLS LSSHWIRLIY KIIKTTRFTG SHVDLSKEVE
KHLKGYNRWI TFNDVRSRSS LLDYSCL
