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L_LNYV3
ID   L_LNYV3                 Reviewed;        2068 AA.
AC   Q4W382;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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: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   Lettuce necrotic yellows virus (isolate 318) (LNYV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC   Cytorhabdovirus.
OX   NCBI_TaxID=928304;
OH   NCBI_TaxID=43191; Embergeria.
OH   NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH   NCBI_TaxID=43208; Reichardia tingitana.
OH   NCBI_TaxID=255580; Sonchus hydrophilus.
OH   NCBI_TaxID=50207; Sonchus oleraceus (Common sowthistle).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16313992; DOI=10.1016/j.virusres.2005.10.024;
RA   Dietzgen R.G., Callaghan B., Wetzel T., Dale J.L.;
RT   "Completion of the genome sequence of Lettuce necrotic yellows virus, type
RT   species of the genus Cytorhabdovirus.";
RL   Virus Res. 118:16-22(2006).
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 rhabdoviridae protein L family.
CC       {ECO:0000305}.
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DR   EMBL; AJ746199; CAG34091.1; -; Genomic_RNA.
DR   EMBL; AJ867584; CAI30426.1; -; Genomic_RNA.
DR   RefSeq; YP_425092.1; NC_007642.1.
DR   SMR; Q4W382; -.
DR   GeneID; 3844362; -.
DR   KEGG; vg:3844362; -.
DR   Proteomes; UP000008592; 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; IDA:UniProtKB.
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   Pfam; PF14318; Mononeg_mRNAcap; 1.
DR   Pfam; PF00946; Mononeg_RNA_pol; 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..2068
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000297837"
FT   DOMAIN          564..750
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          1657..1847
FT                   /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ   SEQUENCE   2068 AA;  236583 MW;  45AD5205F9A1B6EE CRC64;
     MDLWNEETTP KKNAYDSLPD YHLQNPLYAI TDQLSMLKRG KRLNYRLTSS YKLMKSQSTD
     IKEGDPILLK EWARNWFSET ELYVVDQTLS DCENRLSLDE TDDLHFDTHL LRESVRMWRC
     EFPHDDWVRM RGMQNLLIVM NAISSRRPPP PRHTCIIPGL SKITVEGGVV LVTSSLLGFQ
     PEGDKETTVF AADWVRAVSD VYTERFLVLS GAILGRCLSD EHYPQVLDLE FIINWGDTVL
     RRKGNKGFKL LKAYEALVLG VVQGKSESDF IDPDRFLRNT LNDIIDDDKD LGAYAVLLIQ
     RLQQIDSAHH LIQLFGLHRI WGHPLVDPAK GMEKMIIIGQ KDIVRETSRP EVMGVHFKKL
     MAQGYREKHG VYPNVKGNGE LETLIKNNHD WKEVGSLDND NHWRLLRFDK TFSIPESFNL
     SMIVADKSVS PTLSELKENI LRKKTVMNQE LRRGVLRWIN HDSIDPREFL EQVNDKKFPD
     DHKIIGLRSK EREMNPTPRM FALMSHLMRV YVVITESMLS EHILPYFPQI TMTDSQLDLT
     KKTYSTVKNQ AAKIRRSGAL YDTKTVCMSL DFEKWNGHMR KESTFHVFEA LGDLFGMENL
     YNETYDIFKD SYFYLADGSY VPSMDAQGNF TPEPPYSFTG HKGGQEGLRQ KGWTIFTVVC
     LDWICRKHNC TYKIMGMGDN QVLQLTMYTY RVDASGKATE RGREDMRRVL FGLFDDLLDV
     FSDLGLPLKP LETWISEDLF VYGKYPVLKG VPLSMDLKKI MRIFPFSNQE TMTIENALNT
     IAGNAQAATQ AAPFLGVSYL VGIFMISLCS HDMLVYHPLI AKGLREVLRE NRTWGLKFKG
     AHQVKTDIKG EMVDETNLRR LMMNVPRILG GYVSFNLYGL MMRGFPDPVS LAYSQLFSWG
     VPTGGSDQRD YMLRWLKPIF MPERSMRLLV EDVSSVNLLA PVTPTAGLRR VVEQYLTDGR
     VIKNAEFRDL MMSRDNELED VISEHLCSGE HLHIRLIHDI MESTIFGYVK SITSKVTKSS
     TIVSLAIGKA KGDPLTRLMS DEENYFRFFM WRSVINPHYD IPACPTDLAK QVRRIGWGKE
     LIGVTVAYPW SFLKKTDCYE SGCLCTCDDG FISLFLPDSP VTPQEWDRSI GKNPPYLGSM
     TKEKVVISTG SKVYSGEPLV RRPINLMRVI GWFVPEESET AKIIMSCVSA VSDVNPLIFK
     GMTEGTSGSE IHRFRDTSLK HGALCSSNYL YSTRYHVSTD TFTRYAKGAQ NYDMLFQANL
     CAIVETTHQY VLKTNQSKEP QRKTHHYKQT CYSCINPLDE SFYDVKSSKL SQLIPSKKTN
     KYLYVPEAKI SMTLEHVPAK SWEFGTLSSD GFDQLSVNLR LQWLTDAVAD NVVIDILNPA
     GEESYTTTSL MDIKEHNRLF YLTIRPRDFY DQLCNRILIL AEWRCMSLSD WKTPTTEAIS
     RAAEAIIGDT PISRWYGVTG FFSWPSSMER YYVYPEIQEP DSIPVTALSA CRSVRNSLLG
     LLGSSRKFRG RNTRIFSEDA KASKLSLKLM VYDWVKKKKK CRACHREIGI MSAHQLSSTL
     PNSIICPKGH YVTQGLKDLD IMRSRVTLDS LRKCCSSDEI PTEPMEKKIT EWAPLTSTTC
     RTLFDSSSMR SELIPYSPTG IESSINVQPI PKSDLYKLIS LPTNAMYKYM EVISRNIEGI
     MNCKTAFVTG NGLGGTSKVL SNMWPGRIIT STLLDTGDAI PQVYPNCDKG SSSYARGTVI
     SDLMVTRVND VNHLLWGEDW KPVFQSYETD LCISDIEING ELNGESRQTM IATVTMAHDW
     KMVIMKDYIY NMREMENRLS ILLPVFKSLE LITCNSRQRV MPEVWWIMKA RRSSGKLLGY
     HRSVIRQIWD GVKEGINTAD WAMESVFSEI NRTIASTADM IAMTIRLKAF FSLPIVGSVL
     PYKGSYTRLL GYLQRGKKPE DISLITSDDG KRLYLSDYEK VRSVLFGLAV GMCSSATERD
     RMLDESEYWA IDWIPSGPHI WLPYLFKGVE RSTLIHVYDY IPMLTLIMKR ERLLFKSSSD
     IIEFKYTNNR DSCCFPITKT AKIKFNIK
 
 
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