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L_SENDO
ID   L_SENDO                 Reviewed;        2228 AA.
AC   O55528; O55530;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
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   Sendai virus (strain Ohita) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=302272;
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate M1, and Isolate MVC11;
RX   PubMed=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA   Itoh M., Isegawa Y., Hotta H., Homma M.;
RT   "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT   mutations from a highly virulent field strain through adaptation to LLC-MK2
RT   cells.";
RL   J. Gen. Virol. 78:3207-3215(1997).
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: Homooligomer. Interacts with the P and C proteins. The L
CC       protein complexes with P protein to form the functional polymerase. C
CC       protein binding to L has an inhibitory effect (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal part (about 1-400) seems to be involved in
CC       binding to the P protein. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Least abundant structural protein (approximately 50
CC       copies per virion). Unstable in the absence of P protein (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxovirus L protein family.
CC       {ECO:0000305}.
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DR   EMBL; AB005795; BAA24392.1; -; Genomic_RNA.
DR   EMBL; AB005796; BAA24401.1; -; Genomic_RNA.
DR   RefSeq; NP_056879.1; NC_001552.1.
DR   SMR; O55528; -.
DR   PRIDE; O55528; -.
DR   GeneID; 1489777; -.
DR   KEGG; vg:1489777; -.
DR   Proteomes; UP000006563; Genome.
DR   Proteomes; UP000007311; 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; IPR024352; L_methyltrans_paramyxo.
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; IPR016269; RNA-dir_pol_paramyxovirus.
DR   Pfam; PF12803; G-7-MTase; 1.
DR   Pfam; PF14318; Mononeg_mRNAcap; 1.
DR   Pfam; PF00946; Mononeg_RNA_pol; 1.
DR   PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 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..2228
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000142739"
FT   DOMAIN          656..840
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          1771..1978
FT                   /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT   REGION          1..174
FT                   /note="Oligomerization domain"
FT                   /evidence="ECO:0000250"
FT   REGION          607..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1756..2228
FT                   /note="Involved in mRNA cap methylation"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        613..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1801..1810
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VARIANT         2050
FT                   /note="E -> A (in avirulent isolate MVC11)"
SQ   SEQUENCE   2228 AA;  253061 MW;  9BDAC6F266B13B1F CRC64;
     MDGQESTQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYILKDDSII NITKHKIRNG
     GLSLRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL
     TKELSNGFQD LWLNIFKQLG NIEGREGYDP LQDISTIPEI TERYSRNKWY RPFLTWFSIK
     YDMRWMQKTR PGGPLDTSNS HNLLECKSYT LVTYGDLVMI LNKSTLTGYI LTPELVLMYC
     DVVEGRWNMS AAGQLDKRST GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ
     LSDPVIPLRG AFMRHVLTEL QTVLTSKDVY TDPEADAIVE SLLAIFHGTS IDEKAEIFSF
     FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLHECHAVF CTIIINGYRE RHGGQWPPCD
     FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR
     KEAWDSVYPD SNLYYKVPES EETRRLIEVF INDENFNPED IIDYVESGDW LKDEKFNISY
     SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF SENGMVKGEI DLLKRLTTLS
     VSGVPRTDSV YNNPRSSEKR NESMKKRNSK GYWDEKKRSR HEFKATDSST DGYETLSCFL
     TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPVL EKCTIYVGDP YCPVADRMHR
     QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT
     SRVPVAQTYK QKKNHVYEEI TRYFGALRHV MFDIGHELKL NETIISSKMF VYSKRIYYDG
     KILPQCLKAL TRCVFWSETL VDENRSACSN ISTSIAKAIE NGYSPILGYC IALYKTCQQV
     CISLGMTINP TISPTVRDQY FKGKNWLRCA VLIPANVGGF NYMSTSRCFV RNIGDPAVAA
     LADLKRFIRA DLLDKQVLYR VMNQEPGDSS FLDWASDPYS CNLPHSQSIT TIIKNITARS
     VLQESPNPLL SGLFTETSGE EDLNLASFLM DRKVILPRVA HEILSNSLTG VREAIAGMLD
     TTKSLVRASV KRGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL
     RQKMWIHLTY GRPIHGLETP DPLELLRGTF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL
     DTLTNGSPAI RIPYFGSATD ERSEAQLGYV RNLSKPAKAA IRIAMVYTWA YGTDEISWME
     AALIAQTRAN LSLENLKLLT PVSTSTNLSH RLKDTATQMK FSSATLVRAS RFITISNDNM
     ALKEAGESKD TNLVYQQIML TGLSLFEFNM RYKKGSLEKP LILHLHLNNG CCIMESPQEA
     NIPPRSTLDL EITQENNKLI YDPDPLRDVD LELFSKVRDV VHTVDMTYWS DDEVIRATSI
     CTAMTIADTM SQLDRDNLKE MIALVNDDDV NSLITEFMVI DVPLFCSTFG GILVNQFAYS
     LYGLNIRGRE EIWGHVVRIL KDTSHAVLKV LSNALSHPKI FKRFWNAGVV EPVYGPNLSN
     QDKTLLALSV CEYSVDLFMH DWQGGVPLEV FICDNDPDVA DMRRSSFLAR HLAYLCSLAE
     ISRDGPRLES MNSLERLETL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK
     VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR
     GYEEITRGEV GRSGVGLTLP FDGRYLSHQL RLFGVNSTSC LKALELTYLL SPLVDKDKDR
     LFLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL
     GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNNSIGLVHC DMEGGDHKDD QVVLHEHYSV
     IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLVVLKTSNP ASTEMYLLSR
     HPKSDIIEDS KTVLASLHPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY
     HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMTAFNRVL KDTIFEWARI TESDKRLKLT
     GKYDLYPVRD SGKLKTISRR LVLSWVSLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI
     RNLRVITKTI LDRFENTIHS ITYRFLTKEV KILMKILGAV KMFGARQNEY TTVVDDGSLD
     DIEPYDSL
 
 
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