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L_RABVE
ID   L_RABVE                 Reviewed;        2127 AA.
AC   A3F5L9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
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   Rabies virus (strain ERA) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11295;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA   Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA   Cox J., Mueller T.;
RT   "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT   virus vaccine strains.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; EF206707; ABN11295.1; -; Viral_cRNA.
DR   SMR; A3F5L9; -.
DR   Proteomes; UP000008619; 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; 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_0000294420"
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          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1562..2127
FT                   /note="Interaction with P protein"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2127 AA;  243070 MW;  BAA9B514E59B6115 CRC64;
     MLDPGEVYDD PIDPIELEDE PRGTPTVPNI LRNSDYNLNS PLIEDPARLM LEWLKTGNRP
     YRMTLTDNCS RSFRVLKDYF KKVDLGSLKV GGMAAQSMIS LWLYGAHSES NRSRRCITDL
     AHFYSKSSPI EKLLNLTLGN RGLRIPPEGV LSCLERVDYD NAFGRYLANT YSSYLFFHVI
     TLYMNALDWD EEKTILALWK DLTSVDIGKD LVKFKDQIWG LLIVTKDFVY SQSSNCLFDR
     NYTLMLKDLF LSRFNSLMVL LSPPEPRYSD DLISQLCQLY IAGDQVLSMC GNSGYEVIKI
     LEPYVVNSLV QRAEKFRPLI HSLGDFPVFI KDKVSQLEET FGPCARRFFR ALDQFDNIHD
     LVFVYGCYRH WGHPYIDYRK GLSKLYDQVH IKKVIDKSYQ ECLASDLARR ILRWGFDKYS
     KWYLDSRFLA RDHPLTPYIK TQTWPPKHIV DLVGDTWHKL PITQIFEIPE SMDPSEILDD
     KSHSFTRTRL ASWLSENRGG PVPSEKVIIT ALSKPPVNPR EFLRSIDLGG LPDEDLIIGL
     KPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
     TGQGLLDYSR VTYAFHLDYE KWNNHQRLES TEDVFSVLDQ VFGLKRVFSR THEFFQKAWI
     YYSDRSDLIG LREDQIYCLD ASNGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQIRNT
     RTKILAQGDN QVLCPTYMLS PGLSQEGLLY ELERISRNAL SIYRAVEEGA SKLGLIIKKE
     ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCVSNDQI VNLANIMSTV STNALTVAQH
     SQSLIKPMRD FLLMSVQAVF HYLLFSPILK GRVYKILSAE GDSFLLAMSR IIYLDPSLGG
     VSGMSLGRFH IRQFSDPVSE GLSFWREIWL SSHESWIHAL CQEAGNPDLG ERTLESFTRL
     LEDPTTLNIR GGASPTILLK DAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLTSV
     EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRKS LSKTLEESFY NSEIHGISRM
     TQTPQRVGGV WPCSSERADL LREISWGRKV VGTTVPHPSE MLGLLPKSSI SCTCGATGGG
     NPRVSVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
     WFITRDSNLA QALIRNIMSL TGPDFPLEEA PVFKRTGSAL HRFKSARYSE GGYSSVCPNL
     LSHISVSTDT MSDLTQDGKN YDFMFQPLML YAQTWTSELV QRDTRLRDST FHWHLRCNRC
     VRPIDDVTLE TSQIFEFPDV SKRISRMVSG AVPHFQRLPD IRLRPGDFES LSGREKSHHI
     GSAQGLLYSI LVAIHDSGYN DGTIFPVNIY GKVSPRDYLR GLARGVLIGS SICFLTRMTN
     ININRPLELI SGVISYILLR LDNHPSLYIM LREPSLRGEI FSIPQKIPAA YPTTMKEGNR
     SILCYLQHVL RYEREIITAS PENDWLWIFS DFRSAKMTYL TLITYQSHLL LQRVERNLSK
     SMRDNLRQLS SLMRQVLGGH GEDTLESDDN IQRLLKDSLR RTRWVDQEVR HAARTMTGDY
     SPNKKVSRKV GCSEWVCSAQ QVAVSTSANP APVSELDIRA LSKRFQNPLI SGLRVVQWAT
     GAHYKLKPIL DDLNVFPSLC LVVGDGSGGI SRAVLNMFPD AKLVFNSLLE VNDLMASGTH
     PLPPSAIMRG GNDIVSRVID FDSIWEKPSD LRNLATWKYF QSVQKQVNMS YDLIICDAEV
     TDIASINRIT LLMSDFALSI DGPLYLVFKT YGTMLVNPNY KAIQHLSRAF PSVTGFITQV
     TSSFSSELYL RFSKRGKFFR DAEYLTSSTL REMSLVLFNC SSPKSEMQRA RSLNYQDLVR
     GFPEEIISNP YNEMIITLID SDVESFLVHK MVDDLELQRG TLSKVAIIIA IMIVFSNRVF
     NVSKPLTDPL FYPPSDPKIL RHFNICCSTM MYLSTALGDV PSFARLHDLY NRPITYYFRK
     QFIRGNVYLS WSWSNDTSVF KRVACNSGLS LSSHWIRLIY KIVKTTRLVG SIKDLSREVE
     RHLHRYNRWI TLEDIRSRSS LLDYSCL
 
 
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