ID   L_RABVH                 Reviewed;        2127 AA.
AC   Q8B6J5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   07-JUL-2009, entry version 27.
DE   RecName: Full=Large structural protein;
DE            Short=Protein L;
DE   AltName: Full=Transcriptase;
DE   AltName: Full=Replicase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.56;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.-;
GN   Name=L;
OS   Rabies virus (strain HEP-Flury) (RABV).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Rhabdoviridae; Lyssavirus.
OX   NCBI_TaxID=11296;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=22393783; PubMed=12505638; DOI=10.1016/S0166-0934(02)00249-5;
RA   Inoue K., Shoji Y., Kurane I., Iijima T., Sakai T., Morimoto K.;
RT   "An improved method for recovering rabies virus from cloned cDNA.";
RL   J. Virol. Methods 107:229-236(2003).
RN   [2]
RP   INTERACTION WITH PROTEIN P.
RC   STRAIN=CVS;
RX   PubMed=9499045;
RA   Chenik M., Schnell M., Conzelmann K.K., Blondel D.;
RT   "Mapping the interacting domains between the rabies virus polymerase
RT   and phosphoprotein.";
RL   J. Virol. 72:1925-1930(1998).
CC   -!- FUNCTION: Displays RNA-directed RNA polymerase, mRNA guanylyl
CC       transferase, mRNA (guanine-7-N-)-methyltransferase and poly(A)
CC       synthetase activities. The viral mRNA guanylyl transferase
CC       displays a different biochemical reaction than the cellular
CC       enzyme. The template is composed of the viral RNA tightly
CC       encapsidated by the nucleoprotein (N). Functions either as
CC       transcriptase or as replicase. The transcriptase synthesizes
CC       subsequently five subgenomic RNAs, assuring their capping and
CC       polyadenylation by a stuttering mechanism. The replicase mode is
CC       dependent on intracellular N protein concentration. In this mode,
CC       the polymerase replicates the whole viral genome without
CC       recognizing the transcriptional signals (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBUNIT: Interacts with the P protein to form the functional
CC       polymerase (By similarity).
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the rhabdoviruses protein L family.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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DR   EMBL; AB085828; BAC53869.1; -; Genomic_RNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR017234; RNA-dir_RNA_pol_rhabdovir.
DR   InterPro; IPR014023; RNA_pol_cat.
DR   InterPro; IPR001016; RNA_pol_L_viral.
DR   Pfam; PF00946; Paramyx_RNA_pol; 1.
DR   PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Methyltransferase;
KW   mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA replication;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW   Virion.
FT   CHAIN         1   2127       Large structural protein.
FT                                /FTId=PRO_0000294421.
FT   DOMAIN      611    799       RdRp catalytic.
FT   REGION     1562   2127       Interaction with P protein.
SQ   SEQUENCE   2127 AA;  242955 MW;  E9B31C8642375518 CRC64;
     MLDPGEVYDD PIDPIESEAE PRGTPTVPNI LRNSDYNLNS PLIEDSAKLM LEWLKTGNRP
     YRMTLTDNCS RSYKDLKDYF KKVDLGSLKV GGTAAQSMIS LWLYGAHSES NRSRRCITDL
     AHFYSKSSPI EKLLNCTLGN RGLRIPPEGV LSCLERVDYD KAFGRYLANT YSSYLFFHVI
     TLYMNALDWE EEKTILALWK DLTSVDTGKD LVKFKDQIWG LLIVTKDFVY SQSSNCLFDR
     NYTLMLKDLF LSRFNSLMIL LSPPEPRYSD DLISQLCQLY IAGDQVLSLC GNSGYEVIKI
     LEPYVVNSLV QRAEKFRPLI HSLGDFPMFI KDKVNQLEGT FGPSAKRFFR VLDQFDNIHD
     LVFVYGCYRH WGHPYIDYRK GLLKLYDQVH IKKVIDKSYQ ECLASDLARR ILRWGFDKYS
     KWYLDSRFLA RDHPLAPYIK TQTWPPKHIV DLVGDTWHKL PITQIFEIPE SMDPSEILDD
     KSHSFTRTRL ASWLSENRGG PVPSEKVIIT ALSQPPVNPR EFLKSIDLGG LPDDDLIIGL
     RPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
     TGQGLLDYSR VTYAFHLDYE KWNNHQRLES TEDVFSVLDQ VFGLKRVFSR THEFFQKSWI
     YYSDRSDLIG LREDQIYCLD MSNGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQTRNT
     RTKILAQGDN QVLCPTYMLS PGLSQEGLLY ELESISRNAL SIYRAIEEGA SKLGLIIKKE
     ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCISNDQI VNLANIMSTV STNALTVAQH
     SQSLIKPMRD FLLMSVQAVF HYLLFSPILK GRVYKILSAE GESFLLAMSR IIYLDPSLGG
     VSGMSLGRFH IRQFSDPVSE GLSFWREIWL SSHESWIHAL CQEAGNPDLG ERTLESFTRL
     LEDPTTLNIK GGASPTILLK DAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLKSV
     EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRKS LSRTLEESFY NSEIHGINRM
     TQTPQRVGRV WPCSSERADL LREISWGRKV VGTTVPHPSE MLGLLPKSSI SCTCGATGGG
     NPRVSVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RAISLKESIN
     WFINRNSNLA QTLIRNIMSL TGPDFSLEEA PVFKRTGSAL HRFKSARYSE GGYSSVCPNL
     LSHISVSTDT MSDLTQDGKN YDFMFQPLML YAQTWTSELV QRDTRLRDST FHWHLRCNRC
     VRPIEDITLE TSQIFEFPDV SKRISRMVSG AVPHFQKLPD IRLRPGDFES LSGREKSRHI
     GSAQGLLYSI LVAIHDSGYN DGTIFPVNIY GKVSPRDYLR GLARGILIGS SICFLTRMTN
     INIKRPLELI SGVISYILLR LDNHPSLYIM LREPSLRGEI FSIPQKIPAA YPTTMKEGNR
     SILCYLQHVL RYEREVITAS PENDWLWIFS DFRSAKMTYL TLITYQSHLL LQRVERNLSK
     SMRATLQQMG SLMRQVLGGH GEDTLESDDD IQRLLKDSLR RTRWVDQEVR HAARTMSGDY
     SPNKRVSRKA GCSEWVCSAQ QVAVSTSANP APVSELDIRA LSKRFQNPLI SGLRVVQWAT
     GAHYKLKPIL DDLNVFPSLC LVVGDGSGGI SRAVLNMFPD SKLVFNSLLE VNDLMASGTR
     PLPPSAIMSG GDDIISRVID FDSIWEKPSD LRNLATWRYF QSVQKQVNMS YDLIICDAEV
     TDIASINRIT LLMSDFALSI DGPLYLVFKT YGTMLVNPDY KAIQHLSRAF PSVTGFITQV
     TSSFSSELYL RFSKRGKFFR DAEYLTSSTL REMSLVLFNC SSPKSEMQRA RSLNYQDLVR
     GFPEEIISNP YNEMIITLID SDVESFLVHK MVDDLELQRG TLSKVAIIIS IMIVFSNRVF
     NISKPLTDPL FYPPSDPKIL RHFNICCSTM MYLSTALGDV PSFARLHDLY NRPITYYFRK
     QVIRGNIYLS WSWSDDTPVF KRVACNSSLS LSSHWIRLIY KIVKTTRLVG RIEDLSGEVE
     RHLHGYNRWI TLEDIRSRSS LLDYSCL
//