ID   L_VSIVS                 Reviewed;        2109 AA.
AC   Q8B0H5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 32.
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   Vesicular stomatitis Indiana virus (strain 85CLB South America)
OS   (VSIV).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Rhabdoviridae; Dimarhabdovirus supergroup; Vesiculovirus.
OX   NCBI_TaxID=434490;
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=7190; Simuliidae (black flies).
OH   NCBI_TaxID=7370; Musca domestica (House fly).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9793; Equus asinus (Donkey).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=58271; Culicoides.
OH   NCBI_TaxID=252607; Lutzomyia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=22222605; PubMed=12237430;
RA   Rodriguez L.L., Pauszek S.J., Bunch T.A., Schumann K.R.;
RT   "Full-length genome analysis of natural isolates of vesicular
RT   stomatitis virus (Indiana 1 serotype) from North, Central and South
RT   America.";
RL   J. Gen. Virol. 83:2475-2483(2002).
CC   -!- FUNCTION: Displays RNA-directed RNA polymerase, mRNA guanylyl
CC       transferase, mRNA (guanine-N(7)-)-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 rhabdoviridae protein L family.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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DR   EMBL; AF473865; AAN16989.1; -; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN         1   2109       Large structural protein.
FT                                /FTId=PRO_0000287262.
FT   DOMAIN      598    784       RdRp catalytic.
SQ   SEQUENCE   2109 AA;  240642 MW;  C67CEB691F80CBE7 CRC64;
     MEVHDFETEE SNDFNEDDYA TREFLNPDER MTYLNHADYN LNSPLISDDI DNLIRKFNSL
     PIPSMWDSKK WDGVLEMLTA CQANPIPTSQ MHKWMGSWLM SDNHDASQGY SFLHEVDKEA
     EITFDVVETF IRGWGNKQIE YIKKEKWTDS FKILAYLCQK FLDLHKLTLI LNAVSEVELL
     NLARTFKGKV RKSSHGTNIC RLRVPSLGPT FISEGWAYFK KLDILMDRNF LLMVKDVIIG
     RMQTVLSMVC RIDNLFSEQD IFSLLNIYRI GDKIVERQGN FSYDLIKMVE PICNLKLMKL
     ARESRPLVPQ FPHFENHIKT SVDEGAKIDR GIKFLHDQIM SVKTVDLTLV IYGSFRHWGH
     PFIDYYAGLE KLHSQVTMKK DIDVSYAKAL ASDLARIVLF QQFNDHKKWF VNGDLLPHDH
     PFKSHVKENT WPTAAQVQDF GDKWHELPLI KCFEIPDLLD PSIIYSDKSH SMNRSEVLKH
     VRTNPNTPIP SKKVLQTMLD TKATNWKEFL KEIDEKGLDD DDLIIGLKGK ERELKLAGRF
     FSLMSWKLRE YFVITEYLIK THFVPMFKGL TMADDLTAVI KKMLDSSSGQ GLKSYEAICI
     ANHIDYEKWN NHQRKLSNGP VFRVMGQFLG YPSLIERTHE FFEKSLIYYN GRPDLMRVHN
     NTLVNSTSQR VCWQGQEGGL EGLRQKGWSI LNLLVIQREA KIRNTAVKVL AQGDNQVICT
     QYKTKKSRNV VELQGALNQM VSNNEKIMTA IKIGTGKLGL LINDDETMQS ADYLNYGKIP
     IFRGVIRGLE TKRWSRVTCV TNDQIPTCAN IMSSVSTNAL TVAHFAENPI NAMIQYNYFG
     TFARLLLMMH DPALRQSLYE VQDKIPGLHS STFKYAMLYL DPSIGGVSGM SLSRFLIRAF
     PDPVTESLSF WRFIHVHARS EHLKEMSAVF GNPEIAKFRI THIDKLVEDP TSLNIAMGMS
     PANLLKTEVK KCLIESRQTI KNQVIKDATI YLYHEEDRLR SFLWSINPLF PRFLSEFKSG
     TFLGVADGLI SLFQNSRTIR NSFKKKYHRE LDDLIVRSEV SSLTHLGKLH LRRGSCKMWT
     CSATHADTLR YKSWGRTVIG TTVPHPLEML GPQHRKETPC APCNTSGFNY VSVHCPDGIH
     DVFSSRGPLP AYLGSKTSES TSILQPWERE SKVPLIKRAT RLRDAISWFV EPDSKLAITI
     LSNIHSLTGE EWTKRQHGFK RTGSALHRFS TSRMSHGGFA SQSTAALTRL MATTDTMSDL
     GDQNFDFLFQ ATLLYAQITT TVARDGWTTS CTDHYHITCK SCLRPIEEIT LDSNMDYTPP
     DVSHVLKTWR NGEGSWGQEI KQIYPLEGNW KNLAPAEQSY QVGRCIGFLY GDLAYRKSNH
     AEDSSLFPLS IQSRIRGRGF LKGLLDGLMR ASCCQVIHRR SLAHLKRPAN AVYGGLIYLI
     DKLSVSPPFL SLTRSGPIRD ELETIPHKIP TSYPTSNRDM GVIVRNYFKY QCRLIEKGKY
     RSHYSQLWLF SDVLSIDFLG PFSISTTLLQ ILYKPSLSGK DKNELRELAN LSSLLRSGEG
     WEDIHVKFFT KDILLCPEEI RHACKFGIAK DNNKDMSYPP WGRESRGTIT TIPVYYTTTP
     YPKMLEVPPR IQNPLLSGIR LGQLPTGAHY KIRSILHGMG IHYRDFLSCG DGSGGMTAAL
     LRENVHSRGI FNSLLELSGS VMRGASPEPP SALETLGGDR SRCVNGETCW EHPSDLCDPR
     TWDYFLRLKA GLGLQIDLIV MDMEVRDSST SLKIESNVRN YVHRILDEQG VLIYKTYGTY
     ICESEKNAVT ILGPLFKTVD LVQTEFSSSQ TSELYMVCKG LKKLIDEPNP DWSSINESWK
     NLYAFQSSEK EFARAKKVST YFTLTGIPTQ FIPDPFVNLE TMLQIFGVPT GVSHAAALKS
     SDRPADLLTI SLFYMAIISY YNINHIRVGP IPPNPPSDGI AQNVGIAITG ISFWLSLMEK
     DIPLYQQCLA VIRQSFPIRW EAVSVKGGYK QKWSTRGDGL PKDTRISDSL APIGNWIRSL
     ELVRNQVHLN PFNEILFNQL CRTVDNHLKW SNLRKNTGII EWINRRISKE DRSILILKSD
     LHEENSWRD
//