L_VSIVA
ID L_VSIVA Reviewed; 2109 AA.
AC P03523; Q86125;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 148.
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:0000305};
DE EC=3.6.1.- {ECO:0000269|PubMed:18003731};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE EC=2.7.7.88 {ECO:0000269|PubMed:26602696, ECO:0000269|PubMed:28053102};
DE AltName: Full=PRNTase {ECO:0000305};
DE Includes:
DE RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE EC=2.1.1.375 {ECO:0000269|PubMed:19710136, ECO:0000269|PubMed:201777};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000303|PubMed:19710136};
DE Short=G-N7-MTase {ECO:0000303|PubMed:31354644};
DE AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000303|PubMed:19710136};
DE Short=N1-2'-O-MTase {ECO:0000303|PubMed:31354644};
GN Name=L;
OS Vesicular stomatitis Indiana virus (strain San Juan) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11285;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6086959; DOI=10.1128/jvi.51.2.505-514.1984;
RA Schubert M., Harmison G.G., Meier E.;
RT "Primary structure of the vesicular stomatitis virus polymerase (L) gene:
RT evidence for a high frequency of mutations.";
RL J. Virol. 51:505-514(1984).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=201777; DOI=10.1128/jvi.24.3.786-793.1977;
RA Testa D., Banerjee A.K.;
RT "Two methyltransferase activities in the purified virions of vesicular
RT stomatitis virus.";
RL J. Virol. 24:786-793(1977).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=2999788; DOI=10.1073/pnas.82.23.7984;
RA Schubert M., Harmison G.G., Richardson C.D., Meier E.;
RT "Expression of a cDNA encoding a functional 241-kilodalton vesicular
RT stomatitis virus RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7984-7988(1985).
RN [4]
RP REVIEW.
RX PubMed=12213662; DOI=10.1016/s0167-4781(02)00462-1;
RA Barr J.N., Whelan S.P., Wertz G.W.;
RT "Transcriptional control of the RNA-dependent RNA polymerase of vesicular
RT stomatitis virus.";
RL Biochim. Biophys. Acta 1577:337-353(2002).
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-1651; GLY-1674; PHE-1691; ASP-1762; LYS-1795
RP AND GLU-1833, AND CATALYTIC ACTIVITY.
RX PubMed=16227259; DOI=10.1128/jvi.79.21.13373-13384.2005;
RA Li J., Fontaine-Rodriguez E.C., Whelan S.P.;
RT "Amino acid residues within conserved domain VI of the vesicular stomatitis
RT virus large polymerase protein essential for mRNA cap methyltransferase
RT activity.";
RL J. Virol. 79:13373-13384(2005).
RN [6]
RP FUNCTION.
RX PubMed=16709677; DOI=10.1073/pnas.0509821103;
RA Li J., Wang J.T., Whelan S.P.;
RT "A unique strategy for mRNA cap methylation used by vesicular stomatitis
RT virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8493-8498(2006).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=18003731; DOI=10.1128/jvi.02107-07;
RA Li J., Rahmeh A., Morelli M., Whelan S.P.;
RT "A conserved motif in region v of the large polymerase proteins of
RT nonsegmented negative-sense RNA viruses that is essential for mRNA
RT capping.";
RL J. Virol. 82:775-784(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-1651; ASP-1762;
RP LYS-1795 AND GLU-1833.
RX PubMed=19710136; DOI=10.1128/jvi.01426-09;
RA Rahmeh A.A., Li J., Kranzusch P.J., Whelan S.P.;
RT "Ribose 2'-O methylation of the vesicular stomatitis virus mRNA cap
RT precedes and facilitates subsequent guanine-N-7 methylation by the large
RT polymerase protein.";
RL J. Virol. 83:11043-11050(2009).
RN [9]
RP SUBUNIT.
RX PubMed=21041632; DOI=10.1073/pnas.1013559107;
RA Rahmeh A.A., Schenk A.D., Danek E.I., Kranzusch P.J., Liang B., Walz T.,
RA Whelan S.P.;
RT "Molecular architecture of the vesicular stomatitis virus RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20075-20080(2010).
RN [10]
RP REVIEW.
RX PubMed=21945214; DOI=10.1016/j.virusres.2011.09.012;
RA Ogino T., Banerjee A.K.;
RT "An unconventional pathway of mRNA cap formation by vesiculoviruses.";
RL Virus Res. 162:100-109(2011).
RN [11]
RP FUNCTION.
RX PubMed=22908284; DOI=10.1073/pnas.1209147109;
RA Rahmeh A.A., Morin B., Schenk A.D., Liang B., Heinrich B.S., Brusic V.,
RA Walz T., Whelan S.P.;
RT "Critical phosphoprotein elements that regulate polymerase architecture and
RT function in vesicular stomatitis virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14628-14633(2012).
RN [12]
RP FUNCTION.
RX PubMed=22246179; DOI=10.1038/emboj.2011.483;
RA Morin B., Rahmeh A.A., Whelan S.P.;
RT "Mechanism of RNA synthesis initiation by the vesicular stomatitis virus
RT polymerase.";
RL EMBO J. 31:1320-1329(2012).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=24055706; DOI=10.1016/j.bbrc.2013.09.064;
RA Hodges J., Tang X., Landesman M.B., Ruedas J.B., Ghimire A., Gudheti M.V.,
RA Perrault J., Jorgensen E.M., Gerton J.M., Saffarian S.;
RT "Asymmetric packaging of polymerases within vesicular stomatitis virus.";
RL Biochem. Biophys. Res. Commun. 440:271-276(2013).
RN [14]
RP FUNCTION.
RX PubMed=24526687; DOI=10.1074/jbc.m113.542761;
RA Morin B., Whelan S.P.;
RT "Sensitivity of the polymerase of vesicular stomatitis virus to 2'
RT substitutions in the template and nucleotide triphosphate during initiation
RT and elongation.";
RL J. Biol. Chem. 289:9961-9969(2014).
RN [15]
RP REVIEW.
RX PubMed=23602472; DOI=10.1016/j.coviro.2013.03.008;
RA Morin B., Kranzusch P.J., Rahmeh A.A., Whelan S.P.;
RT "The polymerase of negative-stranded RNA viruses.";
RL Curr. Opin. Virol. 3:103-110(2013).
RN [16]
RP MUTAGENESIS OF LYS-1651; GLY-1670; GLY-1674 AND ASP-1735.
RC STRAIN=NL;
RX PubMed=25056882; DOI=10.1128/jvi.00876-14;
RA Zhang Y., Wei Y., Zhang X., Cai H., Niewiesk S., Li J.;
RT "Rational design of human metapneumovirus live attenuated vaccine
RT candidates by inhibiting viral mRNA cap methyltransferase.";
RL J. Virol. 88:11411-11429(2014).
RN [17]
RP CATALYTIC ACTIVITY.
RX PubMed=26602696; DOI=10.1093/nar/gkv1286;
RA Neubauer J., Ogino M., Green T.J., Ogino T.;
RT "Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented
RT negative strand RNA viral mRNA capping enzyme, domain in the L protein are
RT required for covalent enzyme-pRNA intermediate formation.";
RL Nucleic Acids Res. 44:330-341(2016).
RN [18]
RP ACTIVE SITE, AND CATALYTIC ACTIVITY.
RX PubMed=28053102; DOI=10.1128/jvi.02322-16;
RA Ogino M., Ogino T.;
RT "5'-Phospho-RNA Acceptor Specificity of GDP Polyribonucleotidyltransferase
RT of Vesicular Stomatitis Virus in mRNA Capping.";
RL J. Virol. 91:0-0(2017).
RN [19]
RP REVIEW.
RX PubMed=31354644; DOI=10.3389/fmicb.2019.01490;
RA Ogino T., Green T.J.;
RT "RNA Synthesis and Capping by Non-segmented Negative Strand RNA Viral
RT Polymerases: Lessons From a Prototypic Virus.";
RL Front. Microbiol. 10:1490-1490(2019).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), DOMAIN, AND
RP ZINC-BINDING.
RX PubMed=26144317; DOI=10.1016/j.cell.2015.06.018;
RA Liang B., Li Z., Jenni S., Rahmeh A.A., Morin B.M., Grant T.,
RA Grigorieff N., Harrison S.C., Whelan S.P.;
RT "Structure of the L protein of vesicular stomatitis virus from electron
RT cryomicroscopy.";
RL Cell 162:314-327(2015).
RN [21] {ECO:0007744|PDB:6U1X}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), AND ZINC-BINDING.
RX PubMed=31914397; DOI=10.1016/j.celrep.2019.12.024;
RA Jenni S., Bloyet L.M., Diaz-Avalos R., Liang B., Whelan S.P.J.,
RA Grigorieff N., Harrison S.C.;
RT "Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its
RT Phosphoprotein Cofactor.";
RL Cell Rep. 30:53-60.e5(2020).
CC -!- FUNCTION: Responsible for RNA synthesis (replicase and transcriptase),
CC cap addition, and cap methylation (PubMed:24526687). Performs also the
CC polyadenylation of subgenomic mRNAs by a stuttering mechanism at a
CC slipery stop site present at the end of viral genes (By similarity).
CC The template is composed of the viral RNA tightly encapsidated by the
CC nucleoprotein (N) (Probable). The viral polymerase binds to the genomic
CC RNA at the 3' leader promoter, thereby initiating either genome
CC replication or mRNA transcription. In the transcription mode, the
CC polymerase performs the sequential transcription of all mRNAs using a
CC termination-reinitiation mechanism responding to gene start and gene
CC end signals. Some polymerase disengage from the template at each gene
CC junction, resulting in a decreasing abundance of transcripts from the
CC 3' to the 5' end of the genome (By similarity). The first gene is the
CC most transcribed, and the last the least transcribed (Probable). The
CC viral phosphoprotein helps the polymerase to engage the N-RNA template
CC and acts as processivity factor (PubMed:22908284, PubMed:22246179).
CC Polyribonucleotidyl transferase (PRNTase) adds the cap structure when
CC the nascent RNA chain length has reached few nucleotides
CC (PubMed:19710136). Ribose 2'-O methylation of viral mRNA cap precedes
CC and facilitates subsequent guanine-N-7 methylation, both activities
CC being carried by the viral polymerase (PubMed:19710136,
CC PubMed:16227259, PubMed:16709677). In the replication mode, the
CC polymerase replicates the whole viral genome without recognizing the
CC gene end transcriptional signals (By similarity). The ability of the
CC polymerase to override the gene end signals as it is producing the
CC antigenome is probably due to replicative RNA becoming encapsidated
CC with nucleoprotein as it is synthesized (By similarity).
CC {ECO:0000250|UniProtKB:P28887, ECO:0000269|PubMed:16227259,
CC ECO:0000269|PubMed:16709677, ECO:0000269|PubMed:19710136,
CC ECO:0000269|PubMed:22246179, ECO:0000269|PubMed:22908284,
CC ECO:0000269|PubMed:24526687, ECO:0000305}.
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=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:0000269|PubMed:19710136};
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:0000269|PubMed:18003731, ECO:0000269|PubMed:26602696,
CC ECO:0000269|PubMed:28053102};
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:0000269|PubMed:16227259, ECO:0000269|PubMed:19710136,
CC ECO:0000269|PubMed:201777};
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:0000269|PubMed:16227259, ECO:0000269|PubMed:19710136,
CC ECO:0000269|PubMed:201777};
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:0000269|PubMed:19710136,
CC ECO:0000269|PubMed:201777};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for mRNA (nucleoside-2'-O-)-methyltransferase
CC {ECO:0000269|PubMed:201777};
CC KM=10 uM for mRNA (guanine-N(7)-)-methyltransferase
CC {ECO:0000269|PubMed:201777};
CC -!- SUBUNIT: May form homodimer (PubMed:21041632). Interacts with the P
CC protein; the association of P and L forms the polymerase complex (By
CC similarity). {ECO:0000250|UniProtKB:Q98776,
CC ECO:0000269|PubMed:21041632}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24055706}. Host
CC cytoplasm {ECO:0000269|PubMed:2999788}. Note=L and P are packaged
CC asymmetrically towards the blunt end of the virus.
CC {ECO:0000269|PubMed:24055706}.
CC -!- DOMAIN: Contains an RNA-dependent RNA polymerase (RdRp) domain, a
CC polyribonucleotidyl transferase (PRNTase or capping) domain and a
CC methyltransferase (MTase) domain. {ECO:0000269|PubMed:26144317}.
CC -!- SIMILARITY: Belongs to the rhabdoviridae protein L family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X00939; CAA25453.1; -; Genomic_RNA.
DR EMBL; J02428; AAA48371.1; -; Genomic_RNA.
DR PIR; A04119; ZLVN.
DR RefSeq; NP_041716.1; NC_001560.1.
DR PDB; 5A22; EM; 3.80 A; A=1-2109.
DR PDB; 6U1X; EM; 3.00 A; A=1-2109.
DR PDBsum; 5A22; -.
DR PDBsum; 6U1X; -.
DR SMR; P03523; -.
DR GeneID; 1489835; -.
DR KEGG; vg:1489835; -.
DR BRENDA; 2.1.1.375; 14216.
DR BRENDA; 2.7.7.88; 14216.
DR Proteomes; UP000002327; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Host cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
KW Transferase; Viral RNA replication; Viral transcription; Virion; Zinc.
FT CHAIN 1..2109
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000222844"
FT DOMAIN 598..784
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1640..1837
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT ACT_SITE 1227
FT /note="Nucleophile; for GDP polyribonucleotidyltransferase"
FT /evidence="ECO:0000269|PubMed:28053102"
FT ACT_SITE 1651
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000305|PubMed:16227259"
FT ACT_SITE 1762
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000305|PubMed:16227259"
FT ACT_SITE 1795
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000305|PubMed:16227259"
FT ACT_SITE 1833
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000305|PubMed:16227259"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P28887"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P28887"
FT BINDING 1081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317,
FT ECO:0000269|PubMed:31914397"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317,
FT ECO:0000269|PubMed:31914397"
FT BINDING 1120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317"
FT BINDING 1294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317"
FT BINDING 1296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317"
FT BINDING 1299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317,
FT ECO:0000269|PubMed:31914397"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:26144317,
FT ECO:0000269|PubMed:31914397"
FT BINDING 1667..1676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 228
FT /note="P -> R"
FT VARIANT 467
FT /note="H -> D"
FT VARIANT 548..549
FT /note="FP -> LR"
FT VARIANT 670
FT /note="P -> R"
FT VARIANT 910
FT /note="S -> F"
FT VARIANT 1026
FT /note="P -> A"
FT VARIANT 1348
FT /note="A -> G"
FT VARIANT 1589
FT /note="P -> A"
FT VARIANT 2026
FT /note="I -> T"
FT MUTAGEN 1651
FT /note="K->A: Complete loss of G-N-7 and 2'-O methylation
FT activity."
FT /evidence="ECO:0000269|PubMed:16227259,
FT ECO:0000269|PubMed:19710136, ECO:0000269|PubMed:25056882"
FT MUTAGEN 1670
FT /note="G->A: Complete loss of G-N-7 methylation activity
FT but not 2'-O methylation activity."
FT /evidence="ECO:0000269|PubMed:25056882"
FT MUTAGEN 1674
FT /note="G->A: No effect on G-N-7 and 2'-O methylation
FT activity, but sensitive to the substrate concentration."
FT /evidence="ECO:0000269|PubMed:19710136,
FT ECO:0000269|PubMed:25056882"
FT MUTAGEN 1691
FT /note="F->A: About 95% loss of G-N-7 and 2'-O methylation
FT activity."
FT /evidence="ECO:0000269|PubMed:16227259"
FT MUTAGEN 1735
FT /note="D->A: 70%loss of G-N-7 and methylation activity and
FT 2'-O methylation activity."
FT /evidence="ECO:0000269|PubMed:16227259,
FT ECO:0000269|PubMed:19710136, ECO:0000269|PubMed:25056882"
FT MUTAGEN 1762
FT /note="D->A: Almost complete loss of G-N-7 and 2'-O
FT methylation activity."
FT /evidence="ECO:0000269|PubMed:16227259,
FT ECO:0000269|PubMed:19710136"
FT MUTAGEN 1795
FT /note="K->A: Almost complete loss of G-N-7 and 2'-O
FT methylation activity."
FT /evidence="ECO:0000269|PubMed:16227259,
FT ECO:0000269|PubMed:19710136"
FT MUTAGEN 1833
FT /note="E->A,Q: Almost complete loss of G-N-7 and 2'-O
FT methylation activity."
FT /evidence="ECO:0000269|PubMed:16227259,
FT ECO:0000269|PubMed:19710136"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 107..134
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 148..171
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 228..246
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 353..358
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 384..406
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 474..483
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 494..500
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 506..516
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 546..562
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 576..586
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 595..604
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 607..611
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 615..628
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 632..635
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 638..642
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 660..669
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 685..703
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 707..714
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 716..724
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 730..758
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 768..778
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 790..794
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 795..798
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 810..824
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 831..849
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 852..855
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 862..865
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 871..879
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 892..895
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 903..917
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 921..930
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 940..942
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 943..948
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 955..957
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 961..975
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 976..979
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 983..994
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 997..1005
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1007..1009
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1011..1019
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1024..1030
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1037..1042
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1046..1068
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1069..1071
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1072..1075
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1082..1094
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1106..1109
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1114..1118
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1122..1125
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1130..1135
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1136..1139
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1151..1156
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1166..1168
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1175..1180
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1181..1185
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1186..1188
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1192..1194
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1197..1207
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1226..1228
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1231..1233
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1244..1247
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1251..1254
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1259..1262
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1269..1283
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1284..1286
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1291..1296
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1300..1303
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1327..1329
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1351..1353
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1355..1376
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1380..1382
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1383..1387
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1389..1391
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1397..1416
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1417..1419
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1422..1424
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1428..1443
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1447..1450
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1451..1453
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1454..1456
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1457..1462
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1472..1474
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1477..1492
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1493..1498
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1505..1507
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1511..1513
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1516..1533
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1534..1536
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1539..1556
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1565..1567
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1571..1575
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1580..1582
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1609..1613
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1635..1639
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1644..1646
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1649..1658
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1664..1670
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1672..1674
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1675..1683
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1689..1692
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1711..1715
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1720..1722
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1724..1730
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1736..1738
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1739..1752
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1758..1761
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1768..1779
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1782..1785
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1791..1797
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1798..1803
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1805..1807
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1808..1815
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1816..1824
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1833..1841
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1852..1854
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1856..1859
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1863..1865
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1868..1879
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1883..1886
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1889..1891
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1895..1905
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1910..1922
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1928..1942
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1949..1951
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 1958..1961
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1962..1979
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 1982..1993
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 1999..2003
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 2008..2021
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 2030..2044
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 2054..2062
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 2072..2075
FT /evidence="ECO:0007829|PDB:6U1X"
FT HELIX 2079..2083
FT /evidence="ECO:0007829|PDB:6U1X"
FT STRAND 2106..2109
FT /evidence="ECO:0007829|PDB:6U1X"
SQ SEQUENCE 2109 AA; 240883 MW; 011EC2C0B5967C27 CRC64;
MEVHDFETDE FNDFNEDDYA TREFLNPDER MTYLNHADYN LNSPLISDDI DNLIRKFNSL
PIPSMWDSKN WDGVLEMLTS CQANPISTSQ MHKWMGSWLM SDNHDASQGY SFLHEVDKEA
EITFDVVETF IRGWGNKPIE YIKKERWTDS FKILAYLCQK FLDLHKLTLI LNAVSEVELL
NLARTFKGKV RRSSHGTNIC RIRVPSLGPT FISEGWAYFK KLDILMDPNF LLMVKDVIIG
RMQTVLSMVC RIDNLFSEQD IFSLLNIYRI GDKIVERQGN FSYDLIKMVE PICNLKLMKL
ARESRPLVPQ FPHFENHIKT SVDEGAKIDR GIRFLHDQIM SVKTVDLTLV IYGSFRHWGH
PFIDYYTGLE KLHSQVTMKK DIDVSYAKAL ASDLARIVLF QQFNDHKKWF VNGDLLPHDH
PFKSHVKENT WPTAAQVQDF GDKWHELPLI KCFEIPDLLD PSIIYSHKSH SMNRSEVLKH
VRMNPNTPIP SKKVLQTMLD TKATNWKEFL KEIDEKGLDD DDLIIGLKGK ERELKLAGRF
FSLMSWKFPE YFVITEYLIK THFVPMFKGL TMADDLTAVI KKMLDSSSGQ GLKSYEAICI
ANHIDYEKWN NHQRKLSNGP VFRVMGQFLG YPSLIERTHE FFEKSLIYYN GRPDLMRVHN
NTLINSTSQP VCWQGQEGGL EGLRQKGWTI LNLLVIQREA KIRNTAVKVL AQGDNQVICT
QYKTKKSRNV VELQGALNQM VSNNEKIMTA IKIGTGKLGL LINDDETMQS ADYLNYGKIP
IFRGVIRGLE TKRWSRVTCV TNDQIPTCAN IMSSVSTNAL TVAHFAENPI NAMIQYNYFG
TFARLLLMMH DPALRQSLYE VQDKIPGLHS STFKYAMLYL DPSIGGVSGM SLSRFLIRAF
PDPVTESLSS WRFIHVHARS EHLKEMSAVF GNPEIAKFRI THIDKLVEDP TSLNIAMGMS
PANLLKTEVK KCLIESRQTI RNQVIKDATI YLYHEEDRLR SFLWSINPLF PRFLSEFKSG
TFLGVPDGLI SLFQNSRTIR NSFKKKYHRE LDDLIVRSEV SSLTHLGKLH LRRGSCKMWT
CSATHADTLR YKSWGRTVIG TTVPHPLEML GPQHRKETPC APCNTSGFNY VSVHCPDGIH
DVFSSRGPLP AYLGSKTSES TSILQPWERE SKVPLIKRAT RLRDAISWFV EPDSKLAMTI
LSNIHSLTGE EWTKRQHGFK RTGSALHRFS TSRMSHGGFA SQSTAALTRL MATTDTMRDL
GDQNFDFLFQ ATLLYAQITT TVARDGWITS CTDHYHIACK SCLRPIEEIT LDSSMDYTPP
DVSHVLKTWR NGEGSWGQEI KQIYPLEANW KNLAPAEQSY QVGRCIGFLY GDLAYRKSTH
AEDSSLFPLS IQGRIRGRGF LKGLLDGLMR ASCCQVIHRR SLAHLKRPAN AVYGGLIYLI
DKLSVSPPFL SLTRSGPIRD ELETIPHKIP TSYPTSNRDM GVIVRNYFKY QCRLIEKGKY
RSHYSQLWLF SDVLSIDFIG PFSISTTLLQ ILYKPFLSGK DKNELRELAN LSSLLRSGEG
WEDIHVKFFT KDILLCPEEI RHACKFGIPK DNNKDMSYPP WGRESRGTIT TIPVYYTTTP
YPKMLEMPPR IQNPLLSGIR LGQLPTGAHY KIRSILHGMG IHYRDFLSCG DGSGGMTAAL
LRENVHSRGI FNSLLELSGS VMRGASPEPP SALETLGGDK SRCVNGETCW EYPSDLCDPR
TWDYFLRLKA GLGLQIDLIV MDMEVRDSST SLKIETNVRN YVHRILDEQG VLIYKTYGTY
ICESEKNAVT ILGPMFKTVD LVQTEFSSSQ TSEVYMVCKG LKKLIDEPNP DWSSINESWK
NLYAFQSSEQ EFARAKKVST YFTLTGIPSQ FIPDPFVNIE TMLQIFGVPT GVSHAAALKS
SDRPADLLTI SLFYMAIISY YNINHIRVGP IPPNPPSDGI AQNVGIAITG ISFWLSLMEK
DIPLYQQCLA VIQQSFPIRW EAVSVKGGYK QKWSTRGDGL PKDTRISDSL APIGNWIRSL
ELVRNQVRLN PFNEILFNQL CRTVDNHLKW SNLRRNTGMI EWINRRISKE DRSILMLKSD
LHEENSWRD
