L_VSNJO
ID L_VSNJO Reviewed; 2109 AA.
AC P16379; Q8B544;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
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: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 Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan)
OS (VSNJV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11283;
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=2155516; DOI=10.1016/0042-6822(90)90218-g;
RA Barik S., Rud E.W., Luk D., Banerjee A.K., Kang C.Y.;
RT "Nucleotide sequence analysis of the L gene of vesicular stomatitis virus
RT (New Jersey serotype): identification of conserved domains in L proteins of
RT nonsegmented negative-strand RNA viruses.";
RL Virology 175:332-337(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kang C.Y., Kim G.N.;
RT "Cloning and expression of functional L proteins of VSV NJ-Haz and VSV NJ-
RT Ogd.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for RNA synthesis (replicase and transcriptase),
CC cap addition, and cap methylation (By similarity). 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) (By similarity). The viral polymerase binds to the
CC genomic 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. The viral
CC phosphoprotein helps the polymerase to engage the N-RNA template and
CC acts as processivity factor. 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 (By similarity). In the replication
CC mode, the polymerase replicates the whole viral genome without
CC recognizing the gene end transcriptional signals. 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:P03523, ECO:0000250|UniProtKB:P28887}.
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: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:P03523};
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 (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 -!- SUBUNIT: Interacts with the P protein; the association of P and L forms
CC the polymerase complex. {ECO:0000250|UniProtKB:Q98776}.
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 rhabdoviridae protein L family.
CC {ECO:0000305}.
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DR EMBL; M29788; AAA48442.1; -; Genomic_RNA.
DR EMBL; AY074804; AAL73076.1; -; mRNA.
DR PIR; A46309; A46309.
DR SMR; P16379; -.
DR Proteomes; UP000007626; 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; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion; Zinc.
FT CHAIN 1..2109
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000222843"
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:0000250|UniProtKB:P03523"
FT ACT_SITE 1651
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1762
FT /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1795
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1833
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
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_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1667..1676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 102
FT /note="I -> V (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> P (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> T (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..234
FT /note="NFLLMC -> TSFSCV (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="R -> Q (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="E -> Q (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="K -> N (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="D -> E (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="R -> K (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="A -> E (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 931..935
FT /note="GDPPI -> ETPQG (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="L -> F (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="S -> R (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1503
FT /note="C -> Y (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1523
FT /note="A -> R (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1564
FT /note="S -> L (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1610
FT /note="I -> T (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1626
FT /note="K -> R (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1668
FT /note="A -> D (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1840
FT /note="G -> R (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1942
FT /note="T -> H (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1971
FT /note="T -> A (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1976
FT /note="S -> D (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1987
FT /note="T -> H (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
FT CONFLICT 2061
FT /note="P -> T (in Ref. 1; AAA48442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2109 AA; 241613 MW; 478961139980690B CRC64;
MDFDLIEDSA NWEDDESDFF LRDILSQEDQ MSYLNTADYN LNSPLISDDM VYIIKRMNHE
EVPPIWRSKE WDSPLDMLRG CQAQPMSHQE MHNWFGTWIQ NIQHDSAQGF TFLKEVDKES
EMTYDLVSTF LKGWVGKDYP FKSKNKEIDS MALVGPLCQK FLDLHKITLI LNAVSLGETK
ELLATFKGKY RMSCENIPIA RLRLPSLGPV FMCKGWTYIH KERVLMDRNF LLMCKDVIIG
RMQTFLSMIG RSDNKFSPDQ IYTLANVYRI GDKILEQCGN KAYDLIKMIE PICNLKMMEL
ARLHRPKIPK FPHFEEHVKG SVRELTQRSN RIQTLYDLIM SMKDVDLVLV VYGSFRHWGH
PFIDYFEGLE KLHTQVNMEK HIDKEYPQQL ASDLARLVLN KQFSESKKWF VDPSKMSPKH
PFYEHVINKT WPTAAKIQDF GDNWHKLPLI QCFEIPDLID PSVIYSDKSH SMNKKEVIQH
VRSKPNIPIP SKKVLQTMLT NRATNWKAFL KDIDENGLDD DDLIIGLKGK ERELKIAGRF
FSLMSWRLRE YFVITEYLIK TYYVPLFKGL TMADDLTSVI KKMMDSSSGQ GLDDYSSVCL
ANHIDYEKWN NHQRKESNGP IFRVMGQFLG YPSLIERTHE FFEKSLIYYN GRPDLMTIRN
GTLCNSTKHR VCWNGQKGGL EGLRQKGWSI VNLLVIQREA KIRNTAVKVL AQGDNQVICT
QYKTKKTRSE LELRAVLHQM AGNNNKIMEE IKRGTEKLGL IINDDETMQS ADYLNYGKIP
IFRGVIRGLE TKRWSRVTCV TNDQIPTCAN LMSSVSTNAL TVAHFAENPI NAMIQYNYFG
TFARLLLFMH DPAIRQSLYK VQDKIPGLHT RTFKYAMLYL DPSIGGVCGM ALSRFLIRAF
PDPVTESLSF WKFIYEHASE PHLRKMAVMF GDPPIAKFRI EHINKLLEDP TSLNISMGMS
PANLLKSEVK KCLIESRSSI KNEIIKDATI YMHQEEEKLR GFLWSIKPLF PRFLSEFKAG
TFLGVSEGLI NLFQNSRTIR NSFKKRYHKD LDELIIKSEI SSLSHLGSMH YRLGDNQIWS
CSASRADILR YKSWTRKVVG TTVPHPLEMH GPPSKKERPC QLCNSSGLTY ISVHCPKGII
DVFNRRGPLP AYLGSNTSES TSILQPWEKE SKIPIIKRAT RLRDAISWFI PPESPLSTCI
LNNIQALTGE DWSSKQHGFK RTGSALHRFS TSRMSNGGFA SQSPATLTRM IATTDTMRDF
GTKNYDFMFQ ASLLYGQMTT SISRYGTPGS CTDHYHIRCK GCIREIEEVE LNTSLEYKTP
DVSHILEKWR NNTGSWGHQI KQLKPAEGNW ESLSPVEQSY QVARCIGFLY GELTHKKSRQ
ADDSSLFPLS IQLKVRGRGF LRGLLDGLMR SSCCQVIHRR SVSTLKRPAN AVYGGLIYLI
DKLSASSPFL SLVRTGPIRQ ELEQVPHKMS TSYPTNIRDL GSIVRNYFKY QCRPVERGNY
KTCYNQIWLF SDVLSTEFIG PMAISSSLLR LLYRPSLTKK DREELRELAA LSSNLRSGED
WDDSHIKFFS NDLLFCSQEI RHACKFGIKK DNEDITFYPN WGTEYIGNVI DIPVFYRAQN
VKKDIKVPPR IQNPLMSGLR LGQLPTGAHY KMRAIVFRLK IPYHDFLACG DGSGGMTAAL
LRYNRTSRGI FNSLLDLSDT MLRGSSPEPP SALETLGGER VRCVNGDSCW EHPSDLSDEN
TWKYFLHLKK GCGMSINLIT MDMEVQDSVI SYKIESLVRQ YVPVLLESDG CLIYKTYGTY
IATQEDNSLT LIGSLFHSVQ LVQTDLSSSN TSELYLVCRG LKDYVDTPFV DWIELYDNWE
KQYAFRSFKD EFQRAQSLTP ETTLIGIPPQ FVPDPGVNLE TLFQIAGVPT GVAHGITHHI
LQSKDKLISN AIGSMCVISH FTINTIRTTD SMPGPPSDGD VNKMCSALIG TCFWLSWMES
DLNLYKTCLR SIMKSMPVRW FRTLKNEKWS QKWDCKGDAI PKDSRLGDSL ANIGNWIRAW
ELIRNGNKSE PFDSMVAEAL PKSVDKSLSW RKISKSTGIP RLLNSDIDLV DQSILNVQID
IVENQAWQN
