ID POLG_AEVL2 Reviewed; 2134 AA.
AC Q6WQ42;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=VP4-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP4;
DE AltName: Full=P1A;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.1.15;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=Protein 3B;
DE Short=P3B;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28;
DE AltName: Full=Picornain 3C;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE Short=P3D-POL;
DE EC=2.7.7.48;
OS Avian encephalomyelitis virus (strain L2Z) (AEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Heptrevirinae; Tremovirus; Tremovirus A.
OX NCBI_TaxID=475780;
OH NCBI_TaxID=8835; Anas (ducks).
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9005; Phasianidae (turkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Wei L., Liu J., Yao W.;
RT "Determination of the whole genome of avian encephalomyelitis virus isolate
RT from China.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Capsid proteins VP1, VP2, and VP3 form a closed capsid
CC enclosing the viral positive strand RNA genome. All these proteins
CC contain a beta-sheet structure called beta-barrel jelly roll. Together
CC they form an icosahedral capsid (T=3) composed of 60 copies of each
CC VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1
CC is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at
CC the quasi-sixfold axes (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC immature procapsids. The N-terminal domain of VP0, protein VP4, is
CC needed for the assembly of 12 pentamers into the icosahedral structure.
CC Unlike other picornaviruses, AEV VP4 may not be myristoylated (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Protein 2B and 2BC precursor affect membrane integrity and
CC cause an increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes. It displays RNA-binding,
CC nucleotide binding and NTPase activities (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane
CC anchor. {ECO:0000250}.
CC -!- FUNCTION: Protein 3B is covalently linked to the 5'-end of both the
CC positive-strand and negative-strand genomic RNAs. It acts as a genome-
CC linked replication primer (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein. In addition to its proteolytic
CC activity, it binds to viral RNA, and thus influences viral genome
CC replication. RNA and substrate bind cooperatively to the protease (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC {ECO:0000255|PROSITE-ProRule:PRU00539}.
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 ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum. May associate with membranes through a N-
CC terminal amphipathic helix (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3B]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Interacts with
CC membranes in a complex with viral protein 3AB. Probably localizes to
CC the surface of intracellular membrane vesicles that are induced after
CC virus infection as the site for viral RNA replication. These vesicles
CC are derived from the endoplasmic reticulum (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease in vivo yield a
CC variety of precursors and mature proteins. During virion maturation,
CC non-infectious particles are rendered infectious following cleavage of
CC VP0. This maturation cleavage is followed by a conformational change of
CC the particle (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AY275539; AAN09930.2; -; Genomic_RNA.
DR SMR; Q6WQ42; -.
DR MEROPS; C03.005; -.
DR Proteomes; UP000006886; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23193; ps-ssRNA_Picornaviridae; 1.
DR CDD; cd00205; rhv_like; 2.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR024354; Hepatitis_A_VP1-2A.
DR InterPro; IPR007053; LRAT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF12944; HAV_VP; 1.
DR Pfam; PF04970; LRAT; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51934; LRAT; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage; Helicase;
KW Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
KW Host-virus interaction; Hydrolase; Ion channel; Ion transport; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Transport; Viral attachment to host cell; Viral ion channel;
KW Viral RNA replication; Virion; Virus entry into host cell.
FT CHAIN 1..2134
FT /note="Genome polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000310521"
FT CHAIN 1..242
FT /note="Capsid protein VP0"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310522"
FT CHAIN 1..19
FT /note="Capsid protein VP4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310523"
FT CHAIN 20..242
FT /note="Capsid protein VP2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310524"
FT CHAIN 243..487
FT /note="Capsid protein VP3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310525"
FT CHAIN 488..757
FT /note="Capsid protein VP1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310526"
FT CHAIN 758..806
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310527"
FT CHAIN 807..1021
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310528"
FT CHAIN 1022..1347
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310529"
FT CHAIN 1348..1412
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310530"
FT CHAIN 1413..1433
FT /note="Protein 3B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310531"
FT CHAIN 1434..1648
FT /note="Protease 3C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310532"
FT CHAIN 1649..2134
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310533"
FT TOPO_DOM 1..1377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1378..1392
FT /evidence="ECO:0000255"
FT TOPO_DOM 1393..2134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 781..882
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT DOMAIN 1127..1289
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1431..1643
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1880..2001
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 791
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 863
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 1477
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1515
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1603
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 1153..1160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 19..20
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 242..243
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000255"
FT SITE 487..488
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000255"
FT SITE 757..758
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255"
FT SITE 806..807
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250"
FT SITE 1021..1022
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000255"
FT SITE 1347..1348
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000255"
FT SITE 1412..1413
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000255"
FT SITE 1433..1434
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000255"
FT SITE 1648..1649
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250"
FT MOD_RES 1415
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2134 AA; 238653 MW; C194284F02131E6B CRC64;
MSKLFSTVGR TVDEVLSVLN DEDTESYAGP DRTAVVGGGF LTTVDQSSVS TATMGSLQDV
QYRTAVDIPG SRVTQGERFF LIDQREWNST QSEWQLLGKI DIVKELLDQS YAVDGLLKYH
SYARFGLDVI VQINPTSFQA GGLIAALVPY DQVDIESIVA MTTYCHGKVN CNINYVVRMK
VPYIYSRGCY NLRNSAYSIW MLVIRVWSRL QLGSGTSTQI TITTLARFVD LELHGLSPLV
AQMMRNEFRL SSSSNIVNLA NYDDARAKVS LALGQEEFSR DSSSTGGELV HHFSQWTSIP
CLAFTFTFPG TVGPGTHIWS TTVDPFSCNL RASSTVHPTN LSSIAGMFCF WRGDIVFEFQ
VFCTKYHSGR LMFVYVPGDE NTKISTLTAK QASTGLTAVF DINGVNSTLV FRCPFISDTP
YRVNPTTHKS LWPYATGKLV CYVYNILNAP ASVSPSVSIN VYKSAADLEL YAPVYGVSPT
NTSIFAQGKE DEGGFFSVPE VEQHVVEDKE PQGPLHVTPF GAVKAMEDPQ LARKTPGTFP
ELAPGKPRHT VDHMDLYKFM GRAHYLWGHE FTKTDMQYTF QIPLSPIKEG FVTGTLRWFL
SLFQLYRGSL DITMTFAGKT NVDGIVYFVP EGVAIETERE EQTPLLTLNY KTSVGAIRFN
TGQTTNVQFR IPFYTPLEHI ATHSKNAMDS VLGAITTQIT NYSAQDEYLQ VTYYISFNED
SQFSVPRAVP VVSSFTDTSS KTVMNTYWLD DDELVEESSH SSFDEIEEAQ CSKCKMDLGD
IVICSGEKAK HFGVYVGDGV VHVDPEGNAT NWFMKRKATV KKSKNLDKWC FALSPRIDRT
LICETANLMV GREVEYDIFV KNCETYARGI ASGDYGTKEG EKWKTLLSAV GVAAMTTTMM
AMRHQLLDTS LTKLPQKVGE VTNEVRKILE DTSAGVREFK EKVSSILRKT WPGKTSIKIM
KWTFRIVKMC VGVGLCYAHG WDSKPVTAVV TMFSMDFLDL VIDGIEIGRM IIHELTTPKA
QGLSEINQVL SIAKNAKDVI KMLIEIFCKV IERITGEHGK KIQWAQDKKE EIMNVLERAE
KWITTSDDHS EGIECLKLVR SIQSVIRGEE SLKELAGELR AVGTHVLNKL GRLDKPNAPI
LVRAEPTVLY LYGNRGGGKS LASMAIAVKL CKELGISHVE GIYTKPIMSD FWDGYAGQPV
VIMDDLGQST SDEDWTNFCQ LVSSCPLRLN MANLEKKGTQ FNSPFIIASS NLSHPCPKTV
YCTDAIARRL HIKVKVSPKE EFSTHAMLDV AKAKKAGAYC NLDCLDFQKI SDLASTPVSV
QDIVLALLHT NVDKQTVMGN IIQYWAQSNP REVFDTMAEG KNSGKYLWLF EKIKTSKWYI
LGCVGAALSV SVLGVFAYHM IKNHFRDQQH DQSAYSAAIK PLRVVRLEQS DAQSVVDISN
VVHGNLVRVG VGPNEARIHW LNNGWGVYNT YILMPYHGIK DADVDDDLYI ERAGTIYSTN
MKMVQVLFLE SREGDLVLIN VPRLPKFRDI RNHFSTEENI RRAEGMPGTL CTLDHERFTL
VTESDLKMVE AATYVCEDDK GVRTDISVGR SWKAKACTVA GMCGGALVTS NNKMQNAIVG
IHVAGGAPAI SRVITKEMIE EMLKTRAQCS RIWKTEFVEK KISVGSKTKY HKSPLYDFCP
QKVIKCPTKL FYQGEIDVMQ VMLAKYSSPI VSEPLGYATV VEAYTNRMVS FFSEPRQLTY
DECINGIEGL DAIDLKTSAG FPYNTLSLKK SDLIINGKKA QRLQQDVEKM EEDLHMNRSI
QVVFTTCAKD ELRPLSKGML GKTRAIKACP VSFTILFRKY LGYALAQIQS HPGFHTGIAV
GVDPDQDWHC MWYSIVTQCD LVVGLDFSNY DASLSPFMIY HAGRVLGQIC GLDPRLVDRI
MEPIVNSVHQ LGSMRYYVDG SMPSGTPATS VLNSIINVVN ISHVLCALEK ISVFEVFKLS
KILTYGDDVL FCIKKESLDQ KSFPLSSFVQ GLKELGMSPT GADKMEVKVT PVHKMSFLKR
TFYVDEWSIC HPRISEETVY SMLAWKSDNA SMKHVIETSI WFMFHHGPRK YVIFCTCLRG
VLCRVGIGLY IPTYKELEVR YDRLVKDRVI DDSF
//
