ID M9VZ69_CHIKV Unreviewed; 2470 AA. AC M9VZ69; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 25-MAY-2022, entry version 48. DE RecName: Full=Polyprotein P1234 {ECO:0000256|ARBA:ARBA00015868}; DE AltName: Full=Non-structural polyprotein {ECO:0000256|ARBA:ARBA00029613}; OS Chikungunya virus (CHIKV). OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes; OC Martellivirales; Togaviridae; Alphavirus. OX NCBI_TaxID=37124 {ECO:0000313|EMBL:AGJ84081.1, ECO:0000313|Proteomes:UP000098741}; OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OH NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta). OH NCBI_TaxID=299627; Aedes furcifer (Mosquito). OH NCBI_TaxID=188700; Aedes polynesiensis (Polynesian tiger mosquito). OH NCBI_TaxID=9533; Cercopithecus. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9539; Macaca (macaques). OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). OH NCBI_TaxID=9554; Papio (baboons). OH NCBI_TaxID=9573; Presbytis. RN [1] {ECO:0000313|EMBL:AGJ84081.1, ECO:0000313|Proteomes:UP000098741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHIKV-JC2012 {ECO:0000313|EMBL:AGJ84081.1}; RA Zhou D., Sun D., Zheng J., Ni M., Qiu J., Wan Y., Yang T., Long Z., Zai M.; RT "Sequence analysis of Chikungunya virus strain CHIKV-JC2012."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inactive precursor of the viral replicase, which is activated CC by cleavages carried out by the viral protease nsP2. CC {ECO:0000256|ARBA:ARBA00002589}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose CC + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA- CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967, CC ChEBI:CHEBI:138102; Evidence={ECO:0000256|ARBA:ARBA00000002}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429; CC Evidence={ECO:0000256|ARBA:ARBA00000002}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose CC + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA- CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967, CC ChEBI:CHEBI:142540; Evidence={ECO:0000256|ARBA:ARBA00000461}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249; CC Evidence={ECO:0000256|ARBA:ARBA00000461}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP-D-ribose 1''-phosphate + H2O = ADP-D-ribose + phosphate; CC Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84; CC Evidence={ECO:0000256|ARBA:ARBA00001508}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25030; CC Evidence={ECO:0000256|ARBA:ARBA00001508}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000256|ARBA:ARBA00001556}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, CC ChEBI:CHEBI:173115; EC=2.7.7.19; CC Evidence={ECO:0000256|ARBA:ARBA00024620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl- CC L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; CC Evidence={ECO:0000256|ARBA:ARBA00023718}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[nsP1 protein]-L-histidine + N(7)-methyl-GTP = [nsP1 protein]- CC N(tele)-(N(7)-methylguanosine 5'-phospho)-L-histidine + diphosphate; CC Xref=Rhea:RHEA:54792, Rhea:RHEA-COMP:13994, Rhea:RHEA-COMP:13995, CC ChEBI:CHEBI:29979, ChEBI:CHEBI:33019, ChEBI:CHEBI:87133, CC ChEBI:CHEBI:138334; Evidence={ECO:0000256|ARBA:ARBA00023734}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54793; CC Evidence={ECO:0000256|ARBA:ARBA00023734}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[nsP1 protein]-N(tele)-(N(7)-methylguanosine 5'-phospho)-L- CC histidine + a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) CC = [nsP1 protein]-L-histidine + a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-(purine-ribonucleoside) in mRNA; CC Xref=Rhea:RHEA:54800, Rhea:RHEA-COMP:12925, Rhea:RHEA-COMP:13929, CC Rhea:RHEA-COMP:13994, Rhea:RHEA-COMP:13995, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29979, ChEBI:CHEBI:133968, ChEBI:CHEBI:138276, CC ChEBI:CHEBI:138334; Evidence={ECO:0000256|ARBA:ARBA00023699}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a CC 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate; CC Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33; CC Evidence={ECO:0000256|ARBA:ARBA00023738}; 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 Evidence={ECO:0000256|ARBA:ARBA00001491}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004342}. Cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004594}; Lipid-anchor CC {ECO:0000256|ARBA:ARBA00004594}. Cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004284}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004112}; Lipid-anchor CC {ECO:0000256|ARBA:ARBA00004112}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004112}. Host cell projection, host filopodium CC {ECO:0000256|ARBA:ARBA00004490}. Host cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004615}; Lipid-anchor CC {ECO:0000256|ARBA:ARBA00004615}. Host cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004350}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004350}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Membrane CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004423}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; KC488650; AGJ84081.1; -; Genomic_RNA. DR Proteomes; UP000098741; Genome. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044176; C:host cell filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0008174; F:mRNA methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW. DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR CDD; cd21557; Macro_X_Nsp3-like; 1. DR Gene3D; 3.40.220.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR Gene3D; 3.90.70.110; -; 1. DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom. DR InterPro; IPR002588; Alphavirus-like_MT_dom. DR InterPro; IPR002620; Alphavirus_nsp2pro. DR InterPro; IPR044936; Alphavirus_nsp2pro_sf. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR002589; Macro_dom. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR044371; Macro_X_NSP3-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol. DR Pfam; PF01661; Macro; 1. DR Pfam; PF01707; Peptidase_C9; 1. DR Pfam; PF00978; RdRP_2; 1. DR Pfam; PF01443; Viral_helicase1; 1. DR Pfam; PF01660; Vmethyltransf; 1. DR SMART; SM00506; A1pp; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF52949; SSF52949; 1. DR SUPFAM; SSF56672; SSF56672; 1. DR PROSITE; PS51743; ALPHAVIRUS_MT; 1. DR PROSITE; PS51154; MACRO; 1. DR PROSITE; PS51520; NSP2PRO; 1. DR PROSITE; PS51657; PSRV_HELICASE; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|ARBA:ARBA00023247}; KW Eukaryotic host transcription shutoff by virus KW {ECO:0000256|ARBA:ARBA00022731}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host cell projection {ECO:0000256|ARBA:ARBA00022791}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488}; KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995}; KW Host membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host RNA polymerase II by virus KW {ECO:0000256|ARBA:ARBA00023103}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00022511}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW mRNA capping {ECO:0000256|ARBA:ARBA00023042}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU00853}; KW RNA suppression of termination {ECO:0000256|ARBA:ARBA00023151}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 28..259 FT /note="Alphavirus-like MT" FT /evidence="ECO:0000259|PROSITE:PS51743" FT DOMAIN 690..991 FT /note="(+)RNA virus helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51657" FT DOMAIN 1004..1327 FT /note="Peptidase C9" FT /evidence="ECO:0000259|PROSITE:PS51520" FT DOMAIN 1324..1493 FT /note="Macro" FT /evidence="ECO:0000259|PROSITE:PS51154" FT DOMAIN 2224..2339 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 485..505 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1013 FT /note="For cysteine protease nsP2 activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00853" FT ACT_SITE 1083 FT /note="For cysteine protease nsP2 activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00853" SQ SEQUENCE 2470 AA; 275428 MW; 8F90B3C1ECC25235 CRC64; MDSVYVDIDA DSAFLKALQR AYPMFEVEPR QVTSNDHANA RAFSHLAIKL IEQEIDPDST ILDIGSAPAR RMMSDRKYHC VCPMRSAEDP ERLANYARKL ASAAGKVLDR NISGKIGDLQ EVMAVPDTET PTFCLHTDVS CRQRADVAIY QDVYAVHAPT SLYHQAIKGV RVAYWVGFDT TPFMYNAMAG AYPSYSTNWA DEQVLKAKNI GLCSTDLTEG RRGKLSIMRG KKLKPCDRVL FSVGSTLYPE SRMLLKSWHL PSVFHLKGKL SFTCRCDTVV SCEGYVVKRI TMSPGLYGKT TGYAVTHHAD GFLMCKTTDT VDGERVSFPV CTYVPATICD QMTGILATEV TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FSKWAKECRK DMEDEKLLGV RERTLTCCCL WAFKKQKTHT VYKRPDTQSI QKVQAEFDSF VVPGLWSSGL SIPLRTRIKW LLRKVPKADL IPYSGNAQEA QDAEKEAEEE REAELTHEAL PPLQAAQEDV QVEIDVEQLE DRAGAGIIET PRGAIKVTAQ LTDHVVGEYL VLSPQTVLRS QKLSLIHALA EQVKTCTHSG RVGRYAVEAY DGRVLVPSGY AISPEDFQSL SESATMVYNE REFVNRKLHH IAMHGPALNT DEESYELVRA ERTEHEYVYD VDQRRCCKKE EAAGLVLVGD LTNPPYHEFA YEGLKIRPAC PYKIAVIGVF GVPGSGKSAI IKNLVTRQDL VTSGKKENCQ EISTDVMRQR GLEISARTVD SLLLNGCNRP VDVLYVDEAF ACHSGTLLAL IALVRPRLKV VLCGDPKQCG FFNMMQMKVN YNHNICTQVY HKSISRRCTL PVTAIVSSLH YEGKMRTTNE YNMPIVVDTT GSTKPDPGDL VLTCFRGWVK QLQIDYRGHE VMTAAASQGL TRKGVYAVRQ KVNENPLYAS TSEHVNVLLT RTEGKLVWKT LSGDPWIKTL QNPPKGNFKA TIKEWEVEHA SIMAGICSHQ VTFDTFQNKA NVCWAKSLVP ILETAGIKLN DRQWSQIIQA FKEDKAYSPE VALNEICTRM YGVDLDSGLF SKPLVSVYYA DNHWDNRPGG KMFGFNPEAA SILERKYPFT KGKWNINKQI CVTTRRIEDF NPTTNIIPAN RRLPHSLVAE HRPVKGERME WLVNKINGHH VLLVSGYNLA LPTKRVTWVA PLGVRGADYT YNLEMGLPAT LGRYDLVVIN IHTPFRIHHY QQCVDHAMKL QMLGGDSLRL LKPGGSLLIR AYGYADRTSE RVICVLGRKF RSSRALKPPC ITSNTEMFFL FSSFDNGRRN FTTHVMNNQL NAAFVGQATR AGCAPSYRVK RMDIAKNDEE CVVNAANPRG LPGDGVCKAV YKKWPESFKN SATPVGTAKT VMCGTYPVIH AVGPNFSNYT ESEGDRELAA AYREVAKEVT RLGVNSVAIP LLSTGVYSGG KDRLTQSLNH LFTAMDSTDA DVVIYCRDKE WEKKISEAIQ MRTQVELLDE HISIDCDVIR VHPDSSLAGR KGYSTTEGAL YSYLEGTRFH QTAVDVAEIH TMWPKQIEAN EQVCLYALGE SIESIRQKCP VDDADASSPP KTVPCLCRYA MTPERVTRLR MNHVTNIIVC SSFPLPKYKI EGVQKVKCSK VMLFDHNVPS RVSPREYRSS QESVREVSMT TSLTHSQFDL SADGETLPVP SDLDADAPAL EPALDDGAIH TTGNLAAVSD WVMSTVPVAP PRRRRGRNLT VICDEREGNI TPMASVRFFR AEQCPTVQET AETRDTAISF RAPPSITVEL SHPPISFGAP SETFPITFGD FNDGEIESLS SELLTFGDFL PGEVDDLTDS DWSTCSDTDD ELXLDRAGGY IFSSDTGPGH LQQKSVRQSV LPVNTLEEVH EEKCYPPKLD ELKEQLLLKK LQESASTANR SRYQSRKVEN MKATIIQRLK RGCKLYLMAE TPKVPTYRTV YPAPVYSPPI NVRLSNPESA VAACNEFLAR NYPTVSSYQI TDEYDAYLDM VDGSESCLDR ATFNPSKLRS YPKQHAYHAP SIRSAVPSPF QNTLQNVLAA ATKRNCNVTQ MRELPTLDSA VFNVECFKKF ACNREYWEEF AASPIRITTE NLTTYVTKLK GPKAAALLAR THNLLPLQDV PMDRFTVDMK RDVKVTPGTK HTEERPKVQV IQAAEPLATA YLCGIHRELV RRLNAVLLPN VHTLFDMSAE DFDAIIAAHF KPGDAVLETD IASFDKSQDD SLALTALMLL EDLGVDHSLL DLIEAAFGEI SSCHLPTGTR FKFGAMMKSG MFLTLFVNTL LNITIASRVL EDRLTKSACA AFIGDDNIIH GVVSDELMAA RCATWMNMEV KIIDAVVSQK APYFCGGFIL HDTVTGTACR VADPLKRLFK LGKPLAAGDE QDEDRRRALA DEVIRWQRTG LIDELEKAVY SRYEVQGISV AVMSMATFAS SRSNFEKLRG PVITLYGGPK //