POLG_RGMVD
ID POLG_RGMVD Reviewed; 3086 AA.
AC O11436;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE AltName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Helper component proteinase;
DE Short=HC-pro;
DE EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
DE Contains:
DE RecName: Full=Protein P3;
DE Contains:
DE RecName: Full=6 kDa protein 1;
DE Short=6K1;
DE Contains:
DE RecName: Full=Cytoplasmic inclusion protein;
DE Short=CI;
DE EC=3.6.4.-;
DE Contains:
DE RecName: Full=6 kDa protein 2;
DE Short=6K2;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Nuclear inclusion protein A;
DE Short=NI-a;
DE Short=NIa;
DE EC=3.4.22.44;
DE AltName: Full=49 kDa proteinase;
DE Short=49 kDa-Pro;
DE AltName: Full=NIa-pro;
DE Contains:
DE RecName: Full=Nuclear inclusion protein B;
DE Short=NI-b;
DE Short=NIb;
DE EC=2.7.7.48;
DE AltName: Full=RNA-directed RNA polymerase;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
OS Ryegrass mosaic virus (isolate Denmark/Danish) (RGMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Rymovirus.
OX NCBI_TaxID=652106;
OH NCBI_TaxID=4509; Dactylis glomerata (Orchard grass) (Cock's-foot grass).
OH NCBI_TaxID=4520; Lolium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Schubert J., Merits A., Jaervekuelg L., Paulin L., Rubenstein F.;
RT "The complete nucleotide sequence of the Ryegrass mosaic virus genomic
RT RNA.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC dipeptide at its own C-terminus. Interacts with virions and aphid
CC stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC known as post-transcriptional gene silencing (PTGS), a mechanism of
CC plant viral defense that limits the accumulation of viral RNAs. May
CC have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It
CC may be involved in replication.
CC -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P13529}.
CC -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P09814}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
CC -!- FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-
CC cell and systemis movement, encapsidation of the viral RNA and in the
CC regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
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=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC potyviral polyprotein.; EC=3.4.22.45;
CC Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle
CC membrane. Note=Probably colocalizes with 6K2-induced vesicles
CC associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with
CC host chloroplasts. {ECO:0000250|UniProtKB:P09814}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- DOMAIN: [Helper component proteinase]: The N-terminus is involved in
CC interaction with stylets. The central part is involved in interaction
CC with virions and the C-terminus is involved in cell-to cell movement of
CC the virus.
CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC -!- PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes
CC post-translational proteolytic processing by the main proteinase NIa-
CC pro resulting in the production of at least ten individual proteins.
CC The P1 proteinase and the HC-pro cleave only their respective C-termini
CC autocatalytically. 6K1 is essential for proper proteolytic separation
CC of P3 from CI (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; Y09854; CAA70983.1; -; Genomic_RNA.
DR RefSeq; NP_044727.1; NC_001814.1.
DR MEROPS; C04.012; -.
DR GeneID; 1403650; -.
DR KEGG; vg:1403650; -.
DR Proteomes; UP000000568; Genome.
DR GO; GO:0019029; C:helical 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:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; 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 Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001456; HC-pro.
DR InterPro; IPR031159; HC_PRO_CPD_dom.
DR InterPro; IPR042308; HC_PRO_CPD_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002540; Pept_S30_P1_potyvir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR039560; Potyvirid-P3.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF01577; Peptidase_S30; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF13608; Potyvirid-P3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51744; HC_PRO_CPD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS51871; PV_P1_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Helical capsid protein; Helicase; Host cytoplasmic vesicle; Host membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; RNA-directed RNA polymerase;
KW Serine protease; Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..3086
FT /note="Genome polyprotein"
FT /id="PRO_0000420021"
FT CHAIN 1..256
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146992"
FT CHAIN 257..711
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146993"
FT CHAIN 712..1063
FT /note="Protein P3"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146994"
FT CHAIN 1064..1116
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146995"
FT CHAIN 1117..1753
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146996"
FT CHAIN 1754..1806
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146997"
FT CHAIN 1807..1999
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146998"
FT CHAIN 2000..2240
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000146999"
FT CHAIN 2241..2758
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000255"
FT /id="PRO_5000147000"
FT CHAIN 2759..3086
FT /note="Capsid protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5000147001"
FT DOMAIN 122..256
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 590..711
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1189..1341
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 2000..2217
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2482..2606
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1970..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2762..2822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1291..1294
FT /note="DEAH box"
FT ACT_SITE 173
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 182
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 215
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 598
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 670
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2045
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2080
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2149
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1202..1209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 256..257
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 711..712
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1063..1064
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1116..1117
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1753..1754
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1806..1807
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1999..2000
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2240..2241
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2758..2759
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1870
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3086 AA; 347695 MW; 662EB273DD2CAE72 CRC64;
MMNFGSLNVG LKQVDGTWVP RVFEEKEMAR LLAEKQHARV MRATQEMMKA PNPFAEFDEM
HQRGNPFAGR VRKCETREPK SAQKPIVTVD TVPVAIYTDV IWPENGKVHA LSRRRAPRKH
ARRSKILACD LLTQVLNISR RAGKSVEVIG KRRCCLKPRR RDGKSCFGVI TKHHKGVLSS
RDMVKDLFVD SIIEHIAYTG HTPLIDAADI KPGDSGLIYR EKKDGYVTRV VRGRHDGDII
DARDYVRAGI HTIKHYSDDG KSLVKYAPYC QPSHHTFGHM CRVTWSDTEI LQFREMLSQA
IMPQRDPRCD ICAEVAGQRT KDEILQHART SQMMQMLEFG KEDERWKAPR RVMETLLEES
NWPSMDYSTS SEITTICCGN NDEPFRRIYS IMKVLAEPNL ADVSAWQEAN SSLLQLARYM
KNREMSVQAG NSATFTNPFP PTVHTFGPTN NGADILQGPW DNWGDKQPIA LAFFEKHFNK
WQINEFSIDR RVRKHIRGTR KLALMDLNQS RSIKDLEDHV QEEEIPYERK TESCITMYKD
QYLYSCSCVT ARDGKPYLSM RYLQATGLIP IARGADVQHM PNSDSWQGFY YVAPEGYCYI
NIFLPMLALA PYYKVGKLSE LIGKLIKVLG KWPKLKDVAL ACLYITEYHT YAQNALLPPI
LVHHSTRTMH VVDTLGSLSV GYHVLKAGTV KHLVNLASRL ATGEMLDYNV GGSLGGIHAY
DLLIRSTFDH VLLERALETD PYYILYSALS PTVLKQMYTS KSYANALRVF VRSNQSLFQV
VCTLENLARR MTRAQSIEQQ IMQLQSLYPQ LLDMLADNIP DSPLSWLSHH VTTDSMQRAI
ELNNCDIELA RGGYASINTS WRKKKEQYYA DLIKEYYNAL SPQAKIFVSR AYIGYLHATT
PLFANARKIS SEIASNICTQ AYSRTIGRGI SIVSSGGRKG KTWLTARGDS FYKTMISRAI
KLYTPEVSAV IGVATVVGIL LSTMTTLHTY LVKNKQTAQK TNEKFEELMY DKVALYIPKY
DAEHSHLQGK DLDFEHFARW LMARDKKLSS FVQSHLVDTV THQAKDDTNV WIEKCIATIV
LMMMAIDSNK SDKLYQILCK LRTVFSTMGQ TVVTHQSIDE ILDIDESKRT TIDFERVEVM
QPTQPILKTT FEGFWDMQIQ MGRTVAHYRT TGRLVELTRE NIAEVVATIS SDTANAEFIV
RGGVGTGKST SLPTALCERG RVLMLEPTRP LTENVAQQLR GEPHFKSPSV HMRGLNTFGS
SRITIMTSGY ALHYYANNRQ LLRDFEFIMF DECHVMDSSA MAFYSLCNDA KVAAKLLKVS
ATPAGRECEF KPMFPVRVSE AAQLSFESFV TAQGSKSTYD IIQYGNNILV YVASYNEVDK
LAAMLLEKRF RVTKVDGRTM KLNTHGIELH GTAQVKHFIV ATNIIENGVT LEIDCLVDFG
TKVVAQLDTE GRRIMYMKVP ISYGERIQRL GRVGRTKPGA RLKVGHTMRG IVEIPEVIAT
EAAFQCFMYD LPVMTGQVSV SLLSKCTREQ ARTMAAFELS PFTMSNLVAF DGTMHPAIHD
LLKKFKLRDS TVVLRRTALP LRASASWYTV REYETIIGDL HIENKDVRIP FVANDLSNSL
LEGLWDAIQC NRSDVSTTKL TTVSANKIAY TLKTDTSSIQ RTISIIDDLL AEERKKQEMF
THHLSTTSGG YTFGLNAIAM CIKSRYAKGY CIENIATLTN VRNQLTEFSG MSEDQYTSEI
IQNYPDLTLV HHQSKQEIIR NLKLKAKYDQ TLIASDLLLG TAVLIGGGAM LYKTFMTETN
TRVHLEGDGK RQREKLQYRA ARDSKQDYEV YADEREIQEN YGEAYTKHGR KGPAHEKGTG
SKTREFTNFY GFDPAEYDTV RLVDPITGKT CDKAVRDLLR MRDVADTFAE IRESMDEDMI
LQPGVNFAPA LIEAYFMNSR TNAARRVDLV PHNPMQVGRL SNNIAGFPTH DGELRQSRPS
RPIQKDQVPA ANEYSVQHES KSIAKGLRDY HPVSSNLCAL EYYCGDMRTS IYGVCYGPYI
LTTAHLIKEK GGWLKIRTKH GLFKLEAMDR VQIRELCGSD IIVIKGPKDM PPAPMRLKFR
APKSGERAVL VGFVDDNLDR QLVSDSSAVY RRENTGFWKH WITTKYGNCG LPMVSVDTMD
IIGLHSLGAQ NSNENYFAAL TDDFSKQFFE PETDVPWQRK WSYNADKVNY GTMDLTSNQP
SGAFKTTKLL EDLLEAVSHQ SQEYTWLTKY CGANLLVIGK CPGNLITKHV IKGKSPTFDL
FLSVDAQASD FFKPLMGDYA PSRLNREAFV KDITKYDTEI PIGNLSITDF ENAVEDTYYI
LKDSGIEQCN YITDAIPIFD SMNMKAATGA LYGGKKKDYF ENYTDDMKQN ILKESYIRLR
EGKMGIWNGS LKAELRSKEK VEANKTRVFT AAPLDTLLAG KGCVDDFNNQ FYAAHLKGPW
TVGITKFFGR WNDFLSELPP GWDYFDADGS RFDSSLTPFL LNAVLNIRKK FMINWAFGQR
CLGNLYTEII YTPIATPDGS VVKKMRGNNS GQPSTVVDNT IMVIIAMQYA ISKAEFPAGR
LRDQIRYFAN GDDLVVAVEP SLSDKISSFS ASFAELGLSY DFSNKVNDRS ELQFMSHTGK
LIDGMYIPML ERERICAILE WSRSDEPQFQ LDAISAAMIE AWGDDELLYQ IRRYYSWLLE
QEPYKSIAEL GHAPYLAEAA LKALYTGKDP DAELIAIYER AMLNTPPTED RPTKVVHEAN
VTAASSAATQ TSTTSPTVTS TSGASTSTSS GTTSAPLAST TPPVSATTTP STGTTAPTTP
TVRAANLPDI AGHRKAKANG ESQLNVRGEN DDEDVPAASE FALPRLPTLG AKIRVPKFKG
AIVLNKDHLI KYTPDQRDLS NTRATQEQFE KWYSGVRNEV EKTDEEMALL LNGSMVWCME
NGTSPDLSGS WTMMEGEEQI AYPLEPFCRH AQPTLRSIMA HFSDAATAYV VLRNQKSRYM
PRYGLKRGLN DYSLAPYAFD FYEITSTSPL RARERHAQMK AAAIRGKASR MFGLDGNVSA
QSENTERHTV EDVNTRVHSL SGANML
