POLG_TRMVU
ID POLG_TRMVU Reviewed; 3112 AA.
AC A4KZ49;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE AltName: Full=N-terminal protein;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
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 Triticum mosaic virus (isolate Triticum aestivum/United
OS States/U06-123/2006) (TriMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Poacevirus.
OX NCBI_TaxID=1289472;
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=19649764; DOI=10.1007/s00705-009-0462-1;
RA Fellers J.P., Seifers D., Ryba-White M., Martin T.J.;
RT "The complete genome sequence of Triticum mosaic virus, a new wheat-
RT infecting virus of the High Plains.";
RL Arch. Virol. 154:1511-1515(2009).
RN [2]
RP PROTEIN SEQUENCE OF 2819-2918; 2953-2968; 2988-3000; 3005-3012 AND
RP 3016-3112.
RA Seifers D.L., Martin T.J., Harvey T.L., Fellers J.P., Stack J.P.,
RA Ryba-White M., Haber S., Krokhin O.V., Spicer V., Lovat N., Yamchuk A.,
RA Standing K.G.;
RT "Triticum mosaic virus: A new virus isolated from wheat in Kansas.";
RL Plant Dis. 92:808-817(2008).
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 Note=Probably colocalizes with 6K2-induced vesicles associated with
CC 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; FJ263671; ABO41208.2; -; Genomic_RNA.
DR RefSeq; YP_002956073.1; NC_012799.1.
DR PRIDE; A4KZ49; -.
DR GeneID; 7984336; -.
DR KEGG; vg:7984336; -.
DR Proteomes; UP000008255; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR025910; P1_Ser_Pept_dom.
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; 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; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF13611; Peptidase_S76; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 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; 1.
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 1: Evidence at protein level;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Direct protein sequencing; Helical capsid protein; Helicase;
KW Host cytoplasmic vesicle; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3112
FT /note="Genome polyprotein"
FT /id="PRO_0000420027"
FT CHAIN 1..383
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395486"
FT CHAIN 384..850
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395487"
FT CHAIN 851..1148
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395488"
FT CHAIN 1149..1204
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395489"
FT CHAIN 1205..1852
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395490"
FT CHAIN 1853..1902
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395491"
FT CHAIN 1903..2095
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395492"
FT CHAIN 2096..2328
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395493"
FT CHAIN 2329..2818
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000395494"
FT CHAIN 2819..3112
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000288836"
FT DOMAIN 234..383
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 729..850
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1278..1429
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1444..1627
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2096..2311
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2569..2687
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2818..2867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1379..1382
FT /note="DECH box"
FT COMPBIAS 2841..2867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 301
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 333
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 737
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 809
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2140
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2174
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2243
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1291..1298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 383..384
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 850..851
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1148..1149
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1204..1205
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1852..1853
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1902..1903
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2095..2096
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2328..2329
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2818..2819
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT CONFLICT 2819
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3112 AA; 352841 MW; 5B066BBD6C5D5151 CRC64;
MSSKKMMWVP KSAHKAPVVS REPVIRKKEW VARQIPKYIP VSNPSDCRDE ISQTLLHFDS
EEAVYDFVWR FPMGSIFWDT NGRIKPVVNC LLRATRMNLD YDVAADVYVC RDCLSCASSY
MYFSNYHYDC RELRENHEAV VSCKYEQHIV STFDVFPRYC TQEIEQNVVN WMTETLERYD
NEPLRIEKQL QFYNHKTEQM ESRVQEVQVT TAEYAVSDTY VPQQLSRKGS VSAKLTQRRA
NKIIMRTHEV ENLIRETIDL CDERQIPITF VDVKHKRCLP RIPLRHMQAK PDISEIVEQG
DMYNEVGQFI EQYQNLAEPF RVIRDYEVTR GWSGVILHRD DLALDPQTQA RCLNNLFVVM
GRCEHGHLQN ALRPDCLEGL TYYSDTFGKV FNESLVKHHP GKHQFRIGSR TDYEWEELAM
WVNAVCPVSF RCADCRPPQS LNEYIENIRM SKAMAELAGR QDALSKTLHK WTTMLISSVL
TTEIRARDNL EPIQERIFTR NMPLGPLYDV AGAMNRAVID IQTAVQNMQL SIGNSNMNEQ
QRNQTLLNEI NKIKQHSFMQ TKEMLSRFEN IAQTYQNIIS SASQPLSIHS MRQLMMDSRM
DESFEFDIMR KKGSIASIAP MAFRTFEDIY SQPGVYNQKW LNLTPSGRFQ TDIDYLRLDL
PIDVIQKKKH VVNRNEIKEE TCYVIVGQVN VSFCEVVARC FVPIPHVLRV GSPQNPTMIK
IQDQEGGKTL VPKSGFCYVL QLVLMLGYVP DQLTAAFVKD VGIVVESLGP WPLFVDYLGA
IKNLIIRYPT TIKAPTALHI VDHVDTVIHV MTTLGCVNKG EHYLTLQSVA QLHDAAMTVN
IETFKDYRIG GVVPQLKHML QSEEHMLEVL EAKPQWLVHL LLSPTQIWAL SQSVVKYQVI
HKVMTSNPDL AVALAQLVAI SSNFSIFKNT EHVIQKYFEV SKQLQNVSGV ILGEHNEYFE
TAFAQYSALR FSTDVVLLMD QFSTRKKTLD DLEDYYRKTI PSILIECGLL GPSDFGWRKR
LVRGVVDRGS GLKSTVKSLG SFSTKEKWIS WSGLGSGTIT CVKFPFVCLQ RSGSWLYSST
KTTAFNAVWM AGIKCVKSNV RSILLDSALY GAITLALLCA IKLIRKAFRF VEGLIKEDTS
DDEDYVLHAK AASDSLYIQC LAWLALVVGC FNSGLANDIY FSTTKYRTLL DMVKTAHSDS
FVFHAGDEEE GEIVELITRD NFVDYVYNHS DPLMEFDSET LLGWYTRISY QGRVLEHPLR
VGTNCHLTRE NVDEIAKNIA TGAGNEFIVV GDVGSGKSTK LPIAVSTYGP VLILVPSREL
VNNLCSSIWH VGKKQASTYM MNCITRGTSN ISIMTYGYAL ALFSHCPIEL QKYRFIQMDE
CHEFSSHMIT FYSWWRESGK FTKLFKTTAT PPGTVIKGGC VPTNHKVDVI EIRDVSVEEF
CRRSIDSHAE GLRSLMPNGG RVIMFVPSRR ECELARSSLI SIPGARTWVV YRAAATQATK
LVAELADDKH YFQIIITTTV LQNGVNLDPD CVVDFGQTFE AAYDRDSRQL GVRRRNINPG
ELIQRVGRVG RNKPGKFIQV GKRLEHEVVP NSCCVTDAIL MSFTLELAPF ISSHLIDEVN
FVTREQVRTA MKFSAPLLFM IHYVRRDGRM LNGYYQQLKG LLLQTSDVAL CDTLVGDAET
NSFLTLRQYQ LRGIIEAQEV LPDLPIPFYS SEFALPFYLE IGQITKEAIR ARSFTLRIKT
PDVKKAVMRL STSATQIDQT IGILRTRLQL TRERLSKFSE LKATAHNLRL TPIFNTCFDM
GAAKSESTLR ASLTAGEELL SALELARTEK SDKALEKLIL DNPVLGDCLV FHGGPEEYFD
QTLFQTSTGL INKYTVGIAC LTVGLGCTIW YYLKKREKYV MHGKVHTRET GLTTNHLFVP
GMKEHIQEWT GGDHEIGNRF GEAYKRRFIG RQPTEEQKLS KEKWDKREGQ QTSVYKTLYD
LDPTKFKYVV VECPDFDLKK KLNRQEKKQL DTTIVEACRT RMLDKGQHDF KDVERATVYL
FNDNGVGHKV QLTPHNPLAV SRTTTHPVGF PAEAGRLRQT GQAMEMTPEE LEKALDDNYV
PHSRCQIDIS HLHRHLAIVN TGGMSTQCFI TQTMCVAPYH LAMGFKDNTK LTIYCSNGVY
VMPVPKVEKM ENMDLVVFRM PQDFPPLKRC ATIREPKSSD EVTLITGKRT THGIQLQFSK
VVSIDRKSDT VWKYMIDSVP GVCGGMVMCV EDGCVVGFHS AAAIRNKVSN GSIFTPVTPQ
LLDSLQSSEG HLFDWYFNDD LISWKGVPTN MDPRNFPVSE TISEFIFHND SKGHGTDKYY
GENLTIEGRV LQSFNTRHVV KGLDDAFAEY VNKFGEPPAD TFTHLPSDLS SDAFYKDFMK
YSTPVEVGTV NIENFEKAVQ AVVELLEQQG FEQGEFSPEM DFYKILNSFN LDTAMGALYQ
CKKKDVLPMA SHEQLATWFW NSLENLATGK LGLWKASLKA ELRPKEKVLE KKTRVFTAAP
FDVSFGAKAF VDDFNNKFYA TQAGSNWTVG INKFNCGWDE LARRFNPDWK FIDADGSRYD
SSLTPLLFNA VLRIRQHFLR ANGFERRMLS NFYTQLVWTP ISTITGQIVK KNKGGPSGQP
STVVDNTMML MIAVEYAKLQ YGVTDLKYVC NGDDLILNAP QGVCETIRAN FSHSFKELGL
TYEFEQEVDS IDQVEYMSHK WIDCGGVLIP KLKPERIVSV LQWNKSLDLA SQANKINAAW
IESFGYGDLS KFIREYANWW GERNGQVGFL CSEEKVASLY LTNDVTIHTE EHDEFVFHSG
ADQSGVVKDQ TGDKAEGSGT KTEDPPNQTT DPVNNPSNGG NKDAPQNLNA TVVTKSYTYI
PPIMKSLVTI DTAKKMADYT PPDALISTQA CTLEQFGRWA NAAANGLGLS MQAFQTDVVP
YWIYWCIVNS ASDEHKKLSS WTKVNMTIDD ATGQINLNEG EAQTIYEMSP MFDEAKPTLR
AVMRHFGALA YRWVKFSIAK RKPIIPHNAI KAGLMDVTYF PCCIDFVTVD QLSPQEQNVR
NQVINARVSD TPRALFKHAQ RAGAGEEDTN LRRDDDANYG RTRVGGAMFG TR
