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   27-MAR-2024, entry version 83.
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; Triticum mosaic virus.
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}.
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; FJ263671; ABO41208.2; -; Genomic_RNA.
DR   RefSeq; YP_002956073.1; NC_012799.1.
DR   GeneID; 7984336; -.
DR   KEGG; vg:7984336; -.
DR   Proteomes; UP000008255; Segment.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
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-dependent 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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.90.70.150; Helper component proteinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW   Thiol protease; Transferase; Viral immunoevasion; Viral RNA replication;
KW   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
//