GenomeNet

Database: UniProt
Entry: P18247
LinkDB: P18247
Original site: P18247 
ID   POLG_PVYN               Reviewed;        3063 AA.
AC   P18247; Q85266; Q85267; Q85268; Q85269; Q85270; Q85271; Q85272; Q85273;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   11-DEC-2019, entry version 155.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
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   Potato virus Y (strain N) (PVY).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12219;
OH   NCBI_TaxID=4071; Capsicum (peppers).
OH   NCBI_TaxID=4085; Nicotiana.
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2732709; DOI=10.1099/0022-1317-70-4-935;
RA   Robaglia C., Durand-Tardif M., Tronchet M., Boudazin G.,
RA   Astier-Manifacier S., Casse-Delbart F.;
RT   "Nucleotide sequence of potato virus Y (N Strain) genomic RNA.";
RL   J. Gen. Virol. 70:935-947(1989).
RN   [2]
RP   SEQUENCE REVISION.
RA   Durand-Tardif M.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=10570213; DOI=10.1073/pnas.96.24.14147;
RA   Voinnet O., Pinto Y.M., Baulcombe D.C.;
RT   "Suppression of gene silencing: a general strategy used by diverse DNA and
RT   RNA viruses of plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14147-14152(1999).
RN   [4]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
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:0000269|PubMed:10570213}.
CC   -!- FUNCTION: [Nuclear inclusion protein B]: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC       {ECO:0000269|PubMed:10570213}.
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:0000269|PubMed:10570213}.
CC   -!- FUNCTION: [Cytoplasmic inclusion protein]: has helicase activity. It
CC       may be involved in replication. {ECO:0000269|PubMed:10570213}.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus replication.
CC       {ECO:0000250}.
CC   -!- FUNCTION: [Nuclear inclusion protein A]: has RNA-binding and
CC       proteolytic activities. {ECO:0000269|PubMed:10570213}.
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=P18247-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ93-1; Sequence=External;
CC   -!- DOMAIN: The N-terminus of helper component proteinase 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: VPg is uridylylated by the polymerase and is covalently attached
CC       to the 5'-end of the genomic RNA. This uridylylated form acts as a
CC       nucleotide-peptide primer for the polymerase (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo post-
CC       translational proteolytic processing. Genome polyprotein is processed
CC       by NIa-pro, P1 and HC-pro proteinases resulting in the production of at
CC       least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1
CC       and HC-pro proteinases resulting in the production of three individual
CC       proteins. The P1 proteinase and the HC-pro cleave only their respective
CC       C-termini autocatalytically. 6K1 is essential for proper proteolytic
CC       separation of P3 from CI (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC       translation.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; X12456; CAA30988.1; -; Genomic_RNA.
DR   EMBL; D00441; BAA00342.1; -; Genomic_RNA.
DR   PIR; JS0166; JS0166.
DR   RefSeq; NP_056759.1; NC_001616.1.
DR   MEROPS; C04.002; -.
DR   PRIDE; P18247; -.
DR   GeneID; 1494052; -.
DR   KEGG; vg:1494052; -.
DR   BRENDA; 3.4.22.45; 5005.
DR   Proteomes; UP000000520; 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: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: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; 3.90.70.150; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   InterPro; IPR013648; PP_Potyviridae.
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; 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   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; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW   Suppressor of RNA silencing; Thiol protease; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..3063
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420017"
FT   CHAIN           1..284
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040407"
FT   CHAIN           285..740
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040408"
FT   CHAIN           741..1105
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040409"
FT   CHAIN           1106..1157
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040410"
FT   CHAIN           1158..1791
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040411"
FT   CHAIN           1792..1843
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040412"
FT   CHAIN           1844..2031
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040413"
FT   CHAIN           2032..2275
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040414"
FT   CHAIN           2276..2796
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040415"
FT   CHAIN           2797..3063
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040416"
FT   DOMAIN          141..284
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          618..740
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1229..1381
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1400..1559
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2032..2250
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2519..2643
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1242..1249
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           334..337
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           592..594
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1331..1334
FT                   /note="DECH box"
FT   MOTIF           1884..1892
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        192
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        201
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        235
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        626
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        699
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2077
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2112
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2182
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            284..285
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            740..741
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1105..1106
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1157..1158
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1791..1792
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1843..1844
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2031..2032
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2275..2276
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2796..2797
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1907
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3063 AA;  347539 MW;  3EC79125DE33F1BB CRC64;
     MATYMSTICF GSFECKLPYS PASCEHIVKE REVPASVDPF ADLETQLSAR LLKQKYATVR
     VLKNGTFTYR YKTDAQIMRI QKKLERKDRE EYHFQMAAPS IVSKITIAGG DPPSKSEPQA
     PRGIIHTTPR MRKVKTRPII KLTEGQMNHL IKQIKQIMSE KRGSVHLISK KTTHVQYKKI
     LGAYSAAVRT AHMMGLRRRV DFRCDMWTVG LLQRLARTDK WSNQVRTINI RRGDSGVILN
     TKSLKGHFGR SSGGLFIVRG SHEGKLYDAR SRVTQSILNS MIQFSNADNF WKGLDGNWAR
     MRYPSDHTCV AGLPVEDCGR VAALMAHSIL PCYKITCPTC AQQYASLPVS DLFKLLHKHA
     RDGLNRLGAD KDRFIHVNKF LIALEHLTEP VDLNLELFNE IFKSIGEKQQ APFKNLNVLN
     NFFLKGKENT AHEWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
     NQLDKNANFL WGQREYHAKR FFSNFFEEID PAKGYSAYEI RKHPSGTRKL SIGNLVVPLD
     LAEFRQKMKG DYRKQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG
     NSGDQKFVDL PKGDSEMLYI AKQGYCYINV FLAMLINISE EDAKDFTKKV RDMCVPKLGT
     WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV VDSFGSQTTG YHILKASSVS
     QLILFANDEL ESDIKHYRVG GVPNASPELG STISPFREGG VIMSESAALK LLLKGIFRPK
     VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
     SAAETLVAQR IIIDAAATDL LDATCDGFNL HLTYPTALMV LQVVKNRNEC DDTLFKAGFP
     SYNTSVVQIM EKNYLNLLND AWKDLTWREN YPQHGTHTEQ NALSTRYIKP TEKADLKGLY
     NISPQAFLGR SAQVVKGTAS GLSERFNNYF NTKCVNISSF FIRRIFRRLP TFVTFVNSLL
     VISMLTSVVA VCQAIILDQR KYRREIELMQ IEKNEIVCME LYASLQRKLE RDFTWDEYIE
     YLKSVNPQIV QFAQAQMEEY DVRHQRSTPV VKNLEQVVAF MALVIMVFDA ERSDCVFKTL
     NKFKGVLSSL DYEVRHQSLD DVIKNFDERN EIIDFELSED TIRTSSVLDT KFSDWWDRQI
     QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST GLPVHLSVAG
     SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSIFGS SPISVMTSGF ALHYFANNRS
     QLAQFNFVIF DECHVLDPSA MAFRSLLSVY HQACKVLKVS ATPVGREVEF TTQQPVKLIV
     EDTVSFQSFV DAQGSKTNAD VVQFGSNVLV YVSSYNEVDT LAKLLTDKNM MVTKVDGRTM
     KHGCLEIVTK GTSARPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKVS
     VSYGERIQRL GRVGRFKKGV ALRIGHTEKG IIEIPSMVAT EAALACFAYN LPVMTGGVST
     SLIGNCTVRQ VKTMQQFELS PFFIQNFVAH DGSMHPVIHD ILKKYKLRDC MTPLCDQSIP
     YRASSTWLSV SEYERLGVAL EIPKQVKIAF HIKEIPPKLH EMLWETVVKY KDVCLFPSIR
     ASSISKIAYT LRTDLFAIPR TLILVERLLE EERVKQSQFR SLIDEGCSSM FSIVNLTNTL
     RARYAKDYTA ENIQKLEKVR SQLKEFSNLD GSACEENLIK RYESLQFVHH QAATSLAKDL
     KLKGIWNKSL VAKDLIIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR IQALKFRHAR
     DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS RRFINMYGFD PTEYSFIQFV
     DPLTGRQIEE NVYADIRDIQ ERFSEVRKKM VENDDIEMQA LGSNTTIHAY FRKDWCDKAL
     KIDLMPHNPL KVCDKTNGIA KFPERELELR QTGPAVEVDV KDIPAQEVEH EAKSLMRGLR
     DFNPIAQTVC RLKVSVEYGA SEMYGFGFGA YIVANHHLFR SYNGSMEVQS MHGTFRVKNL
     HSLSVLPIKG RDIILIKMPK DFPVFPQKLH FRAPTQNERI CLVGTNFQEK YASSIITETS
     TTYNIPGSTF WKHWIETDNG HCGLPVVSTA DGCIVGIHSL ANNAHTTNYY SAFDEDFESK
     YLRTNEHNEW VKSWVYNPDT VLWGPLKLKD STPKGLFKTT KLVQDLIDHD VVVEQAKHSA
     WMFEALTGNL QAVATMKSQL VTKHVVKGEC RHFTEFLTVD AEAEAEAFFR PLMDAYGKSL
     LNRDAYIKDI MKYSKPIDVG VVDRMHLRKP SIGLSSTCNV HGFKKCAYVT DEQEIFKALN
     MKAAVGASYG CKKKDYFEHF TDADKEEIVM QSCLRLYKGL LGIWNGSLKA ELRCKEKILA
     NKTRTFTAAP LDTLLGGKVC VDDFNNQFYS KNIECCWTVG MTKFYGGWDK LLRRLPENWV
     YCDADGSQFD SSLTPYLINA VLTIRSTYME DWDVGLQMLR NLYTEIVYTP ISTPDGTIVK
     KFRGNNSGQP STVVDNSLMV VLAMHYALIK ECVEFEEIDS TCVFFVNGDD LLIAVNPEKE
     SILDRMSQHF SDLGLNYDFS SRTRRKEELW FMSHRGLLIE GMYVPKLEEE RIVSILQWDR
     ADLPEHRLEA ICAAMIESWG YSELTHQIRR FYSWLLQQQP FATIAQEGKA PYIASMALRK
     LYMDRAVDEE ELRAFTEMMV ALDDEFELDS YEVHHQANDT IDAGGSNKKD AKPEQGSIQP
     NPNKGKDKDV NAGTSGTHTV PRIKAITSKM RMPTSKGATV PNLEHLLEYA PQQIDISNTR
     ATQSQFDTWY EAVRMAYDIG ETEMPTVMNG LMVWCIENGT SPNVNGVWVM MDGNEQVEYP
     LKPIVENAKP TLRQIMAHFS DVAEAYIEMR NKKEPYMPRY GLIRNLRDMG LARYAFDFYE
     VTSRTPVRAR EAHIQMKAAA LKSAQPRLFG LDGGISTQEE NTERHTTEDV SPSMHTLLGV
     KNM
//
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