POLG_PVYHU
ID POLG_PVYHU Reviewed; 3061 AA.
AC Q02963;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Potato virus Y (strain Hungarian) (PVY).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=31739;
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=8428653; DOI=10.1016/0378-1119(93)90118-m;
RA Thole V., Dalmay T., Burgyan J., Balazs E.;
RT "Cloning and sequencing of potato virus Y (Hungarian isolate) genomic
RT RNA.";
RL Gene 123:149-156(1993).
RN [2]
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: [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 -!- SUBUNIT: [Viral genome-linked protein]: Interacts with host eIF4E
CC protein (via cap-binding region); this interaction mediates the
CC translation of the VPg-viral RNA conjugates (By similarity). Part of a
CC complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction
CC mediates the translation of the VPg-viral RNA conjugates (By
CC similarity). {ECO:0000250|UniProtKB:P18247}.
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: [Viral genome-linked protein]: Host nucleus
CC {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins
CC in the host nucleus. {ECO:0000250|UniProtKB:P21231}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=Q02963-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK06-1; Sequence=External;
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]: Potyviral RNA is expressed as two
CC polyproteins which undergo post-translational proteolytic processing.
CC Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases
CC resulting in the production of at least ten individual proteins. P3N-
CC PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC the production of three individual proteins. The P1 proteinase and the
CC HC-pro cleave only their respective C-termini autocatalytically. 6K1 is
CC essential for proper proteolytic separation of P3 from CI (By
CC 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}.
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DR EMBL; M95491; AAB59762.1; -; Genomic_RNA.
DR PIR; JN0545; JN0545.
DR MEROPS; C04.002; -.
DR PRIDE; Q02963; -.
DR Proteomes; UP000008616; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
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:0019048; P:modulation by virus of host process; ISS:UniProtKB.
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; 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; 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 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 nucleus;
KW Host-virus interaction; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3061
FT /note="Genome polyprotein"
FT /id="PRO_0000420016"
FT CHAIN 1..284
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040397"
FT CHAIN 285..740
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040398"
FT CHAIN 741..1105
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040399"
FT CHAIN 1106..1157
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040400"
FT CHAIN 1158..1791
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040401"
FT CHAIN 1792..1843
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040402"
FT CHAIN 1844..2031
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040403"
FT CHAIN 2032..2275
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040404"
FT CHAIN 2276..2794
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040405"
FT CHAIN 2795..3061
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040406"
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 2517..2641
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2795..2835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 1242..1249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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 2794..2795
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|UniProtKB:P09814"
SQ SEQUENCE 3061 AA; 347330 MW; 737FFBA215B56F99 CRC64;
MATYTSTIQI GSIECKLPYS PAPFGLVAGK REVSTTTDPF ASLEMQLSAR LRRQEFATIR
TSKNGTCMYR YKTDAQIARI QKKREERERE EYNFQMAASS VVSKITIAGG EPPSKLESQV
RKGVIHTTPR MRTAKTYRTP KLTEGQMNHL IKQVKQIMST KGGSVQLISK KSTHVHYKEV
LGSHRAVVCT AHMRGLRKRV DFRCDKWTVV RLQHLARTDK WTNQVRATDL RKGDSGVILS
NTNLKGHFGR SSEGLFIVRG SHEGKIYDAR SKVTQGVMDS MVQFSSAESF WEGLDGNWAQ
MRYPTDHTCV AGIPVEDCGR VAAIMTHSIL PCYKITCPTC AQQYANLPAS DLLKILHKHA
SDGLNRLGAD KDRFVHVKKF LTILEHLTEP VDLSLEIFNE VFKSIGEKQQ SPFKNLNILN
NFFLKGKENT AREWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
NQLDKNANFL WGQREYHAKR FFSNYFEEID PAKGYSAYEN RLHPNGTRKL AIGNLIVPLD
LAEFRRKMKG DYKRQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAVESTFY PPTKKHLVIG
NSGDQKYVDL PKGNSEMLYI ARQGFCYINI FLAMLINISE EDAKDFTKKV RDMCVPKLGT
WPTMMDLATT CAQMKIFYPD VHDAELPRIL VDHETQTCHV VDSFGSQTTG YHILKASSVS
QLILFANDEL ESDIKHYRVG GIPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPK
VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVKLWI NEKQSIAMIA SLLSALALRV
SAAETLVAQR IIIDTAATDL LDATCDGFNL HLTYPTALMV LQVVKNRNEC DDTLFKAGFP
SYNTSVVQIM EKNYLNLLND AWKDLTWREK LSATWYSYRA KRSITRYIKP TGRADLKGLY
NISPQAFLGR GAQVVKGTAS GLSERFNNYF NTKCVNISSF FIRRIFRRLP TFVTFVNSLL
VISMLTSVVA VCQAIILDQR KYRREIELMQ IEKNEIVCME LYASLQRKLE RDFTWDEYIE
YLKSVNPQIV QFAQAQMEEY DVRHQRSTPG VKNLEQVVAF MALVIMVFDA ERSDCVFKTL
NKFKGVLSSL DHEVRHQSLD DVIKNFDERN ETIDFELSED TIRTSSVLDT KFSDWWDRQI
QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST GLPVHLSVAG
SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSIFGS SPISVMTSGF ALHYFANNRS
QLAQFNFVIF DECHVLDPSA MAFRSLLSVY HQACKVLKVS ATPVGREVEF TTQQPVKLIV
EDTLSFQSFV DAQGSKTNAD VVQFGSNVLV YVSSYNEVDT LAKLLTDKNM MVTKVDGRTM
KHGCLEIVTR GTSARPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKVS
VSYGERIQRL GRVGRFKKGV ALRIGHTEKG IIENPSMIAT 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
KLKGTWKKSL VAKDLIIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR IQALKFRHAR
DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS RRFVNMYGFD PTEYSFIQFV
DPLTGAQIEE NVYADIRDIQ ERFSDVRKKM VEDDEIELQA LGSNTTIHAY FRKDWSDKAL
KIDLMPHNPL KICDKSNGIA KFPERELELR QTGPAIEVDV KDIPKQEVEH EAKSLMRGLR
DFNPIAQTVC RVKVSAEYGT SEMYGFGFGA YIIVNHHLFK SFNGSMEVRS MHGTFRVKNL
HSLSVLPIKG RDIIIIKMPK DFPVFPQKLH FRAPVQNERI CLVGTNFQEK HASSIITETS
TTYNVPGSTF WKHWIETNDG HCGLPVVSTA DGCLVGIHSL ANNVQTTNYY SAFDEDFESK
YLRTNEHNEW TKSWVYNPDT VLWGPLKLKE STPKGLFKTT KLVQDLIDHD VVVEQAKHSA
WMYEALTGNL QAVATMKSQL VTKHVVKGEC RHFKEFLTVD SEAEAFFRPL MDAYGKSLLN
REAYIKDIMK YSKPIDVGIV DCDAFEEAIN RVIIYLQVHG FQKCNYITDE QEIFKALNMK
AAVGAMYGGK KKDYFEHFTE ADKEEIVMQS CPRLYKGSLG IWNGSLKAEL RCKEKILANK
TRTFTAAPLD TLLGGKVCVD DFNNQFYSKN IECCWTVGMT KFYGGWDRLL RRLPENWVYC
DADGSQFDSS LTPYLINAVL IIRSTYMEDW DLGLQMLRNL YTEIIYTPIS TPDGTIVKKF
RGNNSGQPST VVDNSLMVVL AMHYALIKEC VEFEEIDSTC VFFVNGDDLL IAVNPEKESI
LDRMSQHFSD LGLNYDFSSR TRRKEELWFM SHRGLLIEGM YVPKLEEERI VSILQWDRAD
LPEHRLEAIC AAMIESWGYS ELTHQIRRFY SWLLQQQPFS TIAQEGKAPY IASMALKKLY
MNRTVDEEEL KAFTEMMVAL DDELECDTYE VHHQGNDTID AGGSTKKDAK QEQGSIQPNL
NKEKEKDVNV GTSGTHTVPR IKAITSKMRM PKSKGAAVLN LKHLLEYAPQ QIDISNTRAT
QSQFDTWYEA VQLAYDIGET EMPTVMNGLM VWCIENGTSP NINGVWVMMD GDEQVEYPLK
PIVENAKPTL RQIMAHFSDV AEAYIEMRNK KEPYMPRYGL VRNLRDGSLA RYAFDFYEVT
SRTPVRAREA HIQMKAAALK SAQSRLFGLD GGISTQEENT ERHTTEDVSP SMHTLLGVKN
M
