POLG_ZYMVS
ID POLG_ZYMVS Reviewed; 3083 AA.
AC O36979;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Zucchini yellow mosaic virus (strain Singapore) (ZYMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=117130;
OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Lee K.C., Wong S.M.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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=O36979-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK15-1; 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; AF014811; AAB72004.2; -; Genomic_RNA.
DR MEROPS; C06.001; -.
DR Proteomes; UP000008612; 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: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; IPR011492; DEAD_Flavivir.
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; PF07652; Flavi_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; Suppressor of RNA silencing; Thiol protease;
KW Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3083
FT /note="Genome polyprotein"
FT /id="PRO_0000420037"
FT CHAIN 1..313
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040520"
FT CHAIN 314..769
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040521"
FT CHAIN 770..1115
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040522"
FT CHAIN 1116..1167
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040523"
FT CHAIN 1168..1801
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040524"
FT CHAIN 1802..1854
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040525"
FT CHAIN 1855..2044
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040526"
FT CHAIN 2045..2287
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040527"
FT CHAIN 2288..2804
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040528"
FT CHAIN 2805..3083
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040529"
FT DOMAIN 173..313
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 647..769
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1239..1391
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1410..1569
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2045..2263
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2529..2653
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2808..2855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 365..368
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 621..623
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1341..1344
FT /note="DECH box"
FT MOTIF 1894..1903
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2813..2834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 655
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 728
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2090
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2125
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2195
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1252..1259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 313..314
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255"
FT SITE 769..770
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1115..1116
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1167..1168
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1801..1802
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2044..2045
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2287..2288
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2804..2805
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1918
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3083 AA; 351033 MW; B4B6C53C14524A88 CRC64;
MAAIMIGSIS VPIIGSAQCA TAPIGNRVNI VAPGHMAICK PQMRSHAYYK HASQKLSEQS
SRGIEVLNSF FNNDPEDAFR LTRNGMSKVK KGPNGRIILR KPKARHVFER INLEKSEKEQ
KGKFFNGEYD TTVTSIKGVT TSKENDLGAF SLRSPFYKRT CKKEKRRITR ENIVCVDDVN
NLCERILKIT RDKNIPVEII GKRRNHHTLT FKKFKGSFVG KVSLAPERSQ MKHVEMSYGQ
FDYILQAICR ITSTKHVRDE DIKPGCSGWV FSTDHALTQK YSRLPYLVIR GRDDDGIVNA
LEPVLFYSDV EHYSFQNEVQ FFNGWRKMFD KLKPHSDHTC KVDHNNEECG EMAAVLSQAI
FPVLKLSCQV CREKLSRVSF EEFKDFLSRN FMTHESEWST LRDGVHCDNV LKLIKGAVQT
TQNLKLSSDI MKLVQNHTST HMKQIQDINK ALMKGSLVTQ DELDLALKQL LEMTQWFKNH
MHLTGEEALK TFRNKRSNKA MINPSLLCDN QLDKNGNFIW GERGYHSKRL FKNFFEEVIP
SEGYTKYIVR NFPNGTRKLA IGSLIVPLNL DRARTALLGE SIEKEPLTSA CISQQNENYI
HSCCCVTMDD GTPMYSELKS PTKRHLVIGA SGDPKYIDLP ASEAERMYIA KEGYCYLNIF
LAMLVNVNEN EAKDFTKMIR DVLIPMLGQW PSLMDVATAA YILGVFHPET RCAELPRILV
DHATQTMHVI DSYGSLTVGY HVLKAGTVNH LIQFASNDLQ SEMKHYRVGG TPTQRIRLEE
QLIKGIFKPK IMMQLLHDDP YILLLGMISP TILVHMYRMR HFERGIEIWI KRDHEIGKIF
VILEQLTRKV ALAEILVDQL DLISEASPHL LEIMNGCQDN QRAYAPALDL LTIQVEREFS
NKELKTNGYP DLHQTLHDMR EKMYAKQLHN SWQELSLLEK SCVTVRLKQF SIFTERNLTQ
RAKERKHASS LQFVHECFIT TRVHAKSIRD AGVRKLNEAL VGTCKFFFSC GFRIFARCYS
DIIYFVNVCL VFSLVLQMSN TVRNMIAATR EEKERAMANK ADENERTLMH MYHIFCKKQD
DAPIYNDFLE HVRSVRPDLE ETLLYMAGGE VVTAQAKSAV QIQFEKIIAV LALLTMCFDA
ERSDAIFKIL TKLKIVFGTV GETVRLQGLE DIENLEDDKR LTIDFDINTN EAQSSTTFDV
HFEDWWNRQL QQNRTVPHYR TTGKFLEFTR STAAYVANEI ASSSEGEFLV RGAVGSGKST
SLPAHLAKKG KVLLLEPTRP LAENVSRQLA GDPFFQNVTL RMRGLSCFGS SNITVMTSGF
AFHYYVNNPH QLMEFDFVII DECHVTDSAT IAFNCALKEY SFAGKLIKVS ATPPGRECDF
DTQFAVKVKT EDHLSFNAFV GAQKTGSNAD MVQHGNNILV YVASYNEVDM LSKLLTERQF
SVTKVDGRTM QLGKTTIETH GTSQKPHFIV ATNIIENGVT LDVECVVDFG LKVVAELDSE
KRCVRYSKKP VSYGERIQRL GRVGRSKPGT ALRIGHTEKG IENIPEFIAT EAAALSFAYG
LSVTTHGVST NNLGKCTVKQ MKCALNFELT PFFTTHLIRH DGSMHPLIHE ELKQFKLRDS
EMVLNKVALP HQFVSQWMDQ SEYERIGVHI QCHESTRIPF YTNGIPDKVY ERIWKCIQEN
KNDALFGKLS SAFPSKVSYT LSTDPAALPR TIAIIDHLLA EEMMKRNHFD MISSAVTGYS
FSLAGIADSF RKRYMRDHTA HHIAILQQAR AQLLEFNSKN VNINNLSDLE GIGVIKSVVL
QSKQEVSSFL GLRGKWDGRK FANDVILAVM TLFGGGWFMW EYFTKKVNEP VRVESKKRRS
QKLKFRDAYD RKVGREIFGD NDTIGRTFGE AYTKRGKVKG NNSTKGMGRK TRNFVHLYGV
EPEIYSFIRF VDPLTGHTLD ESTHTDISLV QEEFGNIREK FLENDLISRQ SIINKPGIQA
YFMGKGTEEA LKVDLTPHVP LLLCRNTNAI AGYPERENEL RQTGTPIKVS FKEVPEKNEH
VELESKSIYK GVRDYNGIST IVCQLTNDSD GLKETMYGIG YGPIIITNGH LFRKNNGTLL
VRSWHGEFTV KNTTTLKVHF IEGKDVVLVR MPKDFPPFRS NASFRAPKRE ERACLVGTNF
QEKSLRSTVS ESSMTIPEGT GSYWIHWIST NEGDCGLPMV STTDGKIIGI HGLASTVSSK
NYFVPFTDDL LTTHLSKLDD LTWTQHWLWQ PSKIAWGSLN LVDEQPGPEF RISNLVKDLL
TSGVETQSKR ERWVYESCEG NLRAVGSAQS ALVTKHVVKG KCPFFEEYLQ THAEANTYFR
PLMGEYQPSK LNKEAFKKDF FKYNKPVVVN QLDHDKFLGA VNGVIRMMCD FEFNECRFIT
DPEEIYDSLN MKAAIGAQYR GKKKEYFEGL DNFDRERLLF QSCERLFNGH KGLWNGSLKA
ELRPLEKVQA NKTRTFTAAP IDTLLGAKVC VDDFNNEFYS KNLKCPWTVG MTKFYGGWDK
LMRELPDGWL YCHADGSQFD SSLTPALLNA VLIIRSFYME DWWVGQEMLE NLYAEIVYTP
ILAPDGTIFK KFRGNNSGQP STVVDNTLMV VISIYYACMK FGWSYEEIEN KLVFFANGDD
LILAVKDEDS GLLDNMSASF SELGLNYDFS ERTHKREDLW FMSHQAMLVD GMYIPKLEKE
RIVSILEWDR SKEIMHRTEA ICAAMIEAWG HTDLLREIRK FYLWFVEKEE VRELATLGKA
PYIAETALRK LYTDKGAETG ELARYLQALH QDIFFEQGDT VMLQSDTQTR EAGAGASKKD
KDEDKDKKKD VASSSASEKA VATATKDKDV NAGSHGKIVP RLSKITKKMS LPRVKGSVIL
DIDHLLEYKP DQIELYNTRA SHQQFASWFN QVKAEYDLNE QQMGVVMNGF MVWCIENGTS
PDINGVWVMM DGNEQVEYPL KPIVENAKPT LRQIMHHFSD AAEAYIEMRN AEAPYMPRYG
LLRNLRDRSL ARYAFDFYEV NSKTPDRARE AVAQMKAAAL SNVSSRLFGL DGNVATTSED
TERHTARDVN RNMHTLLGVN TMQ
