POLG_PPVSK
ID POLG_PPVSK Reviewed; 3140 AA.
AC Q84934;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
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 Plum pox potyvirus (strain SK 68) (PPV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=103927;
OH NCBI_TaxID=36596; Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OH NCBI_TaxID=36595; Prunus cerasifera (cherry plum).
OH NCBI_TaxID=3758; Prunus domestica (Garden plum).
OH NCBI_TaxID=105665; Prunus glandulosa.
OH NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH NCBI_TaxID=88123; Prunus salicina.
OH NCBI_TaxID=114937; Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8122394; DOI=10.1007/bf01703390;
RA Palkovics L., Burgyan J., Balazs E.;
RT "Comparative sequence analysis of four complete primary structures of plum
RT pox virus strains.";
RL Virus Genes 7:339-347(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=Q84934-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK04-1; 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; M92280; AAB05823.1; -; Genomic_RNA.
DR MEROPS; C04.001; -.
DR Proteomes; UP000007637; 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; 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; Serine protease; Suppressor of RNA silencing;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3140
FT /note="Genome polyprotein"
FT /id="PRO_0000420009"
FT CHAIN 1..308
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040351"
FT CHAIN 309..766
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040352"
FT CHAIN 767..1116
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040353"
FT CHAIN 1117..1168
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040354"
FT CHAIN 1169..1803
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040355"
FT CHAIN 1804..1856
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040356"
FT CHAIN 1857..2049
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040357"
FT CHAIN 2050..2292
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040358"
FT CHAIN 2293..2810
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040359"
FT CHAIN 2811..3140
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040360"
FT DOMAIN 165..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 644..766
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1240..1392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1411..1570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2050..2268
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2534..2658
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2883..2905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..363
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 618..620
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1342..1345
FT /note="DECH box"
FT MOTIF 1897..1904
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2887..2902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 225
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 259
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 725
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2095
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2130
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2200
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1253..1260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 308..309
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 766..767
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1116..1117
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1168..1169
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1803..1804
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1856..1857
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2049..2050
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2292..2293
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2810..2811
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1919
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3140 AA; 355997 MW; 837A5A692B56436A CRC64;
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLKKQYKE ERERFQFLNG
PDAIVNQISV DKCEASVWVP FPHIIEKPSF TTPSMKKKVV FTKVRMSEAS LQLFMRRVAA
NAKANGQKVE IIGRKRVVGH YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
NTSGFHHVHK KGEITPGMSG FVVNPMNLSD PMHVYDTDLF IVRGKHNSIL VDSRCKVSKE
QSNEIVHYSD PGKQFWDGFT NSFMQCKLRE TDHQCTSDLD VKECGYVAAL VCQAIIPCGK
ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTVMDNYPQF SHVLAFLKRY RELMRVENQN
YEAFKDITHM IGERKEAPFS HLNKINELII KGGMMSAQDY IEASDHLREL ARYQKNRTEN
IRSGSIKAFR NKISSKAHVN MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFDVIDVSEG
YRRHIVRENP RGIRKLAIGN LVMSTNLAAL RKQLLGEECI HFEVSKECTS KRGENFVYQC
CCVTHEDGTP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG YCYINIFLAM
LININEDEAK SFTKTVRDTI VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
AKIFHVVDSF GSLSTGMHVL KANTINQLIS FASDTLDSSM KTYLVGGLEV DKCDEFKNVK
LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI ARSHSLAAIT
AMLSALAAKV SLASTLNAQM SVIDEHAAVL CDSVFVGTKP YASYMMAVKT LERMKARTES
DHTLNDLGFS VLRQATPHLV EKSYLQELEQ AWRELSWSER FSAILESQRW RKHIPKPFIP
KDAADLGGRY DISVRSLLGS QYKRLKDVVR RKRDDVVCYT HQSMGKLFCK AIGISTSFLP
STLKMFDMLI IFGLLLSIGA TCNSMINEHK HLKQVAADRE DKKRFKRLQV LYTRLLEKIG
CTPTADEFLE YVQGENPDLS KYAEDLIGDG QVVVHQSKRD SQANLERVAA FVALVMMLFD
SERSDGVYKI LNKLKGVMGS IDQTVHHQNL DDIEDMLDEK KLTVDFVLQS NEVAPTVPFD
STFEKWWTNQ LETGNVIPHY RTEGHFLEFT RENAAHIANE VMHGSHQDIL IRGAVGSGKS
TGLPFHLSKK GHVLLIEPTR PLAENVCKQL RGQPFNVNPT LRMRGMSTFG STPITVMTSG
YALHFLANNP TYLDNYKCII FDECHVHDAS AMAFRCLLSE YSYPGKILKV SATPPGYEVD
FKTQKEVKVI VEEALSFQQF VSNLGTGCNS DILKHGVNVL VYVASYNEVD TLSKLLTDRS
FKVSKVDGRT MKVGNVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPILDI
DNRLVRYTKK SISYGERIQR LGRVGRNKPG MALRIGFTEK GLTQIPPIIA TEAAFLCFTY
GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVALVR FDGTMHQEIF RLLKSYRLRD
SEVILNKLAI PNSNVCGWMS VRDYKRQGCN LDLDENIRVP FYVKDIPETL HDKVWQAVET
HKSDAGFGRI CSSSACKIAY TLQTDIHSIP RTVKIIDALL EQERTKQAHF RAMTSQSCSS
SNFSLSSITS AIRSKYAKDH TEENIGVLQM AKSQLLEFKN LNIDPSYPEL VRNFGALECV
HHQTKEGVSK TLQLKGHWNK RLITRDATLM LGVLGGGAWM IFTYLKDSFQ EEVVHQGFNR
RQRQKLKFRQ ARDNRMAREV YGDDSTMEDY FGSAYSKKGK SKGKTRGMGT KTRKFVNMYG
YDPTDYNFVR FVDPLTGHTL DENPLMDINL VQEHFSQIRN DYIGDDKITM QHIMSNPGIV
AYYIKDATQK ALKVDLTPHN PLRVCDKTAT IAGFPEREFE LRQTGHPTFV EPNAIPKINE
VGQEEVDHES KSLFRGLRDY NPIASSICQL NNSSGTRHSE MFGLGFGGLI VTNQHLFKRN
DGELTIRSHH GEFVVKDTKT LKLLPCKGRD ILIIRLPKDF PPFPKRLQFR TPTTEDRVCL
IGSNFQTKSI SSTMSETSAT YSVDNSHFWK HWISTKDGHC GLPIVSTRDG SILGLHSLAN
STNTQNFYAA FPDNFETTYL SNQDNDNWIK QWRYNPDEVC WGSLELKRDI PQMPFTVCKL
LTDLDREFVY NQSKTTHWLR DKLEGNLKAV GACPGQLVTK HVVKGKCTLF ETYLLTHPEE
HEFFRPLMGA YQKSALNKDE YVKDLMKYSK PIVVGAVDCE QFERALDVVI SMLISKGFEE
CNYVTDPDDI FSALNMKAAV GALYSGKKRD YFKNASEQDK EDFIKASCKR LFMGKKGVWN
GSLKAELRPK EKVEANKTRS FTAAPIDTLL GGKVCVDDFN NQFYSLNLHC PWSVGMTKFR
GGWDKLLRAL PDGWIYCDAD GSQFDSSLSP YLINAVLNIR LAFMEEWDIG EQMLSNLYTE
IVYTPIATPD GTIVKKFKGN NSGQPSTVVD NTLMVILAMT YSLLKLGYHP DTHECICRYF
VNGDDLVLAV HPAYESMYDE LQEHFSQLGL NYTFTTKTEN KEELWFMSHR GVLFEDMYIP
KLEPERIVSI LEWDRSNEPI HRLEAICASM VEAWGYKELL REIRKFYSWV LEQAPYNALS
KDGKAPYIAE TALRKLYTDS EASETEIERY LEAFYNDVDD SLDSNIVIHQ ADEEEDDEEV
DAGRPTVVTA PAATVATTQP APVIQPAPQT TAPMFNPIFT PATTQPAVRP VPPISGAKPR
SFGVYGNEDA SPSTSNTLVN TGRDRDVDAG SIGTFAVPRL KTMTSKLSLP KVKGKAIMNL
NHLAHYSPAQ VDLSNTRAPQ SCFQTWYEGV KRDYDVTDEE MSIILNGLMV WCIENGTSPN
INGMWVMMDG ETQVEYPIKP LLDHAKPTFR QIMAHFSNVA EAYIEKRNYE KAYMPRYGIQ
RNLTDYSLAR YAFDFYEMTS TTPVRAREAH IQMKAAALRN VQNRLFGLDG NVGTQEEDTE
RHTAGDVNRN MHNLLGVRGV
