POLG_PRSVH
ID POLG_PRSVH Reviewed; 3344 AA.
AC Q01901;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 151.
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 Papaya ringspot virus (strain P / mutant HA).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=31731;
OH NCBI_TaxID=3649; Carica papaya (Papaya).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX AGRICOLA=IND20450567;
RA Wang C.H., Bau H.J., Yeh S.D.;
RT "Comparison of the nuclear inclusion b protein and coat protein genes of
RT five papaya ringspot virus strains distinct in geographic origin and
RT pathogenicity.";
RL Phytopathology 84:1205-1210(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1402799; DOI=10.1099/0022-1317-73-10-2531;
RA Yeh S.D., Jan F.J., Chiang C.H., Doong T.J., Chen M.C., Chung P.H.,
RA Bau H.J.;
RT "Complete nucleotide sequence and genetic organization of papaya ringspot
RT virus RNA.";
RL J. Gen. Virol. 73:2531-2541(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2561-3344.
RX PubMed=1456896; DOI=10.1007/bf01309597;
RA Wang C.H., Yeh S.D.;
RT "Nucleotide sequence comparison of the 3'-terminal regions of severe, mild,
RT and non-papaya infecting strains of papaya ringspot virus.";
RL Arch. Virol. 127:345-354(1992).
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: [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=Q01901-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CJ98-1; 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; X67673; CAA47905.1; -; Genomic_RNA.
DR EMBL; S46722; AAB23789.1; -; Genomic_RNA.
DR EMBL; X67672; CAA47904.1; -; Genomic_RNA.
DR PIR; JQ1899; JQ1899.
DR RefSeq; NP_056758.1; NC_001785.1.
DR MEROPS; C04.009; -.
DR PRIDE; Q01901; -.
DR GeneID; 1494043; -.
DR KEGG; vg:1494043; -.
DR Proteomes; UP000006688; Genome.
DR Proteomes; UP000007380; 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; IPR022199; DUF3725.
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; PF12523; DUF3725; 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..3344
FT /note="Genome polyprotein"
FT /id="PRO_0000420010"
FT CHAIN 1..547
FT /note="P1 proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040361"
FT CHAIN 548..1004
FT /note="Helper component proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040362"
FT CHAIN 1005..1349
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040363"
FT CHAIN 1350..1401
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040364"
FT CHAIN 1402..2036
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040365"
FT CHAIN 2037..2093
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040366"
FT CHAIN 2094..2282
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040367"
FT CHAIN 2283..2520
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040368"
FT CHAIN 2521..3057
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040369"
FT CHAIN 3058..3344
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040370"
FT DOMAIN 408..547
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 882..1004
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1473..1625
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1644..1803
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2283..2499
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2761..2885
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 3059..3116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 598..601
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 856..858
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1575..1578
FT /note="DECH box"
FT MOTIF 2134..2141
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 3063..3095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 465
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 499
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 890
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 963
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2327
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2362
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2431
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1486..1493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 547..548
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 1004..1005
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1349..1350
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1401..1402
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2036..2037
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2093..2094
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2282..2283
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2520..2521
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 3057..3058
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 2156
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3344 AA; 381046 MW; E90CD7523AC5243D CRC64;
MSSLYTLRAA AQYDRRLESK KGSGWVEHKL ERKGERGNTH YCSEFDISKG AKILQLVQIG
NTEVGRTFLE GNRFVRANIF EIIRKTMVGR LGYDFESELW VCRNCDKTSE KYFKKCDCGE
TYYYSERNLM RTMNDLMYQF DMTPSEINSV DLEYLANAVD YAEQLVKRSQ VPEPVELAMM
EPIVASGEGI LMVSEPEVMP VTTKVEEAWT IQIGEIPVPL VVIKETPVIS GVEGTLNSTG
FSLEADITKL VEKEILQEEV KEAVHLALEV GNEIAEKKPE LKLIPYWSAS LELHKRIRKH
KEHAKIAAIQ VQKEREKDQK VFSALELRLN LKSRRRNQAV VCDKRGTLKW ETQRGHKKSK
LMQQASDFVV TQIHCDFGCK TQYSEPHIPG IKQSTSKKIC KPRKHSRIVG NSKINYIMKN
LCDTIIERGI PVELVTKRCK RRILQKEGRS YVQLRHMNGI RARQDVSSSP DMELLFTQFC
KFLVGHKPLK SKNLTFGSSG LIFKPKFADN VGRYFGDYFV VRGRLGGKLF DGRSKLARSV
YAKMDQYNDV AEKFWLGFNR AFLRHRKPTD HTCTSDMDVT MCGEVAALAT IILFPCHKIT
CNTCMSKVKG RVIDEVGEDL NCELERLRET LSAYGGSFGH VSTLLDQLNR VLNARNMNDG
AFKEIAKKID EKKESPWTHM TTINNTLYKG SLATGYEFER ASNSLREIVR WHLKRTESIK
AGSVESFRNK RSGKAHFNPA LTCDNQLDKN GNFLWGERQY HAKRFFANYF EKIDHSKGYE
YYSQRQNPNG IRKIAIGNLV FSTNLERFRQ QMVEHHIDQG PITRECIALR NNNYVHVCSC
VTLDDGTPAT SELKTPTKNH IVLGNSGDPK YVDLPTLESD SMYIAKKGYC YMNIFLAMLI
NIPENEAKDF TKRVRDLVGS KLGEWPTMLD VATCANQLVV FHPDAANAEL PQILVDHRQK
TMHVIDSFGS VDSGYHILKA NTVNQLIQFA RDPLDSEMKH YIVGGEFDPT TNCLHQLIRV
IYKPHELRSL LRNEPYLIVI ALMSPSVLLT LFNSGAVEHA LNYWIKRDQD VVEVIVLVEQ
LCRKVTLART ILEQFNEIRQ NARDLHELMD RNNKPWISYD RSLELLSVYA NSQLTDEGLL
KQGFSTLDPR LREAVEKTYA TLLQEEWRAL SLFQKLHLRY FAFKSQPSFS EYLKPKGRAD
LKIVYDFSPK YCVHEVGKAF LLPVKAGAKI ASRIINGCGA FIRKSAAKGC AYIFKDLFQF
VHVVLVLSIL LQIFRSAQGI ATEHLQLKQA KAEVERQKDF DRLEALYAEL CVKSGEQPTT
EEFLDFVMER EPRLKDQAYN LIYIPVIHQA KSDNEKKLEQ VIAFITLILM MIDVDKSDCV
YRILNKFKGV INSSNTNVYH QSLDDIRDFY EDKQLTIDFD ITGENQINRG PIDVTFEKWW
DNQLSNNNTI GHYRIGGTFV EFSRVNAATV ASEIAHSPER EFLVRGAVGS GKSTNLPFLL
SKHGSVLLIE PTRPLCENVC KQLRGEPFHC NPTIRMRGLT AFGSTNITIM TSGFALHYYA
HNIQQLRLFD FIIFDECHVI DSQAMAFYCL MEGNAIEKKI LKVSATPPGR EVEFSTQFPT
KIVTEQSISF KQLVDNFGTG ANSDVTAFAD NILVYVASYN EVDQLSKLLS DKGYLVTKID
GRTMKVGKTE ISTSGTKFKK HFIVATNIIE NGVTLDIEAV IDFGMKVVPE MDSDNRMIRY
SKQAISFGER IQRLGRVGRH KEGIALRIGH TEKGIQEIPE MAATEAAFLS FTYGLPVMTH
NVGLSLLKNC TVRQARTMQQ YELSPFFTQN LVNFDGTVHP KIDVLLRPYK LRDCEVRLSE
AAIPHGVQSI WLSARDYEAV GGRLCLEGDV RIPFLIKDVP ERLYKELWDI VQTYKRDFTF
GRINSVSAGK IAYTLRTDVY SIPRTLITID KLIESENMKH AHFKAMTSCT GLNSSFSLLG
VINTIQSRYL VDHSVENIRK LQLAKAQIQQ LEAHMQENNV ENLIQSLGAV RAVYHQSVDG
FKHIKRELGL KGVWDGSLMI KDAIVCGFTM AGGAMLLYQH FRDKFTNVHV FHQGFSARQR
QKLRFKSAAN AKLGREVYGD DGTIEHYFGE AYTKKGNKKG KMHGMGVKTR KFVATYGFKP
EDYSYVRYLD PLTGETLDES PQTDISMVQD HFSDIRRKYM DSDSFDRQAL IANNTIKAYY
VRNSAKAALE VDLTPHNPLK VCDNKLTIAG FPDREAELRQ TGPPRTIQVD QVPPPSKSVH
HEGKSLCQGM RNYNGIASVV CHLKNTSGKG KSLFGIGYNS FIITNRHLFK ENNGELIVKS
QHGKFIVKNT TTLQIAPVGK TDLLIIRMPK DFPPFHSRAR FRAMKAGDKV CMIGVDYQEN
HIASKVSETS IISEGTGDFG CHWISTNDGD CGNPLVSVSD GFIVGLHSLS TSTGDQNFFA
KIPAQFEEKV LRKIDDLTWS KHWSYNINEL SWGALKVWES RPEAIFNAQK EVNQLNVFEQ
SGGRWLFDKL HGNLKGVSSA PSNLVTKHVV KGICPLFRNY LECDEEAKAF FSPLMGHYMK
SVLSKEAYIK DLLKYSSDIV VGEVNHDVFE DSVAQVIELL NDHECPELEY ITDSEVIIQA
LNMDAAVGAL YTGKKRKYFE GSTVEHRQAL VRKSCERLYE GRMGVWNGSL KAELRPAEKV
LAKKTRSFTA APLDTLLGAK VCVDDFNNWF YSKNMECPWT VGMTKFYKGW DEFLKKFPDG
WVYCDADGSQ FDSSLTPYLL NAVLSIRLWA MEDWDIGEQM LKNLYGEITY TPILTPDGTI
VKKFKGNNSG QPSTVVDNTL MVLITMYYAL RKAGYDTKTQ EDMCVFYING DDLCIAIHPD
HEHVLDSFSS SFAELGLKYD FAQRHRNKQN LWFMSHRGIL IDDIYIPKLE PERIVAILEW
DKSKLPEHRL EAITAAMIES WGYGDLTHQI RRFYQWVLEQ APFNELAKQG RAPYVSEVGL
RRLYTSERGS MDELEAYIDK YFERERGDSP ELLVYHESRG TDDYQLVCSN NTHVFHQSKN
EAVDAGLNEK LKEKEKQKEK EKEKQKEKEK DGASDGNDVS TSTKTGERDR DVNVGTSGTF
TVPRIKSFTD KMVLPRIKGK TVLNLNHLLQ YNPQQIDISN TRATHSQFEK WYEGVRNDYG
LNDNEMQVML NGLMVWCIEN GTSPDISGVW VMMDGETQVD YPIKPLIEHA TPSFRQIMAH
FSNAAEAYIA KRNATERYMP RYGIKRNLTD ISLARYAFDF YEVNSKTPDR AREAHMQMKA
AALRNTSRRM FGMDGSVSNK EENTERHTVE DVNRDMHSLL GMRN
