POLG_BYMV
ID POLG_BYMV Reviewed; 3056 AA.
AC P17765; Q65887; Q6Y1D8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Bean yellow mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12197;
OH NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH NCBI_TaxID=4627; Canna.
OH NCBI_TaxID=3828; Crotalaria.
OH NCBI_TaxID=52517; Eustoma.
OH NCBI_TaxID=58987; Freesia.
OH NCBI_TaxID=49747; Gladiolus.
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3873; Lupinus luteus (European yellow lupine).
OH NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH NCBI_TaxID=3469; Papaver somniferum (Opium poppy).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=35938; Robinia pseudoacacia (Black locust).
OH NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
OH NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
OH NCBI_TaxID=57577; Trifolium pratense (Red clover).
OH NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
OH NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
OH NCBI_TaxID=97047; Trifolium vesiculosum.
OH NCBI_TaxID=78534; Trigonella foenum-graecum (Fenugreek).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
OH NCBI_TaxID=3908; Vicia sativa (Spring vetch) (Tare).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate GDD;
RX PubMed=14648299; DOI=10.1007/s00705-003-0185-7;
RA Hammond J., Hammond R.W.;
RT "The complete nucleotide sequence of isolate BYMV-GDD of Bean yellow mosaic
RT virus, and comparison to other potyviruses.";
RL Arch. Virol. 148:2461-2470(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2775-3056.
RX PubMed=2671258; DOI=10.1099/0022-1317-70-8-1961;
RA Hammond J., Hammond R.W.;
RT "Molecular cloning, sequencing and expression in Escherichia coli of the
RT bean yellow mosaic virus Capsid protein gene.";
RL J. Gen. Virol. 70:1961-1974(1989).
RN [3]
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=P17765-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CJ95-1; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY192568; AAP30002.1; -; Genomic_RNA.
DR EMBL; D00490; BAA00378.1; -; Genomic_RNA.
DR PIR; JU0115; JU0115.
DR MEROPS; C04.008; -.
DR MEROPS; C06.001; -.
DR MEROPS; S30.002; -.
DR PRIDE; P17765; -.
DR Proteomes; UP000007620; 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..3056
FT /note="Genome polyprotein"
FT /id="PRO_0000419996"
FT CHAIN 1..284
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040256"
FT CHAIN 285..741
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040257"
FT CHAIN 742..1089
FT /note="Protein P3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040258"
FT CHAIN 1090..1142
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040259"
FT CHAIN 1143..1777
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040260"
FT CHAIN 1778..1830
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040261"
FT CHAIN 1831..2021
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040262"
FT CHAIN 2022..2264
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040263"
FT CHAIN 2265..2783
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040264"
FT CHAIN 2784..3056
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040265"
FT DOMAIN 139..284
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 619..741
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1214..1366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1385..1544
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2022..2240
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2507..2630
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2788..2820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..338
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 593..595
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1316..1319
FT /note="DECH box"
FT MOTIF 1871..1878
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2788..2810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 232
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 627
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 700
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2067
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2102
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2172
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1227..1234
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 741..742
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1100..1101
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1152..1153
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1787..1788
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1840..1841
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2021..2022
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2274..2275
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2793..2794
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1893
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
FT VARIANT 2775
FT /note="D -> G"
FT VARIANT 2805
FT /note="D -> N"
FT VARIANT 2855
FT /note="L -> F"
FT VARIANT 2862
FT /note="E -> K"
FT VARIANT 2897
FT /note="Q -> R"
FT VARIANT 2975
FT /note="G -> E"
FT VARIANT 2994
FT /note="K -> E"
FT VARIANT 3017
FT /note="G -> A"
SQ SEQUENCE 3056 AA; 347722 MW; BA4D2F2D2D4624B3 CRC64;
MTTINIGTIP VVINQNADTQ MGEGTKNIFP IVKDFVDPFA DLEMRCAERV KRMGELCFSK
KGRYITMIPK PDYIKAREKE QREEELNFQN SEHVLNSLDT TCTPEHHSSR NNGMQVSFKT
QHYKRTFRKP RIQAKKRDLK GQHTIHYVAK ELLSIVKKRD MVLEVVDKRK HANFATFRRY
GKTYGMHITL NHMVRKRRRV DVTLNKLMTE IAMHCAIPFE CLNTLTLRKG HSGLVLQTET
VPNVHKIKSK ITIVRGVVNE GNIPVLIDAR KKLSGRDMST IREFSAGDLF WKGYNQTFID
NRPTDLNHQC TSDLNVTQCG SVMALLTLAL FPCGRITCKK CVENFLNQNN KERFNNASVF
INQVIQLLEK GFSEFKHSKE ILLMFKERLQ MENPATDQCM EIAKATAALP EAPFSHIKEI
NNVLLKYGSL SNEEVGGASK HLLEVVRYIR NRTDSIQRND LSKFRNKISS KTHINLDLMC
DNQLDKNANF VWGQRAYHAK RFLSNYFNEI NPSEGYDKFI FRKLPNGARE LAIGRLIMPT
NFEAFREQMK GKMIDNGPIG KDCVSRMRGS FCYPCCCTTD DVGTAVISDF KMPTKYHLVL
GGNDLAKYIK LPTDTTGNMY IAKDGFCHIN IFFAMLVNVS EEKSKDFTKM VRDQIMPKLG
EWPTMMDVAT ACWQLTVWFP DTLSAELPRI LVDHKLGIMH VLDSYGSISA GYHVLKANIV
SQLIKFASDD LESELKYYRV GGDCNFGSRV RIDTKFLLKS IYRPDLLERI IEHEPFVLVL
AMQSPAVLLA LFNSASLEKA VQYWMHREMQ VSHIMTLLAV LASNVSASKL LTTQFEIIEA
SAPQILAEMD KVHLPMHSIH SANVFLMNMS ESRETDKTID ELGFYSFKKS SRILMEKTLM
ADLEEQWQGL GLLERLSLIK RSWRVRAKYS SFAIQREEPG IRDKFTTSLK LSGAQIKQQL
LAQKDQAVHF VERRIEGTKK FVANQSISLI KMCLPRLADI VNILTVIALL NAILAFMLDH
IKRFNEARRI AQEKKEKQHL KELNTLYNKY WDNEKPTYLE FKSDVIEKLP HTLATFEKYY
FEDDKYTFQA KPNDMVALEK IIAVTALVLM IFDAERSDCV YKVLNKLKGI LSTTTQDAYR
FQSLDTSKTL LEEKEMTIDF EINEGEVKAF SGTQTTFSEW WDNQLQNGNV ITHYRTEGQF
MEFTRANAQP VANEIAHNDA HDILVRGAVG SGKSTGLPFY LSNKGKVLMI ESTRPLAENV
FKQLKSEPFY ASPTLRMRGT TSYGASPITI MTSGYALHYY ANNPAMMKEY KFVIIDECHV
HDANAIAFVS LLKEYSFDGK LIKVSATPPG REVEFTTQYP VTLVTEESLS FEQFVSQQGT
GANCDMLDVC DNILVYVASY NEVDQLSKML LDRGHIVTKV DGRTMKNGKT EIESKGSRSK
RHFIVATNII ENGVTLDIEG VVDFGLKVVP ELDVDNRLMR YTKQNVSYGE RIQRLGRVGR
HKAGKALRIG VTEKGLVKPP SVITTEAAFY CFAYGLPVMA EGVTPSLLSK CTVQQARSMM
SFELPIMYTV NLVRFDGTMH PSVHNLLKPY KLRDSNVVLN KMAIPHGNVR NWPTVRDFKC
MGVRIDAPED TRVPFHARDI PDKLHKEIFE VCCKYKGDAG FSKLNVVNAC KIAYTLQTDP
SSIQRTIKIL DELIAREQQK REYFQNVANT SCAGSSYSLS NIINAIRARS TSDYTQENLS
VLHSARAQLL EFKNINSDFS NLSTLSEFGA LECLQFESLQ EISKHLQLKG HWNKPVLIQD
FLIAAGVLGG GCWMLYQYFK QETSKAFVFQ GKNRRTKQKL RFRDARDMKG RMEVYADEGT
IVENFGSKYT KKGKVRGTTT GMGTKTRRFT NMYGFDPTEY SFARYLDPIT GETLDEQPIT
NLNLVSEHFQ EMRRKYRENE IMESQQFAAN PRIEAYFVKD AGQKVLKVDL TPHKPLLYSD
KFGNIMGYPE REGELRQTGA AEFIDPKELP EPKESTDFDF ESLSKIGGLR DYNPIAANVC
LLENESAEYC DEIYGIGYGN VIITNQHLFR HNNGELTIKS KHGTFKCKNT CALKLLPIEG
HDLLLIQMPK DFPVFPQKLR FREPTHEDKI VLVSTNFQEK SFSSVVSESS NISRVKQANF
FKHWISTVAG QCGNPMVSTK DGFIVGIHSL TAVSGDLNVF TSIPPNFEDE VLKQMSKKSW
CCGWKLNMSQ IGWDGIKIVD DQPKDPFPVS KMVGLLNDLQ LSFQSAKNTK WLLERAHGNI
KAVAQASSAL VTKHVVKGKC RLFEVYLTTD EEAEKFFRPL MGAYQKSRLN KEAYVKDLMK
YATPIEVGLV DTRCFERSFE KVQNMLELKG FSKCNYVTYG PDILSALNMK AAMGALYSGK
KKDHFSEISE EKFDNILQAS CERLYSGRMG VWNGSLKAEL RPQEKVLANK TRSFTAAPID
TLLAGKVCVD DFNNKFYSLH LKIPSTVGIT KFYGGWDRLL DSLPDGWVYC DADGSQFDSS
LTPYLLNAVL EMRLRLMEEW DLGEQMLKNL YTEIVYTPIL TPDGTIVKKF KGNNSGQPST
VVDNTLMVIM AVYYAAEKLG IKGNLEDTLV FFANGDDLLI AIKPECESYL DKFEGLFSEL
GLKYDFSSRT KNKGDLWFMS HRGIQIDGMW IPKLEEERIV SILEWDRAIQ PEHRLEAICA
AMIEAWGYPT LLNHIRKFYL WVLGQAPYSQ LSAEGKAPYI SEVALKHLYT EEKVTPTELE
RYNIALIDCF ESESDEVLTC RFQSDQEQLN AGEEKKDKRK KNEGDPNKDS EGQSVRQIVP
DRDVNAGTVG TFSVPRLKKI AGKLNIPKIG GKIVLNLDHL LEYNPPQDDI SNVIATQAQF
EAWYNGVKQA YEVEDSQMGI ILNGLMVWCI ENGTSGDLQG EWTMMDGEEQ VTYPLKPILD
NAKPTFRQIM SHFSEVAEAY IEKRNATERY MPRYGLQRNL TDYGLARYAF DFYKLTSRTP
VRAREAHMQM KAAAVRGKST RLFGLDGNVG TDEENTERHT AGDVNRDMHT MLGVRI
