POLG_BCMNN
ID POLG_BCMNN Reviewed; 3066 AA.
AC Q65399; Q7TL25;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE AltName: Full=N-terminal protein;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
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 common mosaic necrosis virus (strain NL-3) (BCMNV) (Bean common mosaic
OS virus serotype A (strain NL-3)).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=500578;
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Michigan;
RX PubMed=8607279; DOI=10.1016/s0168-1702(95)00072-0;
RA Fang G.W., Allison R.F., Zambolim E.M., Maxwell D.P., Gilbertson R.L.;
RT "The complete nucleotide sequence and genome organization of bean common
RT mosaic virus (NL3 strain).";
RL Virus Res. 39:13-23(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Infectious clone Calhoun;
RA Calhoun C.L., Allison R.F.;
RT "Construction of a BCMNV-full length infectious clone.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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=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=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 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=Q65399-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CJ94-1; 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]: Genome polyprotein of potyviruses undergoes
CC post-translational proteolytic processing by the main proteinase NIa-
CC pro resulting in the production of at least ten individual proteins.
CC The P1 proteinase and the HC-pro cleave only their respective C-termini
CC autocatalytically. 6K1 is essential for proper proteolytic separation
CC of P3 from CI (By 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; U19287; AAB02170.1; -; Genomic_RNA.
DR EMBL; AY282577; AAP38183.1; -; mRNA.
DR RefSeq; NP_660175.1; NC_004047.1.
DR MEROPS; C06.001; -.
DR MEROPS; S30.001; -.
DR PRIDE; Q65399; -.
DR GeneID; 949209; -.
DR KEGG; vg:949209; -.
DR BioCyc; MetaCyc:MON-7715; -.
DR Proteomes; UP000007452; 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 2: Evidence at transcript level;
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..3066
FT /note="Genome polyprotein"
FT /id="PRO_0000419991"
FT CHAIN 1..317
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040223"
FT CHAIN 318..774
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040224"
FT CHAIN 775..1121
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040225"
FT CHAIN 1122..1173
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040226"
FT CHAIN 1174..1807
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040227"
FT CHAIN 1808..1860
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040228"
FT CHAIN 1861..2045
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040229"
FT CHAIN 2046..2288
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040230"
FT CHAIN 2289..2805
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040231"
FT CHAIN 2806..3066
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040232"
FT DOMAIN 176..317
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 652..774
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1245..1397
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1416..1575
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2046..2264
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2530..2654
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2797..2839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 370..373
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 626..628
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1347..1350
FT /note="DECH box"
FT MOTIF 1900..1909
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2802..2833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 239
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 271
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 660
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 733
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2091
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2126
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2196
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1258..1265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 317..318
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 774..775
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1121..1122
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1173..1174
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1807..1808
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1860..1861
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2045..2046
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2288..2289
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2805..2806
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1924
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
FT VARIANT 2029
FT /note="T -> TGLPQT (in strain: Infectious clone Calhoun)"
FT VARIANT 3022
FT /note="R -> A (in strain: Infectious clone Calhoun)"
SQ SEQUENCE 3066 AA; 350390 MW; E358955297FA3F59 CRC64;
MATIMFGSIA AEIPVIKEAI MIAMPKSKHT LHVVQVEAKH MATEIRSERG KLYVAKRFAD
NAIKAYDSQL KAFDELLKKN SDLQKRLFIG QNSPIKQKKG GACFVRSLSF KQAEERHAKY
LKLQEEEHQF LSGAYGDKAY VGSVQGTLDR KVAEKVSFKS PYYKRTCKAV RQVKVLKKAV
GSGKVLDQVL EIVAETGVPV TFVGKGANKT LRAQYVRRYG LVIPKIFLCH ESGRKVHREM
SYWHHKETLQ YLCKHGKYGA LNENALCKGD SGLLFDQRTA FVKRVTYLPH FIVRGRQEGQ
LVCATEYLDN VYTIEHYTHK PEEQFFKGWK QVFDKMAPHT FEHDCTIDYN NEQCGELAAT
ICQTLFPVRK LSCNKCRHRI KDLSWEEFKQ FILAHLGCCA KLWEEQKNLP GLEKIHSFVV
QATSENMIFE TSMEIVRLTQ NYTSTHMLQI QDINKALMKG SSATQEDLKK ASEQLLAMTR
WWKNHMTLTN EDALKTFRNK RSSKALINPS LLCDNQLDRN GNFVWGERGR HSKRFFENFF
EEVVPSEGYK KYVIRNNPNG FRKLAIDSLI VPMDLARARI ALQGESIKRE DLTLACVSKQ
DGNFVYPCCC VTQDDGRPFY SELKSPTKRH LVVGTSGDPK YIDLPATDSD RMYIAKEGYC
YLNIFLAMLV NVNEDEAKDF TKMVRDVVVP KLGTWPSMMD VATAVYIMTV FHPETRSAEL
PRILVDHASQ TMHVIDSFGS LSVGYHVLKA GTVNQLIQFA SNDLEGEMKH YRVGGDAEQR
MRCERALISS IFKPKKMMQI LENDPYTLVL GLVSPTVLIH MFRMKHFEKG VELWINKDQS
VVKIFLLLEH LTRKIAMNDV LLEQLEMISQ QAGRLHEIIC DCPKNIHSYR AVKDFLEVKM
EAALTNKELA NNGFFDINES LGHVSEKIYA KALEKEWRAL SWLEKSSVTW QLKKFSKVTE
EHLTKKAAEG RKESSRKFVS ACFMNAQTHL GNARITISNK VNEVTNLGVR RIVEMCLRLI
HRCYSDMIFL VNISIIFSLF VQMCATLRNT LSIIHRDRTT LARVQAESNE RSIMQMYDLM
TKAGNGPPKM EDFFKHIEMV RPDLLPTAKY MVQDSEAVDT QAKTQTQLQL EKIVAFMALL
TMCIDSERSD AVFKILQKLK SVFGTMGEDV RPQSLDDILD LDEAKQLTVD FDLSTSKEST
STSFDVTFED WWNRQLQQNR VIPHYRTSGE FLEFTRETAA KVANTITLST STEFLIRGAV
GSGKSTGLPH HLSKKGKVLL LEPTRPLAEN VSKQLGRDPF FHAVTLRMRG LNRFGSSNIT
VMTSGFAFHY YVNNPHQLSD FDFIIIDECH VLDSATIAFN CALKEFEFPG KLLKVSATPP
GRECEFTTQH PVKLKVEEHL SFQQFAQAQG TGSNADMVQY GHNLLVYVAS YNEVDQMSRH
LLDRQFHVTK VDGRTMQMGN IEIETHGTEG KPHFIVATNI IENGVTLDVD CVIDFGLKVV
AQLDSDNRCV RYEKKAVSFG ERIQRLGRVG RHKAGFALRI GHTEKSLEEI PEFIATEAAF
LSFAYGLPVT TQGVSTNILS RCTVKQARNA LNFELTPFFT TNFIRYDGSI HPEVHKLLCK
FKLRESEMLL SKLAIPHQYT SQWITVKDYN RIGIQVNCDE KVKIPFYVHG IPDKLFEMLW
NTVCKYKCDA GFGRISSVNA TKISYTLSTD PSALPRTIAI LDHLISEEIM KKNHFDTISS
SLTGHSFSLA GIADGIRKRY LKDYTQQNIA ILQQARAQLL EFNSNTVDLN NLQNYEDLGV
LNTVRLQGKA EVCEFLGLKG KWDGKKFFND VVVAIFTLIG GGWMLWDYFR HYMQEPVSTQ
GRKRMMQKLK FRDAFDRKVG REVYADDYTM EHTFGEAYTK KGKQKGSTHT KGMGKKSRGF
IHMYGVEPEN YSTLRFVDPL TGHTMDESPR VDIRIVQDEF GEIRRQKINE GELDKQAVVA
RPGLQAYFLG KGTEEALKVD LTPHRPTLLC MNSNAIAGFP EREDELRQTV PMSAVPKPNE
VVELESKSTY KGLRDYSSVS TLICRLVNSS DGHNETIYGI GYGSYIITNG HLFRRNNGTL
TVKTWHGDFI IPNTTQLKIH FIEGKDAILI RMPRDFPPFA QRSCFRSPKK EERVCMVGTN
FQEKSLRSTV SESSIIVPEG KGSFWVHWIT TQDGDCGLPM VSVNDGYIVG IHGLTSNETS
RNFFVPFIDE FKNKYLDKLE DLTWNKHWLW QPDRIAWGSL NLVDDQPKSE FKISKLVTDL
FGSEVSVQSK KDRWVLEAVE GNLVACGQAE SALVTKHVVK GKCCHFAQYL SLHPDAQAFF
KPLMSAYQPS KLNKEAFKKD FFKYNKPVML NEVNFEAFEK AVEGVKIMMI EFGFNECVYV
TDPDDIYDSL NMKAAVGAQY KGKKQDYFQD MDSFDKERLL FLSCERLFYG QKGIWNGSLK
AELRPLEKVQ ANKTRTFTAA PIDTLLGAKV CVDDFNNQFY SFNLICPWTV GMTKFYGGWD
KLMRALPDGW VYCHADGSQF DSSLTPLLLN SVLSIRSFFM EDWWVGKEML ENLYAEIVYT
PILTPDGTIF KKFRGNNSGQ PSTVVDNTLM VVISMYYSCI KEGWTYDDIQ ERLVFFANGD
DIILAVQKED VWLYNTLSNS FKELGLNYDF SEQTTKREEL WFMSHQAMLI DDIYIPKLEQ
ERIVSILEWD RSKELMHRTE AICAAMIEAW GHTELLTEIR KFYLWLMGKE EFKELALNGK
APYIAETALR KLYTDKDAKM EEMQEYLKQL EFDSDDEVYE SVSTQSSKKE EEKDAGADER
EKDKGKGPAD KDVGAGSKGK VVPRLQKITK KMNLPMVGGR MILNLDHLIE YKPQQTDLYN
TRATKAQFER WYEAVKTEYE LNDQQMGVVM NGFMVWCIDN GTSPDVNGVW VMMDGDEQIE
YPLKPMVENA KPTLRQVMHH FSDAAEAYIE MRNSEGFYMP RYGLLRNLRD KSLARYAFDF
YEVNSKTSDR AREAVAQMKA ARLANVNTRL FGLDGNVATT SENTERHTAR DVNQNMHHLL
GMTSGQ
