POLG_BTMV
ID POLG_BTMV Reviewed; 3085 AA.
AC Q6XW15;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Beet mosaic virus (BtMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=114921;
OH NCBI_TaxID=124763; Amaranthus retroflexus (Redroot amaranth) (American pigweed).
OH NCBI_TaxID=350892; Beta vulgaris subsp. maritima (Sea beet) (Beta maritima).
OH NCBI_TaxID=3555; Beta vulgaris subsp. vulgaris (Beet).
OH NCBI_TaxID=3559; Chenopodium album (Fat-hen).
OH NCBI_TaxID=200951; Melilotus indicus (Sourclover) (Yellow sweet clover).
OH NCBI_TaxID=50192; Sonchus arvensis (Perennial sowthistle).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15168206; DOI=10.1007/s00705-003-0278-3;
RA Nemchinov L.G., Hammond J., Jordan R., Hammond R.W.;
RT "The complete nucleotide sequence, genome organization, and specific
RT detection of beet mosaic virus.";
RL Arch. Virol. 149:1201-1214(2004).
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=Q6XW15-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CJ96-1; 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; AY206394; AAP41071.1; -; Genomic_RNA.
DR RefSeq; NP_954611.1; NC_005304.1. [Q6XW15-1]
DR MEROPS; C06.001; -.
DR PRIDE; Q6XW15; -.
DR GeneID; 2943205; -.
DR KEGG; vg:2943205; -.
DR Proteomes; UP000007617; 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..3085
FT /note="Genome polyprotein"
FT /id="PRO_0000419994"
FT CHAIN 1..313
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040246"
FT CHAIN 314..770
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040247"
FT CHAIN 771..1117
FT /note="Protein P3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040248"
FT CHAIN 1118..1169
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040249"
FT CHAIN 1170..1803
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040250"
FT CHAIN 1804..1855
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040251"
FT CHAIN 1856..2046
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040252"
FT CHAIN 2047..2293
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040253"
FT CHAIN 2294..2809
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040254"
FT CHAIN 2810..3085
FT /note="Capsid protein"
FT /id="PRO_0000040255"
FT DOMAIN 170..313
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 648..770
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1241..1393
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1412..1571
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2047..2266
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2535..2659
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2801..2869
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 622..624
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1343..1346
FT /note="DESH box"
FT MOTIF 1895..1904
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2811..2841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 233
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 266
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 656
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 729
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2092
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2127
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2198
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1254..1261
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|PROSITE-ProRule:PRU01219"
FT SITE 770..771
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1117..1118
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1169..1170
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 1855..1856
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2046..2047
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2293..2294
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2809..2810
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 3085 AA; 349731 MW; 918576B242794C0D CRC64;
MATMMHFGQF PSNIPLRAAT CCTKVHSTLV TKEMMASSVK PAESSSVARP IIYSSAATDG
YEKAQRAFEA SFREKYSGKL EAMKYGKMVK KGGLTYVKRA GPQAIAKGIE MDAAIEKFNT
AFNAGELENV TLEGDITAGI SVARGESVWL RSVFWSRSLK KQARKKTPKL VAKSDFDDLF
NKVLKVASLG NIPVEIVGKK ANKILRCGYR RVNTSTIPYF HLPHHNSNYI CRELHPQRVR
WLVPLLVRHR KIRDQFSDSM IARGWSGLIL PKYIASTCGR RYDEVIVRGR LYGRVEDART
KLPAGDVGRT MHYSSGEERF FAGWKEGFEK LVPAQKEHIC KIVQDNKFCG KLAASIVQIA
FPCHKMACDV CRNKFNEMTP EAYSELIDKH IDQRMNEINE AIVRFPGLKQ VVSNFRSKHI
ASTNIKDNLE VAKLTQGHKA NQMMQLARIN SILIKGNTAT PSEISDASGL LLEITRWFNN
HLSVIDKGSL RAFRNKRSSK ALVNPSLLCD NQRDKNGNFI WGERGYHSKR FFASHFDEVT
PGDGYKEYII RKGPQGQRKL AIGNLIVSFD LEKTRQALKG EEVEKLPLSN SCVSKRNGNY
VYTSCCVTLD DGTPLYSNIK NPTKRHLVVG TTGDPKIVDL PATDTDKMYI AKEGYCYLNI
FLAMLINVNE NEAKAFTKMV RDIIIPMLGT WPTMQDLATA CFMMTAFFPE TSSAELPRIL
VDHTNQTMHV IDSFGSLTTG YHVLKAGTAA QLIDFASTEL EGEMKWYRVG GHGLPVKEKM
ISALITSIFR PKKLVYLIEE DPYVLIMAMC SPRLIISLFN NGALELAAKH WISRDKNVSA
IFAMLMDLST EMSKAELLIE QHRMINECAK RVHDTQNYLD EVGPHQQEVR TFLALISDEL
EADKELHKTG FANFSERFHS LTEKMYVDAL EEEWRGLSLL DRFSYATFVY KHKPRSTSVL
PPKKSEDIDA KFVISPSWFV GKTKEHLSGG RKYVTSQITQ FTSYIKRATL DRAMRIMCSC
LKDLAYFMNV ALVTHLLISM IAAVYNMLND HRIAKRRLYI LEMQETNTAI WHLYDTWKTV
NQRDPTHEEF RKYVAKVNKN LLRHLPEEED KAEVEYQANK VYEKKLEKAV ALMALFTMIF
DTEKSGAVFS ILRNIKSVFS TLGEEVKYQS LDEIQSIEDE KKLTIDFDLD TEITAEHTTM
DVQFEKWWDK QLSQNRVVPH YRVGGTFIEF TRHTAASVCN TICASSEQEF VVRGAVGSGK
STGLPSHLSR KGRVLLLEPT RPLAENVCKQ LRKEPFHLSP TLRMRGLTTF GSSNISVMTS
GYALHFHANN PQRLEEFDFI MIDESHTMDS STMAFYCLLR EYEFKGKILK VSATPPGREC
EFKTQHDVLI KIEESLSYNS FVTAQGTGSN ADVVQNGDNI LVYVPSYNDV DQLSKGLMEK
GHLVTKVDGR TMKMGNVEIP TKGTSSKKHF IVATNIIENG VTLDIDVVVD FGLKVVAELD
SDSRCMRYKK VSISYGERLQ RLGRVGRVKQ GTALRIGHTE TGMTEIPVAI ATEAAFICFA
YNLPVMTHNV TSSLLSRCTN RQARTMMQYE LSPFFMVELV HFNGCVHPQI ESKLKAYKLR
DSETQLSTLA IPNSGTSRWK TVGEYKKLGV RIEADDNVRV PFAANGVPDR LYADLWETIQ
QHKSDAGFGR LTSACASKIS YTLTTQPNAI PRTLAIIEHL LREEQQKKAY FESLNDTLCA
TSFSLAGMVN NIRRRYLKDH SAHNINVLQN AKSQLNEFNS KAIDPERVGD IMGYGVLDTV
QYQSATDVQK RLKLKGRWNG SLAATDLLIA GAVFAGGCWM LWEYTKSGNE IVQYQGKRRQ
MQKLKFRNAR DNKVGREVYG DDGTIEHFFG AAYTERGKRK GNNSTKGMGT KTRRFVHMYG
FDPTEYSFVR FVDPLTGYSK DESVQTDISL VQSEIGEYRQ KCMEDDDELI DFIKQKPGIQ
AYFMKNGSDK ALQVDLTPHI PLLSCAKTAT IAGFPERESE LRQTGTPIVV NKNVVPGEHK
EVVREEGKSI VKGLRNYNPI SSVVCRLTND SNGNAQTLYG VGFGPLIITN SHLFKMNNGT
LFVRSHQGEF TVQNTTQLQI YHVKDKDMIL IRMPKDFPPF PMKLKFRAPH SEERACLVGS
RFQQKSLSSE VSDSTLIRPT DSGSGYWKHW VSTKEGDCGL PMVALKDGSL IGIHGLTSVR
SELNYFVPFT DDFQSKYLSN IESLEWVKHW RHTPDKVAWN GMTLRENGPA SEFSVSKLIA
DLTHGYVDEV VEQGYSSKWV ANRLDGNLKA VASSSSQLVT KHVVKGPCVL FQEFLATHEE
AARYFVPRMG EYGPSRLNKE AFLKDFLKYA GPITVGVVNT NSFEDAVASV INMLEDLDYG
ECAYVTDPDS IFDSLNMKAA VGALYKGKKK EYFEQLNTTE REDLLRLSCE RLYEGKMGVW
NGSLKAELRP KEKLEQNKTR TFTAAPIDTL LGGKVCVDDF NNRFYSLNLK GPWSVGMTKF
YGGWNELLQK LPDGWIYCDA DGSQFDSSLT PYLINAVVQI REHFMEDWEI GRTMLRNFYT
EIVYTPILTP DGTIVKKFKG NNSGQPSTVV DNTLMVILAM HYAMHQQCWK EEEMKEKIRF
FANGDDLLIA IYPSKEKFLN VLSEYFHELG LKYDFSSRST VRETLWFMSH RGLYLDDMYI
PKLEEERIVS ILEWDRSNEA THRAEAICAA MIEAWGYPEL LKYIREFYLW MMQHECYRDL
VRDGKLPYIA ETALRKLYTD KSVDENELVK YWKALAPEED DGPDIVTYQG DEKPSKSSQP
QSSSPQVPQQ VDAGASSQGR DKQSVIKHDS TKSKDVGQSS TAVPRLKQIS KMRMPVSKGR
QVLALDHLLD YKPEQVDLSN TRATKEQFDN WYEAVMREYD VSDSQMGVIM NGLMVWCIEN
GTSPNLSGDW VMMDGEEQVS FPLKPIVENA KPSFRQIMHH FSDAAEAYIE MRNRERPYMP
RYGAQRNLRD KTLARYAFDF YEVTSRTTDR AREAHFQMKA AALASVSNKL FGLDGSVATT
SEDTERHTAT DVNAHMHHMM GVRQG
