POLG_BVY3
ID POLG_BVY3 Reviewed; 3491 AA.
AC A0AUJ5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Blackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005)
OS (BVY).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Brambyvirus.
OX NCBI_TaxID=686949;
OH NCBI_TaxID=211815; Rubus plicatus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17933412; DOI=10.1016/j.virusres.2007.09.001;
RA Susaimuthu J., Tzanetakis I.E., Gergerich R.C., Martin R.R.;
RT "A member of a new genus in the Potyviridae infects Rubus.";
RL Virus Res. 131:145-151(2008).
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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
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: [Capsid protein]: Virion {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AY994084; AAX87001.1; -; Genomic_RNA.
DR RefSeq; YP_851006.1; NC_008558.1.
DR PRIDE; A0AUJ5; -.
DR GeneID; 5076635; -.
DR KEGG; vg:5076635; -.
DR Proteomes; UP000006703; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 2.60.120.590; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR037151; AlkB-like_sf.
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; IPR005123; Oxoglu/Fe-dep_dioxygenase.
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; 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; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51471; FE2OG_OXY; 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; Dioxygenase;
KW Helical capsid protein; Helicase; Host cytoplasmic vesicle; Hydrolase;
KW Iron; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Oxidoreductase; Phosphoprotein; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3491
FT /note="Genome polyprotein"
FT /id="PRO_0000419995"
FT CHAIN 1..745
FT /note="P1 proteinase"
FT /id="PRO_5000147981"
FT CHAIN 746..1070
FT /note="Helper component proteinase"
FT /id="PRO_5000147982"
FT CHAIN 1071..1420
FT /note="Protein P3"
FT /id="PRO_5000147983"
FT CHAIN 1421..1476
FT /note="6 kDa protein 1"
FT /id="PRO_5000147984"
FT CHAIN 1477..2096
FT /note="Cytoplasmic inclusion protein"
FT /id="PRO_5000147985"
FT CHAIN 2097..2163
FT /note="6 kDa protein 2"
FT /id="PRO_5000147986"
FT CHAIN 2164..2353
FT /note="Viral genome-linked protein"
FT /id="PRO_5000147987"
FT CHAIN 2354..2590
FT /note="Nuclear inclusion protein A"
FT /id="PRO_5000147988"
FT CHAIN 2591..3143
FT /note="Nuclear inclusion protein B"
FT /id="PRO_5000147989"
FT CHAIN 3144..3491
FT /note="Capsid protein"
FT /id="PRO_5000147990"
FT DOMAIN 183..277
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 589..745
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 948..1070
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1540..1692
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1696..1869
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2354..2570
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2850..2974
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 559..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3200..3279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3471..3491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1642..1645
FT /note="DEAH box"
FT COMPBIAS 3216..3252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 640
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 651
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 692
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 956
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 1029
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2400
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2435
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2504
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 268
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 1553..1560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 745..746
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 1070..1071
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1420..1421
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1476..1477
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2096..2097
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2163..2164
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2353..2354
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2590..2591
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 3143..3144
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 2238
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 3491 AA; 393838 MW; E548F95E522B9155 CRC64;
MPTRYRGADR YGNLGYDKVL QSKADAAKRR GLLFDHGSET YECPRCGEIW RNLDDYMAEG
GKMHPKKCLP EECDSDEEQI SSCNAALIHE KWGDLDSDTS SKLSEFYKEP SILTYTTRTH
CVVEKMRSMT APQCIEDIVG VRLHGRTAWF FSKDPTLQYG HHPIYYDTHP WNDELDKYLG
GAKYNTALVQ VYDGTRDLPY HKDDEPCYDI TNNPIRTVNV TGTGDLCISK DKRRLYETIP
MTSGTVITFP ATMQENFYHA VRNPSAGRIS ITFRNQIRTV ERQVAHSANK RWVPIVEARV
TTNESRRGDN KQFQEAQSKL QTKTTINFGE FAAEVDGYYP TLSQDHKPAL PKIIPELGLP
TVDFIYVGNM RVPIDFKKNN VPAIVDTARH VAKIIDSQAL TSEPIKVFTE QREVVGNVVT
CTGTGFSVAD AKEAKALLNG LMYNRASNLF ICPSCSDAAV LPEALLTLEH KRSCELASMK
KISLARNMQV HVKQEAVARL ISQQNSISVP IATLSSCVRG SADTTQVSLH IDEEDSIVDA
IHLPNDFITC DHEHAFETDS ASDNDVETMK KSEKRRKRRK RNPPPVRQVI TRAPVSNIIC
DVILTCLETQ IPVEFIGKSC ITFKPVRVGP VHTVGIQLKH QLHKTGFEVD DLPDRETTSD
IILAATRALR RLRHAHSNAQ QVHNSDITFG TSGAILPWSW LAHDVIVEGP VQDSLVVRGR
NVVSGHVTNA LNLQQDCLAD DYLQYSEELQ PLHDDLSELK PLNVINNELI RQNMHITTLY
SNMSKLQNDA LATKAEMKLP LFGVAQLVVN QLKYNTTTHE WGERGDYVRK FVGKFFADFP
TTQVPKQYMT RTTNGHIRIT AYKALSLTSD PEIMMSRRMT QPMLTTAKQA DCVFQSTTGA
TCTSASCTTN SSGVVLSNKC ADPAPNTLRV RTMWDDIIIE LPLQGGRVHV PLEGLCFSTI
FLHMYLLVPD ESVKLFHRTV TERAMPSLGQ WPTLRHLATW VLNLVAMFPV LSTTPMPEIL
VHHESQSVHI PDCLGTATSG YHRLNIVTPY DFIIFATEIG RNGCQEYRVG GFAHDIKYTV
SLMQDKRKLL HELMLTPTWA FYALSSPTLL KILYRSGALK RTYEHAVMAN HNAVDLVHEL
NFLPERVSRA QTLQDEITAW EANVGRVLQQ VDGYLTRNHD PPLQRWYADA SARLQHLKID
VDLLKNGFRS SQREHVEKKE QLLCDSFERL YNEQNSSLES LKTRCGMGSA RALIKPSGKC
ESPEPAKQLS CKDLICSTKD KYALMLYTQA DALKRKIVAG SQSAFTTVCA GVAYRATKVM
LRTPFNLLNA LNTYSLLIAA VNVMVLVQNY RRDQRKRAQY VNNLETQSMI RHYFAHLEQY
IVNYVPRDEQ FEVIKAKFDE EFPEYNVMFK EVYKERIQFQ SADEGKNMCK IFASAILVMM
VFDAHRADLM YKSFSQVRAL FNTLYDSGNP FNIIFQAERT IAPTMDVIIQ EPKPAIPSTS
SCTFETWFRN CVNANNVIPV IPECDLLDFT RDTASSVVAT LTSSVKREFV IRGFVGSGKS
TYLPHLLTKH GKVLLCEPVR VLASNVFEAL SGSPFYQSPT LLMRGTTKFG SGKITVATSG
YAANYYNANR HRLNEFAYII FDESHQHTAH NFLLRSILDV IGYEGTVLHV SATPIGKEIP
FRTMHPVEVV NMSTLSFEDF AIGQRKQVRC DVFNKGANIL VYVASYNDVD RMSTLLLERG
LRVKKIDART VANVNNITCD GSDGEPLYLV ATNIVENGVT LNVDVVVDFG LCVKPVINAL
QRRVDYVKTP ITWGQRIQRN GRVGRYKNGF CLNVGDVYKT PPIISEDVAL ESALMCFAAN
VPPIFDNVDP ALFGQVTRPQ VQTAQMFELP IYITTPMISD AGALQSDIYQ VIKKFVLREG
SIQLTQDATY LSNMSNWKTI ADYFPDISDT HAMRHEKVPF FVKDFGENSY IALAEAIRKA
RNKSLGARGK LYGDVDATAL LLQTDPGSLD RSIMIVETEL VAQRSKLEDL NHHVHESTGM
FQRYVSHLNH CLRGRYQTDQ IQKNIEVLSN MRSTLVGYRQ VVDKVEPEEI PHFVQQNPNI
TMIIDFQSDR TKADGFVKHG INGIYNYTKI ASDTFSLLLI ACVVIYYVVQ YFFREMKSHI
TFEASGSRRN RLHLRDNKLI KGGYTWAGPS DDMEREFGPE YALKRDKFSE KKARKHMRER
IQPRTNMGVK LAPFQVFYGF DVADYDVLQL FDPITGVKID MDPRATAKEI TEEVEDTPFN
KEVWSDTHMP EKIQATFVKK GGVNREDVLK QVRVDMTTHN PTMVTGSGGI MGYPEHKGDF
RQTGPPKFSI VPEGRSTIKS GNNIAPFISA MGTIKNVYMN GDFDTLACTQ IGNKLVVNAH
IFMEPVKKQE LILQHGVYEL PNNGTINIKH VPGIDMVIQT LPMDVPLARQ IKAYRGPIPG
ELIRLLKIER NTKTNSTSLS DPGTARVGPG TIWYHNITTK HGDCGSLVLS EKDNKIVGIH
TGQQDGTNLN LFAPITKDAI VAIETVLPGE LNDWVFTPDM LDVGSNNAIR KQASDPFPVV
KKLLEGITFQ NNRTTTTDSV SNTAILPARK YWVASDLPVN IKYQCDMPTF FNTRHTYEGE
SQPFMAYLRE CGDAETFFRP LLSHYIPSNL NGDAFKKDFF KYGKPVPVGL VHGPSFKIAS
DRVIKRFERV GYERHSIPFE FDAEAIRDDL NKHAAMGAQY VGKKEQHLDG ISEEQFCDEF
VASCCRLANN CDGVWKGSLK AELRSKEKVQ ENKTRVFTSA PYDVLLGGKA CVMHFNKKFY
ANNTKGPWTV GINKLGLGWH RLLKSLPEGF VYGTGDGSQF DSSLTPLLIN EVCRIRMYFM
QDDELGQAML RGLYRQIIWT LISMPDGSVV RKAKGNPSGQ PSTVDDNTIM VMLAVEYVFA
YLGITQEEMD TIFKYYANGD DLIFAIHPDR ESILNEFTHL FAHLGLNYIF EDRTRNRAEL
EYMSLTGIER EGFYIPKLSR ERISSIVQWR RKGDTRAMFD ALNAAILESW GYDDLTYWLR
KYYEWLIINR YDIDLPEGEK LPYHTETAVE TLYTCDDNTT VYDGRYDFEV PTDASGGVFI
IDFQSSSGTD TPPVIPPATS EPALQPVLTR QTSRPPTPPN TILTGQQQQQ LMPKSSQPYQ
LEPLLAPTGV QQPTFGTFGM PQAQQTTTEP VVAAARVRGK QKEGDTSLSQ VRDHRRLSPE
RIVRHDDDLA PPNESTSGES SHYDELTLPD VPRDKRKGLG ARLKGKPIIT QTQIYNYRPA
FGSIHNNKAT DIELEAWKKQ IADYFQVDDV STLILGFMAY VIENGTSPEI FTNQKFVMAT
SSGEQREYPL APFRSRSVEL RKIMRRFSEE AIDYIQIQRE HNPQYVPRQA VVRNVKRAIY
FPYCFDFIDE TILTPDALEI VHQMKAAALE SASSKVLGLD GGSARAIDTE RHTTEDATAR
THNLRGAAMM A
